Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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O00488 | ZN593_HUMAN | MGRSRRTGAHRAHSLARQMKAKRRRPDLDEIHRELRPQGSARPQPDPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVPPRRLAVPTEVSTEVPEMDTST | null | null | negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding [GO:1903026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; preribosome binding [GO:1990275]; zinc ion binding [GO:0008270] | PF12171; | 3.30.160.60; | ZNF593/BUD20 C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Cytoplasm {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q08004}. | null | null | null | null | null | FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:32669547). Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity (PubMed:9115366). {ECO:0000269|PubMed:9115366, ECO:0000305|PubMed:32669547}. | Homo sapiens (Human) |
O00499 | BIN1_HUMAN | MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP | null | null | cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; lipid tube assembly [GO:0060988]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902960]; negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ventricular cardiac muscle cell action potential [GO:1903946]; nucleus localization [GO:0051647]; nucleus organization [GO:0006997]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of apoptotic process [GO:0043065]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of endocytosis [GO:0045807]; regulation of cell cycle process [GO:0010564]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of neuron differentiation [GO:0045664]; synaptic vesicle endocytosis [GO:0048488]; T-tubule organization [GO:0033292] | actin cytoskeleton [GO:0015629]; axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; cerebellar mossy fiber [GO:0044300]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; I band [GO:0031674]; lipid tube [GO:0060987]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RNA polymerase II transcription repressor complex [GO:0090571]; synaptic vesicle [GO:0008021]; T-tubule [GO:0030315]; varicosity [GO:0043196]; vesicle [GO:0031982]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; clathrin binding [GO:0030276]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein-folding chaperone binding [GO:0051087]; RNA polymerase binding [GO:0070063]; tau protein binding [GO:0048156] | PF03114;PF14604; | 1.20.1270.60;2.30.30.40; | null | PTM: Phosphorylated by protein kinase C. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform BIN1]: Nucleus {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.; SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm {ECO:0000269|PubMed:9182667}. | null | null | null | null | null | FUNCTION: Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863). {ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:24755653, ECO:0000269|PubMed:27179792, ECO:0000269|PubMed:28893863, ECO:0000269|PubMed:8782822}. | Homo sapiens (Human) |
O00501 | CLD5_HUMAN | MGSAALEILGLVLCLVGWGGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYDSVLALSTEVQAARALTVSAVLLAFVALFVTLAGAQCTTCVAPGPAKARVALTGGVLYLFCGLLALVPLCWFANIVVREFYDPSVPVSQKYELGAALYIGWAATALLMVGGCLLCCGAWVCTGRPDLSFPVKYSAPRRPTATGDYDKKNYV | null | null | bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell-cell junction assembly [GO:0007043]; establishment of blood-retinal barrier [GO:1990963]; face morphogenesis [GO:0060325]; learning [GO:0007612]; maintenance of blood-brain barrier [GO:0035633]; myelination [GO:0042552]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell migration [GO:0030336]; negative regulation of gene expression [GO:0010629]; negative regulation of vascular permeability [GO:0043116]; outflow tract morphogenesis [GO:0003151]; positive regulation of bicellular tight junction assembly [GO:1903348]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of establishment of endothelial barrier [GO:1903142]; positive regulation of gene expression [GO:0010628]; positive regulation of protein binding [GO:0032092]; response to ethanol [GO:0045471]; roof of mouth development [GO:0060021]; tight junction assembly [GO:0120192]; transforming growth factor beta receptor signaling pathway [GO:0007179] | apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cell-cell junction [GO:0005911]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]; tight junction [GO:0070160] | identical protein binding [GO:0042802]; structural molecule activity [GO:0005198] | PF00822; | 1.20.140.150; | Claudin family | null | SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}. | Homo sapiens (Human) |
O00505 | IMA4_HUMAN | MAENPSLENHRIKSFKNKGRDVETMRRHRNEVTVELRKNKRDEHLLKKRNVPQEESLEDSDVDADFKAQNVTLEAILQNATSDNPVVQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVKCLERDDNPSLQFEAAWALTNIASGTSAQTQAVVQSNAVPLFLRLLRSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVIVNLCRNKDPPPPMETVQEILPALCVLIYHTDINILVDTVWALSYLTDGGNEQIQMVIDSGVVPFLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDVLSHFPNLLSHPKEKINKEAVWFLSNITAGNQQQVQAVIDAGLIPMIIHQLAKGDFGTQKEAAWAISNLTISGRKDQVEYLVQQNVIPPFCNLLSVKDSQVVQVVLDGLKNILIMAGDEASTIAEIIEECGGLEKIEVLQQHENEDIYKLAFEIIDQYFSGDDIDEDPCLIPEATQGGTYNFDPTANLQTKEFNF | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; protein-containing complex assembly [GO:0065003]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | cytosol [GO:0005829]; host cell [GO:0043657]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:34564892}. Nucleus {ECO:0000269|PubMed:34564892}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9. | Homo sapiens (Human) |
O00506 | STK25_HUMAN | MAHLRGFANQHSRVDPEELFTKLDRIGKGSFGEVYKGIDNHTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYFGSYLKSTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWKSEGHGEESSSEDSDIDGEAEDGEQGPIWTFPPTIRPSPHSKLHKGTALHSSQKPAEPVKRQPRSQCLSTLVRPVFGELKEKHKQSGGSVGALEELENAFSLAEESCPGISDKLMVHLVERVQRFSHNRNHLTSTR | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | axonogenesis [GO:0007409]; cellular response to oxidative stress [GO:0034599]; establishment of Golgi localization [GO:0051683]; establishment or maintenance of cell polarity [GO:0007163]; Golgi localization [GO:0051645]; Golgi reassembly [GO:0090168]; intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:0036481]; positive regulation of axonogenesis [GO:0050772]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; response to oxidative stress [GO:0006979]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF20929;PF00069; | 1.10.12.70;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15037601}. Golgi apparatus {ECO:0000269|PubMed:15037601}. Note=Localizes to the Golgi apparatus. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753). {ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:18782753}. | Homo sapiens (Human) |
O00507 | USP9Y_HUMAN | MTAITHGSPVGGNDSQGQVLDGQSQHLFQQNQTSSPDSSNENSVATPPPEEQGQGDAPPQHEDEEPAFPHTELANLDDMINRPRWVVPVLPKGELEVLLEAAIDLSVKGLDVKSEACQRFFRDGLTISFTKILMDEAVSGWKFEIHRCIINNTHRLVELCVAKLSQDWFPLLELLAMALNPHCKFHIYNGTRPCELISSNAQLPEDELFARSSDPRSPKGWLVDLINKFGTLNGFQILHDRFFNGSALNIQIIAALIKPFGQCYEFLSQHTLKKYFIPVIEIVPHLLENLTDEELKKEAKNEAKNDALSMIIKSLKNLASRISGQDETIKNLEIFRLKMILRLLQISSFNGKMNALNEINKVISSVSYYTHRHSNPEEEEWLTAERMAEWIQQNNILSIVLQDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPGQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAQSDDVPVDIMDLALSAHIKILDYSCSQDRDAQKIQWIDHFIEELRTNDKWVIPALKQIREICSLFGEASQNLSQTQRSPHIFYRHDLINQLQQNHALVTLVAENLATYMNSIRLYAGDHEDYDPQTVRLGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCRERKLIAKRRSYMMDDLELIGLDYLWRVVIQSSDEIANRAIDLLKEIYTNLGPRLKANQVVIHEDFIQSCFDRLKASYDTLCVFDGDKNSINCARQEAIRMVRVLTVIKEYINECDSDYHKERMILPMSRAFRGKHLSLIVRFPNQGRQVDELDIWSHTNDTIGSVRRCIVNRIKANVAHKKIELFVGGELIDSEDDRKLIGQLNLKDKSLITAKLTQINFNMPSSPDSSSDSSTASPGNHRNHYNDGPNLEVESCLPGVIMSVHPRYISFLWQVADLGSNLNMPPLRDGARVLMKLMPPDRTAVEKLRAVCLDHAKLGEGKLSPPLDSLFFGPSASQVLYLTEVVYALLMPAGVPLTDGSSDFQVHFLKSGGLPLVLSMLIRNNFLPNTDMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPVVDGTDPITQINQVTHDQAVVLQSALQSIPNPSSECVLRNESILLAQEISNEASRYMPDICVIRAIQKIIWASACGALGLVFSPNEEITKIYQMTTNGSNKLEVEDEQVCCEALEVMTLCFALLPTALDALSKEKAWQTFIIDLLLHCPSKTVRQLAQEQFFLMCTRCCMGHRPLLFFITLLFTILGSTAREKGKYSGDYFTLLRHLLNYAYNGNINIPNAEVLLVSEIDWLKRIRDNVKNTGETGVEEPILEGHLGVTKELLAFQTSEKKYHFGCEKGGANLIKELIDDFIFPASKVYLQYLRSGELPAEQAIPVCSSPVTINAGFELLVALAIGCVRNLKQIVDCLTEMYYMGTAITTCEALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIEGTGSDLHDDMFGDEKQDSESNVDPRDDVFGYPHQFEDKPALSKTEDRKEYNIGVLRHLQVIFGHLAASQLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMGPYTVAGVANLERDNVNSENELIEQKEQSDNETAGGTKYRLVGVLVHSGQASGGHYYSYIIQRNGKDDQTDHWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYEQMDMIDEDDEMIRYISELTIARPHQIIMSPAIERSVRKQNVKFMHNRLQYSLEYFQFVKKLLTCNGVYLNPAPGQDYLLPEAEEITMISIQLAARFLFTTGFHTKKIVRGPASDWYDALCVLLRHSKNVRFWFTHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGSCPSPFASPGPSSQACDNLSLSDHLLRATLNLLRREVSEHGHHLQQYFNLFVMYANLGVAEKTQLLKLNVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSTMQSSINGNPPLPNPFGDLNLSQPIMPIQQNVLDILFVRTSYVKKIIEDCSNSEDTIKLLRFCSWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLFQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSSCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYSYNNWSPPVQSNETANGYFLERSHSARMTLAKACELCPEEEPDDQDAPDEHEPSPSEDAPLYPHSPASQYQQNNHVHGQPYTGPAAHHLNNPQKTGQRTQENYEGNEEVSSPQMKDQ | 3.4.19.12 | null | BMP signaling pathway [GO:0030509]; cell migration [GO:0016477]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; spermatogenesis [GO:0007283]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | co-SMAD binding [GO:0070410]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type peptidase activity [GO:0008234] | PF12030;PF00443; | 3.90.70.10; | Peptidase C19 family | null | null | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:12895410}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12895410}. | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins (PubMed:12895410). May stabilize target proteins that are important for male germ cell development (PubMed:12895410). {ECO:0000269|PubMed:12895410}. | Homo sapiens (Human) |
O00512 | BCL9_HUMAN | MHSSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKQGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQDSQHTPHSMTPSNATAPRSSTPSHGQTTATEPTPAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNNKTERSTAPLNTQISALRNDPKPLPQQPPAPANQDQNSSQNTRLQPTPPIPAPAPKPAAPPRPLDRESPGVENKLIPSVGSPASSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSSGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNPGVLDGPQKKPEGPIQAMMAQSQSLGKGPGPRTDVGAPFGPQGHRDVPFSPDEMVPPSMNSQSGTIGPDHLDHMTPEQIAWLKLQQEFYEEKRRKQEQVVVQQCSLQDMMVHQHGPRGVVRGPPPPYQMTPSEGWAPGGTEPFSDGINMPHSLPPRGMAPHPNMPGSQMRLPGFAGMINSEMEGPNVPNPASRPGLSGVSWPDDVPKIPDGRNFPPGQGIFSGPGRGERFPNPQGLSEEMFQQQLAEKQLGLPPGMAMEGIRPSMEMNRMIPGSQRHMEPGNNPIFPRIPVEGPLSPSRGDFPKGIPPQMGPGRELEFGMVPSGMKGDVNLNVNMGSNSQMIPQKMREAGAGPEEMLKLRPGGSDMLPAQQKMVPLPFGEHPQQEYGMGPRPFLPMSQGPGSNSGLRNLREPIGPDQRTNSRLSHMPPLPLNPSSNPTSLNTAPPVQRGLGRKPLDISVAGSQVHSPGINPLKSPTMHQVQSPMLGSPSGNLKSPQTPSQLAGMLAGPAAAASIKSPPVLGSAAASPVHLKSPSLPAPSPGWTSSPKPPLQSPGIPPNHKAPLTMASPAMLGNVESGGPPPPTASQPASVNIPGSLPSSTPYTMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNNMPGMGINTQNPRISGPNPVVPMPTLSPMGMTQPLSHSNQMPSPNAVGPNIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPSGGQGSFPGGMGFPGEGPLGRPSNLPQSSADAALCKPGGPGGPDSFTVLGNSMPSVFTDPDLQEVIRPGATGIPEFDLSRIIPSEKPSQTLQYFPRGEVPGRKQPQGPGPGFSHMQGMMGEQAPRMGLALPGMGGPGPVGTPDIPLGTAPSMPGHNPMRPPAFLQQGMMGPHHRMMSPAQSTMPGQPTLMSNPAAAVGMIPGKDRGPAGLYTHPGPVGSPGMMMSMQGMMGPQQNIMIPPQMRPRGMAADVGMGGFSQGPGNPGNMMF | null | null | canonical Wnt signaling pathway [GO:0060070]; myoblast differentiation [GO:0045445]; myotube differentiation involved in skeletal muscle regeneration [GO:0014908]; positive regulation of transcription by RNA polymerase II [GO:0045944]; skeletal muscle cell differentiation [GO:0035914]; somatic stem cell population maintenance [GO:0035019]; transcription by RNA polymerase II [GO:0006366] | beta-catenin-TCF complex [GO:1990907]; cis-Golgi network [GO:0005801]; nucleoplasm [GO:0005654]; sarcoplasm [GO:0016528] | beta-catenin binding [GO:0008013]; transcription coactivator activity [GO:0003713] | PF11502; | 3.30.40.10; | BCL9 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11955446}. | Homo sapiens (Human) |
O00519 | FAAH1_HUMAN | MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS | 3.1.1.-; 3.5.1.99 | null | arachidonic acid metabolic process [GO:0019369]; fatty acid catabolic process [GO:0009062]; monoacylglycerol catabolic process [GO:0052651]; positive regulation of vasoconstriction [GO:0045907] | cytoskeleton [GO:0005856]; endoplasmic reticulum membrane [GO:0005789]; organelle membrane [GO:0031090] | acylglycerol lipase activity [GO:0047372]; amidase activity [GO:0004040]; fatty acid amide hydrolase activity [GO:0017064]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543] | PF01425; | 3.90.1300.10; | Amidase family | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:17015445}; Single-pass membrane protein {ECO:0000269|PubMed:17015445}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17015445}. Note=Seems to be attached to intracellular membranes and a portion of the cytoskeletal network. | CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine; Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788, ECO:0000269|PubMed:9122178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788, ECO:0000269|PubMed:9122178}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenamide + H2O = (9Z)-octadecenoate + NH4(+); Xref=Rhea:RHEA:26506, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30823, ChEBI:CHEBI:116314; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:9122178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:9122178}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:21049984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:21049984}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl) ethanolamine = (9Z)-octadecenoate + ethanolamine; Xref=Rhea:RHEA:45060, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57603, ChEBI:CHEBI:71466; Evidence={ECO:0000269|PubMed:17015445}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45061; Evidence={ECO:0000269|PubMed:17015445}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine + hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanamide = hexadecanoate + NH4(+); Xref=Rhea:RHEA:62984, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:74475; Evidence={ECO:0000269|PubMed:9122178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62985; Evidence={ECO:0000269|PubMed:9122178}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecamide = NH4(+) + tetradecanoate; Xref=Rhea:RHEA:62992, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30807, ChEBI:CHEBI:137125; Evidence={ECO:0000269|PubMed:9122178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62993; Evidence={ECO:0000269|PubMed:9122178}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-taurine = (9Z)-octadecenoate + taurine; Xref=Rhea:RHEA:63148, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:146191, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17015445}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63149; Evidence={ECO:0000269|PubMed:17015445}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienamide + H2O = (9Z,12Z,15Z)-octadecatrienoate + NH4(+); Xref=Rhea:RHEA:62976, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32387, ChEBI:CHEBI:142684; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62977; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenamide + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + NH4(+); Xref=Rhea:RHEA:63016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32395, ChEBI:CHEBI:137830; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63017; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(6Z)-octadecenamide + H2O = (6Z)-octadecenoate + NH4(+); Xref=Rhea:RHEA:63008, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32375, ChEBI:CHEBI:146168; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63009; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(15Z)-tetracosenamide + H2O = (15Z)-tetracosenoate + NH4(+); Xref=Rhea:RHEA:63028, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32392, ChEBI:CHEBI:146166; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63029; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienamide + H2O = (8Z,11Z,14Z)-eicosatrienoate + NH4(+); Xref=Rhea:RHEA:62996, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:71589, ChEBI:CHEBI:146163; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62997; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z,17Z)-eicosatrienamide + H2O = (11Z,14Z,17Z)-eicosatrienoate + NH4(+); Xref=Rhea:RHEA:63000, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:77223, ChEBI:CHEBI:146164; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63001; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienamide + H2O = (11Z,14Z)-eicosadienoate + NH4(+); Xref=Rhea:RHEA:63004, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:77220, ChEBI:CHEBI:146165; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63005; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienamide + H2O = (9Z,12Z)-octadecadienoate + NH4(+); Xref=Rhea:RHEA:63020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30245, ChEBI:CHEBI:82984; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63021; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + methanol; Xref=Rhea:RHEA:63052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:32395, ChEBI:CHEBI:78033; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63053; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z)-eicosenamide + H2O = (11Z)-eicosenoate + NH4(+); Xref=Rhea:RHEA:63120, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32426, ChEBI:CHEBI:146167; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63121; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-hexadecenoyl) ethanolamine = (9Z)-hexadecenoate + ethanolamine; Xref=Rhea:RHEA:35563, ChEBI:CHEBI:15377, ChEBI:CHEBI:32372, ChEBI:CHEBI:57603, ChEBI:CHEBI:71465; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35564; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl ethanolamine = ethanolamine + octadecanoate; Xref=Rhea:RHEA:63124, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:57603, ChEBI:CHEBI:85299; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63125; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-docosanoyl-ethanolamine = docosanoate + ethanolamine; Xref=Rhea:RHEA:63128, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858, ChEBI:CHEBI:57603, ChEBI:CHEBI:146186; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63129; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetracosanoyl-taurine = taurine + tetracosanoate; Xref=Rhea:RHEA:63140, ChEBI:CHEBI:15377, ChEBI:CHEBI:31014, ChEBI:CHEBI:132049, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63141; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)-ethanolamine = (15Z)-tetracosenoate + ethanolamine; Xref=Rhea:RHEA:63144, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57603, ChEBI:CHEBI:146187; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63145; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-docosanoyl-taurine = docosanoate + taurine; Xref=Rhea:RHEA:63156, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858, ChEBI:CHEBI:146196, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63157; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)-taurine = (15Z)-tetracosenoate + taurine; Xref=Rhea:RHEA:63160, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:146198, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63161; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-tricosanoyl-taurine = taurine + tricosanoate; Xref=Rhea:RHEA:63164, ChEBI:CHEBI:15377, ChEBI:CHEBI:79007, ChEBI:CHEBI:146197, ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63165; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, ChEBI:CHEBI:59002; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; Evidence={ECO:0000250|UniProtKB:O08914}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, ChEBI:CHEBI:149697; Evidence={ECO:0000250|UniProtKB:O08914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; Evidence={ECO:0000250|UniProtKB:O08914}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.7 nmol/min/mg enzyme for the hydrolysis of oleamide ((9Z)-octadecenamide) {ECO:0000269|PubMed:17015445}; Vmax=2.1 nmol/min/mg enzyme for the hydrolysis of N-palmitoyl ethanolamine (N-hexadecanoyl ethanolamine) {ECO:0000269|PubMed:17015445}; Vmax=5.6 nmol/min/mg enzyme for the hydrolysis of N-oleoyl ethanolamine (N-(9Z-octadecenoyl)-ethanolamine) {ECO:0000269|PubMed:17015445}; Vmax=17 nmol/min/mg enzyme for the hydrolysis of anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) {ECO:0000269|PubMed:17015445}; Vmax=0.75 nmol/min/mg enzyme for the hydrolysis of N-oleoyltaurine (N-(9Z-octadecenoyl)-taurine) {ECO:0000269|PubMed:17015445}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 9.0. {ECO:0000269|PubMed:17015445}; | null | FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:17015445, PubMed:19926788, PubMed:9122178). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed:17015445, PubMed:9122178). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:21049984). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity). {ECO:0000250|UniProtKB:O08914, ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788, ECO:0000269|PubMed:21049984, ECO:0000269|PubMed:9122178}. | Homo sapiens (Human) |
O00522 | KRIT1_HUMAN | MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS | null | null | angiogenesis [GO:0001525]; cell redox homeostasis [GO:0045454]; endothelium development [GO:0003158]; integrin activation [GO:0033622]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; regulation of angiogenesis [GO:0045765]; regulation of establishment of cell polarity [GO:2000114]; small GTPase-mediated signal transduction [GO:0007264] | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | GTPase regulator activity [GO:0030695]; microtubule binding [GO:0008017]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF13857;PF00373;PF16705; | 1.20.80.10;1.25.40.20;3.30.70.2240;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in a ITGB1BP1-dependent manner. | null | null | null | null | null | FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (PubMed:26417067). {ECO:0000250|UniProtKB:Q6S5J6, ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20616044, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21633110, ECO:0000269|PubMed:23317506, ECO:0000269|PubMed:26417067}. | Homo sapiens (Human) |
O00526 | UPK2_HUMAN | MAPLLPIRTLPLILILLALLSPGAADFNISSLSGLLSPALTESLLVALPPCHLTGGNATLMVRRANDSKVVTSSFVVPPCRGRRELVSVVDSGAGFTVTRLSAYQVTNLVPGTKFYISYLVKKGTATESSREIPMSTLPRRNMESIGLGMARTGGMVVITVLLSVAMFLLVLGFIIALALGSRK | null | null | epithelial cell differentiation [GO:0030855] | apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | null | PF07353; | null | Uroplakin-2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00533 | NCHL1_HUMAN | MEPLLLGRGLIVYLMFLLLKFSKAIEIPSSVQQVPTIIKQSKVQVAFPFDEYFQIECEAKGNPEPTFSWTKDGNPFYFTDHRIIPSNNSGTFRIPNEGHISHFQGKYRCFASNKLGIAMSEEIEFIVPSVPKFPKEKIDPLEVEEGDPIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQKGDLYFANVEEKDSRNDYCCFAAFPRLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPTESGSESSITILKGEILLLECFAEGLPTPQVDWNKIGGDLPKGRETKENYGKTLKIENVSYQDKGNYRCTASNFLGTATHDFHVIVEEPPRWTKKPQSAVYSTGSNGILLCEAEGEPQPTIKWRVNGSPVDNHPFAGDVVFPREISFTNLQPNHTAVYQCEASNVHGTILANANIDVVDVRPLIQTKDGENYATVVGYSAFLHCEFFASPEAVVSWQKVEEVKPLEGRRYHIYENGTLQINRTTEEDAGSYSCWVENAIGKTAVTANLDIRNATKLRVSPKNPRIPKLHMLELHCESKCDSHLKHSLKLSWSKDGEAFEINGTEDGRIIIDGANLTISNVTLEDQGIYCCSAHTALDSAADITQVTVLDVPDPPENLHLSERQNRSVRLTWEAGADHNSNISEYIVEFEGNKEEPGRWEELTRVQGKKTTVILPLAPFVRYQFRVIAVNEVGRSQPSQPSDHHETPPAAPDRNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYRVTWKPQGAPVEWEEETVTNHTLRVMTPAVYAPYDVKVQAINQLGSGPDPQSVTLYSGEDYPDTAPVIHGVDVINSTLVKVTWSTVPKDRVHGRLKGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDAFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPTFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYEIGELNDINITTPSKPSWHLSNLNATTKYKFYLRACTSQGCGKPITEESSTLGEGSKGIGKISGVNLTQKTHPIEVFEPGAEHIVRLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLLLLTVCFVKRNRGGKYSVKEKEDLHPDPEIQSVKDETFGEYSDSDEKPLKGSLRSLNRDMQPTESADSLVEYGEGDHGLFSEDGSFIGAYAGSKEKGSVESNGSSTATFPLRA | null | null | adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; brain development [GO:0007420]; cell adhesion [GO:0007155]; cognition [GO:0050890]; exploration behavior [GO:0035640]; negative regulation of neuron apoptotic process [GO:0043524]; neuron migration [GO:0001764]; signal transduction [GO:0007165] | apical part of cell [GO:0045177]; axon [GO:0030424]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632]; protease binding [GO:0002020] | PF13882;PF00041;PF07679;PF00047;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, L1/neurofascin/NgCAM family | PTM: Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors (By similarity). Cleaved by BACE1 (By similarity). {ECO:0000250|UniProtKB:P70232}.; PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc) (By similarity). {ECO:0000250}.; PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Soluble forms produced by cleavage/shedding also exist. {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like protein]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons and in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00541 | PESC_HUMAN | MGGLEKKKYERGSATNYITRNKARKKLQLSLADFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIRFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNTVERLKDNKPNYKLDHIIKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFMHYIIAARALRKVFLSIKGIYYQAEVLGQPIVWITPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQLLNLHYPPKLEGQAQAEAKAGEGTYALDSESCMEKLAALSASLARVVVPATEEEAEVDEFPTDGEMSAQEEDRRKELEAQEKHKKLFEGLKFFLNREVPREALAFIIRSFGGEVSWDKSLCIGATYDVTDSRITHQIVDRPGQQTSVIGRCYVQPQWVFDSVNARLLLPVAEYFSGVQLPPHLSPFVTEKEGDYVPPEKLKLLALQRGEDPGNLNESEEEEEEDDNNEGDGDEEGENEEEEEDAEAGSEKEEEARLAALEEQRMEGKKPRVMAGTLKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDEAVRSEKKAKKARPE | null | null | cell population proliferation [GO:0008283]; maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000466]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; regulation of cell cycle [GO:0051726]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364] | chromosome [GO:0005694]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; PeBoW complex [GO:0070545]; preribosome, large subunit precursor [GO:0030687] | ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723] | PF16589;PF06732; | 3.40.50.10190; | Pescadillo family | PTM: Sumoylated. | SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. {ECO:0000255|HAMAP-Rule:MF_03028}. | null | null | null | null | null | FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269}. | Homo sapiens (Human) |
