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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O14216 | SLD2_SCHPO | MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS | null | null | DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication initiation [GO:1902975]; mitotic DNA replication preinitiation complex assembly [GO:1902977] | cytoplasm [GO:0005737]; DNA replication preinitiation complex [GO:0031261]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634] | DNA replication origin binding [GO:0003688]; single-stranded DNA binding [GO:0003697] | PF11719; | 1.10.10.1460; | SLD2 family | PTM: Phosphorylated by cdc2 at the onset of S-phase. {ECO:0000269|PubMed:11937031, ECO:0000269|PubMed:18257517}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Has a role in the initiation of DNA replication. Required at S-phase checkpoint. {ECO:0000269|PubMed:11937031}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14222 | FSV1_SCHPO | MSNLLLIIDSVSQKIRDRRKLEEFGQNPDEEIESSLKDVRQELQKLNEEQSRLEKNAQIPEYRVRESEAFLIRMQRRLESAEEEFEKQRRASSIPADGTSAFSANPQVASTNNKLTPLPSLQKTTSSSEGSDIEMEAMYPVDGNDPDPINVNVLAQMHQQMLNEQEESLGGIEASVQRQKRMGYAMNTELSEQNVLLDNMNNDADRIERRFDHAKNRLNKVSRKAKQYPRCFIILLLCALLLLVASI | null | null | endosomal vesicle fusion [GO:0034058]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; vacuole fusion [GO:0097576]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906] | endomembrane system [GO:0012505]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF05739; | 1.20.5.110; | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:14575697}; Peripheral membrane protein {ECO:0000269|PubMed:14575697}. Prevacuolar compartment membrane {ECO:0000269|PubMed:14575697}; Peripheral membrane protein {ECO:0000269|PubMed:14575697}. Note=Associated with the Golgi and prevacuolar membrane. | null | null | null | null | null | FUNCTION: Involved in vesicle-mediated protein transport between the Golgi and the vacuole. {ECO:0000269|PubMed:14575697}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14227 | RDP1_SCHPO | MAVSLNDFISVKLKRYSRESPWERLRVPYRNKKQKKWASVHNNEAQLHSANKRNDNCLIQRSSTWRLGDMITLVIKDIPVTWLSNEGGKLYNLWEPLHDYGTIEFMKINEPLNGQTSTTAIVQFAPPPKVPFWEPNGKINVKGVDLAVQIDITAHRSHISRQVFSKNSFRSDQLVKIPLSSFKLGQVYDERIVPLFGVDCGITVTESNLLVYFNFKKLCVLFDASFDKQIETFRLDFDFHSIIGDVGTDYYDDHISLVFRFRFSPLIFRKSKNATESRVQTFWTASHLWRRHYDILPFNVSPTTASPIELLNCHNAPIGRCNVLVLSFSIRDESDKDDIAFLLHNLEKFNLKSQLDKVVFHLVPDYKHRCSLINDKEIEEEIAYLLQACLSKNLLSEIDLPIILANLKKLSKERAKKFLRLILTSKTALINPSELDFTKSFVFYDLSSASSIHIKKLYVTPTTLRIVEDSLEAGNRVIRNFKDFANRFMRVQITDEYYKQKIRGGSDGFRNEKLYSRIQQLLTYGIKVGNQIYEFLAFGNSQLREHGAYFFASGSDLNAKQIREWMGDFSEINSVSKYAARMGQCFSTTKEINRFCVDISLQDDIVRNNHCFTDGVGMASLSVIRRLSLEVKNHDMFPSAFQFRMGGYKGVLSLAPPTKLEYHQGNLVFPRRSQDKFKSFHSTLEVIKISRFSNAHLNMQLITLLEGLGVEKTVFLELTRSQLSKMNESINSKQKSILMLRDNVDEYHSTLIIADFIQAGFLERDDAFTENLLNLYYEWVLRLIKEKQKVSVPKGAYLLGVADETGTLKGHYDDAVLSVPEIFIQITDTSTSFGSYSTGKLKTRVIVGLCIVARNPSLHPGDVRVCKAVRCDELMHLKNVIVFPTTGDRSIPAMCSGGDLDGDEYTVIWDQRLLPKIVNYPPLLESSPKKSIDFLEGKPLIDSVKEFFVNYIKYDSLGLISNAWKAWAHDHDNNPEGIFGNVCLELAEMHSKAVDFAKSGVACKMQAKYHPKRYPDFMQKTKTRSFRSETAVGKIFRYAARFQRESGRPATYNPIMNTVYDPCMKLPRFKTEYLNVAEEVKKHYDNDLRSIMARFDISTEYEVYTAFILFKDDLAKTVNEYGLREEVSFQFDLLKKKYTQEYLEKCALSNQSAFDSSEYEERINSAVAATYDVTYDQRVKSVGNGTTEVLISFPYLFSSRLCQLSRKAMLTANNF | 2.7.7.48 | null | chromosome segregation [GO:0007059]; co-transcriptional gene silencing by RNA interference machinery [GO:0033562]; negative regulation of G0 to G1 transition [GO:0070317]; pericentric heterochromatin formation [GO:0031508]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; siRNA processing [GO:0030422]; siRNA-mediated pericentric heterochromatin formation [GO:0140727] | chromatin [GO:0000785]; chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mating-type