O00548 | DLL1_HUMAN | MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHERGHRYVCECARGYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWVAVCAGVILVLMLLLGCAAVVVCVRLRLQKHRPPADPCRGETETMNNLANCQREKDISVSIIGATQIKNTNKKADFHGDHSADKNGFKARYPAVDYNLVQDLKGDDTAVRDAHSKRDTKCQPQGSSGEEKGTPTTLRGGEASERKRPDSGCSTSKDTKYQSVYVISEEKDECVIATEV | null | null | astrocyte development [GO:0014002]; cell differentiation [GO:0030154]; cell fate determination [GO:0001709]; cerebellar molecular layer formation [GO:0021688]; cerebellar Purkinje cell layer structural organization [GO:0021693]; clathrin-dependent endocytosis [GO:0072583]; compartment pattern specification [GO:0007386]; determination of left/right symmetry [GO:0007368]; endothelial tip cell fate specification [GO:0097102]; energy homeostasis [GO:0097009]; heart looping [GO:0001947]; hemopoiesis [GO:0030097]; inhibition of neuroepithelial cell differentiation [GO:0002085]; inner ear auditory receptor cell differentiation [GO:0042491]; lateral inhibition [GO:0046331]; left/right axis specification [GO:0070986]; loop of Henle development [GO:0072070]; marginal zone B cell differentiation [GO:0002315]; myeloid cell differentiation [GO:0030099]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of cell differentiation [GO:0045596]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epidermal cell differentiation [GO:0045605]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of hemocyte differentiation [GO:0045611]; negative regulation of inner ear auditory receptor cell differentiation [GO:0045608]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of Notch signaling pathway [GO:0045746]; nephron development [GO:0072006]; neuroepithelial cell differentiation [GO:0060563]; neuron fate specification [GO:0048665]; neuronal stem cell population maintenance [GO:0097150]; Notch signaling pathway [GO:0007219]; Notch signaling pathway involved in arterial endothelial cell fate commitment [GO:0060853]; organ growth [GO:0035265]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endocytosis [GO:0045807]; positive regulation of gene expression [GO:0010628]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of skeletal muscle tissue growth [GO:0048633]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal tubule development [GO:0072014]; proximal/distal pattern formation [GO:0009954]; regulation of blood pressure [GO:0008217]; regulation of cell adhesion [GO:0030155]; regulation of cell division [GO:0051302]; regulation of growth [GO:0040008]; regulation of neurogenesis [GO:0050767]; regulation of skeletal muscle tissue growth [GO:0048631]; regulation of somitogenesis [GO:0014807]; regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030947]; regulation of vascular endothelial growth factor signaling pathway [GO:1900746]; retina development in camera-type eye [GO:0060041]; retina morphogenesis in camera-type eye [GO:0060042]; skeletal muscle tissue growth [GO:0048630]; skin epidermis development [GO:0098773]; somite specification [GO:0001757]; somitogenesis [GO:0001756]; spinal cord development [GO:0021510]; type B pancreatic cell development [GO:0003323] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018]; scaffold protein binding [GO:0097110]; Tat protein binding [GO:0030957] | PF21700;PF01414;PF00008;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation (By similarity). Ubiquitinated; promotes recycling back to the plasma membrane and confers a strong affinity for NOTCH1. Multi-ubiquitination of Lys-613 by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as activation of Notch signaling. Ubiquitinated by NEURL1B (By similarity). {ECO:0000250|UniProtKB:P10041, ECO:0000250|UniProtKB:Q61483}.; PTM: Phosphorylated in a membrane association-dependent manner. Phosphorylation at Ser-697 requires the presence of Ser-694, whereas phosphorylation at Ser-694 occurs independently of the other site. Phosphorylation is required for full ligand activity in vitro and affects surface presentation, ectodomain shedding, and endocytosis. {ECO:0000250|UniProtKB:Q61483}.; PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG. {ECO:0000250|UniProtKB:P97677}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q61483}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q61483}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q61483}. Membrane raft {ECO:0000250|UniProtKB:Q61483}. Note=Distributed around adherens junction in the apical endfeet through interactions with MAGI1. {ECO:0000250|UniProtKB:Q61483}. | null | null | null | null | null | FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:11006133). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (By similarity). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation (PubMed:11581320). Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B-cells (By similarity). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (PubMed:11581320). Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation through regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis (By similarity). {ECO:0000250|UniProtKB:P97677, ECO:0000250|UniProtKB:Q61483, ECO:0000269|PubMed:11006133, ECO:0000269|PubMed:11581320}. | Homo sapiens (Human) |
O00555 | CAC1A_HUMAN | MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDGEQRHPFDALRRTTIKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSAKLENSTFFHKKERRMRFYIRRMVKTQAFYWTVLSLVALNTLCVAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYGLGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAAIMTVFQILTGEDWNEVMYDGIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTSEMRKQNLLASREALYNEMDPDERWKAAYTRHLRPDMKTHLDRPLVVDPQENRNNNTNKSRAAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREGPYGRESDHHAREGSLEQPGFWEGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESAAPHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEDDRGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIALAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIVVSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNILIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFEKDCRGKYLLYEKNEVKARDREWKKYEFHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMWQFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAFGILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDVEDEDSDEDEFQITEHNNFRTFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGILTRECGNEFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAAWGRMPYLDMYQMLRHMSPPLGLGKKCPARVAYKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMDAELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQDRTPLMFQRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWVTQRAQEMFQKTGTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAENQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRSHRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHHPPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQQQAVARPGRAATSGPRRYPGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGPPGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGPACASPSRHGRRLPNGYYPAHGLARPRGPGSRKGLHEPYSESDDDWC | null | null | calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cellular response to amyloid-beta [GO:1904646]; chemical synaptic transmission [GO:0007268]; modulation of chemical synaptic transmission [GO:0050804]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; response to amyloid-beta [GO:1904645] | cell projection [GO:0042995]; cytoplasm [GO:0005737]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891] | amyloid-beta binding [GO:0001540]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; syntaxin binding [GO:0019905]; voltage-gated calcium channel activity [GO:0005245] | PF08763;PF16905;PF00520; | 1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350; | Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:26716990}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:10753886, ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:15293273, ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:24836863, ECO:0000269|PubMed:26716990}; | null | null | null | null | FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are specifically blocked by the spider omega-agatoxin-IVA (AC P54282) (By similarity). They are however insensitive to dihydropyridines (DHP). {ECO:0000250|UniProtKB:P54282, ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:10753886, ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:15293273, ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:24836863, ECO:0000269|PubMed:26716990}. | Homo sapiens (Human) |
O00559 | RCAS1_HUMAN | MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS | null | null | adaptive immune memory response involving T cells and B cells [GO:0090717]; regulation of cell growth [GO:0001558]; T cell mediated cytotoxicity [GO:0001913] | Golgi membrane [GO:0000139]; secretory granule [GO:0030141] | peptidase activator activity involved in apoptotic process [GO:0016505] | null | null | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12672804}; Single-pass type III membrane protein {ECO:0000269|PubMed:12672804}. Note=According to PubMed:10426319, it also exists as a soluble form which has the same biological activities. The existence of such soluble form is however uncertain. | null | null | null | null | null | FUNCTION: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases. {ECO:0000269|PubMed:12054692, ECO:0000269|PubMed:12138241, ECO:0000269|PubMed:12672804}. | Homo sapiens (Human) |
O00560 | SDCB1_HUMAN | MSLYPSLEDLKVDKVIQAQTAFSANPANPAILSEASAPIPHDGNLYPRLYPELSQYMGLSLNEEEIRANVAVVSGAPLQGQLVARPSSINYMVAPVTGNDVGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTITMHKDSTGHVGFIFKNGKITSIVKDSSAARNGLLTEHNICEINGQNVIGLKDSQIADILSTSGTVVTITIMPAFIFEHIIKRMAPSIMKSLMDHTIPEV | null | null | actin cytoskeleton organization [GO:0030036]; chemical synaptic transmission [GO:0007268]; intracellular signal transduction [GO:0035556]; negative regulation of receptor internalization [GO:0002091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; presynapse assembly [GO:0099054]; protein targeting to membrane [GO:0006612]; Ras protein signal transduction [GO:0007265]; regulation of mitotic cell cycle [GO:0007346]; substrate-dependent cell migration, cell extension [GO:0006930] | adherens junction [GO:0005912]; azurophil granule lumen [GO:0035578]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; focal adhesion [GO:0005925]; interleukin-5 receptor complex [GO:0005895]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | cell adhesion molecule binding [GO:0050839]; cytoskeletal anchor activity [GO:0008093]; ephrin receptor binding [GO:0046875]; frizzled binding [GO:0005109]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-5 receptor binding [GO:0005137]; ionotropic glutamate receptor binding [GO:0035255]; neurexin family protein binding [GO:0042043]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein heterodimerization activity [GO:0046982]; protein sequestering activity [GO:0140311]; protein-containing complex binding [GO:0044877]; syndecan binding [GO:0045545] | PF00595; | 2.30.42.10; | null | PTM: Phosphorylated on tyrosine residues. | SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:11179419}. Cell junction, adherens junction {ECO:0000269|PubMed:11179419}. Cell membrane {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:27386966}; Peripheral membrane protein {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:27386966}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17081065}; Peripheral membrane protein {ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:11179419}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cytoplasm, cytosol {ECO:0000269|PubMed:11179419}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11179419}. Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}. Membrane raft {ECO:0000269|PubMed:25893292}. Note=Mainly membrane-associated. Localized to adherens junctions, focal adhesions and endoplasmic reticulum. Colocalized with actin stress fibers. Also found in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) (PubMed:27386966). {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:27386966}. | null | null | null | null | null | FUNCTION: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis (PubMed:26291527). Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1 (PubMed:25893292). In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (PubMed:22660413). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types (PubMed:26539120). In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) (PubMed:11498591). May also play a role in vesicular trafficking (PubMed:11179419). Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (PubMed:10230395). {ECO:0000269|PubMed:10230395, ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:11498591, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:26539120, ECO:0000303|PubMed:26291527}. | Homo sapiens (Human) |
O00562 | PITM1_HUMAN | MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMADIRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSEEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELGAEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLSPEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMTQPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDFLRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE | null | null | brain development [GO:0007420]; lipid metabolic process [GO:0006629]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid transport [GO:0015914]; phototransduction [GO:0007602]; protein transport [GO:0015031] | cell body [GO:0044297]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; intracellular membrane-bounded organelle [GO:0043231]; lipid droplet [GO:0005811]; membrane [GO:0016020]; midbody [GO:0030496] | calcium ion binding [GO:0005509]; phosphatidic acid binding [GO:0070300]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine transporter activity [GO:0008525]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol transfer activity [GO:0008526]; receptor tyrosine kinase binding [GO:0030971] | PF02862;PF02121; | 3.30.530.20;3.40.50.1000; | PtdIns transfer protein family, PI transfer class IIA subfamily | PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid.; PTM: Phosphorylated on tyrosine residues by PTK2B. | SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Lipid droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow {ECO:0000269|PubMed:15125835}. Midbody {ECO:0000269|PubMed:15125835}. Note=Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets (PubMed:12225667). Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis (PubMed:15125835). {ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:15125835}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; Evidence={ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:22822086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; Evidence={ECO:0000305|PubMed:22822086}; | null | null | null | null | FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between membranes (PubMed:10531358, PubMed:22822086). Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (PubMed:22822086). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (PubMed:11909959). Necessary for normal completion of cytokinesis (PubMed:15125835). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (PubMed:15723057). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (PubMed:15545272). Required for protein export from the endoplasmic reticulum and the Golgi (PubMed:15723057). Binds calcium ions (PubMed:10022914). {ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057, ECO:0000269|PubMed:22822086}. | Homo sapiens (Human) |
O00566 | MPP10_HUMAN | MAPQVWRRRTLERCLTEVGKATGRPECFLTIQEGLASKFTSLTKVLYDFNKILENGRIHGSPLQKLVIENFDDEQIWQQLELQNEPILQYFQNAVSETINDEDISLLPESEEQEREEDGSEIEADDKEDLEDLEEEEVSDMGNDDPEMGERAENSSKSDLRKSPVFSDEDSDLDFDISKLEQQSKVQNKGQGKPREKSIVDDKFFKLSEMEAYLENIEKEEERKDDNDEEEEDIDFFEDIDSDEDEGGLFGSKKLKSGKSSRNLKYKDFFDPVESDEDITNVHDDELDSNKEDDEIAEEEAEELSISETDEDDDLQENEDNKQHKESLKRVTFALPDDAETEDTGVLNVKKNSDEVKSSFEKRQEKMNEKIASLEKELLEKKPWQLQGEVTAQKRPENSLLEETLHFDHAVRMAPVITEETTLQLEDIIKQRIRDQAWDDVVRKEKPKEDAYEYKKRLTLDHEKSKLSLAEIYEQEYIKLNQQKTAEEENPEHVEIQKMMDSLFLKLDALSNFHFIPKPPVPEIKVVSNLPAITMEEVAPVSVSDAALLAPEEIKEKNKAGDIKTAAEKTATDKKRERRKKKYQKRMKIKEKEKRRKLLEKSSVDQAGKYSKTVASEKLKQLTKTGKASFIKDEGKDKALKSSQAFFSKLQDQVKMQINDAKKTEKKKKKRQDISVHKLKL | null | null | maturation of SSU-rRNA [GO:0030490]; ribosomal small subunit biogenesis [GO:0042274]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375] | chromosome [GO:0005694]; Mpp10 complex [GO:0034457]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732] | RNA binding [GO:0003723] | PF04006; | null | MPP10 family | PTM: Phosphorylated in M (mitotic) phase. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:9450966}. Chromosome {ECO:0000269|PubMed:9450966}. Note=Fibrillar region of the nucleolus (PubMed:9450966). After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase (PubMed:9450966). In telophase localized to small cellular prenucleolar bodies that not always contain fibrillarin (PubMed:9450966). The reassociation with nucleolus is preceeded by the arrival of fibrillarin (PubMed:9450966). {ECO:0000269|PubMed:9450966}. | null | null | null | null | null | FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (PubMed:12655004). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:34516797}. | Homo sapiens (Human) |
O00567 | NOP56_HUMAN | MVLLHVLFEHAVGYALLALKEVEEISLLQPQVEESVLNLGKFHSIVRLVAFCPFASSQVALENANAVSEGVVHEDLRLLLETHLPSKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIINDNATYCRLAQFIGNRRELNEDKLEKLEELTMDGAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQVEERLSFYETGEIPRKNLDVMKEAMVQAEEAAAEITRKLEKQEKKRLKKEKKRLAALALASSENSSSTPEECEEMSEKPKKKKKQKPQEVPQENGMEDPSISFSKPKKKKSFSKEELMSSDLEETAGSTSIPKRKKSTPKEETVNDPEEAGHRSGSKKKRKFSKEEPVSSGPEEAVGKSSSKKKKKFHKASQED | null | null | ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364] | box C/D RNP complex [GO:0031428]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; pre-snoRNP complex [GO:0070761]; small-subunit processome [GO:0032040]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732] | cadherin binding [GO:0045296]; histone methyltransferase binding [GO:1990226]; RNA binding [GO:0003723]; snoRNA binding [GO:0030515] | PF01798;PF08156; | 1.10.287.4070;1.10.246.90; | NOP5/NOP56 family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:9372940}. Cytoplasm {ECO:0000250|UniProtKB:Q9D6Z1}. Nucleus, nucleoplasm {ECO:0000305|PubMed:15574333}. | null | null | null | null | null | FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (PubMed:12777385, PubMed:15574333). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:34516797}. | Homo sapiens (Human) |
O00571 | DDX3X_HUMAN | MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN | 3.6.4.13 | null | cell differentiation [GO:0030154]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to osmotic stress [GO:0071470]; cellular response to virus [GO:0098586]; chromosome segregation [GO:0007059]; cytosolic ribosome assembly [GO:0042256]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; gamete generation [GO:0007276]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; lipid homeostasis [GO:0055088]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of chemokine (C-C motif) ligand 5 production [GO:0071651]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 8 signaling pathway [GO:0034161]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation [GO:0045727]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; positive regulation of translational initiation [GO:0045948]; positive regulation of type I interferon production [GO:0032481]; positive regulation of viral genome replication [GO:0045070]; protein localization to cytoplasmic stress granule [GO:1903608]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; stress granule assembly [GO:0034063]; translational initiation [GO:0006413]; Wnt signaling pathway [GO:0016055] | cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; lamellipodium [GO:0030027]; NLRP3 inflammasome complex [GO:0072559]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P granule [GO:0043186]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; CTPase activity [GO:0043273]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; eukaryotic initiation factor 4E binding [GO:0008190]; gamma-tubulin binding [GO:0043015]; GTPase activity [GO:0003924]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; protein serine/threonine kinase activator activity [GO:0043539]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA stem-loop binding [GO:0035613]; RNA strand annealing activity [GO:0033592]; signaling adaptor activity [GO:0035591]; transcription factor binding [GO:0008134]; translation initiation factor binding [GO:0031369] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | PTM: Phosphorylated by TBK1; the phosphorylation is required for the synergistic induction of IFNB mediated by TBK1 and DDX3X (PubMed:18583960). Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3 (PubMed:18583960, PubMed:23478265). The cytoplasmic form is highly phosphorylated in the G1/S phase of the cell cycle and much less at G2/M (PubMed:22034099). Phosphorylation by CSNK1E may inhibit RNA-stimulated ATPase activity (PubMed:29222110). {ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:29222110}.; PTM: Upon stimulation of death receptors, including TNFRSF10B, recruited to receptors and cleaved by caspases. Proteolytic fragments remain associated with the receptors. This cleavage presumably inactivates DDX3X anti-apoptotic function. {ECO:0000269|PubMed:18846110}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:29899501}. Nucleus {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:29899501, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}. Cytoplasm {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:27105836, ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:30341167, ECO:0000269|PubMed:31575075}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:29062139}. Inflammasome {ECO:0000250|UniProtKB:Q62167}. Cell projection, lamellipodium {ECO:0000269|PubMed:28733330}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28842590}. Note=Shuttles between the nucleus and the cytosol (PubMed:15507209, PubMed:18636090, PubMed:29899501, PubMed:30131165, PubMed:31575075). Exported from the nucleus partly through the XPO1/CRM1 system and partly through NXF1/TAP (PubMed:15507209, PubMed:18596238, PubMed:18636090, PubMed:30131165, PubMed:31575075). Localizes to nuclear pores on the outer side of the nuclear membrane (PubMed:15507209). In the cytosol, partly colocalizes with mitochondria (PubMed:20127681). At G0, predominantly located in nucleus. In G1/S phase, predominantly cytoplasmic (PubMed:22034099). During prophase/prometaphase, localizes in close proximity to the condensing chromosomes (PubMed:21730191, PubMed:30131165). During telophase, localizes around the newly synthesized nuclear membrane and in the cytoplasm (PubMed:22034099). Colocalizes with TRPV4 at the plasma membrane. When TRPV4 channel is activated, intracellular Ca(2+) levels increase and the calmodulin/CAMKII pathway is activated, relocalizes to the nucleus (PubMed:29899501). WNT3A stimulation promotes DDX3 recruitment to the plasma membrane (PubMed:23413191). At the leading edge of migrating fibroblasts, colocalizes with CAPRIN1 and PABPC1 (PubMed:28733330). Localizes to centrosome throughout the cell cycle and associates with TP53 at centrosome during mitosis (PubMed:28842590). Translocates to the nucleus in response to HPIV-3 virus-mediated infection (PubMed:31575075). {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:29899501, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:31300642, ECO:0000269|PubMed:31575075}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for ATP (in the absence of nucleic acid) {ECO:0000269|PubMed:17357160}; KM=0.03 mM for ATP (in the presence of ssDNA oligonucleoside dA200) {ECO:0000269|PubMed:17357160}; KM=0.062 mM for ATP (in the absence of nucleic acid) {ECO:0000269|PubMed:21589879}; KM=0.045 mM for ATP (in the presence of RNA oligo(rU)20) {ECO:0000269|PubMed:21589879}; KM=0.047 mM for ATP (in the presence of DNA oligo(dT)20) {ECO:0000269|PubMed:21589879}; Note=kcat is 14 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:17357160). kcat is 36 min(-1) for ATP hydrolysis in the presence of ssDNA oligonucleoside dA200 (PubMed:17357160). kcat is 1.6 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:21589879). kcat is 3.2 min(-1) for ATP hydrolysis in the presence of RNA oligo(rU)20 (PubMed:21589879). kcat is 3.8 min(-1) for ATP hydrolysis in the presence of DNA oligo(dT)20 (PubMed:21589879). {ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:21589879}; | null | null | null | FUNCTION: Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250|UniProtKB:Q62167, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17095540, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19913487, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:28128295, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110, ECO:0000269|PubMed:30256975, ECO:0000269|PubMed:30341167, ECO:0000269|PubMed:31575075, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269|PubMed:27105836}. | Homo sapiens (Human) |
O00574 | CXCR6_HUMAN | MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; viral genome replication [GO:0019079] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine receptor activity [GO:0016494]; coreceptor activity [GO:0015026]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1. | Homo sapiens (Human) |
O00584 | RNT2_HUMAN | MRPAALRGALLGCLCLALLCLGGADKRLRDNHEWKKLIMVQHWPETVCEKIQNDCRDPPDYWTIHGLWPDKSEGCNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTCAAQVDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQCLPPSQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVWLANGAAESRGLRVCEDGPVFYPPPKKTKH | 4.6.1.19 | null | innate immune response [GO:0045087]; RNA catabolic process [GO:0006401] | azurophil granule lumen [GO:0035578]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; mitochondrial intermembrane space [GO:0005758] | ribonuclease T2 activity [GO:0033897]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; RNA nuclease activity [GO:0004540] | PF00445; | 3.90.730.10; | RNase T2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15809705, ECO:0000269|PubMed:16620762}. Lysosome lumen {ECO:0000269|PubMed:16620762}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:16620762}. Mitochondrion intermembrane space {ECO:0000269|PubMed:28730546, ECO:0000269|PubMed:30184494, ECO:0000269|PubMed:30385512}. Note=Full-length RNASET2 is found in the endoplasmic reticulum while smaller RNASET2 proteolytic products are found in the lysosome fraction. {ECO:0000269|PubMed:16620762}. | CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10046}; | null | null | null | null | FUNCTION: Ribonuclease that plays an essential role in innate immune response by recognizing and degrading RNAs from microbial pathogens that are subsequently sensed by TLR8 (PubMed:31778653). Cleaves preferentially single-stranded RNA molecules between purine and uridine residues, which critically contributes to the supply of catabolic uridine and the generation of purine-2',3'-cyclophosphate-terminated oligoribonucleotides (PubMed:31778653). In turn, RNase T2 degradation products promote the RNA-dependent activation of TLR8 (PubMed:31778653). Also plays a key role in degradation of mitochondrial RNA and processing of non-coding RNA imported from the cytosol into mitochondria (PubMed:28730546, PubMed:30184494). Participates as well in degradation of mitochondrion-associated cytosolic rRNAs (PubMed:30385512). {ECO:0000269|PubMed:16620762, ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:22735700, ECO:0000269|PubMed:28730546, ECO:0000269|PubMed:30184494, ECO:0000269|PubMed:30385512, ECO:0000269|PubMed:31778653}. | Homo sapiens (Human) |
O00585 | CCL21_HUMAN | MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP | null | null | cell chemotaxis [GO:0060326]; cell maturation [GO:0048469]; cell-cell signaling [GO:0007267]; cellular response to chemokine [GO:1990869]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine (C-C motif) ligand 21 signaling pathway [GO:0038116]; chemokine-mediated signaling pathway [GO:0070098]; dendritic cell chemotaxis [GO:0002407]; dendritic cell dendrite assembly [GO:0097026]; establishment of T cell polarity [GO:0001768]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; immunological synapse formation [GO:0001771]; inflammatory response [GO:0006954]; lymphocyte chemotaxis [GO:0048247]; mesangial cell-matrix adhesion [GO:0035759]; monocyte chemotaxis [GO:0002548]; negative regulation of dendritic cell apoptotic process [GO:2000669]; negative regulation of dendritic cell dendrite assembly [GO:2000548]; negative regulation of leukocyte tethering or rolling [GO:1903237]; neutrophil chemotaxis [GO:0030593]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cell motility [GO:2000147]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of chemotaxis [GO:0050921]; positive regulation of dendritic cell antigen processing and presentation [GO:0002606]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of glycoprotein biosynthetic process [GO:0010560]; positive regulation of JNK cascade [GO:0046330]; positive regulation of myeloid dendritic cell chemotaxis [GO:2000529]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of pseudopodium assembly [GO:0031274]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of T cell chemotaxis [GO:0010820]; positive regulation of T cell migration [GO:2000406]; release of sequestered calcium ion into cytosol [GO:0051209]; response to prostaglandin E [GO:0034695]; ruffle organization [GO:0031529]; T cell costimulation [GO:0031295] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR7 chemokine receptor binding [GO:0031732]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. | Homo sapiens (Human) |
O00587 | MFNG_HUMAN | MQCRLPRGLAGALLTLLCMGLLCLRYHLNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGAR | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O09008}; Note=Has some activity with cobalt, magnesium and calcium, but not zinc. {ECO:0000250|UniProtKB:O09008}; | blastocyst formation [GO:0001825]; marginal zone B cell differentiation [GO:0002315]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence={ECO:0000250|UniProtKB:O09008}; CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence={ECO:0000250|UniProtKB:O09008}; | null | null | null | null | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). {ECO:0000250|UniProtKB:O09008}. | Homo sapiens (Human) |
O00590 | ACKR2_HUMAN | MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDKYLEIVHAQPYHRLRTRAKSLLLATIVWAVSLAVSIPDMVFVQTHENPKGVWNCHADFGGHGTIWKLFLRFQQNLLGFLLPLLAMIFFYSRIGCVLVRLRPAGQGRALKIAAALVVAFFVLWFPYNLTLFLHTLLDLQVFGNCEVSQHLDYALQVTESIAFLHCCFSPILYAFSSHRFRQYLKAFLAAVLGWHLAPGTAQASLSSCSESSILTAQEEMTGMNDLGERQSENYPNKEDVGNKSA | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | actin filament [GO:0005884]; cytosol [GO:0005829]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; intracellular membrane-bounded organelle [GO:0043231]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000269|PubMed:18201974}. | SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane. | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. {ECO:0000269|PubMed:23479571, ECO:0000269|PubMed:23633677}. | Homo sapiens (Human) |
O00591 | GBRP_HUMAN | MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAAKDRGTTKEVEEVSITNIINSSISSFKRKISFASIEISSDNVDYSDLTMKTSDKFKFVFREKMGRIVDYFTIQNPSNVDHYSKLLFPLIFMLANVFYWAYYMYF | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRP sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O09028}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000250|UniProtKB:O09028}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10462548}; | null | null | null | null | FUNCTION: Pi subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA) (PubMed:10462548). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interfaces (By similarity). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:10462548). Pi-containing GABAARs are mostly located in peripheral tissues. In the uterus, pi subunits modulate uterus contraction by altering the sensitivity of GABAARs to pregnanolone (PubMed:9182563). In the lungs, pi-containing GABAARs contribute to pulmonary fluid transport via luminal secretion of chloride (By similarity). {ECO:0000250|UniProtKB:O09028, ECO:0000250|UniProtKB:P47870, ECO:0000269|PubMed:10462548, ECO:0000269|PubMed:9182563}. | Homo sapiens (Human) |
O00592 | PODXL_HUMAN | MRCALALSALLLLLSTPPLLPSSPSPSPSPSQNATQTTTDSSNKTAPTPASSVTIMATDTAQQSTVPTSKANEILASVKATTLGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLMKISSSSSTVAIPGYTFTSPGMTTTLLETVFHHVSQAGLELLTSGDLPTLASQSAGITASSVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAHESNWAKCEDLETQTQSEKQLVLNLTGNTLCAGGASDEKLISLICRAVKATFNPAQDKCGIRLASVPGSQTVVVKEITIHTKLPAKDVYERLKDKWDELKEAGVSDMKLGDQGPPEEAEDRFSMPLIITIVCMASFLLLVAALYGCCHQRLSQRKDQQRLTEELQTVENGYHDNPTLEVMETSSEMQEKKVVSLNGELGDSWIVPLDNLTKDDLDEEEDTHL | null | null | cell adhesion [GO:0007155]; cell migration [GO:0016477]; epithelial tube formation [GO:0072175]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell-cell adhesion [GO:0022408]; podocyte development [GO:0072015]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; regulation of microvillus assembly [GO:0032534] | apical plasma membrane [GO:0016324]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; microvillus membrane [GO:0031528]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; slit diaphragm [GO:0036057] | null | PF06365; | null | Podocalyxin family | PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Apical cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus {ECO:0000250}. Membrane raft {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with NHERF2 at the apical plasma membrane during epithelial polarization. Colocalizes with NHERF1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Colocalizes with actin filaments, EZR and NHERF1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and NHERF2 at the apical cell membrane of glomerular epithelium cells (By similarity). Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. {ECO:0000269|PubMed:17616675, ECO:0000269|PubMed:18456258}. | Homo sapiens (Human) |
O00602 | FCN1_HUMAN | MELSGATMARGLAVLLVLFLHIKNLPAQAADTCPEVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQSQSCATGPRNCKDLLDRGYFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNIHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSEMKVRPA | null | null | cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of opsonization [GO:1903028]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; recognition of apoptotic cell [GO:0043654] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774]; serine-type endopeptidase complex [GO:1905370] | antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; G protein-coupled receptor binding [GO:0001664]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; sialic acid binding [GO:0033691]; signaling receptor binding [GO:0005102] | PF01391;PF00147; | 3.90.215.10; | Ficolin lectin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Cell membrane {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Peripheral membrane protein {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Extracellular side {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Note=Found on the monocyte and granulocyte surface (PubMed:20400674). | null | null | null | null | null | FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. {ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}. | Homo sapiens (Human) |
O00622 | CCN1_HUMAN | MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD | null | null | apoptotic process involved in heart morphogenesis [GO:0003278]; atrial septum morphogenesis [GO:0060413]; atrioventricular valve morphogenesis [GO:0003181]; cell adhesion [GO:0007155]; chemotaxis [GO:0006935]; chondroblast differentiation [GO:0060591]; chorio-allantoic fusion [GO:0060710]; extracellular matrix organization [GO:0030198]; intussusceptive angiogenesis [GO:0002041]; labyrinthine layer blood vessel development [GO:0060716]; negative regulation of apoptotic process [GO:0043066]; osteoblast differentiation [GO:0001649]; positive regulation of apoptotic process [GO:0043065]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944]; reactive oxygen species metabolic process [GO:0072593]; regulation of ERK1 and ERK2 cascade [GO:0070372]; signal transduction [GO:0007165]; ventricular septum development [GO:0003281]; wound healing, spreading of cells [GO:0044319] | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615] | extracellular matrix binding [GO:0050840]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00007;PF00219;PF19035;PF00093; | 2.10.70.10;2.20.100.10; | CCN family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CCN1-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3. {ECO:0000269|PubMed:11584015}. | Homo sapiens (Human) |
O00623 | PEX12_HUMAN | MAEHGAHFTAASVADDQPSIFEVVAQDSLMTAVRPALQHVVKVLAESNPTHYGFLWRWFDEIFTLLDLLLQQHYLSRTSASFSENFYGLKRIVMGDTHKSQRLASAGLPKQQLWKSIMFLVLLPYLKVKLEKLVSSLREEDEYSIHPPSSRWKRFYRAFLAAYPFVNMAWEGWFLVQQLRYILGKAQHHSPLLRLAGVQLGRLTVQDIQALEHKPAKASMMQQPARSVSEKINSALKKAVGGVALSLSTGLSVGVFFLQFLDWWYSSENQETIKSLTALPTPPPPVHLDYNSDSPLLPKMKTVCPLCRKTRVNDTVLATSGYVFCYRCVFHYVRSHQACPITGYPTEVQHLIKLYSPEN | null | null | cellular response to reactive oxygen species [GO:0034614]; peroxisome organization [GO:0007031]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein targeting to peroxisome [GO:0006625] | cytosol [GO:0005829]; peroxisomal importomer complex [GO:1990429]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | protein transmembrane transporter activity [GO:0008320]; ubiquitin ligase activator activity [GO:1990757]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF04757; | 3.30.40.10; | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9922452}; Multi-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:24662292}. | null | null | FUNCTION: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:24662292, PubMed:9354782, PubMed:9632816). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (PubMed:24662292). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q04370, ECO:0000269|PubMed:24662292, ECO:0000269|PubMed:9354782, ECO:0000269|PubMed:9632816}. | Homo sapiens (Human) |
O00624 | NPT3_HUMAN | MDGKPATRKGPDFCSLRYGLALIMHFSNFTMITQRVSLSIAIIAMVNTTQQQGLSNASTEGPVADAFNNSSISIKEFDTKASVYQWSPETQGIIFSSINYGIILTLIPSGYLAGIFGAKKMLGAGLLISSLLTLFTPLAADFGVILVIMVRTVQGMAQGMAWTGQFTIWAKWAPPLERSKLTTIAGSGSAFGSFIILCVGGLISQALSWPFIFYIFGSTGCVCCLLWFTVIYDDPMHHPCISVREKEHILSSLAQQPSSPGRAVPIKAMVTCLPLWAIFLGFFSHFWLCTIILTYLPTYISTLLHVNIRDSGVLSSLPFIAAASCTILGGQLADFLLSRNLLRLITVRKLFSSLGLLLPSICAVALPFVASSYVITIILLILIPGTSNLCDSGFIINTLDIAPRYASFLMGISRGFGLIAGIISSTATGFLISQVGPVY | null | null | monoatomic anion transport [GO:0006820]; phosphate-containing compound metabolic process [GO:0006796]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; membrane [GO:0016020]; plasma membrane [GO:0005886] | sodium:phosphate symporter activity [GO:0005436]; transmembrane transporter activity [GO:0022857]; urate transmembrane transporter activity [GO:0015143] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q5SZA1}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q5SZA1}; CATALYTIC ACTIVITY: Reaction=n chloride(in) + urate(out) = n chloride(out) + urate(in); Xref=Rhea:RHEA:72319, ChEBI:CHEBI:17775, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q5SZA1}; | null | null | null | null | FUNCTION: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions (By similarity). Mediates chloride-dependent transport of urate (By similarity). Can actively transport inorganic phosphate into cells via Na(+) cotransport (By similarity). {ECO:0000250|UniProtKB:Q5SZA1}. | Homo sapiens (Human) |
O00625 | PIR_HUMAN | MGSSKKVTLSVLSREQSEGVGARVRRSIGRPELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCGHTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQYQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGAKHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVENKDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFERAKTWKSKIGN | 1.13.11.24 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:14573596, ECO:0000269|PubMed:20711196}; Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:14573596, ECO:0000269|PubMed:20711196}; | digestion [GO:0007586]; monocyte differentiation [GO:0030224]; transcription by RNA polymerase II [GO:0006366] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; quercetin 2,3-dioxygenase activity [GO:0008127]; transcription coregulator activity [GO:0003712] | PF02678;PF05726; | 2.60.120.10; | Pirin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20089166, ECO:0000269|PubMed:9079676}. Cytoplasm {ECO:0000269|PubMed:20089166}. Note=Predominantly localized in dot-like subnuclear structures. Cytoplasmic localization of PIR seems to positively correlate with melanoma progression. {ECO:0000269|PubMed:20089166, ECO:0000269|PubMed:9079676}. | CATALYTIC ACTIVITY: Reaction=O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO; Xref=Rhea:RHEA:15381, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:57628, ChEBI:CHEBI:57694; EC=1.13.11.24; Evidence={ECO:0000269|PubMed:15951572}; | null | PATHWAY: Flavonoid metabolism; quercetin degradation. {ECO:0000305|PubMed:15951572}. | null | null | FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro). {ECO:0000269|PubMed:15951572, ECO:0000269|PubMed:17288615, ECO:0000269|PubMed:20010624, ECO:0000269|PubMed:20711196, ECO:0000269|PubMed:23716661}. | Homo sapiens (Human) |
O00626 | CCL22_HUMAN | MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ | null | null | cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; lymphocyte chemotaxis [GO:0048247]; monocyte chemotaxis [GO:0002548]; neutrophil chemotaxis [GO:0030593]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; response to virus [GO:0009615]; signal transduction [GO:0007165] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: The N-terminal processed forms MDC(3-69), MDC(5-69) and MDC(7-69) are produced by proteolytic cleavage after secretion from monocyte derived dendrocytes. {ECO:0000269|PubMed:11241286}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active. | Homo sapiens (Human) |
O00628 | PEX7_HUMAN | MSAVCGGAARMLRTPGRHGYAAEFSPYLPGRLACATAQHYGIAGCGTLLILDPDEAGLRLFRSFDWNDGLFDVTWSENNEHVLITCSGDGSLQLWDTAKAAGPLQVYKEHAQEVYSVDWSQTRGEQLVVSGSWDQTVKLWDPTVGKSLCTFRGHESIIYSTIWSPHIPGCFASASGDQTLRIWDVKAAGVRIVIPAHQAEILSCDWCKYNENLLVTGAVDCSLRGWDLRNVRQPVFELLGHTYAIRRVKFSPFHASVLASCSYDFTVRFWNFSKPDSLLETVEHHTEFTCGLDFSLQSPTQVADCSWDETIKIYDPACLTIPA | null | null | endochondral ossification [GO:0001958]; ether lipid biosynthetic process [GO:0008611]; fatty acid beta-oxidation [GO:0006635]; neuron migration [GO:0001764]; peroxisome organization [GO:0007031]; protein import into peroxisome matrix [GO:0016558]; protein targeting to peroxisome [GO:0006625] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | enzyme binding [GO:0019899]; peroxisome matrix targeting signal-2 binding [GO:0005053]; protein homodimerization activity [GO:0042803] | PF00400; | 2.130.10.10; | WD repeat peroxin-7 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:25538232}. Peroxisome matrix {ECO:0000269|PubMed:11546814, ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:25538232}. Note=Translocated into the peroxisome matrix together with PTS2-containing cargo proteins and PEX5. {ECO:0000269|PubMed:25538232}. | null | null | null | null | null | FUNCTION: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal (PubMed:11931631, PubMed:22057399, PubMed:25538232, PubMed:9090381). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (PubMed:11931631, PubMed:22057399, PubMed:25538232). Cargo protein-binding triggers interaction with PEX5 and formation of a ternary complex composed of PEX5 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (PubMed:11546814, PubMed:25538232). {ECO:0000269|PubMed:11546814, ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232, ECO:0000269|PubMed:9090381}. | Homo sapiens (Human) |
O00629 | IMA3_HUMAN | MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF | null | null | dopamine secretion [GO:0014046]; gene expression [GO:0010467]; NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. | Homo sapiens (Human) |
O00631 | SARCO_HUMAN | MGINTRELFLNFTIVLITVILMWLLVRSYQY | null | null | calcium ion transport [GO:0006816]; negative regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901895]; negative regulation of calcium ion binding [GO:1901877]; negative regulation of calcium ion import [GO:0090281]; negative regulation of calcium ion transmembrane transporter activity [GO:1901020]; negative regulation of catalytic activity [GO:0043086]; negative regulation of protein-containing complex disassembly [GO:0043242]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of protein depolymerization [GO:1901881]; regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901894]; regulation of calcium ion transport [GO:0051924]; regulation of relaxation of muscle [GO:1901077]; sarcoplasmic reticulum calcium ion transport [GO:0070296] | membrane [GO:0016020]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017] | ATPase binding [GO:0051117]; enzyme inhibitor activity [GO:0004857] | PF05366; | null | Sarcolipin family | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q9CQD6, ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}. | Homo sapiens (Human) |
O00635 | TRI38_HUMAN | MASTTSTKKMMEEATCSICLSLMTNPVSINCGHSYCHLCITDFFKNPSQKQLRQETFCCPQCRAPFHMDSLRPNKQLGSLIEALKETDQEMSCEEHGEQFHLFCEDEGQLICWRCERAPQHKGHTTALVEDVCQGYKEKLQKAVTKLKQLEDRCTEQKLSTAMRITKWKEKVQIQRQKIRSDFKNLQCFLHEEEKSYLWRLEKEEQQTLSRLRDYEAGLGLKSNELKSHILELEEKCQGSAQKLLQNVNDTLSRSWAVKLETSEAVSLELHTMCNVSKLYFDVKKMLRSHQVSVTLDPDTAHHELILSEDRRQVTRGYTQENQDTSSRRFTAFPCVLGCEGFTSGRRYFEVDVGEGTGWDLGVCMENVQRGTGMKQEPQSGFWTLRLCKKKGYVALTSPPTSLHLHEQPLLVGIFLDYEAGVVSFYNGNTGCHIFTFPKASFSDTLRPYFQVYQYSPLFLPPPGD | 2.3.2.27 | null | innate immune response [GO:0045087]; negative regulation of defense response to virus [GO:0050687]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of viral entry into host cell [GO:0046598]; positive regulation of viral genome replication [GO:0045070]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein sumoylation [GO:0016925]; regulation of interferon-beta production [GO:0032648]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5SZ99}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305|PubMed:23056470}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23056470}.; PATHWAY: Protein modification; protein sumoylation. {ECO:0000250|UniProtKB:Q5SZ99}. | null | null | FUNCTION: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity (PubMed:23056470). Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation (By similarity). Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling (PubMed:23056470). Acts as positive regulator of the cGAS-STING pathway by acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and STING, preventing their degradation and thereby activating the innate immune response to DNA virus (By similarity). Also acts as a negative regulator of NF-kappa-B signaling independently of its E3 protein ligase activity by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters (PubMed:24434549). {ECO:0000250|UniProtKB:Q5SZ99, ECO:0000269|PubMed:23056470, ECO:0000269|PubMed:24434549}. | Homo sapiens (Human) |
O00712 | NFIB_HUMAN | MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQSWYLG | null | null | anterior commissure morphogenesis [GO:0021960]; brain development [GO:0007420]; cell differentiation involved in salivary gland development [GO:0060689]; cell proliferation in forebrain [GO:0021846]; chondrocyte differentiation [GO:0002062]; club cell differentiation [GO:0060486]; commissural neuron axon guidance [GO:0071679]; DNA replication [GO:0006260]; exit from mitosis [GO:0010458]; gene expression [GO:0010467]; glandular epithelial cell differentiation [GO:0002067]; glial cell differentiation [GO:0010001]; glial cell fate specification [GO:0021780]; glial cell proliferation [GO:0014009]; hindbrain development [GO:0030902]; lung ciliated cell differentiation [GO:0061141]; negative regulation of DNA binding [GO:0043392]; negative regulation of epithelial cell proliferation involved in lung morphogenesis [GO:2000795]; negative regulation of mesenchymal cell proliferation involved in lung development [GO:2000791]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron fate specification [GO:0048665]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; principal sensory nucleus of trigeminal nerve development [GO:0021740]; regeneration [GO:0031099]; regulation of transcription by RNA polymerase II [GO:0006357]; response to bacterium [GO:0009617]; response to wounding [GO:0009611]; retina development in camera-type eye [GO:0060041]; salivary gland cavitation [GO:0060662]; stem cell population maintenance [GO:0019827]; stem cell proliferation [GO:0072089]; tissue homeostasis [GO:0001894]; type I pneumocyte differentiation [GO:0060509]; type II pneumocyte differentiation [GO:0060510] | cerebellar mossy fiber [GO:0044300]; chromatin [GO:0000785]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription regulator inhibitor activity [GO:0140416] | PF00859;PF03165;PF10524; | null | CTF/NF-I family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator of GFAP, essential for proper brain development (PubMed:30388402). Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. {ECO:0000269|PubMed:30388402}. | Homo sapiens (Human) |
O00716 | E2F3_HUMAN | MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS | null | null | G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of fat cell proliferation [GO:0070345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell apoptotic process [GO:1905461]; protein import into nucleus [GO:0006606]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation at RNA polymerase II promoter [GO:0006367] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF16421;PF02319; | 6.10.250.540;1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity). {ECO:0000250|UniProtKB:O35261}. | Homo sapiens (Human) |