region heterochromatin [GO:0031934]; nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; subtelomeric heterochromatin [GO:0140720] | RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF05183; | null | RdRP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15607976}. Nucleus {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:15607976}. Chromosome, telomere {ECO:0000269|PubMed:15615848}. Chromosome, centromere {ECO:0000269|PubMed:15615848}. Note=Associates with telomeric and mating-type region heterochromatin. {ECO:0000269|PubMed:15615848}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; | null | null | null | null | FUNCTION: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. Required for both post-transcriptional and transcriptional gene silencing. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3 'Lys-10' methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediates their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. Its RNA-dependent RNA polymerase activity is critical in siRNA production necessary for heterochromatin formation. {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:12215653, ECO:0000269|PubMed:12509501, ECO:0000269|PubMed:12733640, ECO:0000269|PubMed:14699070, ECO:0000269|PubMed:15371329, ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:15615848}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14230 | ERG20_SCHPO | MSAVDKRAKFESALPVFVDEIVNYLKTINIPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEILLGHPLDEAAYMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAIYFLLKKHFRQESCYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLSKFSLQKHSFIVIYKTAFYSFYLPVALAMHLAGVATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEKRVKAVFEELNIRGEFENYEESEVSEIKKLIDGVDESTGLKKSIFTTFLGKIYKRNK | 2.5.1.1; 2.5.1.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000305|PubMed:17596513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409; Evidence={ECO:0000305|PubMed:17596513}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000305|PubMed:17596513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362; Evidence={ECO:0000305|PubMed:17596513}; | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305|PubMed:17596513}.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305|PubMed:17596513}. | null | null | FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:17596513). Fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:17596513). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable). {ECO:0000269|PubMed:17596513, ECO:0000305}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14232 | MTR4_SCHPO | MFGGELDDAFGVFEGKVPKSLKEESKNSQNSQNSQKIKRTLTDKNASNQEQGTKKLESSVGEQESATKRAKIENLKDNQDLIPNNDVNGIHINNSAVADTKHKPKIGDIAADDISNEVSIKNEGDTIPEATVADSFEQEASLQVAGKVGMTEAKSSTEEVVELRHQVRHQVSIPPNYDYVPISKHKSPIPPARTYPFTLDPFQAVSIACIERQESVLVSAHTSAGKTVVAEYAVAQSLRDKQRVIYTSPIKALSNQKYRELLAEFGDVGLMTGDVTINPDATCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKSHFVFLSATIPNAMQFAEWITKIHRQPCHVVYTDFRPTPLQHYLFPSGSDGIHLVVDEKSNFREENFQRAMSALMEKQGDDPAAMATKGNAKKGKTGKGGVKGPSDIYKIVKMIMVKNYNPVIVFSFSKRECEALALQMSKLDMNDQTERDLVTTIFNNAVNQLSEKDRELPQIEHILPLLRRGIGIHHSGLLPILKEVIEILFQEGLLKVLFATETFSIGLNMPAKTVVFTNVRKFDGKTFRWISGGEYIQMSGRAGRRGLDDRGIVILMIDEKMDPPVAKSMLKGEADRLDSAFHLSYNMILNLLRVEGISPEFMLERCFFQFQNSLEVPKLEAKLEESQQHYDSFTILDERPLEEYHTLKTQLERYRTDVRTVVNHPNFCLSFLQGGRLVRVKVGNEDFDWGVVVNVSKRPLPKGQSNEYLPQESYIVHTLVMVASDTGPLRIRSGHLPEVHPPAAEDKGKFEVVPFLLSSLDGIAHIRVFLPNDLKSQGQKLTVGKALSEVKRRFPEGITLLDPVENMNIKEPTFIKLMKKVNILESRLLSNPLHNFSELEEKYAEYLRKLALLEEVKDLKKKLSKARSIMQLDELNSRKRVLRRLGFTTSDDVIEVKGRVACEISSGDGLLLTELIFNGMFNDLTPEQCAALLSCLVFQEKSEVENQRMKEELAGPLKILQEMARRIAKVSKESKQELNEEEYVNSFKPSLMEVVYAWAHGASFAQICKMTDVYEGSLIRMFRRLEELIRQMVDAAKVIGNTSLQQKMEDTIACIHRDIVFSASLYL | 3.6.4.