O00743 | PPP6_HUMAN | MAPLDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQFYDLCELFRTGGQVPDTNYIFMGDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P36873}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:P36873}; | COPII vesicle coating [GO:0048208]; G1/S transition of mitotic cell cycle [GO:0000082]; innate immune response [GO:0045087]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; protein dephosphorylation [GO:0006470] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-6 (PP-V) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:29053956}. Cytoplasm {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:17568194}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:32474700}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:17079228, ECO:0000269|PubMed:29053956}; | null | null | null | null | FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6) (PubMed:17079228, PubMed:29053956, PubMed:32474700). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation (PubMed:10227379). N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1 (PubMed:17568194). During mitosis, regulates spindle positioning (PubMed:27335426). Down-regulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7 (PubMed:17079228). Participates also in the innate immune defense against viruses by desphosphorylating RIGI, an essential step that triggers RIGI-mediated signaling activation (PubMed:29053956). Also regulates innate immunity by acting as a negative regulator of the cGAS-STING pathway: mediates dephosphorylation and inactivation of CGAS and STING1 (PubMed:32474700, PubMed:32753499). CGAS dephosphorylation at 'Ser-435' impairs its ability to bind GTP, thereby inactivating it (PubMed:32474700). {ECO:0000269|PubMed:10227379, ECO:0000269|PubMed:17079228, ECO:0000269|PubMed:17568194, ECO:0000269|PubMed:27335426, ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:32474700, ECO:0000269|PubMed:32753499}. | Homo sapiens (Human) |
O00744 | WN10B_HUMAN | MLEEPRPRPPPSGLAGLLFLALCSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRNPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKSFPHSLPSPGPGSSPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAVGAALRERLGRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCERDPTMGSPGTRGRACNKTSRLLDGCGSLCCGRGHNVLRQTRVERCHCRFHWCCYVLCDECKVTEWVNVCK | null | null | bone trabecula formation [GO:0060346]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to cAMP [GO:0071320]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to retinoic acid [GO:0071300]; chondrocyte differentiation [GO:0002062]; epithelial cell differentiation [GO:0030855]; fat cell differentiation [GO:0045444]; fungiform papilla development [GO:0061196]; G2/M transition of mitotic cell cycle [GO:0000086]; hematopoietic stem cell proliferation [GO:0071425]; lipid metabolic process [GO:0006629]; myoblast development [GO:0048627]; myoblast differentiation involved in skeletal muscle regeneration [GO:0014835]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; osteoblast differentiation [GO:0001649]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone mineralization [GO:0030501]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0045899]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of timing of anagen [GO:0051885]; protein stabilization [GO:0050821]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of skeletal muscle tissue development [GO:0048641]; sensory perception of taste [GO:0050909]; skeletal muscle fiber development [GO:0048741]; smoothened signaling pathway [GO:0007224]; T cell differentiation [GO:0030217]; transcription by RNA polymerase II [GO:0006366] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}. | null | null | null | null | null | FUNCTION: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin. {ECO:0000305|PubMed:16477437, ECO:0000305|PubMed:21447090, ECO:0000305|PubMed:27321946}. | Homo sapiens (Human) |
O00746 | NDKM_HUMAN | MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; lipid transport [GO:0006869]; nucleoside metabolic process [GO:0009116]; phosphorylation [GO:0016310]; UTP biosynthetic process [GO:0006228] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; cardiolipin binding [GO:1901612]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550] | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:18635542}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086). {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:10799505}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:10799505}; CATALYTIC ACTIVITY: Reaction=a cardiolipin(in) = a cardiolipin(out); Xref=Rhea:RHEA:38695, ChEBI:CHEBI:62237; Evidence={ECO:0000269|PubMed:23150663}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38696; Evidence={ECO:0000305|PubMed:23150663}; | null | null | null | null | FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis (PubMed:10799505). Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity (PubMed:18635542, PubMed:23150663). Acts as a mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration (PubMed:18635542). Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria (PubMed:24970086). In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (PubMed:17028143, PubMed:18635542, PubMed:23150663). {ECO:0000269|PubMed:10799505, ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663, ECO:0000305, ECO:0000305|PubMed:24970086}. | Homo sapiens (Human) |
O00748 | EST2_HUMAN | MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL | 3.1.1.1; 3.1.1.56; 3.1.1.84 | null | catabolic process [GO:0009056]; prostaglandin metabolic process [GO:0006693]; xenobiotic metabolic process [GO:0006805] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231] | carboxylesterase activity [GO:0106435]; carboxylic ester hydrolase activity [GO:0052689]; methylumbelliferyl-acetate deacetylase activity [GO:0047374] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: Glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9169443}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:22446793}. | CATALYTIC ACTIVITY: Reaction=cocaine + H2O = benzoate + ecgonine methyl ester + H(+); Xref=Rhea:RHEA:27506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; EC=3.1.1.84; Evidence={ECO:0000269|PubMed:9169443}; CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:9169443}; CATALYTIC ACTIVITY: Reaction=4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate + H(+); Xref=Rhea:RHEA:12208, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17224, ChEBI:CHEBI:17763, ChEBI:CHEBI:30089; EC=3.1.1.56; Evidence={ECO:0000269|PubMed:9169443}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:21049984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000305|PubMed:21049984}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) + prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230, ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:21049984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297; Evidence={ECO:0000305|PubMed:21049984}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404, ChEBI:CHEBI:90233; Evidence={ECO:0000269|PubMed:21049984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301; Evidence={ECO:0000305|PubMed:21049984}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for cocaine {ECO:0000269|PubMed:9169443}; KM=0.15 mM for 4-methylumbelliferyl acetate {ECO:0000269|PubMed:9169443}; KM=6.8 mM for heroin {ECO:0000269|PubMed:9169443}; KM=46 uM for 2-arachidonoylglycerol {ECO:0000269|PubMed:21049984}; KM=750 uM for prostaglandin E2 1-glyceryl ester {ECO:0000269|PubMed:21049984}; KM=35 uM for prostaglandin F2alpha 1-glyceryl ester {ECO:0000269|PubMed:21049984}; KM=0.13 mM for 6-monoacetylmorphine {ECO:0000269|PubMed:9169443}; Note=kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively. {ECO:0000269|PubMed:21049984}; | null | null | null | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:9169443). Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine (PubMed:9169443). Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol (PubMed:28677105). Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984). {ECO:0000269|PubMed:21049984, ECO:0000269|PubMed:9169443, ECO:0000303|PubMed:28677105}. | Homo sapiens (Human) |
O00750 | P3C2B_HUMAN | MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHDKEENRAKQNADPSLISWDEPGVDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSLSPQEGPPNHSTSQGPQPGSDPWPKGSLSGDYLYIFDGSDGGVSSSPGPGDIEGSCKKLSPPPLPPRASIWDTPPLPPRKGSPSSSKISQPSDINTFSLVEQLPGKLLEHRILEEEEVLGGGGQGRLLGSVDYDGINDAITRLNLKSTYDAEMLRDATRGWKEGRGPLDFSKDTSGKPVARSKTMPPQVPPRTYASRYGNRKNATPGKNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRSGSDIQDYFLTGYVWSAVTPSPEHLGDEVNLKVTVLCDRLQEALTFTCNCSSTVDLLIYQTLCYTHDDLRNVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDIDIRLQLMEQKVVRSDLARTVNDDQSPSTLNYLVHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAICNALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLAVRENREKVVEALTAAILDLVELYCNTFNADFQTAVPGSRKHDLVQEACHFARSLAFTVYATHRIPIIWATSYEDFYLSCSLSHGGKELCSPLQTRRAHFSKYLFHLIVWDQQICFPVQVNRLPRETLLCATLYALPIPPPGSSSEANKQRRVPEALGWVTTPLFNFRQVLTCGRKLLGLWPATQENPSARWSAPNFHQPDSVILQIDFPTSAFDIKFTSPPGDKFSPRYEFGSLREEDQRKLKDIMQKESLYWLTDADKKRLWEKRYYCHSEVSSLPLVLASAPSWEWACLPDIYVLLKQWTHMNHQDALGLLHATFPDQEVRRMAVQWIGSLSDAELLDYLPQLVQALKYECYLDSPLVRFLLKRAVSDLRVTHYFFWLLKDGLKDSQFSIRYQYLLAALLCCCGKGLREEFNRQCWLVNALAKLAQQVREAAPSARQGILRTGLEEVKQFFALNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKLSFQNVDPLGENIRVIFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTGSFKDRPLADWLQKHNPGEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEANATTYFTRLIESSLGSVATKLNFFIHNLAQMKFTGSDDRLTLSFASRTHTLKSSGRISDVFLCRHEKIFHPNKGYIYVVKVMRENTHEATYIQRTFEEFQELHNKLRLLFPSSHLPSFPSRFVIGRSRGEAVAERRREELNGYIWHLIHAPPEVAECDLVYTFFHPLPRDEKAMGTSPAPKSSDGTWARPVGKVGGEVKLSISYKNNKLFIMVMHIRGLQLLQDGNDPDPYVKIYLLPDPQKTTKRKTKVARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENVLLGEVNIRLRELDLAQEKTGWFALGSRSHGTL | 2.7.1.137; 2.7.1.154 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10805725}; | autophagosome organization [GO:1905037]; cell migration [GO:0016477]; cellular response to starvation [GO:0009267]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091] | PF00168;PF00454;PF00792;PF00794;PF00613;PF00787; | 2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10; | PI3/PI4-kinase family | null | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cell membrane {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cytoplasm, cytosol {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Nucleus {ECO:0000269|PubMed:14563213}. Endoplasmic reticulum {ECO:0000269|PubMed:14563213}. Note=Found mostly in the microsome, but also in the plasma membrane and cytosol. Nuclear in testis. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000305|PubMed:9830063}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000305|PubMed:9830063}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for ATP-Mg(2+) {ECO:0000269|PubMed:9830063}; KM=120 uM for ATP-Ca(2+) {ECO:0000269|PubMed:9830063}; Vmax=737 nmol/min/mg enzyme for ATP-Mg(2+) {ECO:0000269|PubMed:9830063}; Vmax=737 nmol/min/mg enzyme for ATP-Ca(2+) {ECO:0000269|PubMed:9830063}; | null | null | null | FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns (PubMed:10805725, PubMed:11533253, PubMed:9830063). Does not phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF and PDGF signaling cascades (PubMed:10805725). {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063}. | Homo sapiens (Human) |
O00754 | MA2B1_HUMAN | MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | learning or memory [GO:0007611]; mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; oligosaccharide catabolic process [GO:0009313]; protein deglycosylation [GO:0006517]; protein modification process [GO:0036211] | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; nucleoplasm [GO:0005654] | alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074;PF21260; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | PTM: First processed into 3 peptides of 70 kDa, 42 kDa (D) and 13/15 kDa (E). The 70 kDa peptide is further processed into three peptides (A, B and C). The A, B and C peptides are disulfide-linked.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; | null | null | null | null | FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages. | Homo sapiens (Human) |
O00755 | WNT7A_HUMAN | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; asymmetric protein localization involved in cell fate determination [GO:0045167]; axonogenesis [GO:0007409]; canonical Wnt signaling pathway [GO:0060070]; cartilage condensation [GO:0001502]; cell fate commitment [GO:0045165]; cell proliferation in forebrain [GO:0021846]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system vasculogenesis [GO:0022009]; cerebellar granule cell differentiation [GO:0021707]; chondrocyte differentiation [GO:0002062]; dendritic spine morphogenesis [GO:0060997]; dorsal/ventral pattern formation [GO:0009953]; embryonic axis specification [GO:0000578]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; establishment of blood-brain barrier [GO:0060856]; establishment of cell polarity [GO:0030010]; excitatory synapse assembly [GO:1904861]; lens fiber cell development [GO:0070307]; negative regulation of apoptotic process [GO:0043066]; negative regulation of neurogenesis [GO:0050768]; neuron differentiation [GO:0030182]; neurotransmitter secretion [GO:0007269]; oviduct development [GO:0060066]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of excitatory synapse assembly [GO:1904891]; positive regulation of gene expression [GO:0010628]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein localization to presynapse [GO:1905386]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of synapse assembly [GO:0051965]; positive regulation of transcription by RNA polymerase II [GO:0045944]; postsynapse assembly [GO:0099068]; presynapse assembly [GO:0099054]; regulation of axon diameter [GO:0031133]; regulation of postsynapse organization [GO:0099175]; regulation of presynapse assembly [GO:1905606]; regulation of synaptic vesicle exocytosis [GO:2000300]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]; secondary palate development [GO:0062009]; sex differentiation [GO:0007548]; skeletal muscle satellite cell activation [GO:0014719]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; somatic stem cell division [GO:0048103]; somatic stem cell population maintenance [GO:0035019]; stem cell development [GO:0048864]; synaptic vesicle recycling [GO:0036465]; uterus morphogenesis [GO:0061038]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]; wound healing, spreading of epidermal cells [GO:0035313] | cell surface [GO:0009986]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development (PubMed:16826533). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:30026314). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (By similarity). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (By similarity). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (By similarity). Promotes formation of synapses via its interaction with FZD5 (By similarity). {ECO:0000250|UniProtKB:P24383, ECO:0000269|PubMed:16826533, ECO:0000269|PubMed:30026314}. | Homo sapiens (Human) |
O00757 | F16P2_HUMAN | MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQKNQAGS | 3.1.3.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; sucrose biosynthetic process [GO:0005986] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Z disc [GO:0030018] | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00316;PF18913; | 3.40.190.80;3.30.540.10; | FBPase class 1 family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca(2+) concentration (By similarity). In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase (By similarity). Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca(2+) concentration. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:17350621}; KM=2.6 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:17350621}; Note=The kinetic constants are determined for the recombinant enzyme expressed in E.coli.; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | null | null | FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate. {ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, ECO:0000269|PubMed:33977262}. | Homo sapiens (Human) |
O00762 | UBE2C_HUMAN | MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP | 2.3.2.23; 2.3.2.24 | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell division [GO:0051301]; exit from mitosis [GO:0010458]; free ubiquitin chain polymerization [GO:0010994]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; positive regulation of ubiquitin protein ligase activity [GO:1904668]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; ubiquitin-dependent protein catabolic process [GO:0006511] | anaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein ligase binding [GO:0044389]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active until its substrates have been destroyed. {ECO:0000269|PubMed:15558010}. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133, ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386}; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.24; Evidence={ECO:0000269|PubMed:17588522}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18485873}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. {ECO:0000269|PubMed:15558010, ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27259151}. | Homo sapiens (Human) |
O00763 | ACACB_HUMAN | MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST | 6.4.1.2 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:16854592, ECO:0000269|PubMed:18247344}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; | acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]; malonyl-CoA biosynthetic process [GO:2001295]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of gene expression [GO:0010629]; pentose-phosphate shunt [GO:0006098]; positive regulation of heart growth [GO:0060421]; positive regulation of lipid storage [GO:0010884]; protein homotetramerization [GO:0051289]; regulation of cardiac muscle hypertrophy in response to stress [GO:1903242]; regulation of glucose metabolic process [GO:0010906]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; tricarboxylic acid metabolic process [GO:0072350] | cytosol [GO:0005829]; mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786; | 2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10; | null | PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000305|PubMed:18247344}.; PTM: Phosphorylation at Ser-222 by AMPK inactivates the enzyme (PubMed:12488245). Required for the maintenance of skeletal muscle lipid and glucose homeostasis (By similarity). {ECO:0000250|UniProtKB:E9Q4Z2, ECO:0000269|PubMed:12488245}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000269|PubMed:16854592, ECO:0000269|PubMed:19236960, ECO:0000269|PubMed:19900410, ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656, ECO:0000269|PubMed:26976583}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309; Evidence={ECO:0000269|PubMed:19900410, ECO:0000269|PubMed:26976583}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for ATP {ECO:0000269|PubMed:16854592}; KM=110 uM for ATP (isoform 2) {ECO:0000269|PubMed:19190759}; KM=58 uM for acetyl-CoA {ECO:0000269|PubMed:16854592}; KM=94 uM for acetyl-CoA (isoform 3) {ECO:0000269|PubMed:19190759}; KM=6.5 mM for NaHCO3 (isoform 3) {ECO:0000269|PubMed:19190759}; KM=3 mM for NaHCO(3) {ECO:0000269|PubMed:16854592}; | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000269|PubMed:19900410, ECO:0000269|PubMed:26976583}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000305|PubMed:19236960}; | null | FUNCTION: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (PubMed:16854592, PubMed:19236960, PubMed:19900410, PubMed:20457939, PubMed:20952656, PubMed:26976583). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:19236960, PubMed:20457939, PubMed:20952656, PubMed:26976583). Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (By similarity). Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (By similarity). {ECO:0000250|UniProtKB:E9Q4Z2, ECO:0000269|PubMed:16854592, ECO:0000269|PubMed:19236960, ECO:0000269|PubMed:19900410, ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656, ECO:0000269|PubMed:26976583}. | Homo sapiens (Human) |
O00764 | PDXK_HUMAN | MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL | 2.7.1.35 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10987144, ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10987144}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:10987144}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10987144}; Note=Zn(2+) is the most effective divalent metal cation in vitro, followed by Co(2+), Mn(2+) and Mg(2+). {ECO:0000269|PubMed:10987144}; | phosphorylation [GO:0016310]; pyridoxal 5'-phosphate salvage [GO:0009443]; pyridoxal metabolic process [GO:0042817]; pyridoxamine metabolic process [GO:0042818] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; secretory granule lumen [GO:0034774]; specific granule lumen [GO:0035580] | ATP binding [GO:0005524]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803]; pyridoxal kinase activity [GO:0008478]; pyridoxal phosphate binding [GO:0030170]; sodium ion binding [GO:0031402]; zinc ion binding [GO:0008270] | PF08543; | 3.40.1190.20; | Pyridoxine kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9099727}. | CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:10987144, ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:31187503, ECO:0000269|PubMed:9099727}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225; Evidence={ECO:0000269|PubMed:31187503}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000305|PubMed:17766369}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105; Evidence={ECO:0000305|PubMed:17766369}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000305|PubMed:17766369}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109; Evidence={ECO:0000305|PubMed:17766369}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:9099727}; KM=14.5 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:31187503}; KM=97 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:10987144}; KM=75 uM for pyridoxal (in the presence of Na(+)) {ECO:0000269|PubMed:17766369}; KM=24 uM for pyridoxal (in the presence of Na(+)) {ECO:0000269|PubMed:19351586}; KM=58 uM for pyridoxal (in the presence of Na(+)) {ECO:0000269|Ref.16}; KM=12 uM for MgATP (in the presence of K(+)) {ECO:0000269|PubMed:10987144}; KM=500 uM for MgATP (in the presence of Na(+)) {ECO:0000269|PubMed:17766369}; KM=190 uM for MgATP (in the presence of Na(+)) {ECO:0000269|PubMed:19351586}; Note=KM is <10 uM for pyridoxal (in the presence of K(+)) (PubMed:17766369). KM is <25 uM for MgATP (in the presence of K(+)) (PubMed:17766369). kcat is 200 min(-1) for phosphorylase activity using PL as substrate in the presence of Na(+). kcat is 85 min(-1) for phosphorylase activity using PL as substrate in the presence of K(+) (PubMed:17766369). kcat is 29 min(-1) for phosphorylase activity using PL as substrate in the presence of Na(+) (PubMed:19351586). {ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586}; | PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000269|PubMed:31187503, ECO:0000305|PubMed:17766369}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000305|PubMed:17766369}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. {ECO:0000305|PubMed:17766369}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:10987144}; | null | FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (Probable) (PubMed:10987144, PubMed:17766369, PubMed:19351586, PubMed:31187503, PubMed:9099727). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions. {ECO:0000269|PubMed:10987144, ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:31187503, ECO:0000269|PubMed:9099727, ECO:0000305}. | Homo sapiens (Human) |
O00767 | SCD_HUMAN | MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG | 1.14.19.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:18765284, ECO:0000305|PubMed:26098317}; Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+) ions seen in the 3D-structure. {ECO:0000305|PubMed:26098317}; | monounsaturated fatty acid biosynthetic process [GO:1903966]; positive regulation of cold-induced thermogenesis [GO:0120162]; response to fatty acid [GO:0070542]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleolus [GO:0005730] | iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:18765284, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:15610069}; | null | null | null | null | FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}. | Homo sapiens (Human) |
O00835 | ERCC3_DICDI | MSSGDSNLKRRRGGNTGQSSKSYNTWTDYEEDLEESGEFNQSIKKTTNTSSATLTSSEEKGSLLDYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTGFIINKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNSDQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFRNDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQFKLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQGKKKLLYTMNPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDGLYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGIDQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAPAIYKSIPTQHALFKQRAKNKQ | 5.6.2.4 | null | DNA damage response [GO:0006974]; embryonic organ development [GO:0048568]; hair cell differentiation [GO:0035315]; nucleotide-excision repair [GO:0006289]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]; UV protection [GO:0009650] | nucleotide-excision repair factor 3 complex [GO:0000112]; transcription factor TFIIH holo complex [GO:0005675]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:P19447}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:P19447}; | null | null | null | null | FUNCTION: ATP-dependent 3'-5' DNA helicase/translocase; binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity (By similarity). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex. When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening; it may wrap around the damaged DNA wedging it open, causing localized melting and twisting that allows XPD/ERCC2 helicase to anchor. The ATP-dependent helicase activity of XPB/ERCC3 may be required for promoter escape. Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The structure of the TFIIH transcription complex differs from the NER-TFIIH complex (By similarity). {ECO:0000250|UniProtKB:P19447}. | Dictyostelium discoideum (Social amoeba) |
O00841 | CUDA_DICDI | MNQSQNFHNIDLGHYGAQGSNQSFNNNNNGNNGMMMNQQQMQQHVVPHLHHLQQQQQQPQQQQLRNVPDYSNSPNGTTNGSTMSPNCINTNNNNNNNNNNNNNSNNNNNNNNNASNNLTSNKSSSTNTPQIGQLQASPANLTNSPSAISSPITISNNSSLNSPSTTSSPNLLLNGTSNKRIMISQQTCLVEEKFSKNGVQKNVHVVVKNNPFLLTLSLLDSSLNFHQLTPEVQLVYDSESLKEVDSATVKPLEYKTRANEEGDQLTIELRIKVLSSQLEDMLFRAKVKIVDPRTRKETHGLSVITHPIRVVSKPDQVKKKAKKRKRAPTDSLMDTLNRIEHQQKEQQRLLKKLCYHDKENNIIQLIQQQQQQQQLLNNVTNNINNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTSTTTTTTTTTSSCNNNNNNNNENNEHIVKIENTECNNNNNNIINNTENDENINKPILNSKDEFQSAFKEFIGAFKQLQCLDPDGADGAFKINTCANDAQTMCEILEMVKVELKKDENFKDKCGGSSGGACGENNPDNPCSCKVCPYKQKVDHINQSYETYFNMFNPSNSNSVVPQQSQQLQQQQIQQQQQSQQQVQQQQQQQMQQQPQQQQQQPQQQQQNQQQGQQPQQQQQQGQLDYTTYIDPQLQMQQQLQMQQAAQQQYMQQTMDQQQQQQYYMQQYHLQQQQQQQQAQRYLMQQQYMQQQAQQQQQQHQQVAIQQQQQQNQQQNQQQNQQQQNQSPQNQQSLDFQNANNFIDFNSGLGFMNFPNINFGDMGFSAV | null | null | cell differentiation [GO:0030154]; culmination involved in sorocarp development [GO:0031154]; positive regulation of gene expression [GO:0010628]; receptor signaling pathway via STAT [GO:0097696]; sporulation resulting in formation of a cellular spore [GO:0030435] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | sequence-specific DNA binding [GO:0043565] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:9226443}. | null | null | null | null | null | FUNCTION: Essential for normal culmination. May function as a transcriptional regulator. {ECO:0000269|PubMed:9226443}. | Dictyostelium discoideum (Social amoeba) |
O00899 | GAPA_DICDI | MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI | null | null | chemotaxis to cAMP [GO:0043327]; detection of mechanical stimulus [GO:0050982]; hyperosmotic response [GO:0006972]; mitotic actomyosin contractile ring assembly actin filament organization [GO:1903479]; mitotic cytokinesis [GO:0000281]; negative regulation of actin filament polymerization [GO:0030837]; protein localization to cleavage furrow [GO:1905345]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of myosin II filament assembly [GO:0043520]; response to oxidative stress [GO:0006979]; sexual reproduction [GO:0019953]; spindle assembly [GO:0051225] | cell cortex [GO:0005938]; cell trailing edge [GO:0031254]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027] | actin filament binding [GO:0051015]; calmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; small GTPase binding [GO:0031267] | PF00616;PF03836; | null | null | null | null | null | null | null | null | null | FUNCTION: Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell. {ECO:0000269|PubMed:11447112, ECO:0000269|PubMed:11577743, ECO:0000269|PubMed:9151691}. | Dictyostelium discoideum (Social amoeba) |
O00909 | ARF1_DICDI | MGLAFGKLFSRFFGKKDMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMSVAEVTDKLNLHSLRSRKWYIQSTCATSGDGLYEGLDWLSNTLTSSSK | 3.6.5.2 | null | intracellular protein transport [GO:0006886]; mitotic cytokinesis [GO:0000281]; regulation of filopodium assembly [GO:0051489]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; pathogen-containing vacuole [GO:0140220]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P84077}; | null | null | null | null | FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000250}. | Dictyostelium discoideum (Social amoeba) |
O00910 | STATA_DICDI | MSSAEFSMDDFEDTFDSNATISTKDLFEGSDRLPLNQSINTTIQNLYLPNGGFAIGDQSQQQYYQAMPPLNQSDQFNLGRSNNLTPRTNQLQQLQQQQQQQQQPQQQQQQQTYGTQSPIHMSQTPSSPLSSPLPSPTPFSRQQSYNNNNSNNTSSSQNYNNNNININNNNNNNNTNNNNNNNNGNNSNGNNGNNNNNNNNNNNNNTNNNNNNNQQQQQQQQQQQQQQQQQQQQQQQGNPNLSSPQPILDTIYKLLSEQEQTLVQMIHEQSLLLNRLPPTLDENSLAPLKSLSQKQITLSGQMNTEMSALDATKKGMILEPTDLAKLFALKQDLQIQFKQLSLLHNEIQSILNPQHSAPKPNVALVLKSQPFPVVISKGKQLGENQLVVLVLTGARSNFHINGPVKATMICDSHPTNKNNPTTPLEMDSQPIYPATLTAHFPLKFLAGTRKCSVNLKFGVNIRDLDNVTTTVESDASNPFVVITNECQWEGSAGVLLKKDAFDGQLEITWAQFINTLQRHFLIATKQDPVRPKRPLSSYDLKYIQTHFFGNRSIIHQQDFDKFWVWFGKSMQTLRYQRHISTLWQEGIIYGYMGRQEVNDALQNQDPGTFIIRFSERNPGQFGIAYIGVEMPARIKHYLVQPNDTAAAKKTFPDFLSEHSQFVNLLQWTKDTNGAPRFLKLHKDTALGSFAPKRTAPVPVGGYEPLNS | null | null | culmination involved in sorocarp development [GO:0031154]; defense response [GO:0006952]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of gene expression [GO:0010628]; receptor signaling pathway via JAK-STAT [GO:0007259]; receptor signaling pathway via STAT [GO:0097696]; regulation of cell population proliferation [GO:0042127]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; sorocarp development [GO:0030587]; sorocarp stalk cell differentiation [GO:0031149] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF09267;PF17901;PF00017;PF18214; | 1.10.238.10;2.60.40.340;3.30.505.10; | Transcription factor STAT family | PTM: Tyrosine phosphorylated in response to cAMP. Not tyrosine phosphorylated in growing cells. Tyrosine phosphorylation is first detected at the tight mound stage, continues throughout the slug stage and early culmination, and starts to decrease at mid-culmination. Barely detectable in fruiting bodies. {ECO:0000269|PubMed:9670017}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in growing cells. Translocated into the nucleus in response to cAMP-induced tyrosine phosphorylation. Nuclear at the tight mound stage and in the upper, prestalk region of tipped aggregates and in cells at the tip of the slug. Subject to crm1-dependent nuclear export. | null | null | null | null | null | FUNCTION: Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as a repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development. {ECO:0000269|PubMed:10393118, ECO:0000269|PubMed:11254360, ECO:0000269|PubMed:15053873, ECO:0000269|PubMed:9200609}. | Dictyostelium discoideum (Social amoeba) |
O01326 | RNC_CAEEL | MSDEKISMTLNFPKHKRARRKKYQKEYQERHKEEMMQQLGRRFQNQPSTSSAPPDTVEKIPLPTESTSALPFGDSPRLTEKDYETNYMIDPPVVSTHSAELIKSNRVVIKAEEAEKYMMIKAKSTTSKILQDFQTKILETVKTKRRLQADVPYIIHPCHSMKGRKTPKQKGGDESFTASDVSDDSNDSQDEASTSEPTNRQAPEADKTGEVKDEKQTCNRRNQQRKAKRLRNFEEKERQITLLKKGIDRKKTHPNGIHPDISFNEKGLGNEGPECRCPEPIKTCGLKHGYYAGEDKAIDCKKSNGENLHYYTLRVTPLPSENQLYRTHMAINGEEFEFEGFSLITHAPLPDCMTRAPICKYSMDYEFQLVEEFMPDECFDPEDCDMLFEYIFHEIFEMLDFELRPKHIPSDVESCPMIHIMPRFVQTKDDLVQLWSSKTVLAYFTSKGSSEIMSPEDVNRLCDAQIDQFTRNTSKHKQSIVLNTKFKPSAIRADWFERDEEKKEVYVVHNAIRAQTYTAISLPRIAFLEKTLNKMIQEKQSSGVYNKDFEKTKNELEHLKRENRSARNLKLREPVAGFIETGLKPDVAAHVVMTILACHHIRYNFSLDVFEEVIEYKFNDRRVIELALMHSSFKSHYGTPIDHVKNMITNCGYRRKYGAEDKREKKRVAGIMSLFNIMKGTSGGEPILHNERLEYLGDAVVELIVSHHLYFMLTHHFEGGLATYRTALVQNRNLATLAKNCRIDEMLQYSHGADLINVAEFKHALANAFEAVMAAIYLDGGLAPCDVIFSKAMYGHQPVLKEKWDHINEHELKREDPQGDRDLSFITPTLSTFHALEERLGIQFNNIRLLAKAFTRRNIPNNDLTKGHNQRLEWLGDSVLQLIVSDFLYRRFPYHHEGHMSLLRTSLVSNQTQAVVCDDLGFTEFVIKAPYKTPELKLKDKADLVEAFIGALYVDRGIEHCRAFIRIVFCPRLKHFIESEKWNDAKSHLQQWCLAMRDPSSSEPDMPEYRVLGIEGPTNNRIFKIAVYYKGKRLASAAESNVHKAELRVAELALANLESMSFSKMKAKNNSWFQNMRRRLEQDTSD | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9NRR4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NRR4}; Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion. {ECO:0000250|UniProtKB:Q9NRR4}; | cell differentiation [GO:0030154]; gonadal mesoderm development [GO:0007506]; pre-miRNA processing [GO:0031054]; primary miRNA processing [GO:0031053]; rRNA processing [GO:0006364]; sexual reproduction [GO:0019953]; termination of RNA polymerase II transcription [GO:0006369]; U4 snRNA 3'-end processing [GO:0034475] | microprocessor complex [GO:0070877]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525] | PF00035;PF14622;PF00636; | 3.30.160.20;1.10.1520.10; | Ribonuclease III family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; | null | null | null | null | FUNCTION: Executes the initial step of microRNA (miRNA) processing in the nucleus, that is the cleavage of pri-miRNA to release pre-miRNA. Involved in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in fertility. Required for the function or synthesis of the let-7 miRNA. {ECO:0000269|PubMed:15531879}. | Caenorhabditis elegans |
O01346 | EGH_DROME | MNSTTKHLLHCTLLITVIVTFEVFSGGIKIDENSFTLVDPWTEYGQLATVLLYLLRFLTLLTLPQVLFNFCGLVFYNAFPEKVVLKGSPLLAPFICIRVVTRGDFPDLVKTNVLRNMNTCLDTGLENFLIEVVTDKAVNLSQHRRIREIVVPKEYKTRTGALFKSRALQYCLEDNVNVLNDSDWIVHLDEETLLTENSVRGIINFVLDGKHPFGQGLITYANENVVNWLTTLADSFRVSDDMGKLRLQFKLFHKPLFSWKGSYVVTQVSAERSVSFDNGIDGSVAEDCFFAMRAFSQGYTFNFIEGEMYEKSPFTLLDFLQQRKRWLQGILLVVHSKMIPFKHKLLLGISVYSWVTMPLSTSNIIFAALYPIPCPNLVDFVCAFIAAINIYMYVFGVIKSFSLYRFGLFRFLACVLGAVCTIPVNVVIENVAVIWGLVGKKHKFYVVQKDVRVLETV | 2.4.1.- | null | axon guidance [GO:0007411]; border follicle cell migration [GO:0007298]; cell fate commitment [GO:0045165]; dsRNA transport [GO:0033227]; follicle cell of egg chamber development [GO:0030707]; follicle cell of egg chamber-cell adhesion [GO:0007299]; germ cell development [GO:0007281]; germarium-derived egg chamber formation [GO:0007293]; glycosphingolipid biosynthetic process [GO:0006688]; insect visual primordium formation [GO:0001744]; maintenance of polarity of follicular epithelium [GO:0042248]; male courtship behavior [GO:0008049]; morphogenesis of follicular epithelium [GO:0016333]; negative regulation of female receptivity, post-mating [GO:0045434]; oocyte localization involved in germarium-derived egg chamber formation [GO:0030720]; oocyte microtubule cytoskeleton organization [GO:0016325]; peripheral nervous system neuron development [GO:0048935]; regulation of egg-laying behavior [GO:0046662] | cytoplasm [GO:0005737]; membrane [GO:0016020] | beta-1,4-mannosyltransferase activity [GO:0019187] | PF13632; | null | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis. Neurogenic protein implicated in epithelial development. Critical component of a differential oocyte-follicle cell adhesive system. {ECO:0000269|PubMed:12454022}. | Drosophila melanogaster (Fruit fly) |
O01367 | HOW_DROME | MSVCESKAVVQQQLQQHLQQQAAAAVVAVAQQQQAQAQAQAQAQAQQQQQAPQVVVPMTPQHLTPQQQQQSTQSIADYLAQLLKDRKQLAAFPNVFTHVERLLDEEIARVRASLFQINGVKKEPLTLPEPEGSVVTMNEKVYVPVREHPDFNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDANRGKPNWEHLSDDLHVLITVEDTENRATVKLAQAVAEVQKLLVPQAEGEDELKKRQLMELAIINGTYRDTTAKSVAVCDEEWRRLVAASDSRLLTSTGLPGLAAQIRAPAAAPLGAPLILNPRMTVPTTAASILSAQAAPTAAFDQTGHGMIFAPYDYANYAALAGNPLLTEYADHSVGAIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ | null | null | apposition of dorsal and ventral imaginal disc-derived wing surfaces [GO:0007475]; axon ensheathment [GO:0008366]; cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; germ-line stem cell population maintenance [GO:0030718]; glial cell migration [GO:0008347]; mesoderm development [GO:0007498]; mesodermal cell migration [GO:0008078]; muscle attachment [GO:0016203]; muscle cell fate determination [GO:0007521]; muscle organ development [GO:0007517]; negative regulation of RNA export from nucleus [GO:0046832]; oenocyte development [GO:0007438]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of embryonic development [GO:0045995]; regulation of heart contraction [GO:0008016]; regulation of mRNA splicing, via spliceosome [GO:0048024]; sarcomere organization [GO:0045214]; somatic muscle development [GO:0007525]; spermatogonial cell division [GO:0007284] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729] | PF00013;PF16544; | 1.20.5.4010;3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23788626, ECO:0000269|PubMed:9169854}. | null | null | null | null | null | FUNCTION: RNA-binding protein involved in muscle development and dosage compensation (PubMed:23788626, PubMed:9118803, PubMed:9169854, PubMed:9344542). Vital role in steroid regulation of muscle development and to control heart rate (PubMed:9169854). Required during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization (PubMed:9118803). Required for integrin-mediated cell-adhesion in wing blade (PubMed:9344542). Together with Sxl, acts as an inhibitor of dosage compensation in females by preventing production of msl-2 protein, an essential component of the MSL complex (PubMed:23788626). Specifically binds to the 5'-UTR of msl-2 transcripts and cooperates with Sxl to promote nuclear retention of msl-2 mRNAs (PubMed:23788626). {ECO:0000269|PubMed:23788626, ECO:0000269|PubMed:9118803, ECO:0000269|PubMed:9169854, ECO:0000269|PubMed:9344542}. | Drosophila melanogaster (Fruit fly) |
O01382 | DRICE_DROME | MDATNNGESADQVGIRVGNPEQPNDHTDALGSVGSGGAGSSGLVAGSSHPYGSGAIGQLANGYSSPSSSYRKNVAKMVTDRHAAEYNMRHKNRGMALIFNHEHFEVPTLKSRAGTNVDCENLTRVLKQLDFEVTVYKDCRYKDILRTIEYAASQNHSDSDCILVAILSHGEMGYIYAKDTQYKLDNIWSFFTANHCPSLAGKPKLFFIQACQGDRLDGGVTMQRSQTETDGDSSMSYKIPVHADFLIAYSTVPGFYSWRNTTRGSWFMQSLCAELAANGKRLDILTLLTFVCQRVAVDFESCTPDTPEMHQQKQIPCITTMLTRILRFSDKQLAPAGRV | 3.4.22.- | null | apoptotic process [GO:0006915]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; negative regulation of Toll signaling pathway [GO:0045751]; neuron remodeling [GO:0016322]; nurse cell apoptotic process [GO:0045476]; positive regulation of compound eye retinal cell programmed cell death [GO:0046672]; positive regulation of neuron apoptotic process [GO:0043525]; programmed cell death [GO:0012501]; programmed cell death involved in cell development [GO:0010623]; proteolysis [GO:0006508]; response to X-ray [GO:0010165]; salivary gland histolysis [GO:0035070]; spermatid differentiation [GO:0048515] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | BIR domain binding [GO:1990525]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; ubiquitin protein ligase binding [GO:0031625] | PF00656; | 3.40.50.1460; | Peptidase C14A family | null | null | null | null | null | null | null | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro. | Drosophila melanogaster (Fruit fly) |
O01404 | PHM_DROME | MPRISEIAASVGLLLLIGVISVDGLVKEGDYQNSLYQQNLESNSATGATASFPFLMPNVSPQTPDLYLCTPIKVDPTTTYYIVGFNPNATMNTAHHMLLYGCGEPGTSKTTWNCGEMNRASQEESASPCGPHSNSQIVYAWARDAQKLNLPEGVGFKVGKNSPIKYLVLQVHYAHIDKFKDGSTDDSGVFLDYTEEPRKKLAGTLLLGTDGQIPAMKTEHLETACEVNEQKVLHPFAYRVHTHGLGKVVSGYRVRTNSDGEQEWLQLGKRDPLTPQMFYNTSNTDPIIEGDKIAVRCTMQSTRHRTTKIGPTNEDEMCNFYLMYYVDHGETLNMKFCFSQGAPYYFWSNPDSGLHNIPHIEASTL | 1.14.17.3 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000305|PubMed:9006979}; Note=Binds 2 copper ions per subunit. {ECO:0000305|PubMed:9006979}; | memory [GO:0007613]; peptide metabolic process [GO:0006518]; regulation of imaginal disc-derived wing size [GO:0044719]; response to fungus [GO:0009620]; sexual reproduction [GO:0019953] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020] | copper ion binding [GO:0005507]; peptidylglycine monooxygenase activity [GO:0004504] | PF03712;PF01082; | 2.60.120.230;2.60.120.310; | Copper type II ascorbate-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:137000, ChEBI:CHEBI:142768; EC=1.14.17.3; Evidence={ECO:0000269|PubMed:9006979}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 uM for alpha-N-acetyl-Tyr-Val-Gly {ECO:0000269|PubMed:9006979}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:9006979}; | null | FUNCTION: Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides is required for normal developmental transitions and for biosynthesis of secretory peptides throughout the life. {ECO:0000269|PubMed:10993678, ECO:0000269|PubMed:11517257}. | Drosophila melanogaster (Fruit fly) |
O01427 | AIR2_CAEEL | MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH | 2.7.11.1 | null | chromosome condensation [GO:0030261]; chromosome segregation [GO:0007059]; establishment of protein localization [GO:0045184]; meiotic spindle midzone assembly [GO:0051257]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic sister chromatid separation [GO:1901970]; regulation of actomyosin contractile ring contraction [GO:0031991]; regulation of cytokinesis [GO:0032465] | chromosome passenger complex [GO:0032133]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; histone H3 kinase activity [GO:0140996]; kinesin binding [GO:0019894]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Phosphorylated. Increased phosphorylation upon chromatin obstructions at anaphase. {ECO:0000269|PubMed:23684975}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9852156}. Chromosome {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:9852156}. Midbody {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Note=Meiotic and mitotic chromosomes (PubMed:18923084, PubMed:9852156). During each division, relocates to the midbody microtubules (PubMed:23684975, PubMed:9852156). Localizes on chromosomes during metaphase and on the central spindle during anaphase (PubMed:23684975, PubMed:25475837). Localization to homologous chromosomes during segregation is dependent on lab-1 (PubMed:18923084). {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:9852156}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis (PubMed:10354474, PubMed:10975519, PubMed:10983970, PubMed:11050384, PubMed:11050385, PubMed:12707312, PubMed:9852156). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation (PubMed:10983970, PubMed:12707312). Required for histone H3 phosphorylation during segregation of homologous chromosomes in meiosis and mitosis (PubMed:18923084). Required for histone H3 'Ser-10' phosphorylation (PubMed:10354474, PubMed:10975519, PubMed:10983970, PubMed:11050384, PubMed:11050385, PubMed:11940606, PubMed:12015116, PubMed:9852156). Phosphorylates tlk-1 at 'Ser-634', which enhances its activity (PubMed:15916946). Phosphorylates zen-4 at 'Ser-680' (PubMed:15854913). Required for the recruitment of bub-1 to the ring-shaped domain between chromosomes during meiotic anaphase I (PubMed:20729837). Also required for the localization of the condensin I complex subunit smc-4 to mitotic chromosomes (PubMed:11914278). Acts at the spindle midzone and the midbody to prevent cleavage furrow regression upon chromatin obstructions during cytokinesis (PubMed:12213836, PubMed:23684975). {ECO:0000269|PubMed:10354474, ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:10983970, ECO:0000269|PubMed:11050384, ECO:0000269|PubMed:11050385, ECO:0000269|PubMed:11914278, ECO:0000269|PubMed:11940606, ECO:0000269|PubMed:12015116, ECO:0000269|PubMed:12213836, ECO:0000269|PubMed:12707312, ECO:0000269|PubMed:15854913, ECO:0000269|PubMed:15916946, ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:20729837, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. | Caenorhabditis elegans |
O01479 | TMOD_CAEEL | MSQAKTDYYSEEKTFSAPSANSQQGTQLPSKVYNKGLKDLEDNDIEGLLSSLSIDELEDLNNDFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWEDVCPYTPGQKRGKVYDSDSGRNSEEPENGKMEMPIEIDLDDDEEELECALVTAPEKDLVDLAGILGMHNVLNQPQYYNALKGKTQDESTGTTFNGIMQSYVPRIVPDEPDNDTDVESCINRLREDDTDLKEVNINNMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLLRSTLVTQSIVEFKADNQRQSVLGNQVEMDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRLGKDPNV | null | null | actin filament organization [GO:0007015]; embryo development ending in birth or egg hatching [GO:0009792]; locomotion [GO:0040011]; muscle contraction [GO:0006936]; muscle thin filament assembly [GO:0071689]; myofibril assembly [GO:0030239]; negative regulation of actin filament depolymerization [GO:0030835]; nematode larval development [GO:0002119]; pointed-end actin filament capping [GO:0051694]; sarcomere organization [GO:0045214] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]; terminal web [GO:1990357] | actin filament binding [GO:0051015]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as the pointed end capping protein which maintains the length and dynamics of the actin filament. Blocks the elongation and depolymerization of the actin filaments at the pointed end (By similarity). {ECO:0000250}. | Caenorhabditis elegans |
O01498 | STAM1_CAEEL | MKKQKSFPMSAYEDLLGKITAPTITVENWEGILAFCDMINNDFEGSKTGIKSLRKRLNNRDPHVVLLAISVLDSCWANCEERFRKEVSSAQFINELKALCTSSQRQVAEKMRLTVQKWVDTECKTEQSLSLIVTLHKNLVADGYSFVVDDPKSKTKAIDAKFANDPNYVGSAQEEEAIAKAIAASLADAEKQEKAKKSTSTMYPSAKASSPAVQTNSNIPEKNVRALYDFEAAESNELSFVAGDIITITDESNPHWWTGRIGTQQGLFPSSFVTNQLDDLKSKETDSSQKAPEVVASINEAILVRCLQVLHECDPTGERQDPEDLAQLEAASYAQGNLIDAHLASIDRQSNSLAQIDVAIRDVLALYDDAIQKGGFQHQSQGMYQQPMQQYNYQQPPNRAYYPPTGPVQQQQPQQYPPQHYPAPGAQPQYACPPNSVPQPQQQQQQWPAPSSQPQQY | null | null | endosome to lysosome transport [GO:0008333]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of MAPK cascade [GO:0043409]; protein localization to non-motile cilium [GO:0097499]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; response to hermaphrodite contact [GO:0034606] | cilium [GO:0005929]; early endosome [GO:0005769]; endosome [GO:0005768]; ESCRT-0 complex [GO:0033565] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130] | PF00018;PF00790; | 1.20.5.1940;1.25.40.90;2.30.30.40; | STAM family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17581863}. Endosome {ECO:0000269|PubMed:17581863}. Note=Located to early endosomes at the ciliary base but not cilium proper of male-specific sensory neurons. {ECO:0000269|PubMed:17581863}. | null | null | null | null | null | FUNCTION: Binds, sorts and targets the polycystin complex (lov-1 and pkd-2) for lysosomal degradation, acting on early endosomes located at the ciliary base. Functions in the germline together with the ephrin receptor (vab-1) signaling pathway to negatively regulate MAPK activation. May have a role as a positive regulator of meiotic maturation in oocytes, acting independently of vab-1. {ECO:0000269|PubMed:16824915, ECO:0000269|PubMed:17581863}. | Caenorhabditis elegans |
O01501 | CCNE_CAEEL | MAGRKSSRTAERVPTTQKPERKSAILSPHDELRERLLETAIDMKENIPQRNTRNSSVGSQKSDCSETRKRRSTKEGPAAKRHSGEKHRNGSREDSLEYISEYSDDREVGSSSSQSSRTRGQPLPAMPEEEEVFDKSSSSDNLAESEESHEMVRLEERQDIEEEIEDDFDDEEEDVVNDKEEYEEIESEDEDDYPVQNEGFAVTKRLMNDEHMVTAPTFLSTAKCDGIGSPTKVWSLMVKRDEIPRATRFLLGNHPDMDDEKRRILIDWMMEVCESEKLHRETFHLAVDYVDRYLESSNVECSTDNFQLVGTAALFIAAKYEEIYPPKCIDFAHLTDSAFTCDNIRTMEVLIVKYIGWSLGPITSIQWLSTYLQLLGTGKKNKSDHYEEQNMYVPELLRSEYLEMCKILDFLLFEIDSFTFSYRTIAAAVLFVNYEPTCAVEKATGFMQAQLEKVIEYVEPVCRAFAKQRQLLDDVIPKHESIKSDDSHNIQVYVKRSSMEPIVKSERERIQHLKARRLHPQRLF | null | null | cell division [GO:0051301]; DNA endoreduplication [GO:0042023]; embryo development ending in birth or egg hatching [GO:0009792]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell development [GO:0007281]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; gonad development [GO:0008406]; meiotic cell cycle [GO:0051321]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of protein localization to centrosome [GO:1904781]; positive regulation of vulval development [GO:0040026]; post-embryonic development [GO:0009791]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of meiotic cell cycle [GO:0051445]; regulation of mitotic nuclear division [GO:0007088]; regulation of protein localization to cell cortex [GO:1904776] | centriole [GO:0005814]; centrosome [GO:0005813]; chromatin [GO:0000785]; cyclin E1-CDK2 complex [GO:0097134]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF00134; | 1.10.472.10; | Cyclin family, Cyclin E subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12606285}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:17115027}. Note=Co-localizes with cdk-2 in the sperm centrioles before the first embryonic mitosis and then to the male and female nuclei upon entry into mitosis. {ECO:0000269|PubMed:12606285, ECO:0000269|PubMed:17115027}. | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G1/S (start) transition (PubMed:12606285). In association with cdk-2, regulates proliferation, quiescent state and cell fate during the development of several cell lineages (PubMed:10952902, PubMed:17476329, PubMed:21455289, PubMed:21558371). In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal proteins spd-2 and spd-5 during prophase (PubMed:17115027). During the development of the vulva, controls the onset of vulval cell terminal differentiation by controlling the duration of G1 phase (PubMed:10952902, PubMed:20005870). During hypoderm development at early larval stages, controls syncytial fate of seam cell daughter cells (PubMed:17476329). Involved in the progression of cell division in the intestinal lineage in larvae, and in particular in endoreplication, a specific growth pathway in the intestinal epithelium, required for feeding and gut development in growing larvae (PubMed:17466069). By controlling the activity of translational repressor gld-1, regulates the pool of germline stem cells and the size of the mitotic zone by preventing entry into meiosis (PubMed:21455289). In addition, repression of expression by gld-1 prevents mitosis re-entry in meiotic germline cells (PubMed:19758560). {ECO:0000269|PubMed:10952902, ECO:0000269|PubMed:12606285, ECO:0000269|PubMed:17115027, ECO:0000269|PubMed:17466069, ECO:0000269|PubMed:17476329, ECO:0000269|PubMed:19758560, ECO:0000269|PubMed:20005870, ECO:0000269|PubMed:21455289, ECO:0000269|PubMed:21558371}. | Caenorhabditis elegans |