- | null | maturation of 5.8S rRNA [GO:0000460]; polyadenylation-dependent ncRNA catabolic process [GO:0043634]; RNA catabolic process [GO:0006401]; tRNA catabolic process [GO:0016078] | nucleolus [GO:0005730]; nucleus [GO:0005634]; TRAMP complex [GO:0031499] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF08148;PF00271;PF21408;PF13234; | 1.10.3380.30;2.40.30.300;3.40.50.300; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Component of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates (By similarity). Required for heterochromatic gene silencing at centromeric repeats by either exosome- or RNAi-mediated degradation of heterochromatic transcripts. {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14246 | TPZ1_SCHPO | MSNCLKHPWLENGLLNLIKNADVLPIRVFKCQPLQIFEYIRYEHPIRCKLSDTEFYIEAEFSSQSISDLNNFTEKRITSLRGGIVTLGNFLIHLIPSQSGIIPWIQVESFNFQGCEGAVFGNPKAITTSALFNALLQSPYLAALANEFNRSIKEGSSYQEASLSQQEKPNDNTSNSRDIKNNIQFHWKNMTSLSIEECIIPKGQQLILEKESEENTTHGIYLEERKMAQGLHNSVSETPEVKQEDNDEDLDAYSWSSSTDSAGEIPSLPTNRKILEKIAEKPPPFESPLEDDETPDQTNEHEANQVNVSQLPLNPRGSGISGRPVESTEQLNSSLTIERSQSIQSTDSKQRVETQSHRRSKIEIFDAQDELFDRSICTTIDDSTGKLLNAEETPIKTGDLHSTSASSVISCTPPAINFTSDICNEQIELEYKRKPIPDYDFMKGLETTLQELYVEHQSKKRRLELFQLTNNHQKNSEACEMCRLGLPHGSFFELLRDWKKIEEFRNKS | null | null | mitotic telomere maintenance via semi-conservative replication [GO:1902990]; negative regulation of telomere maintenance via telomerase [GO:0032211]; protein localization to chromosome, telomeric region [GO:0070198]; telomere capping [GO:0016233]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]; telomere-telomerase complex assembly [GO:1905324] | chromosome, telomeric repeat region [GO:0140445]; shelterin complex [GO:0070187]; telomere cap complex [GO:0000782] | telomeric DNA binding [GO:0042162] | null | null | null | null | SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000269|PubMed:18535244}. Nucleus {ECO:0000269|PubMed:18535244}. | null | null | null | null | null | FUNCTION: Telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang and involved in telomere length regulation. recruits poz1 and ccq1 to telomeres, regulating telomere length negatively and positively respectively. {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:18535244}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14261 | ATG11_SCHPO | MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSFWLSFYKVSLRYDALYEYLRQIAEELDRSKFVLSQSRNIFSLYIDILMEALRRTEWQESYNVSHDSSLPLDQEKELSLRKSWLSHFSNLLFNHGQLKYLPVLTRDEISNYLLNIQAHPNYQTFHQMLSNRLSEYLGFPGSPREAVSNTVQANNSLHEKLAMYQNRCNNLEAMLSHQNGFNYNINNDGLSPNAPHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDSHILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKIQYLETENEEVLQKYENLQEELSSTRKLLTKNEAAVAEQQSNEEMHSNEPNILNLYSVFEGKVDSLQELYNAFKLQLTSLKQKGEYATLAKDAEAVQHIIEERDYALAEKADLLKLSENRKEQCKILTQKLYTIVFRCNELQSVLRECVTQPGFDSDNERDGHASIPDRQIEFNSKDLQYLYWMDGEDADRNFQEFLNRMSSLDFDSFHNFVVSVLTQAHNHELRWKREFQSNRDKALKAILDSQSKVSLRNFKQGSLVLFLPTRRTAGNKKVWAAFNVNAPHYYLNTQPHLKLESRDWMLGRVTSIEDRTADDSTDKWLRLPSGTIWHLVEAIDERF | null | null | autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; glycophagy [GO:0061723]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of protein phosphorylation [GO:0001934]; protein transport [GO:0015031]; reticulophagy [GO:0061709]; ribophagy [GO:0034517] | Atg1/ULK1 kinase complex [GO:1990316]; cytoplasm [GO:0005737]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045] | molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539] | PF10377;PF19697;PF04108; | null | ATG11 family | null | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. Vacuole membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. | null | null | null | null | null | FUNCTION: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the preautophagosome (PAS), the site of vesicle/autophagosome formation. Required for atg9 anterograde transport from the mitochondria to the PAS (By similarity). Required for nitrogen starvation-induced sexual development and for entering the dormant G0 state (By similarity). {ECO:0000250, ECO:0000269|PubMed:11270572}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14283 | PRR1_SCHPO | MPSSNGSSDFVRKLFNMLEEPEYRHILRWSDSGDSFIVLDTNEFTKTILPRHFKHSNFASFVRQLNKYDFHKVRHEEGAPSIYGEGAWEFRHDDFQLHHKDLLDNIKRKAPSKRNLANENTAPVIENLKQQVDSILDFQKLLDRNLSGLATSYQTILLKMFELKRGIESRDLLMSSIISYLCDLEGSTQRQANPGAMFVPSHPLQELLNAYQALAKGQVATTSPQQIPNQIQQASAATTASSKMTVDTNLGTAQPSLYNTPSSDYELANQEKPADSMASAASLNTPLSSNDHSLNPHAHGSYPMYEKFQPIQHPNPGSFTTHLDSNASMAKSFSQISNDSLAKASSVATSMSQMGAAVPTTGLWKRQPRILLVEDDELSRRMTIKFLTSFDCQVDVAVDGIGAVNKANAGGFDLILMDFILPNLDGLSVTCLIRQYDHNTPILAITSNISMNDAVTYFNHGVTDLLVKPFTKLTLLQLLKKQLLNLLQADNSINMSDVPSTKEAKDDKAPVTFYLENDAPMYPQQMLQDPIQADLQHPH | null | null | positive regulation of induction of conjugation with cellular fusion [GO:1900237]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to stimulus [GO:0050896] | chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00447;PF00072; | 3.40.50.2300;1.10.10.10; | HSF family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in oxidative stress. Transcription factor that acts upon trr1 and ctt1. {ECO:0000269|PubMed:10348908}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14285 | SPC34_SCHPO | MSDLLNYLQSIAATSEKLLEPENPNAARFTDAVLHTHAITDLIRDTQKEELIAAEFKSLPKDWSERLASENPADYVACIEELLDIYPMQGGREYLETLVEKYNLHMSGIENLENVLLEQKEQLQQLEKRQTDQVSARENILQRETSEIQRLEREIEKVKQLIQS | null | null | attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; mitotic sister chromatid biorientation [GO:1990758]; protein transport along microtubule to mitotic spindle pole body [GO:1990976]; spindle attachment to meiosis I kinetochore [GO:0051455] | condensed chromosome, centromeric region [GO:0000779]; cytosol [GO:0005829]; DASH complex [GO:0042729]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; spindle microtubule [GO:0005876] | null | PF08657; | null | DASH complex SPC34 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16079914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16079914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16079914}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis (PubMed:16079914). In the cytoskeleton, localizes to cortical microtubules (Probable). {ECO:0000269|PubMed:16079914, ECO:0000305|PubMed:20624975}. | null | null | null | null | null | FUNCTION: Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase (PubMed:16079914, PubMed:20624975). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules (PubMed:16079914, PubMed:20624975). Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle (PubMed:16079915). The DASH complex mediates bipolar kinetochore-microtubule attachments and facilitates the formation of additional interactions between outer kinetochore components and spindle microtubules (PubMed:16079914). During chromosome movement along the microtubule, it is required both for the sliding of kinetochores along the lateral side of the microtubule and also for microtubule end-on pulling on the kinetochore (PubMed:18256284). Modulates cytoplasmic microtubule dynamics by tracking the plus-end of shortening microtubules and slowing their depolymerization (PubMed:20624975). {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14286 | ATM1_SCHPO | MLERCPWKLISSPRNIPARSFLNSRGTYLVLRKSNILPLQHILRFSNFASKQCFPLRNGNNSASKALWNNKSKEKEPLNTSVKLASDVPDDKNVTGQMIVKDMLQYIWPKGKTNLKVRVVSALALLVAAKILNVQVPFYFKSIIDTMNTTLVQEVGALWSTVGAVVLGYGFARIFSTVFQELRNSVFAIVSQSAIRSVSSNVYQHLLNLDMNFHLSKQTGSITRAMDRGTKGISFILSSMVLHIIPITLEIAMVSGILTYKYGPSFSAIAATTVALYALFTVRTTSWRTVFRRQANAADSKASAAAIESLINYEAVKTFNNESYEMSRYEKHLSAYEKANVKVASSLAFLNSGQAIIFSTALTLMMYMGCRGIVTSNLTVGDLVMINQLVFQLSIPLNFLGSVYREMRQAFTDMEQLFSLKRINIQVKEAPDARDLVLKGGSIQFDNVHFSYNPNRPILNGCSFNIPAGAKVAFVGASGCGKSTILRLLFRFYDTDSGKILIDNQRLDQITLNSLRKAIGVVPQDTPLFNDTILYNIGYGNPKASNDEIVEAAKKAKIHDIIESFPEGYQTKVGERGLMISGGEKQRLAVSRLLLKNPEILFFDEATSALDTNTERALLRNINDLIKGSHKTSVFIAHRLRTIKDCDIIFVLEKGRVVEQGSHEQLMAKNSVYTSMWHSQESPFGESNKSGDA | 7.