O01510 | SMG1_CAEEL | MITSRNNDIGNLIEQFRQRDTPQKERKAILARIEEILQTTKNVESLCVKWTYLLDNLCWPSLTKHDRNDMKTLAGKVIRLVGVLLFDTESYPEFLIYLGTLYQSVTKKSEETRADIVFSVYFIVGVISQKTENRLIATDTENVEKSLDWIIKVLPNSSISVYNHCLKGFVLVANTFPNVYAAMFESTLRAILTNLPDFNSHEKNFELLIDTVMRFSDQLNEKPHLAEEMVRIIRPDIKKNGLGNMRELKKRMKLTMALVKMAKSQKMLEETNQMISEMSIELEENGGKWSSASLITIVCDVFNELLILGKDDVKLQKGVEESLCNVLKDLNLSNQSTMEKQAFFNSLAKIVKQLPAESQVKTRVHQIVFNTETGLFTPKNRDNRMFGHNMIYKDLINLVSVLLTPTSLNHLQATYTDLRKIMIDSMSRLKQSEDTPYSDNIRWNESILLLFFSSLQSISCAKSSLIVMMGIRPSIFEFFSSELPLTEYWLASNHPEVYHLFITIFVGHLKAHDFYIVQSDYIVRGDSIGQSIGQTKRDYARKQVVALQKIINNFGDKLWKKTRLMISSWLHSLIATACEHQIGSDSFSQREWVRLRNTVIHQSVLTWNNECVNQALTILSTATKWSELTSDIHRDIADKTKKAKWKEATTIWESGDCNTYIRQSMSTVYQMSQERQQKTITSTSFGAEEFIIITNFLLKQATPTTFKKGQNSWMDEVLETFTQGCRTLEKPDSYVPETFIEKWDWIINQTANFCIVNKMKTPLGKPMQTFAAFENEIKRLAKEVIVRKNSDKKLNKSSTEDPNQSPPLKYSVQWLRVHLLLKLIVVLEKLMNSAIHGGSSVFNLTEIPVSSRQFFTVNAASCEVWLNRVYYPALLVAYFNGYYGLVIRFGSNALSHFARQKDGDNDKKIVNGVCTASLMSLSMAVLGEPMEIVGLRRKVREEFGTDMGQSLMEALGEMANARYETALVALEAVLVTDAATNETLKMIIQLAMVDILNRIRLPQATDYYKVVLFGEESNDSTITEDFRSVELLTKFEKLNNTVNEKRQVVDWSARERFQFVESAFSQTMRRTELLDIQKDFSAMGALALSADSSCKLYSDISSTSLIIANLVNKMTGVSQWKNKLTDTEIFDRNEEGNDGDKLAICRKLMHWGRHTKSNRGQSCAAHSEIIRLSRKTSNCELAFFHINSAIRGEKLAAWQRLEVERQRLKLVKTQNLDVRIREMNEVFGSLAEVFTTSCQLKSDFQMVDGMIKEKMISEGYNEDIAKREEHMSRASIQLADFFQSLPELENVLAPNLFPTIIWSELQRRSDSLSAGYHGIVGSLFHLASEMCPSLAKAHLKMARWAYEIAKIKNFPAENLSFYKFGKDETENEELLKSLEATSLVNLEKLVRAAISDDLRANNILAPNSHFMHIWKMVRDHRTKFLSIAVTSYFQFIQNMSGDCDNLPYSKKEETTLATLRILELLVKHGDVLIDVINDGLNKTNVHIWKEILPQLFARLSHPSEHIRKTLVDLISKICTAAPHAVVFQVVSGAASSSTDGEELEEQQNDDRNRVRACCEKLETNMSQSYPNLVKDVRQFVAELERINLLNEEKWSVVMGTMEHEMEKRLSLIRTENAKTESALHLTASVKNDIIVKRTQLLTRQIFDVLDELYQQTVIEPPKSKNEEEFVTAFAEVLTNAFQESRISRTTSPEKSWIPFKNLIANFVHRNSKKGMQTFETEDISPYLASLSNSCVPMPGQESVEFDRVVSISRVARQVTILPTKTRPKKLGFVGSDGKQVAFLFKGREDLHLDERVMQFLRLCNVMLQPGKGKHRQSVAAYQAHHYAVIPLGPRSGLIKWVEGATPMFHIYRKWQMKEKALKQATKKNGETVPEIERPSNMYHNMIRLAFADHKIDSSITSDRSKWPAEILEEVFESLTAKTPTDLISRELWMRANDATTWWSVTKRYSRSLAVMSMVGSVLGLGDRHLDNLLVDLKWGHVVHIDYNICFDKGKNLRIPETVPFRLTRNMRHALGPSEMYGTFRESCVHVLSTLRSGHQVLTMLLDAFVFDPLVDWTSHEHTATSGVSLALQLAVYGSNWKTKAKERLTDAMELLNLRMSEVQTLWLANRDDLLHWMKQVTECLLIENSMLGANAIYAQQRVKAGTELREAVTRHHALAKELRPLIRVIGKEREEFADYLKFYKQALFDPLLKGHSALRNELDIDTCVYNFNIVMQNIDNVFGALVNLSFTPIETITSRTSQQEFKPPPGLENVWVVKQDQQENSQAREVVRRVERRLNGWLDGSAGPDRKLSPREEADILIAEATSTPNLSQMYEGWTAWV | 2.7.11.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | male genitalia development [GO:0030539]; negative regulation of macroautophagy [GO:0016242]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; phosphorylation [GO:0016310]; TOR signaling [GO:0031929] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF02260;PF00454;PF15785; | 1.10.1070.11; | PI3/PI4-kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15314158}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in mRNA surveillance. Recognizes the substrate consensus sequence [ST]-Q. Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating smg-2. {ECO:0000269|PubMed:15314158, ECO:0000269|PubMed:2583479}. | Caenorhabditis elegans |
O01583 | MRCK_CAEEL | MAEPPPDDSAPVRLKTLENIYMDGPSKKPEALSFETLIDSLICLYDECCNSTLRKEKCIAEFVESVKTVISKAKKLRLSRDDFEVLKVIGKGAFGEVAVVRMRGVGEIYAMKILNKWEMVKRAETACFREERDVLVYGDRRWITNLHYAFQDEKNLYFVMDYYIGGDMLTLLSKFVDHIPESMAKFYIAEMVLAIDSLHRLGYVHRDVKPDNVLLDMQGHIRLADFGSCLRILADGSVASNVAVGTPDYISPEILRAMEDGRGRYGKECDWWSLGICMYEMLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDWVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIRDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCLQETQPPRVLAAFTGNHLPFVGFSYTHGSLLSDARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSDSAFSSTMGRGDLMISMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVPKRVDDLRYKQKPMKTASGIFSPVSISAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEERRPLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDRQNKMQDVKNEIRLVLDMRDPDFTVCGVSEADVIHAQKGDIPKIFRVTTTQILNSSSEYSSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRSKLADRKAFLVKEVFDVTTLPSIRVAQCCAIIDRSKIVIGFSDHGLYCIEISRQLLIPVGGEKENKQRCVETVEYDEAEQLLMMIVGPAKDRHVRIVPSAALDGRDLKWIKVNDTKGCHLLAVGTNNPGGRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHSFRSWSLVGVDSSPVGSGDASGAVLQHISLVNMEDTSLQFLNQQTSYEAKLIVNVPGSPDEYLLVFNMIGLYVNEMGRRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPLSGDGILSTCLCNDSPIFVLLQNVLQDQDSIEVPVNLASGSTDGRKVTRRKFTFRTIGKDDRSASERRSHIQISTPSDFMHIVHMGPAPVMELQQNFIDLQSNHSHTSSDKDSLNRSVNND | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5VT25}; | actomyosin structure organization [GO:0031032]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; embryonic morphogenesis [GO:0048598]; epithelial tube morphogenesis [GO:0060562]; nematode larval development [GO:0002119]; phosphorylation [GO:0016310]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of GTPase activity [GO:0043547]; regulation of Golgi organization [GO:1903358] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00780;PF00069;PF00433; | 3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, DMPK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675126}. Note=Forms parallel punctate bundles in dorsal and ventral epidermal cells. {ECO:0000269|PubMed:19675126}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q5VT25}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q5VT25}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation (PubMed:19675126). Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation (PubMed:25743393). {ECO:0000269|PubMed:25743393, ECO:0000305|PubMed:19675126}. | Caenorhabditis elegans |
O01658 | NO66_CAEEL | MGKKKNSNKSAAAAPAVKHNDRWSSIELGEAKSAAVSHYKEPSKEPKFVHPAKLEKVKRIHDGLNIDRVLSHGPVPKQNGGTKRKHVEVTTQKLENKKPKVEVKKEDEKSKNKKMKNQNKHTALVQNETSTRSTYFVEEPDNENKVTLISNGREIAFKKTEVVESDDEQMIGLDSDEELEDEDETDIDEDEMMIDPKDIERYINFESVEDEEDMEDEEIEDEEFEDEEFEDEEEEADEQEEEEEDVSDEESVVSEMDADSDDEGFIAGKDREAHVISKDKFTRNAPAVDFDKFPFTDEDSVVTSSRAFGFMISPCDVQTFFDKFYQSNVLVVRRKQPTYFGNLFSTARLGELLEKNHLEYGRNINIAQYKNGVRTTLNGQGRAYPQIVKQHLHNMCSVQLVNPQTYDDRIWYLCEVIQEQFGCFVGANTYLTPAGSSGFAPHWDEIDAFLLQVEGRKYWRVWAPESAEEELPLESSDNFTEDDMKGREPVFEGWIEKGDMIYIPRGYIHQARTDSKVHSLHVTVSTGRQWSFANLMEKVVPEAIGVLTDTRHKLRRGLPTGLFDMGGVIDLDYSQEDHFVEKFKMVVDRHMSMLRNLVADQLLESSVDSLAKEFMKQALPPRLTEQEKKLSVLGSSTNLLGDDLVDFTARTKVRLIRRHTQRLLMESEDACFISHRINNSRLFEGRPEQIVEYPISGIDAYRVLSNSYPEWRTLYEIFSLRETKTKSRKENLAAIQLLFQIGVLLVKN | 1.14.11.-; 1.14.11.27 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; | negative regulation of DNA-templated transcription [GO:0045892]; response to ethanol [GO:0045471]; response to heat [GO:0009408]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979] | nucleolus [GO:0005730]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506] | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.27; | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Mediates response to multiple stress stimuli, including heat shock and osmotic, oxidative, and ethanol stress. {ECO:0000250, ECO:0000269|PubMed:20057358}. | Caenorhabditis elegans |
O01668 | OPS6_DROME | MASLHPPSFAYMRDGRNLSLAESVPAEIMHMVDPYWYQWPPLEPMWFGIIGFVIAILGTMSLAGNFIVMYIFTSSKGLRTPSNMFVVNLAFSDFMMMFTMFPPVVLNGFYGTWIMGPFLCELYGMFGSLFGCVSIWSMTLIAYDRYCVIVKGMARKPLTATAAVLRLMVVWTICGAWALMPLFGWNRYVPEGNMTACGTDYFAKDWWNRSYIIVYSLWVYLTPLLTIIFSYWHIMKAVAAHEKAMREQAKKMNVASLRNSEADKSKAIEIKLAKVALTTISLWFFAWTPYTIINYAGIFESMHLSPLSTICGSVFAKANAVCNPIVYGLSHPKYKQVLREKMPCLACGKDDLTSDSRTQATAEISESQA | null | null | cellular response to light stimulus [GO:0071482]; entrainment of circadian clock by photoperiod [GO:0043153]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phototransduction [GO:0007602]; sensory perception of sound [GO:0007605]; thermotaxis [GO:0043052]; visual perception [GO:0007601] | membrane [GO:0016020]; rhabdomere [GO:0016028] | G protein-coupled photoreceptor activity [GO:0008020] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Drosophila melanogaster (Fruit fly) |
O01683 | SSP1B_CAEEL | MTELKFKGVYVEDIGHLTCGTLTLTENSINFIGDKGGKSVYITGTDVDKLKWQKLGNKPGLRVGLSDGGAHRFGGFLDDDLQKIQSFTSSNWSKSINQSNLFINGWNYGQADVKGKNIEFSWENEPIFEIPCTNVSNVIANKNEAILEFHQNEQSKVQLMEMRFHMPVDLENEEDTDKVEEFKKAVLAYAGLEAETEQPICLLTDILCTTPRGRYDIKVYPTSIALHGKTYDYKIPVKTINRLFLVPHKDGRQVYFVLSLNPPIRQGQTHYSYLIFEFGKDEEEDLELSLTDEQLDYFNGNLQREMTGPIYETISILFKSICNLKVTVPGRFLGSSGTPAIQCTHRQNLGLLYPMEKGFLFIQKPVMYIRFEEISSCHFARSDSGTVTRTFDFEIDLKTGSSLTFSAMDKEENNKLFDYLNKKEIKIRNSHRIDNKSAGYGSSDEDDIDPYKSTVKAEGREQDDDSDDESTDEDYDLDKDMKKQKNDKDSSEGSGSEPDDEYDSGSEKDASGTGESDPDEENIEPKKKESKEKKNKREKKEKPVKEKAVKKGKKTKDPNEPKRATTAYIIWFNANRNSMKEDGDTLGDVAKKAGAKWKSMSADDKKEWNDKAAQDKARYEAEMKEYKKNGGGVEKASGPSTKKSSDQSPGKQFKSKEHISDTDDSDDDEPLKAKKDESDAASESSGESD | null | null | DNA repair [GO:0006281]; DNA replication [GO:0006260]; nematode pharynx development [GO:0160094]; nucleosome assembly [GO:0006334]; nucleosome disassembly [GO:0006337]; pharynx development [GO:0060465]; positive regulation of cell cycle [GO:0045787]; regulation of chromatin organization [GO:1902275]; regulation of embryonic development [GO:0045995] | FACT complex [GO:0035101]; nucleus [GO:0005634] | DNA binding [GO:0003677]; histone binding [GO:0042393]; nucleosome binding [GO:0031491] | PF00505;PF21103;PF17292;PF08512;PF03531; | 2.30.29.150;1.10.30.10;2.30.29.30;2.30.29.220; | SSRP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:30336114}. Chromosome {ECO:0000250|UniProtKB:Q08945}. | null | null | null | null | null | FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity). In embryos, may function redundantly with hmg-4 to promote cell cycle progression and development of the anterior pharynx (PubMed:30336114). In the germline, acts non-redundantly with hmg-4 to play a role in oocyte development (PubMed:30336114). {ECO:0000250|UniProtKB:Q08945, ECO:0000269|PubMed:30336114}. | Caenorhabditis elegans |
O01700 | DLK1_CAEEL | MTSTTMVTTLDLVTPTSEEQPGPAPESSDFSTVVLSPDGSELVTQSAPNTPIQHREQANAEFGQKEGSPDPKNMVAATGNASKPSLNSFYADGLGQLRNGLFSCFQPVFGYFGTKTTVEIEKSEDELWEIPFDAISELEWLGSGSQGAVFRGQLENRTVAVKKVNQLKETEIKHLRHLRHQNIIEFLGVCSKSPCYCIVMEYCSKGQLCTVLKSRNTITRELFAQWVKEIADGMHYLHQNKVIHRDLKSPNILISAEDSIKICDFGTSHMQKKMDSTMMSFCGTVSWMAPEMIKKQPCNEKVDVYSFGVVLWEMLTRETPYANIAQMAIIFGVGTNILSLPMPEEAPKGLVLLIKQCLSQKGRNRPSFSHIRQHWEIFKPELFEMTEEEWQLAWDSYREFAKCIQYPSTVTRDHGGPKSAFAMEEEIQRKRHEQLNHIKDIRNMYEMKLKRTNKMYDKLQGCFTELKLKESELAEWEKDLTEREQWHNQNSPKAVAAPRAQLRGYPNEGYDDMSSDEDVQPCRGSPYRCSNTSSSSGVQSSPFSRQSSSRSSAGQQTRRSEGANPPKILRNDAIRHSGSYWETLGGARGSPARDSGFSQDSGMWSAGAGSCTAINGGGQQVCYSQTLYRNGDGRWSDGRIASRRRVSTSVNKSTAVPGQPVFFTRDSPSRVPHGVISCSSPRSSSKLNRSSYPSRNAPHQLEDGCCCAHARAPRAKSIAVPMTSSSRARSPTPYDNDFENAESFVDPESPKNLKNLEKIVNLPESTSYDEALCNSDVTMNPIYTSPITTYSNPCHVELVDEENANDVDLTSSMDSRRSRSDDADVESSEEDEGNGNNILNTSMESEDLRYRIDTSQSTMMSSLERSLEIGATRSDGLSDNEMRVQAVKMSIKTHRRTGSNPQALIHQCIDEYTTSATDDSDDAGAVRI | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O43283}; | axon extension involved in regeneration [GO:0048677]; axon regeneration [GO:0031103]; formation of growth cone in injured axon [GO:0048689]; MAPK cascade [GO:0000165]; microtubule polymerization [GO:0046785]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension [GO:0045773]; positive regulation of axon extension involved in regeneration [GO:0048691]; regulation of 3'-UTR-mediated mRNA stabilization [GO:1905868]; regulation of axon extension involved in axon guidance [GO:0048841]; regulation of synapse organization [GO:0050807]; signal transduction [GO:0007165] | axon [GO:0030424]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; synapse [GO:0045202] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by fsn-1 bound rpm-1, followed by degradation. {ECO:0000269|PubMed:15707898}.; PTM: [Isoform a]: Phosphorylation at Ser-874 and/or at Ser-878 abolishes interaction with isoform c and promotes binding to isoform a kinase domain (likely in trans) resulting in isoform a self-association and activation. {ECO:0000269|PubMed:23141066}. | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:18224716, ECO:0000269|PubMed:23000142}. Cytoplasm {ECO:0000269|PubMed:26657059}. Cell projection, axon {ECO:0000269|PubMed:26657059}. Cell projection, dendrite {ECO:0000269|PubMed:26657059}. Cell projection, cilium {ECO:0000269|PubMed:26657059}. Note=Observed in the periactive zone of the presynaptic terminal which surrounds the synaptic vesicle clusters and active zones. {ECO:0000269|PubMed:15707898}.; SUBCELLULAR LOCATION: [Isoform a]: Synapse {ECO:0000269|PubMed:23141066}. Cell projection, axon {ECO:0000269|PubMed:23141066}. Note=Co-localizes with isoform c in synapses and axons; however, isoform a localization is independent on its interaction with isoform c. During axonal injury, recruited to the injured site. {ECO:0000269|PubMed:23141066}.; SUBCELLULAR LOCATION: [Isoform c]: Synapse {ECO:0000269|PubMed:23141066}. Cell projection, axon {ECO:0000269|PubMed:23141066}. Note=Co-localizes with isoform c in synapses and axons; however, localization is dependent of its interaction with isoform a. {ECO:0000269|PubMed:23141066}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43283}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43283}; | null | null | null | null | FUNCTION: Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation (PubMed:15707898). Phosphorylates and activates mkk-4 (PubMed:15707898). Has a role in axonal regrowth following injury and synaptogenesis (PubMed:19164707, PubMed:19737525). Plays a role in modulating polymerization of neuronal microtubules (PubMed:21368137). Also promotes tubulin post-translational modifications that protect microtubules (PubMed:23000142). Plays a role in cilium length regulation, possibly by reducing rab-5 mediated endocytosis, and may also have a role in intraflagellar transport in cilia (PubMed:26657059). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord (PubMed:27123983). {ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:19164707, ECO:0000269|PubMed:19737525, ECO:0000269|PubMed:23000142, ECO:0000269|PubMed:26657059, ECO:0000269|PubMed:27123983}.; FUNCTION: [Isoform a]: Has a role in synapse and axon development, and in axonal regrowth following injury. {ECO:0000269|PubMed:23141066}.; FUNCTION: [Isoform c]: By forming heterooligomers with isoform a, acts as an inhibitor of isoform a activation. Its inhibitory function is independent of its catalytic activity. {ECO:0000269|PubMed:23141066}. | Caenorhabditis elegans |
O01704 | EXT1_CAEEL | MQNVMKFHLVIFMLFGSVRLQNPTIERKQCTMSNCFDFSKCSTSKKVYIHPMEKRFEESPQSVIYSKILKHFLESNHYTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPSVWNNGRNHLIFNFYHGTFPDYDDHNLNFDTGEAMIARASSSENNFIKVFDVSLPLFHENHPYEIKESKSERNDDRIENQRKYLVSFKGKRYVYGIGSGTRNLVHHLHNGDDIVMVTTCKHNNDWQVYQDDRCQRDNDEYDRWEYDELLANSTFCLVPRGRRLGSFRFLETLRSGCVPVVISDSWILPFSETIDWNSAAIVVAERDALSIPELLMSTSRRRVKELRESARNVYDAYLRSIQVISDHVLRIIFKRIDNKIELEDHQ | null | null | heparan sulfate proteoglycan biosynthetic process [GO:0015012]; pharynx development [GO:0060465]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; protein-containing complex [GO:0032991] | acetylglucosaminyltransferase activity [GO:0008375]; enzyme binding [GO:0019899]; glucuronosyltransferase activity [GO:0015020]; glycosyltransferase activity [GO:0016757] | PF03016; | null | Glycosyltransferase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Golgi apparatus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for the biosynthesis of heparan sulfate by positively regulating N-acetylglucosamine transferase II (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities of glycosyltransferase rib-2 (PubMed:17237233). Probably not directly involved in chondroitin sulfate biosynthesis but negatively regulates chondroitin sulfate levels (PubMed:16828468, PubMed:17237233). Maternally required for normal ventral epidermal enclosure and for embryo elongation during the early stages of embryonic development (PubMed:17237233). In addition, involved in the elongation of the pharyngeal isthmus and in the organization of the actin cytoskeleton in the pharyngeal muscles during the later stages embryonic development (PubMed:16828468). In adults, regulates egg-laying and the normal morphogenesis of the vulva (PubMed:17237233). Also involved in the directed migration of hermaphrodite-specific neurons (PubMed:17237233, PubMed:24052309). {ECO:0000269|PubMed:16828468, ECO:0000269|PubMed:17237233, ECO:0000269|PubMed:24052309}. | Caenorhabditis elegans |
O01705 | EXT2_CAEEL | MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQENCSLERRRQLIGSSTFCFLLPSEMFFQDFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSFEISDIIEMRRVGRLFYETYLADRHLLARSLLAALRYKLQIPTREVRRNQAIPLFNSSFTAPKGSVVNVQANFDDEYLLGPLESRVESTSYAYNFTEFQLYSYDFWNIIMSPHYTKEFLVNAAELPTEAEFFEDTKIGFRPIEPGSGAEFSKALGGNRQREQFTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAVLSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHARYGDSMFYNSNHTCQMSMILTGAAFIHKNYLTAYTYEMPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHECMRLFTKIYGYNPLKFSQFRADSILFKTRLPQNHQKCFKYV | 2.4.1.223; 2.4.1.224; 2.4.1.225 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9ES89}; | embryonic morphogenesis [GO:0048598]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; pharynx development [GO:0060465]; protein glycosylation [GO:0006486] | endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991] | acetylglucosaminyltransferase activity [GO:0008375]; enzyme binding [GO:0019899]; glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0050508]; glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0001888]; glycosyltransferase activity [GO:0016757]; heparan sulfate N-acetylglucosaminyltransferase activity [GO:0042328]; metal ion binding [GO:0046872]; N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity [GO:0050509] | PF03016;PF09258; | null | Glycosyltransferase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16394}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16394}. | CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16221, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12574, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132093, ChEBI:CHEBI:132104; EC=2.4.1.223; Evidence={ECO:0000269|PubMed:11121397, ECO:0000269|PubMed:17237233}; CATALYTIC ACTIVITY: Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621, Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416; EC=2.4.1.224; Evidence={ECO:0000269|PubMed:11121397, ECO:0000269|PubMed:17237233}; CATALYTIC ACTIVITY: Reaction=3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:20908, Rhea:RHEA-COMP:12623, Rhea:RHEA-COMP:14295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416; EC=2.4.1.225; Evidence={ECO:0000269|PubMed:17237233}; | null | PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000269|PubMed:11121397, ECO:0000269|PubMed:17237233}. | null | null | FUNCTION: Glycosyltransferase required for the biosynthesis of heparan sulfate (PubMed:11121397, PubMed:16828468, PubMed:17237233). Initiates heparan sulfate synthesis by transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core linker (GlcNAcT-I activity) (PubMed:11121397). In association with rib-1, is also responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains (GlcNAcT-II and GlcAT-II activities) (PubMed:11121397, PubMed:17237233). Required for normal ventral epidermal enclosure during the early stages of embryonic development (PubMed:17237233). In addition, involved in the elongation of the pharyngeal isthmus during the later stages of embryonic development (PubMed:16828468). Involved in the directed migration of hermaphrodite-specific neurons (PubMed:17237233, PubMed:24052309). {ECO:0000269|PubMed:11121397, ECO:0000269|PubMed:16828468, ECO:0000269|PubMed:17237233, ECO:0000269|PubMed:24052309}. | Caenorhabditis elegans |
O01737 | SBNO_CAEEL | MDDILSAALAESGLDFLCQQSSPTPSTSGSIHDDAGQSFSNNTHTPSVSQFFDETSNDSHSSSAYYTPMATPFVSTEDGGVPTSFFGMDEEDGGCTIMTTAGTSGSNNIDGIEDAGGGMYYPHVKVIPRKHTAPTVNQSEPSTPTVTIVPKKEDPLFETNTADSPTPSGDTSTTASYEGNDGLEDQETTSDRQNPMFVQTARSTDGRLDTPSTSATVSPHITSSLTQRSHTSSPASSASEGTVVPPRKKGLPITTGSIVKRTVQTKDGLQTQYLKAFVNENGEKIYKLLSPVAASAVARGTLPPGMGRGGSTIGRGGTMVNKNGERLMVVKNHVGPNGQMLVKRMVSPAGTRIVANGGQGRGQPIYRAVDGSNGPTHLLRRTTTTGQPTRGAPVGMAARHAVRGGTVYGGGNGYRVNLVGRGTGGSTMVHHQPLNRISSQRSVAPVGRVLNRGALRNGAQQPLHVSTSSPAFHYMEEQPSPTTNGMVIQAKTPGAGVIQARHMQSQQSFPSGGPARVLMNRSSTNAGLSRMVGGGYDQQLPTAPNGRLMIPSTAVRVPGSGMASPRLQTTPQPLTKSQKAKDEMKMAYQVGREEALQQRRNDLEDDEENLGYAETYSEYTPAKLRSGMAHPDSVVESASLSSVSPPDVKYQISIPEYLIDMGHISALQLEAVIYACQMHERRMPSGERYGYLIGDGAGVGKGRTVACIIFENYLQGRKRAIWLSVSSDLKFDAERDLRDCGAPNIPVYALNKMKYAKISGKENGSIKKGVMFATYTSLIGECRGAKSRKYRSRISQLIQWFGQDYDGVIILDECHRAKNLVPTAGAKPTKTGRMVLELQKALPNARVVYASATGATEPRNMAYMTRLGLWGERQAFPEFHDFISAVERRGVGAMEIVAMDMKQRGLYLARQLSFRGVSFAVQEVQLSSEFVKMYDAAVKLWMEARRQFQTVIETMDEEERSTCKTVWGQFWACHQRFFKYLCIAAKVDTCVQLSREAIKAKKCVVIGLQSTGESATLETLEEMGGELNEFVSTAKTVLYGLIDKHFPTDASFSMGDRDIFKDFDDFERPAKRRKTRETLSFLGDVGFDTWTGVTTGMGGRVGDGVTKNITRGLSGIGRSSMSSSTGNTNNEDANSTTSESSDGSDDEVENDMISENGGESGDLESAREEAEGARTLEDGEQDEWVKALLAEAESSSDDSDEEVVKDEDEDEEAESKSGETHEQEEEFNPFMCDFTNDDPWAHNQQIVEDTPQKDRKAKKRKRDEEEAERLREKVRKREERREKKRRRAIRRAEREKQRRNEELQARGSATDFITSSRICGNGSGEQDDINPMLIKTELLAAVERLAPSLPANTLDQLIDEMGGPEYVAEMTGRRGHMVTSETGDVMYQRRNANAEVSLELINMEEKEKFMRGEKLIAIISEAASSGISLQSDRRAINKRRRVHITLELPWSADKAIQQFGRTHRSNQVSGPEYVFLISELAGEKRFASIVAKRLESLGALTHGDRRATETRDLSQFNMDNKYGRVALDTLLKTVIGQAGTPLIDPPKDYKAGEFFEDMRLYMEGVGLLAKNKTGQYTIEKEAATIPKFLNRILGLPVHAQNSLFHYFSEIVAELIAQSKHDGTYDTGIMDLGTGDDQVRKLETRVFTGRVDNGSFRVEIHKIGVERGVSWEEAMELHKEHSNDDDGFYICHPGGANTANTKKVAALVYGIGKIRMDNGARLYAITRPSTGRSPKLMTMADLSKRFHKVSIDEAKEVWKQQYDSAANMCQHNYVYGKCRTESNGTYCEVGRRTRTYFVLSGSVLSVWPIVEEVLAGSDRKSSRMQVIRVRTEQDQKIVGLLVLPTHVRHLVQQLETHCGRSYVKTEP | null | null | nematode male tail tip morphogenesis [GO:0045138]; positive regulation of cell fate specification [GO:0042660]; positive regulation of Ras protein signal transduction [GO:0046579]; regulation of DNA-templated transcription [GO:0006355]; vulval cell fate specification [GO:0072327] | nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; histone binding [GO:0042393] | PF13872;PF13871; | 3.40.50.300; | SBNO family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20230814}. | null | null | null | null | null | FUNCTION: Transcriptional activator that functions upstream of the let-60/Ras and let-23/EGFR signaling pathways to positively regulate lin-3 expression and thereby promote vulval induction (PubMed:20230814). Plays a role in excretory duct development (PubMed:20230814). Plays a role in male tail development (PubMed:20230814). {ECO:0000269|PubMed:20230814}. | Caenorhabditis elegans |
O01739 | OXDD3_CAEEL | MLYALLLLFGGVSTVSSLRVAVVGEGVIGLSTATAILDLAEKRNIPAPEIHIFHHKPFEKILSRHIAGLFRIDSGSEIDRKYGYDTFEKLATLWREYGGLSGVQLVSGHILSDSKTKLDSQRESYGSLVYNYRDLAEPELFGPTSLFDLPRNTTTRGIHYTAYTSEGLRFCPFLKKELMTKGVRFTQRRIGNLEELGAEFDVVVNSAGLLGGVLAGDDAGNMKPIRGVLIRVDAPWQKHFLYRDFSTITIPVIDHVYMGTVKQEGAFGPNNVTSADIQDITSRYVALQPSFKRVHMLSSFVGYRPGRKQVRVEKQIRETNGSKKFTVVHNYGHSGNGFTLGYGSAVHAAHIVLDLPLDAYHGLVPEPLPINATISEWVKYLDD | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20564561}; | D-amino acid catabolic process [GO:0019478] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; D-glutamate oxidase activity [GO:0047821]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30387556}. Note=In hermaphrodites, protein secreted from proximal gonadal sheath cells may be transferred to the oocyte surface (PubMed:30387556). In males, protein secreted from the seminal vesicle into the seminal fluid is transferred to the hermaphrodite uterus during mating (PubMed:30387556). {ECO:0000269|PubMed:30387556}. | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:20564561}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12513; Evidence={ECO:0000269|PubMed:20564561}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:20564561}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000269|PubMed:20564561}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.81 mM for D-aspartate {ECO:0000269|PubMed:20564561}; KM=0.68 mM for D-glutamate {ECO:0000269|PubMed:20564561}; KM=8.87 mM for N-methyl D-aspartate {ECO:0000269|PubMed:20564561}; Note=The values given are for the recombinant protein. {ECO:0000269|PubMed:20564561}; | null | null | null | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:20564561). Plays a role in the egg-laying events and maturation processes of the reproductive organs (PubMed:22393259, PubMed:30387556). {ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:22393259, ECO:0000269|PubMed:30387556}. | Caenorhabditis elegans |
O01761 | UNC89_CAEEL | MASRRQKQFDRKYSSYRKFTATEDVNYSTHSSRSSYRSESLTSRTDGRGRSTSSEIIAGSESRSYPVYIAIQDYTPDKEDVEAIPLEQGQIVEVLDKKNSVRWLVRTKARPPRSGWVPGSYFETPTEFYKQRRRTREIENVSLSDEQAALVKRDQVYHELLRSEEEFVSSLRTCVDDYIKVLDDPEVPEAVKKNREELTLNIPELYNFHANVMLKGLNYYSDDPGKVGQTFVRLEKDFESHVEFYKQYADTLKLLEEPEIKRFFEGLSAKNDAGASSFVDHVKEIADRMVQYQNYFKEFVKYSARAHGSSKSIQKALELVTTIPQRVHDLEFTNNLKQHPGDTGKLGRIIRHDAFQVWEGDEPPKLRYVFLFRNKIMFTEQDASTSPPSYTHYSSIRLDKYNIRQHTTDEDTIVLQPQEPGLPSFRIKPKDFETSEYVRKAWLRDIAEEQEKYAAERDAISMTATSEMTASSVDFDMNASDQQSEFSEWSGSRKSSLFPGPEEGGPPRKKVKSPPVISPTGSSTSIYSGGSSSIDWTTTGTTLEMQGTRVTRTQYGFRTLQESSAKMCLKVTGYPLPDITWYKDDVQLHEDERHTFYSDEDGFFAMTIDPVQVTDTGRYTCMATNEYGQASTSAFFRVLKVEKEAAPPAFVTKLRDKECKEGDVIDFECEVEGWPEPELVWLVDDQPLRPSHDFRLQYDGQTAKLEIRDAQPDDTGVYTVKIQNEFGSIESKAELFVQADPDKNHVAPEFQATIEYVECDEGEEVRFKSVITGDPNPEIIWFINGKPLSESEKVKFISEDGICILTIKDVTRHFDGMVTCQGSNRLGSASCDGRLKVRVPPAPPTFNKPLEDKTVQEKSTVVFEVDVSGWPEPTLTFTLCGKELKNGEEGVEIVGHDGFYRISIPNTSMDKHDGEIVAKAQNEHGTAESRARLTVEQEEEESRSAPTFLKDIEDQTVKTGEFAVFETTVRGNPNPEVTWFINGHKMDQGSPGVKIEAHNHDHKLTIDSAQYAGTVLCRAENAVGRFETKARLVVLAPEKQKKPPKFVEILVDKTETVDNTVVFEVRVEGEPKPTVTWYLKGEELKQSDRVEIREFDGSIKISIKNIKIEDAGEIRAVATNSEGSDETKAKLTVQKKPFAPEFDLRPVSLTVEKGSEAVFSAHAFGIPLPTYEWSVNGRKVRDGQEGARVTRDESTVDGASILTIDTATYYSEVNHLTISVVAENTLGAEETGAQLTIEPKKESVVVEKQDLSSSEVQKEIAQQVKEASPEATTTITMETSLTSTKTTTMSTTEVTSTVGGVTVETKESESESATTVIGGGSGGVTEGSISVSKIEVVSKTDSQTDVREGTPKRRVSFAEEELPKEVIDSDRKKKKSPSPDKKEKSPEKTEEKPASPTKKTGEEVKSPKEKSPASPTKKEKSPAAEEVKSPTKKEKSPSSPTKKEKSPSSPTKKTGDEVKEKSPPKSPTKKEKSPEKPEDVKSPVKKEKSPDATNIVEVSSETTIEKTETTMTTEMTHESEESRTSVKKEKTPEKVDEKPKSPTKKDKSPEKSITEEIKSPVKKEKSPEKVEEKPASPTKKEKSPEKPASPTKKSENEVKSPTKKEKSPEKSVVEELKSPKEKSPEKADDKPKSPTKKEKSPEKSATEDVKSPTKKEKSPEKVEEKPTSPTKKESSPTKKTDDEVKSPTKKEKSPQTVEEKPASPTKKEKSPEKSVVEEVKSPKEKSPEKAEEKPKSPTKKEKSPEKSAAEEVKSPTKKEKSPEKSAEEKPKSPTKKESSPVKMADDEVKSPTKKEKSPEKVEEKPASPTKKEKTPEKSAAEELKSPTKKEKSPSSPTKKTGDESKEKSPEKPEEKPKSPTPKKSPPGSPKKKKSKSPEAEKPPAPKLTRDLKLQTVNKTDLAHFEVVVEHATECKWFLDGKEITTAQGVTVSKDDQFEFRCSIDTTMFGSGTVSVVASNAAGSVETKTELKVLETPKETKKPEFTDKLRDMEVTKGDTVQMDVIALHSPLYKWYQNGNLLEDGKNGVTIKNEENKSSLIIPNAQDSGKITVEASNEVGSSESSAQLTVNPPSTTPIVVDGPKSVTIKETETAEFKATISGFPAPTVKWTINEKIVEESRTITTIKTEDVYTLKISNAKIEQTGTVKVTAQNSAGQDSKQADLKVEPNVKAPKFKSQLTDKVADEGEPLRWNLELDGPSPGTEVSWLLNGQPLTKSDTVQVVDHGDGTYHVTIAEAKPEMSGTLTAKAKNAAGECETSAKVTVNGGNKKPEFVQAPQNHETTLEESVKFSAIVTGKPMPNVTWYLNNKKLIQSEEVKVKYVHETGKTSIRIQKPLMEHNGTIRVEAENVSGKVQATAQLKVDKKTEVPKFTTNMDDRQVKEGEDVKFTANVEGYPEPSVAWTLNGEPVSKHPNITVTDKDGEHTIEISAVTPEQAGELSCEATNPVGSKKRDVQLAVKKVGDAPTFAKNLEDRLITEGELTLMDAKLNIVKPKPKITWLKDGVEITSDGHYKIVEEEDGSLKLSILQTKLEDKGRITIKAESEFGVAECSASLGVVKGRPMAKPAFQSDIAPINLTEGDTLECKLLITGDPTPFVKWYIGTQLVCATEDTEISNANGVYTMKIHGVTADMTGKIKCVAYNKAGEVSTEGPLKVVAPIPVEFETSLCDATCREGDTLKLRAVLLGEPEPVVSWYVNGKKLEESQNIKIHSEKGTYTVTIKDITCDYSGQVVCEAINEYGKATSEATLLVLPRGEPPDFLEWLSNVRARTGTKVVHKVVFTGDPKPSLTWYINNKEILNSDLYTIVTDDKTSTLTINSFNPDVHVGEIICKAENDAGEVSCTANMITYTSDMFSESESEAQAEEFVGDDLTEDESLREEMHRTPTPVMAPKFITKIKDTKAKKGHSAVFECVVPDTKGVCCKWLKDGKEIELIARIRVQTRTGPEGHITQELVLDNVTPEDAGKYTCIVENTAGKDTCEATLTVIESLEKKSEKKAPEFIVALQDKTTKTSEKVVLECKVIGEPKPKVSWLHDNKTITQESITVESVEGVERVTITSSELSHQGKYTCIAENTEGTSKTEAFLTVQGEAPVFTKELQNKELSIGEKLVLSCSVKGSPQPHVDFYSFSETTKVETKITSSSRIAIEHDQTNTHWRMVISQITKEDIVSYKAIATNSIGTATSTSKITTKVEAPVFEQGLKKTSVKEKEEIKMEVKVGGSAPDVEWFKDDKPVSEDGNHEMKKNPETGVFTLVVKQAATTDAGKYTAKASNPAGTAESSAEAEVTQSLEKPTFVRELVTTEVKINETATLSVTVKGVPDPSVEWLKDGQPVQTDSSHVIAKVEGSGSYSITIKDARLEDSGKYACRATNPAGEAKTEANFAVVKNLVPPEFVEKLSPLEVKEKESTTLSVKVVGTPEPSVEWFKDDTPISIDNVHVIQKQTAVGSFSLTINDARQGDVGIYSCRARNEAGEALTTANFGIIRDSIPPEFTQKLRPLEVREQETLDLKVTVIGTPVPNVEWFKDDKPINIDNSHIFAKDEGSGHHTLTIKQARGEDVGVYTCKATNEAGEAKTTANMAVQEEIEAPLFVQGLKPYEVEQGKPAELVVRVEGKPEPEVKWFKDGVPIAIDNQHVIEKKGENGSHTLVIKDTNNADFGKYTCQATNKAGKDETVGELKIPKYSFEKQTAEEVKPLFIEPLKETFAVEGDTVVLECKVNKESHPQIKFFKNDQPVEIGQHMQLEVLEDGNIKLTIQNAKKEDVGAYRCEAVNVAGKANTNADLKIQFAAKVEEHVTDESGQLEEIGQFETVGDTASSKTDTGRGAPEFVELLRSCTVTEKQQAILKCKVKGEPRPKIKWTKEGKEVEMSARVRAEHKDDGTLTLTFDNVTQADAGEYRCEAENEYGSAWTEGPIIVTLEGAPKIDGEAPDFLQPVKPAVVTVGETAVLEGKISGKPKPSVKWYKNGEELKPSDRVKIENLDDGTQRLTVTNAKLDDMDEYRCEASNEFGDVWSDVTLTVKEPAQVAPGFFKELSAIQVKETETAKFECKVSGTKPDVKWFKDGTPLKEDKRVHFESTDDGTQRLVIEDSKTDDQGNYRIEVSNDAGVANSKVPLTVVPSETLKIKKGLTDVNVTQGTKILLSVEVEGKPKTVKWYKGTETVTSSQTTKIVQVTESEYKLEIESAEMSDTGAYRVVLSTDSFSVESSATVTVTKAAEKISLPSFKKGLADQSVPKGTPLVLEVEIEGKPKDVKWYKNGDEIKDGKVEDLGNGKYRLTIPDFQEKDVGEYSVTAANEAGEIESKAKVNVSAKPEIVSGLVPTTVKQGETATFNVKVKGPVKGVKWYKNGKEIPDAKTKDNGDGSYSLEIPNAQVEDAADYKVVVSNDAGDADSSAALTVKLADDGKDKVKPEIVSGLIPTTVKQGETATFNVKVKGPVKQVKWYKNGKEIPNAKAKDNGDGSYSLEIPNAQLDDTADYKVVVSNDAGDADSSAALTVKLPGIAIVKGLEDAEVPKGKKAVLQVETNKKPKEIKWYKNGKEITPSDKAQPGSDGDNKPQLVIPDAGDDDAAEYKVVLTDEDGNTADSSCALTVKLPAKEPKIIKGLEDQVVSIGSPIKLEIETSGSPKTVKWYKNGKELPGAAAKTIKIQKIDDNKYVLEIPSSVVEDTGDYKVEVANEAGSANSSGKITVEPKITFLKPLKDQSITEGENAEFSVETNTKPRIVKWYKNGQEIKPNSRFIIEQKTDTKYQLVIKNAVRDDADTYKIVLENTAGEAESSAQLTVKKAKAGLCKIVKGLEDQVVAKGAKMVFEVKIQGEPEDVRWLRDANVISAGANAIIEKIDDTTYRLIIPSADLKDAGEYTVEVINESGKAKSDAKGEVDEKPEIVRGLENIEIPEGDDDVFKVEVSAPVRQVKWYKNDQEIKPNSHLEAKKIGPKKYELAINRAQLDDGADYKVVLSNAAGDCDSSAALTVVKPNVLKIVDGLKDVDVEEPQPVELKVKVEGIPKVIKWYKNGQELKPDADGFKFEEKPESGEFSLTIPSSKKSDGGAYRVVLGNDKGEVYSGSVVHVKSAKSSEPTSGANFLSPLKDTEVEEGDMLTLQCTIAGEPFPEVIWEKDGVVLQKDDRITMRVALDGTATLRIRSAKKSDIGQYRVTAKNEAGSATSDCKVTVTEQGEQPSKPKFVIPLKTGAALPGDKKEFNVKVRGLPKPTLQWFLNGIPIKFDDRITLDDMADGNYCLTIRDVREEDFGTLKCIAKNENGTDETVCEFQQGAGHDDGSRDDLRYPPRFNVPLWDRRIPVGDPMFIECHVDANPTAEVEWFKDGKKIEHTAHTEIRNTVDGACRIKIIPFEESDIGVYMCVAVNELGQAETQATYQVEILEHVEEEKRREYAPKINPPLEDKTVNGGQPIRLSCKVDAIPRASVVWYKDGLPLRADSRTSIQYEEDGTATLAINDSTEEDIGAYRCVATNAHGTINTSCSVNVKVPKQEVKKEGEEPFFTKGLVDLWADRGDSFTLKCAVTGDPFPEIKWYRNGQLLRNGPRTVIETSPDGSCSLTVNESTMSDEGIYRCEAENAHGKAKTQATAHVQMALGKTEKPKMDEGKPPKFILELSDMSVSLGNVIDLECKVTGLPNPSVKWSKDGGPLIEDSRFEWSNEASKGVYQLRIKNATVHDEGTYRCVATNENGSATTKSFVRMDDGLGSGVVTASQPPRFTLKMGDVRTTEGQPLKLECKVDASPLPEMVWYKDGAIVTPSDRIQISLSPDGVATLLIPSCVYDDDGIYRVIATNPSGTAQDKGTATVKKLPRDSGARRSADRDVFDANKAPKLMEPLENIRIPEKQSFRLRCKFSGDPKPTIKWFKDGERVFPYGRLQLIESPDGVCELVVDSATRQDAGGYRCVAENTYGSARTSCDVNVIRGDRKPRDIDSSIREGKAPGFTTPLTIRRAKPGDSVTFECLPFGNPFPSIKWLKDGLELFSDEKIKMEAAADGTQRLILSDVTFLSEGYFRCVATNEHGTASTKAELVIEGDRTIGSRPLPEVNGEPEECKPRIRRGLYNMSIHEGNVVEMIVCATGIPTPTVKWYKDGQEIVGDGPDGKRVIFTDERGIHHLVIVNASPDDEGEYSLEATNKLGSAKTEGSLNIIRPRHIADADERGGMPFPPGFVRQLKNKHVFNHMPTIFDCLVVGHPAPEVEWFHNGKKIVPGGRIKIQSCGGGSHALIILDTTLEDAGEYVATAKNSHGSASSSAVLDVTVPFLDSIKFNGEIDVTPYLTEEYGFKKLNTASLPTPPDRGPFIKEVTGHYLTLSWIPTKRAPPRYPQVTYVIEIRELPEKQWSLLEYNIPEPVCKVRNLELGKSYQFRVRAENIYGISDPSPASPPSRLMAPPQPVFDRRTNKVIPLLDPYAEKALDMRYSEQYACAPWFSPGVVEKRYCAENDTLTIVLNVSGFPDPDIKWKFRGWDIDTSSPTSKCKVYTYGGSETTLAITGFSKENVGQYQCFAKNDYGDAQQNIMVDLATRPNFIQPLVNKTFSSAQPMRMDVRVDGEPFPELKWMKEWRPIVESSRIKFVQDGPYLCSLIINDPMWRDSGIYSCVAVNDAGQATTSCTVTVEAEGDYNDVELPRRRVTIESRRVRELYEISEKDEKLAAEGAPFRVKEKATGREFLAQLRPIDDALMRHVDIHNSLDHPGIVQMHRVLRDEKLALVVFDNANSTIDGLSSLAHPGVEIAEPKGVNRETCVRVFVRQLLLALKHMHDLRIAHLDLRPETILLQDDKLKLADFGQARRLLRGLITGEIKGSPEFVSPEIVRSYPLTLATDMWSTGVLTYVLLTGLSPFHGDNDNETLANVDSCQFDSSPLGNFSYDAGDFVKKLLTEIPVSRLTVDEALDHPWINDEKLKTEPLSADTLREFKYQHKWLERRVFVQQTPSEQILEAILGPATAQAQQNAPVAPEGRRPAEIYDYLRIQPKKPPPTVEYVPQPRKEHPPFIDEFGQLIDGDAFDRPEGTGFEGPHRQPPQIPPQPQRPNQAAHDSRRHEQQPQHQGQPQRIPVDQYGRPLVDPRYLNDPSHRPSSLDDAPFYVDKYGNPVHFDKYGRPMAPQNLEKRKLIPQDKGETPSHSKKEKTQHPVATPILASPGGDQQQQKIPMRMIRGERREIEEEIANRILSDISEEGSIAGSLASLEDFEIPKDFQVEASEPSTPTLTPEVTIRETIPKPTPSPTSPQKSPVPQPQGLLIPAKVTYSDSILAGLPAADKKVLEDAENDPSIPVGAPLFLEGLHGSDLTIDTTSASGLIKVTSPAINLSPNPKSPRRSTPGTKSPVVLSPRQEHSMEVLIATKRGKPGFLPPGELAEDIDDEDAFMDDRKKQVKPKDHDGENDFKDEKERLEKDKNRRTVNLDDLDKYRPSAFYKDDSDFGHPGYDIDATPWDSHYQIGPDTYLMAARGAAFNSRVRNYREELFGMGAPTVKQGFLGVRNRDITVRERRRYTDILRETTQGLEPKSHEQSTALLQKAPSATAIERIKADIEKVTPCATKKNDDGTFAPIFTARLRDVYLRKNQPAIFECAVSASPAPKVTWDFQGKILESNDRVTIEQDNNVARLILNHAAPYDLGEYVCTAINEYGTDKSSCRLISGETPSRPGRPEAELSSDTEIFIQWEAPEGPTYLEGITYRLEYRVAGPNDHGDPWITVSEKIDDESVIVKHLSPLGIYQFRVTAQNGFGLGLPSLSSRIVQTHGKGAPKLQIDVLKSEIRLNVVSMPQKSTNQLGGISEESEEDSEARTANEDMKSNLQLQTDDPTGRFQIGGLKFKGRFSVIRDAVDSTTEGHAHCAVKIRHPSSEAISEYESLRDGQHENVQRLIAAFNNSNFLYLLSERLYEDVFSRFVFNDYYTEEQVALTMRQVTSALHFLHFKGIAHLDVNPHNIMFQSKRSWVVKLVDFGRAQKVSGAVKPVDFDTKWASPEFHIPETPVTVQSDMWGMGVVTFCLLAGFHPFTSEYDREEEIKENVINVKCDPNLIPVNASQECLSFATWALKKSPVRRMRTDEALSHKFLSSDPSMVRRRESIKYSASRLRKLAAMIRQPTFSQPISEELESKYGK | null | null | myosin filament assembly [GO:0031034]; nematode pharyngeal gland morphogenesis [GO:1905905]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion [GO:0040017]; positive regulation of protein localization to endoplasmic reticulum [GO:1905552]; positive regulation of sarcomere organization [GO:0060298]; positive regulation of striated muscle contraction [GO:0045989]; protein localization [GO:0008104]; regulation of skeletal muscle contraction by calcium ion signaling [GO:0014722]; sarcomere organization [GO:0045214]; skeletal muscle myosin thick filament assembly [GO:0030241]; striated muscle myosin thick filament assembly [GO:0071688] | A band [GO:0031672]; M band [GO:0031430] | ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; MATH domain binding [GO:0090736]; phosphatase binding [GO:0019902]; protein kinase activity [GO:0004672]; small GTPase binding [GO:0031267] | PF00041;PF07679;PF00069;PF05177;PF00621; | 1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:18337465, ECO:0000269|PubMed:19244614, ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:23283987, ECO:0000269|PubMed:27009202, ECO:0000269|PubMed:8603916}. Note=Colocalizes with scpl-1 (isoform b) to the M line (PubMed:19244614). Colocalizes with cpna-1 to the M line (PubMed:23283987). Colocalizes with mel-26 to the M line (PubMed:22621901). Accumulates at the center of thick myofilaments in M line-like structures in myoepithelial sheath cells (PubMed:17326220). {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:19244614, ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:23283987}. | null | null | null | null | null | FUNCTION: Structural component of the muscle M line which is involved in assembly and organization of sarcomere myofilaments (PubMed:15313609, PubMed:16453163, PubMed:18801371, PubMed:22621901, PubMed:23283987, PubMed:27009202). The large isoform a, isoform b, isoform d and isoform f play an essential role in maintaining the organization of sarcomeres but not myofilament alignment during body wall muscle development whereas the small isoform c and isoform d appear to have a minor role (PubMed:15313609, PubMed:16453163, PubMed:22768340). Isoform b and isoform f are required for the organization of unc-15/paramyosin into sarcomere thick filaments in body wall muscles (PubMed:27009202). By binding mel-26, a substrate adapter of the cul-3 E3 ubiquitin-protein ligase complex, regulates the organization of myosin thick filaments, likely by preventing the degradation of microtubule severing protein mei-1 (PubMed:22621901). Acts as a guanine nucleotide exchange factor (GEF) for Rho GTPase rho-1 but not ced-10, mig-2 and cdc-42 (PubMed:18801371). The large isoforms regulate Ca(2+) signaling during muscle contraction by ensuring the correct localization of sarco-endoplamic reticulum Ca(2+) ATPase sca-1 and ryanodine receptor unc-68 (PubMed:22768340). By controlling the contraction and/or organization of pharyngeal muscles, plays a role in the formation of pharyngeal gland cell extension (PubMed:21868609). {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:16453163, ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:21868609, ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:23283987, ECO:0000269|PubMed:27009202, ECO:0000269|PubMed:8603916}. | Caenorhabditis elegans |
O01767 | EGG4_CAEEL | MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRREDSGHGADIEMAKGHFNNVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDTKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMRLLSHDQTSTWISDIHPEAVKNETMAEYLLRELDASTMQKRVQAFKANVLADRDRVRVAGQFYNNIRIGKRMFGAARKAKYLSTIIGGMERRFEILENSVNHIPFTHSASDNNQEKCRNPRVHCKDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFRDVIGSAKELDVDYERWLQERSERMFLDDLAAPIPGYRLLSPRADPDIVRMVGRPERPNYRREAPDCVGEMPNKVATVDGILSPAKSVFEF | null | null | cortical actin cytoskeleton organization [GO:0030866]; dephosphorylation [GO:0016311]; eggshell formation [GO:0030703]; motor neuron axon guidance [GO:0008045]; oocyte maturation [GO:0001556]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of protein localization to cell cortex [GO:1904778] | cell cortex [GO:0005938]; nucleus [GO:0005634] | protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:19879147}. Note=Co-localizes with egg-3 to the cell cortex in developing oocytes and in newly fertilized embryos; cortical localization requires egg-3 and chitin synthase chs-1. At the beginning of meiosis anaphase I, egg-4 moves away from the cell cortex and is likely degraded. {ECO:0000269|PubMed:19879147}. | null | null | null | null | null | FUNCTION: Inactive phosphatase which acts redundantly with egg-5 in the oocyte-to-zygote transition (PubMed:19879147, PubMed:19879842). Required for the polarization of cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization (PubMed:19879147). Together with egg-5, required for the cortical localization of kinase mbk-2 and for the inhibition of mbk-2 kinase activity in maturing oocyte until the end of meiosis I (PubMed:19879842). Also required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after fertilization (PubMed:19879147). {ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842}. | Caenorhabditis elegans |
O01775 | NEKL2_CAEEL | MDNYEKVRVVGRGAFGVCWLCRGKNDASHQKVIIKLINTHGMTEKEENSIQSEVNLLKKVQHPLIIGYIDSFIMDNQLGIVMQYAEGGTLERLINDQRAIKDSNMREYFPEKTVLDYFTQILIALNHMHQKNIVHRDLKPQNILMNRRKTVLKLSDFGISKELGTKSAASTVIGTPNYLSPEICESRPYNQKSDMWSLGCVLYELLQLERAFDGENLPAIVMKITRSKQNPLGDHVSNDVKMLVENLLKTHTDKRPDVSQLLSDPLVLPYLISIHCDLGRIEPPPTDKRKPSASLSSRLRTYPTQSTLRPYSLSSNAPTTHLTQLTPMPSHIDSGFFSSGRTSNQRTQSRSQVHSKY | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9HC98}; | molting cycle [GO:0042303]; phosphorylation [GO:0016310]; positive regulation of endocytosis [GO:0045807] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25523392}. Note=In hyp7 syncytium, localizes in puncta and small tubules near the plasma membrane apical region. Does not co-localize with nekl-3. {ECO:0000269|PubMed:25523392}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9HC98}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9HC98}; | null | null | null | null | FUNCTION: Probable serine/threonine-protein kinase required for the completion of molting. May play a role in endocytosis in the hypodermis syncytium. {ECO:0000269|PubMed:25523392}. | Caenorhabditis elegans |
O01789 | SMC1_CAEEL | MRGGSSLDSFPGKGTLHTLEIENFKSYKGKHTIGPFTRFTAIIGPNGSGKSNLMDAISFVLGEKPSSLRVRKYADLIHGAPINKPVAKKCRVTMNYKYSDGKVKAFTRGVNNGTSEHLLDGQTVTSAAYSQEMESINIFIKARNFLVYQGAIENIAMKTPKERTQLFEELSRSHEFQAEYERLKVEMTKAEDDTQHNMNKRRGIAQEKREAKMEKDEAEKYQTMKNELAAKSTMLFLHQLFHCERTIDESKEEINAQKKTIASLEATRSKEEAKIAAVHQEHRKALREVQKMTRKLDQKETDLAEKQQNMLTLKVSVAHEHKKLEIAKKMLAAAESKAENNSTQLADLKKSKKELEKKKAAYEAEIQDMMQRGELNLSDEQVREYGQLKDQAQRESAMVQRELLMAEQVFEGDKSSLNHELRRQKEHQERVKAKEGDVRRIETQIATLAQRIKETEEETKILKADLKKIENDVVIDKSAAAEYNKELVAVVRQLSEASGDSAEGERNQRRTEALEGLKKNFPESVYGRLVDLCQPSHKRFNIATTKILQKHMNSIVCDTEETAAKAIVYLKDHRYPPETFLPNDALVVNPLNEKLREIKKPAGVKLVFDVINPQHQAARKALQFVCGNALVCESQEDAKQLAYGGGELKDRFKAVSMDGTLFQQSGVMSGGSADLRQKSKKWDEKVVKQLREKRNQLNEKIADLQKHRRRELEVESVRSKINGNEQRLAMMKRDLKNMREMQLERLQNELEGMTAEMNMLPPRISNCQEKLERSESTLKSLQTKSNEVADRIFADFCTRVGIASIRDYENREMRIKQEMEDKLRSFDDDIQKLAYEIDFVTEQDGNRKVEVEKEKVSQIDRQYKDMKKKEKTAAAALKEHTESMEQDKEVLEEKKALSHKLETEWNEVKKIAQVAMKDFTKAEKELLRLESLLTKKQYERHSLLHSVKLGQIALPLKSGSMADVEYEEDDGDDTASQSSQSATDGPSVSEEQIQREQHIKINYDSLPREYKDVDDDDGVRQMSNRLNVEIDELQKNVSKMNAPNLKANQRMAEVKEREAESTEELENARKKAKRIRQQFEKVKTDRYRRFQDFFDPVANTIDDIYKQLSRNTSAQAFLGADNMEEPYLDGIQYNCVAPGKRFRPMDNLSGGEKTIAALALLFAVHGRNPAPFFVLDEIDAALDNTNIGKVASYICESAREHMQIIVISLKEEFYNKADSLIGIFPYPAACTTSGVLTFDLTRFKQIGLNEMTENPPTPSIAT | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; DNA repair [GO:0006281]; embryo development ending in birth or egg hatching [GO:0009792]; establishment of mitotic sister chromatid cohesion [GO:0034087]; mitotic sister chromatid cohesion [GO:0007064]; response to UV [GO:0009411]; response to X-ray [GO:0010165]; sister chromatid cohesion [GO:0007062] | chromatin [GO:0000785]; cohesin complex [GO:0008278]; meiotic cohesin complex [GO:0030893]; MIS12/MIND type complex [GO:0000444]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Chromosome {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues (PubMed:12827206). Colocalizes with rec-8 along synapsed chromosomes during meiotic pachytene and diakinesis (PubMed:12827206). Diffuse nuclear accumulation in meiotic pachytene (PubMed:21856158). {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair (By similarity). Required for chromosome segregation during mitosis (PubMed:12808038, PubMed:12827206). Central component of cohesin complex (PubMed:12827206). The cohesin complex is required for the cohesion of sister chromatids after DNA replication (PubMed:12827206). The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity). {ECO:0000250|UniProtKB:Q14683, ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}. | Caenorhabditis elegans |
O01798 | SPE8_CAEEL | MRSKSSEGDLQPEDTQSREDKETTATYSEDTKPETQKERNAALDNLAKTPIQLVVQPTPLTPAITPCEAPPPPPPPKPSSDNNNSKRLKVKDQLIEVPSDEVGRVENNIDNFPFYHGFMGRNECEAMLSNHGDFLIRMTEIGKRVAYVISIKWKYQNIHVLVKRTKTKKLYWTKKYAFKSICELIAYHKRNHKPIYEGMTLICGLARHGWQLNNEQVTLNKKLGEGQFGEVHKGSLKTSVFAAPVTVAVKTLHQNHLSANEKILFLREANVMLTLSHPNVIKFYGVCTMKEPIMIVMEFCDGKSLEDALLSKEEKVSAEDKILYLFHAACGIDYLHGKQVIHRDIAARNCLLNSKKILKISDFGLSVKGVAIKERKGGCLPVKYMAPETLKKGLYSTASDIYSYGALMYEVYTDGKTPFETCGLRGNELRKAIIGKRISLAVEVELPVFIANIFEQSRQYETEDRISSKQIIQIFKEEVGFHEIETSGILHKLVNSLPRIHNKERKPAAVAV | 2.7.10.2 | null | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; spermatid development [GO:0007286]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017; | 3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25022984}; Peripheral membrane protein {ECO:0000269|PubMed:25022984}. Cytoplasm {ECO:0000269|PubMed:25022984}. Note=Localizes mainly in the cytoplasm of stage I spermatocytes and at the cell membrane of stage II spermatocytes and spermatids. {ECO:0000269|PubMed:25022984}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; | null | null | null | null | FUNCTION: Probable non-receptor tyrosine-protein kinase which plays a role in spermatid activation (spermiogenesis) in hermaphrodites. {ECO:0000269|PubMed:25022984, ECO:0000269|PubMed:3197956}. | Caenorhabditis elegans |
O01803 | RB11A_CAEEL | MGSRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSISVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHVTYENVERWLKELRDHADQNIVIMLVGNKSDLRHLRAVPTDEAKIYAERNQLSFIETSALDSTNVEAAFTNILTEIYKSVSNKHVGTDRQGYGGGSGTIIPSPASDPPKKQCCIP | null | null | cortical granule exocytosis [GO:0060471]; eggshell formation [GO:0030703]; embryo development ending in birth or egg hatching [GO:0009792]; exocytosis [GO:0006887]; membrane addition at site of mitotic cytokinesis [GO:0061796]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898] | apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; cortical granule [GO:0060473]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi trans cisterna membrane [GO:1990676]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; spindle [GO:0005819]; transport vesicle [GO:0030133] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:22992455}. Endosome {ECO:0000269|PubMed:19158384}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:19158384}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:18385514}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:19158384}. Apical cell membrane {ECO:0000269|PubMed:24843160}. Cytoplasm, cytosol {ECO:0000269|PubMed:24843160}. Recycling endosome membrane {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18472420, ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:22634595, ECO:0000269|PubMed:26506309}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:26506309}. Cytoplasmic granule {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:26506309}. Note=Expressed in endosomal vesicles which localize to the pericentriolar region of embryos during prophase and metaphase (PubMed:19158384). Localizes along the spindle in embryos during anaphase (PubMed:19158384). Transiently accumulates on secretory vesicles before their exocytosis (PubMed:18765566). Localizes to recycling endosomes and Golgi apparatus membrane in growing oocytes (PubMed:18765566, PubMed:26506309). Translocates to cytoplasmic granules and extracellular matrix components in mature oocytes (PubMed:26506309). Accumulates on ring-shaped structures in ovulating oocytes and in early one-cell stage embryos (PubMed:18765566). Redistributes to recycling endosomes and Golgi apparatus in embryos (PubMed:26506309). Co-localizes with rei-1 at Golgi apparatus membrane in embryos (PubMed:26506309). Reycling endosomes co-localize with the endoplasmic reticulum in embryos (PubMed:18385514). Co-localizes with rab-6.1-positive vesicles near the plasma membrane until vesicle exocytosis in embryos (PubMed:22992455). Localizes to the cytosol during the meront-stage of N.parisii infection and around the resulting spores that are to be shed from intestinal cells (PubMed:24843160). {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:19158384, ECO:0000269|PubMed:22992455, ECO:0000269|PubMed:24843160, ECO:0000269|PubMed:26506309}. | null | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21320697, PubMed:24843160). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21320697, PubMed:24843160). Involved in regulating the meiotic maturation of oocytes (PubMed:18472420). Plays a role in egg shell formation, regulating exocytosis of chondroitin proteoglycans following fertilization (PubMed:18765566, PubMed:26506309). Controls cortical granule localization and targets them to the plasma membrane for exocytosis (PubMed:18765566, PubMed:22992455). Acts as a major regulator of membrane delivery during cytokinesis (PubMed:18765566, PubMed:20116245, PubMed:26506309). Regulates the cytoskeleton by facilitating astral microtubule elongation and organization during metaphase to ensure proper spindle alignment and polarity in the first embryonic cell division (PubMed:18385514). Maintains normal endoplasmic reticulum morphology during metaphase (PubMed:18385514). Involved in vesicle formation and plasma membrane repair following exposure to pore forming toxins (PubMed:21320697). Regulates endocytic recycling (PubMed:24843160). May play a role in yolk receptor endocytosis in growing oocytes (PubMed:18354496, PubMed:26506309). Plays a role in the shedding of pathogen spores from intestinal cells via its involvement in spore fusion and endocytic trafficking (PubMed:24843160). {ECO:0000269|PubMed:18354496, ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18472420, ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21320697, ECO:0000269|PubMed:22992455, ECO:0000269|PubMed:24843160, ECO:0000269|PubMed:26506309}. | Caenorhabditis elegans |
O01811 | MEC6_CAEEL | MGLQSAAAHFINRFIIWITIFMVACFLLRLLVVLDLNKRVYNHTPGPCRVLTDNYKGTAGMTYVESQKRVYITLGYGRAHDLKTKTGIAFYKTNRTDGRSQQEMYDLIEMTINWNGYEYKKEFIPTGIDSYSSSNGRVLLYVINAHPNHQCIHFFQIVESSKLNHRKAICDPSFSSLQDIAVVGPDRLFVTNMAAFGRGWAQILEFSLQTGQGAVYYYDGSKLSTAASSLIAPTGIGYDAKRRILYVGSMIRESIFAYKVAKDTTLELLYEMMLLTSPIGVFVESKTGDIWIAAHPVIHESAWHYTHPENQNIHSPSQILRIRIQEEGNSWVTTEPYANDGATISASSSVVFTDEQMLIGSSFGRLLHCDLTHSYIT | null | null | detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; mechanosensory behavior [GO:0007638]; positive regulation of detection of mechanical stimulus involved in sensory perception of touch [GO:1905789]; positive regulation of mechanosensory behavior [GO:1905792]; potassium ion transport [GO:0006813]; response to mechanical stimulus [GO:0009612] | axon [GO:0030424]; plasma membrane [GO:0005886] | arylesterase activity [GO:0004064]; sodium channel activity [GO:0005272] | PF01731; | 2.120.10.30; | Paraoxonase family | PTM: Glycosylated. {ECO:0000269|PubMed:12478294}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12478294}; Single-pass membrane protein {ECO:0000269|PubMed:12478294}. Cell projection, axon {ECO:0000269|PubMed:12478294}. Note=Co-localizes with mec-4 in puncta along the axons of touch cell receptor neurons and in muscles. {ECO:0000269|PubMed:12478294}. | null | null | null | null | null | FUNCTION: Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity) (PubMed:12478294). Interacts with degenerin channel proteins and stabilizes the channel (PubMed:12478294). Plays a role in mechanosensory transduction (touch sensitivity) (PubMed:12385749, PubMed:12478294). {ECO:0000269|PubMed:12385749, ECO:0000269|PubMed:12478294}. | Caenorhabditis elegans |
O01822 | BL1S6_CAEEL | MSNTEHNVESKNVTDTLDEILRLQEDIQARIGSSNHNLETNFESIKDFVSRAHAYIPILNQISKDMIEICERTQALKKKTSQLELSDTNIEDGSTTSTPTTTNKSQ | null | null | endosomal transport [GO:0016197]; positive regulation of gut granule assembly [GO:1904757]; positive regulation of intracellular protein transport [GO:0090316] | BLOC complex [GO:0031082]; BLOC-1 complex [GO:0031083]; cytoplasm [GO:0005737]; endosome [GO:0005768] | protein homodimerization activity [GO:0042803] | null | null | BLOC1S6 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22916203}. Endosome {ECO:0000269|PubMed:22916203}. | null | null | null | null | null | FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis. {ECO:0000269|PubMed:22916203}. | Caenorhabditis elegans |
O01836 | GLH3_CAEEL | MDKSPTKTSIRTKFARHQPISDVDTTEQSSSCIKKDDRGLSSFGVQSSVFSRRSCRMSELEAKPTIISEDQRIAVRSEIGGSFSGFDDKVDNVFHSNNNLHGSPSTTELECPGIMNPRFLVGRSLNSRSRAVTRGSKRTSNVKENEGSIHRSDDQVSTENCSAKDEERDRDSGGVSSYGNKRSDEFCGTSPILEAKGFGISNTCFNCKKYGHRATECSAPQRECANCGDPNHRANECASWSKNGVQEPTKVTYVPVVDKMEEVFSMLKINAGDFFDKFFDASVQLVSRGQPVTIQPCKSFSDSDIPQSMRRNVERAGYTRTTPIQQYTLPLVADGKDILACAQTGSGKTAAFLLPIMSRLILEKDLNYGAEGGCYPRCIILTPTRELADQIYNEGRKFSYQSVMEIKPVYGGINVGYNKSQIMKGCTIIVGTIGRVKHFCEDGAIKLDKCRYLVLDEADRMIDSMGFGPEIEQIINYKNMPKNDKRQTMMFSATFPSSVQEAARKLLREDYTMITIDKIGAANKCVIQEFELCDRTSKVDKLLKLLGIDIDTYTTEKNSDVFVKKTIVFVAQQKMADTLASIMSAAQVPAITIHGAREQKERSAALKLFRSGAKPVLIATAVVERGLDIKGVDHVINYDMPNNIDDYIHRIGRTGRVGNSGRATSFISLADDVQILPQLVRTLADAEQVVPSWMKEAAGGTSNPNKFEKSIDTEEPEEAW | 3.6.4.13 | null | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; germ cell development [GO:0007281] | nucleus [GO:0005634]; P granule [GO:0043186] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DEAD/H-box RNA helicase binding [GO:0017151]; JUN kinase binding [GO:0008432]; mRNA binding [GO:0003729]; protein self-association [GO:0043621]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270] | PF00270;PF00271;PF00098; | 3.40.50.300;4.10.60.10; | DEAD box helicase family, DDX4/VASA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21402787}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Probable ATP-binding RNA helicase. | Caenorhabditis elegans |
O01839 | VPS51_CAEEL | MSSVLDVTKPDFDVEAFVVKLLREKSLDGLVKEEEEMVSAVRRLDSDVHQIVYENYNKFLTATNTVRKIQDEFTQLDSEMKSLSRSMSTISTLIGNLDGVLGEKRDDILQLGSSYKVVNSLKHIFDLPHVLRSEFDERNYGEVLRMFKLAEESLSQYKDVPTVQLVLQKSKKIYDMTENQLMDQLRNPASGAELVSEAVDLLLTIGRDEDEVQKVLLTCSEQSLRVDLKELSANHSDVLDLVDKASESFIPNLTLIATTHDRLFEDKREDLITVLKTEMNSLHALVSKVFLSSSDAKDCSIVVRALDRYFRKISTCRYVIPGLDFLPLTIELINAVSKHEIDLSLTRIKEELKNGLNEVRKALINEEKDLSALASKIEQVFVHQVKTALANLLLFTASDVTFANLPPDEFRQSFSFNAHERLLVQAFHRFSELADEYESGAGEIRFVDPRVHLVFAVALQHLSNKSAVYLLNLCREQFSLSPDDGLTDITVVMSEVKTRAQKLVRCYAEKTGLSMGETLIKGCAMLVQPAATPSAVRASVRRLVEEMNTCDSELTLLLGGDSKPKDSRVSRRPITTALDAARDSLWCERIDFHLQIHFNRASIITVIVKVVLKIFIESIRLQTYSKFGVEQVQVDCYYLQRCLAALVSDEVVVNSMVDQALSSALKRCQDPVLVHPSRLAQLCEQPPANRPSSQASSLGY | null | null | endocytic recycling [GO:0032456]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; lysosomal transport [GO:0007041]; negative regulation of dense core granule transport [GO:1904810]; positive regulation of dense core granule transport [GO:1904811]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; retrograde transport, endosome to Golgi [GO:0042147] | cytosol [GO:0005829]; EARP complex [GO:1990745]; GARP complex [GO:0000938]; membrane [GO:0016020] | syntaxin binding [GO:0019905] | PF08700; | null | VPS51 family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. | null | null | null | null | null | FUNCTION: Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}. | Caenorhabditis elegans |
O01887 | TRYL5_CAEEL | MRPRIIVFLFQVLVVIKGTKLKYYNDELCGRQSTYTSFMLTDAAGNTGNPTHLAPWAVQIRVKARKGDFEVICGGTLITLKHVLTAAHCFQKHFGAKKEGGEENSMSGRYCESNQRFTDSEILTRTVVTVGAMCTRLEQKYGCVNEKQNGKTLKISRFAIGDFYKTHCEQGNDIVILELESTIDDVEGANYACLPFLPEVNIQSGANVTSFGWGSDPGKGFDNAAFPMIQVLTLATETLATCEENWGTSIPFDSFCTAEEEDKNVCSGDSGGGLTFHQSDSAREFIIAIVSYGSDCVQLIGGSEPRSQINTDVRKHQKFIVNFINQA | 3.4.21.- | null | proteolysis [GO:0006508]; spermatid development [GO:0007286] | extracellular space [GO:0005615]; secretory vesicle [GO:0099503] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}. Note=In males, partially colocalizes with swm-1 in vesicles near the apical membrane of cuboidal cells (PubMed:22125495, PubMed:30470702). During the spicule insertion stage of mating, secreted by the male vas deferens and transferred together with sperm into hermaphrodites where it spreads into the uterus (PubMed:22125495). {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}. | null | null | null | null | null | FUNCTION: Serine protease which, in males, acts as a promoting signal during mating to activate sperm. {ECO:0000269|PubMed:22125495}. | Caenorhabditis elegans |
O01901 | WASC3_CAEEL | MNASSRTKPAIDLNKVPPIDHHRTAVTFNCLIMKMTEMLNNFGNKMEDILEKAEQSLDTADRKLRLMESKLAGMSLEDKSTTATPSSAPEIDEIHESNPSSSQIVEETVEEKPEEHTTTVLIKDDPAYSKYFKMLKLGVLEAGVIQKMKSEGVDPSILKRGDEPSRPQAQTSRNYESSGESTASFSDSD | null | null | actin filament polymerization [GO:0030041]; cytoplasmic sequestering of protein [GO:0051220]; determination of adult lifespan [GO:0008340]; exocytosis [GO:0006887]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; WASH complex [GO:0071203] | null | PF10152; | null | CCDC53 family | PTM: Phosphorylated (PubMed:22265419). Phosphorylation on Thr-182 may promote DHIC complex dissociation and consequently the activation of heat-shock transcription factor hsf-1 (PubMed:22265419). Phosphorylation is modulated by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419). {ECO:0000269|PubMed:22265419}. | null | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat-shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity (PubMed:22265419). {ECO:0000250|UniProtKB:Q9Y3C0, ECO:0000269|PubMed:22265419}. | Caenorhabditis elegans |
O01925 | MBOA5_CAEEL | MGVVGALSEVTSASEDALRLLISVLAGYPLAVVHRTFFYNKPAQHQHLFFVIVGLSLWMFNCGSSVIHPILSIFGAFFITNFMAGTDASIYAAHIVFLGHLLIGYWFHETDTYDITWTTPFCIMTLRFIGLVMDVYDGAQKPEHLKPDQKLTAISDKPGLLEIAAFGLFFQGTLVGPQFTLSKFRSFVNGDWLDSDGQPPKSAFLPSIGRFLAGCTYMVLHQWGQFWIPDQYFNSDAYNNLSFFWRWSWVTLWFRLTMYKYCAMWLITEGASILSGLGHNGKDAEGNDRWDGVRDLHIIKWETGHDYNSVVESFNCGTNTFAKNHIHRRLRWVNNKLASHVITLSYLAIWHGYHLGYFLLFGVELGCVQAQNQLYALIKRTPGWSEAISKPISRPFIWIFGKLTISYSMGFAFLMFGLIKTKYWIGPVKSLYFIGFIIYFIVWPILHMVLLRVLPRHPKKAAAEKPEEVKKEL | 2.3.1.-; 2.3.1.23; 2.3.1.n6; 2.3.1.n7 | null | lipid modification [GO:0030258]; nematode larval development [GO:0002119]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylserine biosynthetic process [GO:0006659]; positive regulation of growth rate [GO:0040010]; post-embryonic body morphogenesis [GO:0040032] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-acylglycerophosphoethanolamine O-acyltransferase activity [GO:0106262]; 1-acylglycerophosphoserine O-acyltransferase activity [GO:0106263]; lysophospholipid acyltransferase activity [GO:0071617]; O-acyltransferase activity [GO:0008374] | PF03062; | null | Membrane-bound acyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000269|PubMed:18782225}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191, ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64379; EC=2.3.1.n6; Evidence={ECO:0000269|PubMed:18782225}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7; Evidence={ECO:0000269|PubMed:18782225}; | null | PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:18782225}. | null | null | FUNCTION: Probable acyltransferase which may mediate the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). May also catalyze the conversion of lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), as well as the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Required for incorporation of arachidonic acid into PC, PE, and PS. {ECO:0000269|PubMed:18782225}. | Caenorhabditis elegans |
O01965 | ARI11_CAEEL | MSSDDEINMDDSDSSQGEIDDGCMSDDDGIVLESREQNSSDYKDNGEPDNEVLNHDSLEAEMKKTITDVQAVLQVKTGVCRILLHKYKWNKESLLERFYEHPDTTTFLIDAHVIPRRQERLPAGDAECDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNCKLLIEDEKVMFYITDPTVIATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNCRLLKLWLKKCNDDSETSNWINANTKECPKCMITIEKDGGCNHMTCKNTACRFEFCWMCLGPWEPHGSSWYSCNRFDDSAAKNARDAQEVSRANLQRYLFYYNRYMGHQQSLRLEGKLYATVKSKMEQMQTLSMSWIEVQFLRKAVDVLSECRRTLMFTYAFAFYLKRDNNAIIFESNQKDLEMETEQLSGFLERDLDNENLVTLKQKVQDKYRYVEHRRKVLLDHCSEGADQELWVFNE | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF21235;PF19422;PF01485; | 1.20.120.1750;3.30.40.10; | RBR family, Ariadne subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16457801}. Cytoplasm {ECO:0000269|PubMed:16457801}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5}; | null | null | null | null | FUNCTION: E3 ubiquitin-protein transferase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ubc-18 (By similarity). Acts with ubc-18 to regulate pharyngeal development (PubMed:16457801, PubMed:19521497). {ECO:0000250|UniProtKB:Q9Y4X5, ECO:0000269|PubMed:16457801, ECO:0000269|PubMed:19521497}. | Caenorhabditis elegans |
O01971 | EMR1_CAEEL | MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVSAATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAETNPEDTI | null | null | chromosome segregation [GO:0007059]; mitotic cytokinesis [GO:0000281]; nuclear envelope organization [GO:0006998]; response to X-ray [GO:0010165] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | lamin binding [GO:0005521] | PF03020; | 1.10.720.40; | null | null | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Single-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}. Nucleus envelope {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391}. Note=Lmn-1 and mel-28 are required for its localization to the nuclear envelope (PubMed:11870211, PubMed:16950114). Remains in the nuclear envelope until mid-late anaphase (PubMed:10982402). Recruited to the reforming nuclear envelope from telophase and throughout interphase (PubMed:25653391). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391}. | null | null | null | null | null | FUNCTION: Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:11870211, PubMed:12684533, PubMed:22171324). Involved in chromosome segregation and cell division, probably via its interaction with the nuclear intermediate filament protein lmn-1, the main component of nuclear lamina (PubMed:11870211, PubMed:12684533). Required to organize the distribution of lmn-1, nuclear pore complexes (NPCs) and chromatin in mitotically active cells (PubMed:22171324). Together with lem-2, plays a role in baf-1 enrichment at the nuclear envelope in anaphase (PubMed:12684533). Together with lem-2, involved in muscle cell attachment to hypodermal cells, as well as muscle cell location and sarcomere organization (PubMed:22171324). May play a role in radiation-induced DNA damage repair response (PubMed:22383942). May repress binding of transcription factor pha-4 with target sequences in pharyngeal cells. {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:20714352, ECO:0000269|PubMed:22171324, ECO:0000269|PubMed:22383942}. | Caenorhabditis elegans |
O01991 | EF2K_CAEEL | MTIDTTNESDNSPTNSPGLEASARTFSLNASKMVRITDDYADEVFIEQNDVVIEKPRMDPLHVRKLMETWRKAARRARTNYIDPWDEFNIHEYPVQRAKRYRYSAIRKQWTEDIVDVRLHPDSFARGAMRECYRLKKCSKHGTSQDWSSNYVAKRYICQVDRRVLFDDVRLQMDAKLWAEEYNRYNPPKKIDIVQMCVIEMIDVKGSPLYHLEHFIEGKYIKYNSNSGFVSNAARLTPQAFSHFTFERSGHQMMVVDIQGVGDLYTDPQIHTVVGTDYGDGNLGTRGMALFFHSHRCNDICETMDLSNFELSPPEIEATEVAMEVAAKQKKSCIVPPTVFEARRNRISSECVHVEHGISMDQLRKRKTLNQSSTDLSAKSHNEDCVCPECIPVVEQLCEPCSEDEEDEEEDYPRSEKSGNSQKSRRSRMSISTRSSGDESASRPRKCGFVDLNSLRQRHDSFRSSVGTYSMNSSRQTRDTEKDEFWKVLRKQSVPANILSLQLQQMAANLENDEDVPQVTGHQFSVLGQIHIDLSRYHELGRFVEVDSEHKEMLEGSENDARVPIKYDKQSAIFHLDIARKCGILEAVLTSAHIVLGLPHELLKEVTVDDLFPNGFGEQENGIRADKGQKPCDLEEFGSDLMEIAAEMGDKGAMLYMAHAYETGQHLGPNRRTDYKKSIDWYQRVVGFQEEEELDSDCGKTTFSSFAPLTRHEILAKMAEMYKEGGYGLNQDFERAYGLFNEAAEAAMEAMNGKLANKYYEKAEMCGE | 2.7.11.20 | null | myosin II filament disassembly [GO:0031037]; phosphorylation [GO:0016310]; response to differentiation-inducing factor 1 [GO:1903013] | actomyosin contractile ring [GO:0005826] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905] | PF02816; | 3.20.200.10;1.25.40.10; | Protein kinase superfamily, Alpha-type protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0000269|PubMed:9144159}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21437; Evidence={ECO:0000269|PubMed:9144159}; | null | null | null | null | FUNCTION: Phosphorylates elongation factor-2 (eEF-2) at two threonine residues that are conserved in all eukaryotes and are located within a GTP-binding domain (PubMed:9144159). Calcium(2+)/calmodulin dependent activity (PubMed:9144159). Inactivates eEF-2 by catalyzing its phosphorylation (PubMed:9144159). eEF-2 catalyzes the movement of the ribosome along mRNA during translation in eukaryotic cells (PubMed:9144159). {ECO:0000269|PubMed:9144159, ECO:0000303|PubMed:9144159}. | Caenorhabditis elegans |
O02002 | CASP1_DROME | MTDECVTRNYGVGIRSPNGSENRGSFIMADNTDAKGCTPESLVVGGATAASPLPANKFVARMPVERYASEYNMSHKHRGVALIFNHEFFDIPSLKSRTGTNVDAQELKKAFENLGFAVSVHKDCKLRDILKHVGKAAELDHTDNDCLAVAILSHGEHGYLYAKDTQYKLDNIWHYFTATFCPSLAGKPKLFFIQACQGDRLDGGITLEKGVTETDGESSTSYKIPIHADFLFSYSTIPGYFSWRNINNGSWYMQSLIRELNANGKKYDLLTLLTFVNQRVALDFESNVPATPMMDRQKQIPCLTSMLTRILRFGDKPNGNKAG | 3.4.22.- | null | apoptotic process [GO:0006915]; cellular response to starvation [GO:0009267]; execution phase of apoptosis [GO:0097194]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of Toll signaling pathway [GO:0045751]; neuron remodeling [GO:0016322]; nurse cell apoptotic process [GO:0045476]; oogenesis [GO:0048477]; ovarian nurse cell to oocyte transport [GO:0007300]; positive regulation of autophagy [GO:0010508]; positive regulation of macroautophagy [GO:0016239]; positive regulation of neuron apoptotic process [GO:0043525]; programmed cell death [GO:0012501]; programmed cell death involved in cell development [GO:0010623]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598] | BIR domain binding [GO:1990525]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200] | PF00656; | 3.40.50.1460; | Peptidase C14A family | null | null | null | null | null | null | null | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function causes larval lethality and melanotic tumors. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
O02100 | HOP1_CAEEL | MPRTKRVYSGKTITGVLYPVAICMLFVAINVKLSQPEQQEQSKVVYGLFHSYDTADSGTITLYLIGFLILTTSLGVFCYQMKFYKAIKVYVLANSIGILLVYSVFHFQRIAEAQSIPVSVPTFFFLILQFGGLGITCLHWKSHRRLHQFYLIMLAGLTAIFILNILPDWTVWMALTAISFWDIVAVLTPCGPLKMLVETANRRGDDKFPAILYNSSSYVNEVDSPDTTRSNSTPLTEFNNSSSSRLLESDSLLRPPVIPRQIREVREVEGTIRLGMGDFVFYSLMLGNTVQTCPLPTVVACFVSNLVGLTITLPIVTLSQTALPALPFPLAIAAIFYFSSHIALTPFTDLCTSQLILI | null | null | amyloid-beta formation [GO:0034205]; calcium ion transport [GO:0006816]; egg-laying behavior [GO:0018991]; embryo development ending in birth or egg hatching [GO:0009792]; gonad development [GO:0008406]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; nematode larval development [GO:0002119]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of Notch signaling pathway [GO:0045747]; protein processing [GO:0016485]; regulation of cell fate specification [GO:0042659]; regulation of vulval development [GO:0040028]; reproduction [GO:0000003] | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175] | PF01080; | 1.10.472.100; | Peptidase A22A family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function. {ECO:0000269|PubMed:10051671}. | Caenorhabditis elegans |
O02101 | SWIC2_CAEEL | MHSQQRPNPQMNRHPYGTPGSAPQMRRPGGFAGQPPQMHGPRMVAPPAAPLPKKKKYADKCIHPKIRELEPDAENYMALLASEQKLDSTLSRKKLDIQEALKRPSKVKKRLRIYISHTFIEEKQPEKDTDEASLPMWELRVEGRLLDEQPPAPAIPGQRPVPKRKFSSFFKSLVIELDKEMYGPDQHLVEWHRTPQTNETDGFQVKRAGDRPVKCRILLLLDNHPAKFKLHPRLAKVLGIATETRPKIIEALWQYIKTHGLQDPQERDIINCDTFLSQCFGVNRMRFMEVPNKLHQLLQQTDPLEFNHIIQRPKEGQEQVSTCYDIDVEMEDPVKQFMHTFVHSPGLANDIQTLDQKCYDIIEQINELKTRRDFYARFYTEPAEFIKSWVMSQNSDLKTMNELSGDLEAERFAESYVRPETEEGVQRYMFQKVNQKRHELEQSLGVRSN | null | null | chromatin remodeling [GO:0006338]; positive regulation of double-strand break repair [GO:2000781]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357] | condensed chromosome [GO:0000793]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514] | RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coregulator activity [GO:0003712] | PF02201; | 1.10.245.10; | SMARCD family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:26739451}. Chromosome {ECO:0000269|PubMed:26739451}. Nucleus envelope {ECO:0000269|PubMed:26739451}. Note=Localizes to mitotic chromosomes in the early embryo. {ECO:0000269|PubMed:26739451}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Probably regulates vulva development through the let-60/Ras pathway (PubMed:26739451). Involved in nuclear reassembly after mitosis and recruitment of nuclear envelope protein, mel-28, to the nuclear periphery in the early embryo and in the adult germline (PubMed:26739451). Involved in gonadogenesis (PubMed:24402584, PubMed:26739451). {ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:24402584, ECO:0000269|PubMed:26739451}. | Caenorhabditis elegans |
O02151 | NHR14_CAEEL | MDFLISTSLSESTSTSADFCVVCGDKAIGKHYGAVACNGCKGFFRRSVWQNLQYTCRFNKQCNIDKDHRNACRYCRFQKCLADGMKPEAIQNERDRIGSTKRRKRSGANSENNSDSEGTPSPKIEVMGNSVSRKLIEMLLDIEHRLASNQSMNALLRDESEMKNSRQRAVNYLIGWTNMLHPLPEVPLADKVLLLKKFSSAFTLLGTLQRSMALPHFVLPNDQVLSISASHPPELFEALTRIIDELLTPLRRLRTDHAEFSCLKALLLLNPDVVGISNNTRERIREARDALLKTLFAYMSNTQNSIDASLRVSSLLMIIPSLISVSSSIMEFPALSDLFGLGDVIKRDTISPKIETPPLEMKPMMPKIAQPPVTSAPTVPTNIMMNKDLISQIMNNPQLFPLLPMPQTASPPMSFMGQSEFGCHLQSMPVKVILS | null | null | cell differentiation [GO:0030154]; defense response to Gram-negative bacterium [GO:0050829]; negative regulation of protein localization to nucleus [GO:1900181]; regulation of innate immune response [GO:0045088]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Orphan nuclear receptor (PubMed:10022975). Transcriptional repressor of intestinal metal transporter smf-3 and genes of the innate immune response (PubMed:31532389). Inhibits nuclear localization of transcription factor pqm-1; in response to pathogen stress, may facilitate translocation of pqm-1, leading to transcriptional activation of genes involved in innate immunity and iron uptake (PubMed:31532389). {ECO:0000269|PubMed:10022975, ECO:0000269|PubMed:31532389}. | Caenorhabditis elegans |
O02193 | MOF_DROME | MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLSANVEAISDDSSETSSSDDDEEEEEDEDDALTMEHDNTSRETVITTGDPLMQKIDISENPDKIYFIRREDGTVHRGQVLQSRTTENAAAPDEYYVHYVGLNRRLDGWVGRHRISDNADDLGGITVLPAPPLAPDQPSTSREMLAQQAAAAAAASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRYDEINHVQKSHAELTATQAALEKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTRCAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTSKTIQDHLQLPQFKQPKLTIDTDYLVWSPQTAAAVVRAPGNSG | 2.3.1.48 | null | DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA repair-dependent chromatin remodeling [GO:0140861]; dosage compensation by hyperactivation of X chromosome [GO:0009047]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression, epigenetic [GO:0141137]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sex-chromosome dosage compensation [GO:0007549] | MSL complex [GO:0072487]; NSL complex [GO:0044545]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; polytene chromosome interband [GO:0005705]; transcription regulator complex [GO:0005667]; X chromosome [GO:0000805]; X chromosome located dosage compensation complex, transcription activating [GO:0016456] | chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone H4K16 acetyltransferase activity [GO:0046972]; lncRNA binding [GO:0106222]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712] | PF01853;PF11717;PF17772; | 2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10; | MYST (SAS/MOZ) family | PTM: Autoacetylation at Lys-638 is required for binding histone H4 with high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.; PTM: Ubiquitinated by msl-2. {ECO:0000269|PubMed:23084834, ECO:0000269|PubMed:28510597}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20620954}. Chromosome {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:28510597}. Note=When part of MSL complex, specifically localizes to many sites on the male X chromosome: displays a bimodal distribution binding to promoters and the 3' ends of genes (PubMed:11014199, PubMed:18510926, PubMed:22421046, PubMed:28510597). Recruited to the male X chromosome following association with roX1 and roX2 non-coding RNAs (PubMed:11014199). As part as the NSL complex, associates with promoters of housekeeping genes on X chromosome and autosomes genes (PubMed:18510926, PubMed:20620953). {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:28510597}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:10882077, ECO:0000269|PubMed:11258702, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:32502394, ECO:0000305|PubMed:16543150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:10882077, ECO:0000269|PubMed:11258702, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:32502394, ECO:0000305|PubMed:16543150}; | null | null | null | null | FUNCTION: Histone acetyltransferase that catalyzes the formation of the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction and constitutes the only acetylation mark intergenerationally transmitted (PubMed:10882077, PubMed:18510926, PubMed:20620953, PubMed:22421046, PubMed:32502394). Catalytic component of the male-specific lethal (MSL) complex, a multiprotein complex essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation) (PubMed:10882077, PubMed:11014199, PubMed:16543150, PubMed:18510926, PubMed:34133927, PubMed:9155031). The MSL complex specifically associates with the single X chromosome in males and mediates formation of H4K16ac, promoting a two-fold activation of X chromosome (PubMed:11258702, PubMed:18510926, PubMed:20620953, PubMed:22421046). Dosage compensation ensures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes (PubMed:18510926, PubMed:9155031). In oocytes, mof is also part of a maternal MSL subcomplex that mediates H4K16ac deposition for intergenerational transmission: H4K16ac prepares the chromatin landscape for establishment of nucleosome accessibility and poises genes for future activation (PubMed:32502394). H4K16ac constitutes the only acetylation mark maintained from oocytes to fertilized embryos (PubMed:32502394). Mof also constitutes the catalytic component of the non-specific lethal (NLS) complex, which promotes expression of housekeeping genes on X chromosome and autosomes (PubMed:20620953, PubMed:20620954, PubMed:22723752). The NSL complex promotes strong expression of housekeeping genes compared to the two-fold expression mediated by the MSL complex on X chromosome, suggesting that the activation potential of mof is constrained in the context of dosage compensation (PubMed:20620953). {ECO:0000269|PubMed:10882077, ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:11258702, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620953, ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:22723752, ECO:0000269|PubMed:32502394, ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9155031}. | Drosophila melanogaster (Fruit fly) |
O02194 | PSN_DROME | MAAVNLQASCSSGLASEDDANVGSQIGAAERLERPPRRQQQRNNYGSSNQDQPDAAILAVPNVVMREPCGSRPSRLTGGGGGSGGPPTNEMEEEQGLKYGAQHVIKLFVPVSLCMLVVVATINSISFYNSTDVYLLYTPFHEQSPEPSVKFWSALANSLILMSVVVVMTFLLIVLYKKRCYRIIHGWLILSSFMLLFIFTYLYLEELLRAYNIPMDYPTALLIMWNFGVVGMMSIHWQGPLRLQQGYLIFVAALMALVFIKYLPEWTAWAVLAAISIWDLIAVLSPRGPLRILVETAQERNEQIFPALIYSSTVVYALVNTVTPQQSQATASSSPSSSNSTTTTRATQNSLASPEAAAASGQRTGNSHPRQNQRDDGSVLATEGMPLVTFKSNLRGNAEAAGFTQEWSANLSERVARRQIEVQSTQSGNAQRSNEYRTVTAPDQNHPDGQEERGIKLGLGDFIFYSVLVGKASSYGDWTTTIACFVAILIGLCLTLLLLAIWRKALPALPISITFGLIFCFATSAVVKPFMEDLSAKQVFI | 3.4.23.- | null | amyloid-beta formation [GO:0034205]; apoptotic process [GO:0006915]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch receptor processing, ligand-dependent [GO:0035333]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485]; proteolysis [GO:0006508] | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175] | PF01080; | 1.10.472.100; | Peptidase A22A family | PTM: Cleaved. The cleavage, which probably takes place between the 6th and the 7th transmembrane regions, may be required for activation of the gamma-secretase activity. {ECO:0000269|PubMed:10662508}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptor. Required for S3 cleavage of Notch, which releases activated Notch protein from the cell membrane. Involved in the patterning of the optic lobes. {ECO:0000269|PubMed:10206646, ECO:0000269|PubMed:10206647, ECO:0000269|PubMed:12660785}. | Drosophila melanogaster (Fruit fly) |
O02213 | SER2_CAEEL | MFRNYTDSVQEMVLRAIDSIRDSVINASSAVSTTTLPPLDIPMTSMKPPSIIPTVELVLGTITYLVIIAMTVVGNTLVVVAVFSYRPLKKVQNYFLVSLAASDLAVAIFVMPLHVVTFLAGGKWLLGVTVCQFFTTADILLCTSSILNLCAIALDRYWAIHNPINYAQKRTTKFVCIVIVIVWILSMLISVPPIIGWNNWQENMMEDSCGLSTEKAFVVFSAAGSFFLPLLVMVVVYVKIFISARQRIRTNRGRSALMRIQNAEGDDDYRKMSIKRASVESARTSSRVGEKTPLVIADGQTTVTTLAAHSTDGGSLPKDETTKHMKYHNNGSCKVKVKDVKEDEGNPNPTAVLRKREKISVAKEKRAAKTIAVIIFVFSFCWLPFFVAYVIRPFCETCKLHAKVEQAFTWLGYINSSLNPFLYGILNLEFRRAFKKILCPKAVLEQRRRRMSAQP | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; dopamine receptor signaling pathway [GO:0007212]; octopamine or tyramine signaling pathway [GO:0007211] | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein-coupled amine receptor activity [GO:0008227]; octopamine receptor activity [GO:0004989]; tyramine receptor activity [GO:0008226] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: G-protein coupled receptor for tyramine, a known neurotransmitter and neuromodulator and direct precursor of octopamine. The rank order of potency is tyramine > octopamine > dopamine > serotonin > epinephrine = norepinephrine. {ECO:0000269|PubMed:12354282}. | Caenorhabditis elegans |
O02217 | P2R31_CAEEL | MPTDEPSKRKSILPTIPTSLMLKKSNEALSDFERTFNDRVMDIFAENRRIDVEEFKKNAECFLNIIRSNKIDLNWGEGGESRYVTITRLMKILKTSPQSIKDLLPHNTVSNFVKITNYNLTIDITLLEELVRTVIHAEESYIKLLPFSENSTEISSYSLQDFVATHFIPIMIEEPENPVYYTAYAVGTIFFLLGARRRDCVYLKDLLASTLLLQLEECIHAENHCLSPPKIDVFTVAQFRTTLSEFRFLDSQRKGLLAPADLKFFRDGIFNEVFTKRIFEISITYEDGRIDFKAFVDFVTALKFRHTTASAKYHFEILDLKDDGLLDEEEIRSISSFQLQNLPDYVPEDNSVNPEVATAELRDMMRLNQNGITLEEFLANRMNSTFAGFLSNSDDYMKYERREQ | null | null | cortical cytoskeleton organization [GO:0030865]; embryo development ending in birth or egg hatching [GO:0009792]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; positive regulation of B cell differentiation [GO:0045579]; protein localization to organelle [GO:0033365]; regulation of dephosphorylation [GO:0035303] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; protein phosphatase type 2A complex [GO:0000159]; spindle [GO:0005819] | protein phosphatase 2A binding [GO:0051721] | null | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:23336080}. | null | null | null | null | null | FUNCTION: Regulatory subunit of phosphatase let-92 which recruits let-92/paa-1 complex to the centrosomes, thereby regulating microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules. {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:23336080}. | Caenorhabditis elegans |
O02219 | AHA1_CAEEL | MAQDIFMDPWQSATSFAMEDEDMGMPSGKYARMEDEMGENKERFARENHSEIERRRRNKMTHYINELAEMVPQCASLGRKPDKLTILRMAVSHMKGIRGHTAQDETSYKPSFLTDQELKHLILEAANGFLFVVCCQTGKVLYVADSITPVLNLKQEDWLQRNLNELIHPDDQDKIRDQLCGSEVSVNKVLDLKSGSVKREGASTRVHMSCRRGFICRMRVGALEPLHRLRNRRPLFQHAGQNYVVMHCTGYIKNAPPQGINAPASSCLVAIARLQVASMPVCADPTSTNQFSVRVSEDGKMTFIDARVSDLIGLSSDQLIGRYWWNLAHPADEKTLQDSFVALLSDQPMRINIRVRTSTDYIPCTVSAYKFMNPYSEQFEYVVATHQIAPQEDINNWVTAPTVPQPQASEFGELGGAPSAVDYGQSSSGGWRPEAQGAPQAQWQWDPMNGYNQ | null | null | cell fate specification [GO:0001708]; determination of adult lifespan [GO:0008340]; intracellular receptor signaling pathway [GO:0030522]; neurogenesis [GO:0022008]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation by protein folding [GO:0022417]; regulation of transcription by RNA polymerase II [GO:0006357]; response to xenobiotic stimulus [GO:0009410]; social behavior [GO:0035176] | aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF00010;PF00989;PF14598; | 4.10.280.10;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11427734}. Note=Nuclear location dependent on hif-1 expression in intestinal tissue but not in neuronal cells. {ECO:0000269|PubMed:11427734}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:17628356). Efficient DNA binding requires dimerization with another bHLH protein, such as cky-1 or ahr-1 (PubMed:17628356, PubMed:9501178). Regulates transcription of target genes, probably acting in complex with cky-1 (PubMed:17628356). Has a role in cellular differentiation (PubMed:15136141, PubMed:9501178). Required for pharyngeal development (PubMed:14757639). In collaboration with ahr-1 it is involved in RMEL/R and SDQR neuron cell migration (PubMed:14757639). Acts in the cellular response to hypoxia (PubMed:11427734). Involved in aggregation behavior by regulating soluble guanylate cyclase gene expression in the URX neurons (PubMed:16919260). {ECO:0000269|PubMed:11427734, ECO:0000269|PubMed:14757639, ECO:0000269|PubMed:15136141, ECO:0000269|PubMed:16919260, ECO:0000269|PubMed:17628356, ECO:0000269|PubMed:9501178}. | Caenorhabditis elegans |
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