-.-.- | null | intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]; transmembrane transport [GO:0055085] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ABC-type iron-sulfur cluster transporter activity [GO:0140481]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16306692, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16306692, ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by nfs1 and other mitochondrial proteins (PubMed:16306692). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). {ECO:0000250|UniProtKB:P40416, ECO:0000269|PubMed:16306692}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14295 | PLR1_SCHPO | MPIVSGFKVGPIGFGLMGLTWKPKQTPDEEAFEVMNYALSQGSNYWDAGEFYGVDPPTSNLDLLARYFEKYPENANKVFLSVKGGLDFKTLVPDGNPDFVSKSVENVIAHLRGTKKLDLFQCARVDPNVPIETTMKTLKGFVDSGKISCVGLSEVSAETIKRAHAVVPIAAVEVEYSLFSRDIETNGIMDICRKLSIPIIAYSPFCRGLLTGRIKTVEDLKEFAKSFPFLEYLDRFSPDVFAKNLPFLQAVEQLAKKFGMTMPEFSLLFIMASGNGLVIPIPGSTSVSRTKSNLNALNKSLSPEQFKEAKEVLSKYPIYGLRYNEQLAGTLSV | 1.1.1.65 | null | pyridoxal biosynthetic process [GO:0042821]; vitamin B6 catabolic process [GO:0042820] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | aldo-keto reductase (NADP) activity [GO:0004033]; oxidoreductase activity [GO:0016491]; pyridoxine:NADP 4-dehydrogenase activity [GO:0050236] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10438489}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal; Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65; Evidence={ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 mM for pyridoxal {ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982}; | PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (dehydrogenase route): step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5 for the reverse reaction. {ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982}; | null | FUNCTION: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+). | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14299 | WIS4_SCHPO | MGLEHTFYPAEDRFEPLLEHSEPVNFVPKENAKSYVRQGFASPHQSLMDNLVDSTESTKRSENFVSHIPLTPSHSGQSEKLMSTRTSHSPYISPTMSYTNHSPANLTRNSSFNHQHYSTTLRSPPSMRGRGIDVNSSHYPHISRPRTSSDSQKMYTRAPVDYYYIQENPYFNNIDQDSISDKSLPSTNQSLHHSEEDTESDNDFSESIHPEFDIDVFYKVSNILYDESDLQDPEKRERLEWHSMLSSVLKGDVMQTEKRRLRLTEPDGHSGTYISEVWLGLQAWLHGRLNADQAEVIRKSREGVEPVLREVIDFQIQDEETTKPPLEQVTEILEKVEQCKQFYISSREMEENVPLSASKEFNYKLNALISWSNVMESIQVETLVLQKWVGNDEFDLTMRTPQFNYDGVENTSSFVERIFRQSGLQRTFEQRTLTTLNRIIHQAKQTISENAQAFEEMKLPTYEDKLLPLVRFPIKLLEEALRLRLAYAKKIKGPNFLIVDSMLDDFKIALSVAVRIKREYIKIASPSPGWSLPTNVDEDYDNVLLDSLKFYFKLLTLKLSSGNKNLYFKEIDFLENEWAFLNEHIYWINGGDIHMAGQFSYLSNSLLLNVHRYVESHLNGPTERTAASLTNWYSTLLKNTQIRFRKILRFSETLNSRFENASDFVISEGHLPDLVNRLSTTGHFLAYTANLERDGVFVIADHTLSENPEALKALLFSKDISNLETIQQNCSYVLILCPVHPIVWKGRIEKVDVPDFSVDLKTNRVRIIASNKREHLQAAKSVFQSISGDLVTLAVECRSSITRVYKEFIRLSKLCMRISSTVVDCVSAVREACSGVNCHDLIYHVFSFAAEFGQRILRFLSFDSYWQTKLKRKITSLAVEWISFICDECDLMDRKTFRWGVGALEFLMLMIRGNNILLIDDAMFLKIREKVGKSMAFLLTHFDVLGAKSKVAAKLQRESTEVSSSPRLTSFGDVEEEALSIQLLQKETMLRIDELEIERNNTLLERLAIGHVLDDSVFRNRDFIKLASSFSNITIRWQQGHFVRSGMFGDVYTGVNMETGDLLAVKEIKLQDSRTFRSTVDQIHNEMTVLERLNHPNVVTYYGVEVHREKVYIFMEFCQGGSLADLLAHGRIEDENVLKVYVVQLLEGLAYIHSQHILHRDIKPANILLDHRGMIKYSDFGSALYVSPPTDPEVRYEDIQPELQHLAGTPMYMAPEIILGTKKGDFGAMDIWSLGCVILEMMTGSTPWSEMDNEWAIMYHVAAMHTPSIPQNEKISSLARDFIEQCFERDPEQRPRAVDLLTHPWITDFRKKTIITMPPATITKKTSLSHTITEEKTAQLLAGRHDDSKAETDSLAASYKEESALPVASNVGLRQPNELRIDSINLPPAIVTPDTINYSVD | 2.7.11.25 | null | p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Mcs4 RR-MAPKKK complex [GO:1990315] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | null | 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; 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; | null | null | null | null | FUNCTION: Involved in a signal transduction pathway that is activated in under conditions of heat shock, oxidative stress or limited nutrition. Unlike win1, it is not activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14302 | CYK3_SCHPO | MSIPKQLPCMVRALYAWPGEREGDLKFTEGDLIECLSIGDGKWWIGRHINTNTQGIFPSNFVHCLDIPTVRPGSSMSRTSASSFRYSSPQKSSIDTPITSSDQGLTPDLVGSSNALNKPTRESDSLKHQKSHPMLNSLGSSLSLKKSVSRPPSSMSRTNLDVSSRWDNTADNDSQIDAQDLSRSTPSPLRSAMENVLQSLNAMGKKSFSRANSPLLRLTKSTTTSKETDFIPVPPAHGSTSMTSRSKLDDSTDNSSKPRTSLQPGESPMKSSRDISRKPSMASSVLSPSDYFPQHRRFQSAPAPIPRPVSTLIPLTQVRTTASNVIKPRPQTTERPSTAQSFRKGGGFLKKTFKKLLRRGSSKRKPSLQPTPPVSYPAHNVPQKGVRPASPHTLKSVKDDLKRTKTYTKAEFAAKREEIFNKLSMPVYEPLKDLSECIGNVLADGEPVQFSVGTNIHNMNFSAIDKQIRSIIPQRVQVSPAVLAKNYLAPGQTTALAQMRAVFIYISERITFTNQTLDNDELRTSTQVISEGQGTPFEVALLVKEMLQALDLWCEVIEGYLKSPDDIYYTRDININHAWNVVTFDNEVRLIDASFASPTHPQQALKSSSSNDFYFLMKPNECIFTHVPENPDQQFIMPDLSMPIVMALPWVSSVYFTLGLKLRKFNTSILHLNDLEVLQIEFLAPKDIECVAEVDALSALAPTADVSQCYKYTLTQAFWETPDIRVMRVKAVMPANNRAAVLRIYAGRLGVSSPVRTAPHPMAMSLPFVHHGKNKALEFVTRHPVPHCPSVDLYINSPQCGTLHSGVEYKFNVSAYACQPSTSISNTRLAIQTPTGNIVRLREERSGNGVIFFSLSLTINETGEYRALILAEKIGRWVVYATWQAV | null | null | mitotic actomyosin contractile ring contraction [GO:1902404]; mitotic division septum assembly [GO:0140278] | cell cortex [GO:0005938]; cell cortex of cell tip [GO:0051285]; cell cortex of non-growing cell tip [GO:0140472]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; division septum [GO:0000935]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, intermediate layer [GO:0120105] | null | PF00018;PF01841; | 3.10.620.30;2.30.30.40; | CYK3 family | null | SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:16823372}. Note=Also at the division site. {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Involved in cytokinesis. {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14305 | SID1_SCHPO | MYPLNANSYTLLRKLGSGSFGVVWKARENVSGDIIAIKQIDLETGIDDITDIEQEVFMLSNCNSSNVIQYYGCFVDGYTLWILMEHMDGGSVSGLLKMGRLNEQVISIILREVLYGLNYLHGQNKIHRDIKAANILLSSSTGNVKLADFGVAAQLSNAASRRHTFVGTPFWMAPEVIQQTSYGLAADIWSLGITAIEMANGIPPRATMHPMRVIFEIPQSEPPKLDDHFSPTFRDFVSCCLDLNPNMRWSAKELLQHPFIKSAGTVKDIIPLLVQKENKLFDDSDQSVLEETINNTLKPFEEPIAEGNADIEDWTFETVKKSDSTVLGNTSIPKNSIISSQNKEELPSSIKYLEKTIMSDQATPHPFSKSLSEKGSSYHKSLTSDFAMKHYIKSTIRSMLLNDKLSATQRSSLESFYTSFISLDKNLSSKFVNQITPDNRLHHKKQKRSPISQLLFSRWLEETEKRRSLNG | 2.7.11.1 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; phosphorylation [GO:0016310]; regulation of protein localization to mitotic spindle pole body [GO:1902542]; septation initiation signaling [GO:0031028] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle pole body [GO:0044732]; new mitotic spindle pole body [GO:0071958]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10775265, ECO:0000269|PubMed:11384993}. Note=Localizes to the SPB prior to cytokinesis and leaves once septation is complete. | 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: Has a role in the septation initiation network (SIN) required for cytokinesis. {ECO:0000269|PubMed:10775265, ECO:0000269|PubMed:11384993}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14310 | NP106_SCHPO | MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLAESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEFMEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTTNIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSSSAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLMRSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHRVSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFERAISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPAYQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGDYDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVVKVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYRTISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL | null | null | mRNA export from nucleus [GO:0006406]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein import into nucleus [GO:0006606]; stalled replication fork localization to nuclear periphery [GO:0120290] | cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nucleus [GO:0005634] | structural constituent of nuclear pore [GO:0017056] | PF04097; | null | Nucleoporin interacting component (NIC) family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:9372936}. | null | null | null | null | null | FUNCTION: Has a role in promoting mRNA export from the nucleus. {ECO:0000269|PubMed:9372936}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14313 | PMP20_SCHPO | MVAVGSTLPKVTLWENKPEEVVEFPSQGKFIIVGVPGAFTPPCSSQVPGYIANEKQFAAKGISGIYVVAVNDVFVTKAWKKSFDGGEQSGVHFVADWNGEFTKAFDAGFDASGLLGPLRSKRYAAVVENGKVVKVFIENEVTDVDISSADKVLSSL | null | null | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; protein refolding [GO:0042026] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | peroxidase activity [GO:0004601]; unfolded protein binding [GO:0051082] | PF08534; | 3.40.30.10; | Peroxiredoxin family, Prx5 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: May act as a chaperone rather than a peroxidase. Has no thioredoxin-dependent peroxidase activity. Shows weak chaperone activity. {ECO:0000269|PubMed:20356456}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14327 | PAB2_SCHPO | MSDQDALDTQEKELLEMKERVAEMEAEAAKLRAMQEQLDNETEALRNDKESIDAQSVYVGNVDYSVTPEELQSHFASCGSVNRVTILCDKFTGHPKGFAYIEFSEPSLVPNALLLNGSMLHERPLKVTPKRTNVPGMSRGRGRGRGRGRGRGRGGYRGRARGFAPY | null | null | nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; Mei2 nuclear dot complex [GO:0033620]; nuclear body [GO:0016604]; nuclear exosome focus [GO:1990251]; nucleolar peripheral inclusion body [GO:0140602]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | lncRNA binding [GO:0106222]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | null | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14333 | PSD1_SCHPO | MLKFHRNVKPQFGAFARYSSLGKHNSRKRVGIIRLAYGLTGIGLVGLAGFAWAQDRHEKTYQKKGVQVEGPWQFYVLTTLPLRTLSRWWGYVNRIEIPLWMRVPAFGLYSKIFGCNLTEADPDDVRQYKNLAEFFTRKLKPGARVIDPDAPIVIPADGKILNYGVIEGGQLEQVKGITYSLDALLGDEKLARLKRSHAIPSPDHIPHIRQEEFAKLNGIHYSLQDLMGHDHGERPSHVKDASAQHIDLLSSTKVAAKSQFTLFGSRETNCLYYAVIYLAPGDYHRFHSPTDWVVERRRHFSGELFSVSPFMARRLGNLFILNERVALMGRYKYGFMSMIPVGATNVGSIRIKFDKDLCTNQFGKLGPVGTFDEAVYTSSSSILHGHPLLRGDEVGNFELGSTVVLVFEAPADFEFLVKQGQKVRVGLPLGRVVPSSH | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; | CDP-choline pathway [GO:0006657]; phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | phosphatidylserine decarboxylase activity [GO:0004609] | PF02666; | null | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. | SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208}. | null | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd2 and psd3, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980). {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19286980}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14343 | KLP5_SCHPO | MSRQSSITVTVRVRPFSTAESANLIASSDRLSFGTSSSLRNPGSGRQIRRVVKVLDGRVLVFDPPDETTATLSATNRRLSTSQQSLARLSRKSNNSAGFGRDLRYAFDRVFDETATQQQVYERTARPLLDNILDGFNATIFAYGATGCGKTHTISGTMQDPGLIYLTLKELFERMDHLRDEKIFDLRLSYLEIYNETIRDLLVSPTPNQAKPLNLREDADRRITVPGLTSLSPESLEEIIDIIMKGNANRTMSPTEANAASSRSHAVLQVTLIQKPRTAGINEDHTLATLSIIDLAGSERATATKLRGSRLFEGANINKSLLALGNCINALCDPHRRAHVPYRDSKLTRLLKFSLGGNCRTVMIVCVSPSSVHYEETHNTLKYANRAKNIKTEVLRNMISVDRHVSQYVKAIVELREQISELENRLAQIDLSSQSNGSDQDAVTQSFAHESKLAEARNLLRMTFEETLPLQNDTINKVEKVKHFDDSIRVLKYWLSCYERILPNSADERVFLVRSKLESLLTRRAEIIADIDPELVYQKFQRSVSHIINTYKQEGATMYADVLQDEVDLLKSIIENQVLDAQNKVDEFTPVLESLLRSSFKASSLLKEGGMQELFSILEKWLLGIGLGEKPNISVLSESYKLNSTSDDSRTINRDRVHSFPTQPLLNNNLPRMFFVKSPKKPVVFSKRSPKKRVRFDDSMSTSDSGASAYNSPIQTSKLKNMNFFNTMHMPSTPAHKRPENKNQIDVEINLTSPVSPMLEDKPEPGLLIKSPLEKKQEVNSESTQLDQLLAEDSSTDDVSLPHLDTIDLDGSPVPKVPDLNFSRANMDSPTFILNNEAIHNFDFSKPKTRQSLSSLTTLHLSNPANIIRKSLSMAENEEEKAT | null | null | cell division [GO:0051301]; deactivation of mitotic spindle assembly checkpoint [GO:1902426]; lateral attachment of mitotic spindle microtubules to kinetochore [GO:0099607]; microtubule cytoskeleton organization [GO:0000226]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic metaphase chromosome recapture [GO:1990942]; mitotic sister chromatid biorientation [GO:1990758]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle elongation [GO:0000022]; mitotic spindle formation (spindle phase one) [GO:0061804]; mitotic spindle organization [GO:0007052]; plus-end specific microtubule depolymerization [GO:0070462]; protein transport along microtubule to kinetochore [GO:0140210] | cortical microtubule [GO:0055028]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinesin I complex [GO:0016938]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; mitotic spindle astral microtubule [GO:0061673]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; plus-end kinesin complex [GO:0005873]; post-anaphase microtubule array [GO:1990295] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11967147}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11967147}. Note=Cytoplasmic microtubules in interphase, mitotic kinetochores in metaphase and spindle midzone in anaphase and telophase. | null | null | null | null | null | FUNCTION: Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing. {ECO:0000269|PubMed:11967147}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14350 | SWI3_SCHPO | MSTAASDSGVEKLVEENKREEVKKNEEEKEFDLGLEENPDSVKKPRKRLAKFDEERLISENGIPKLRKMMRKVKLKGKGHEAKDLKQLLGMYHIWTHELYPRATFDDSISYLKTLGKHRSVKVRRRGWINEIAVENGSDSNASLFTGPSSNSLVNLTSGDPYVQDTADDAFVAQDNDTQLE | null | null | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; DNA replication checkpoint signaling [GO:0000076]; gene conversion at mating-type locus [GO:0007534]; mating-type locus imprinting [GO:0071515]; replication fork arrest [GO:0043111]; replication fork processing [GO:0031297] | chromatin [GO:0000785]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; Y-form DNA binding [GO:0000403] | PF07962; | null | CSM3 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367656}. Note=Nuclear throughout the cell cycle. Associated with chromatin during S phase. | null | null | null | null | null | FUNCTION: Forms a fork protection complex (FPC) with swi1. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. It is required for programmed fork-pausing which is necessary for mating-type switching. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors. It is involved in termination at the mat1-proximal polar-terminator of replication (RTS1) and also required for activation of the Rad53-like checkpoint kinase cds1. {ECO:0000269|PubMed:15367656, ECO:0000269|PubMed:15509785}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14352 | LSM4_SCHPO | MLPLTLLNATQGRPILVELKNGETFNGHLENCDNYMNLTLREVIRTMPDGDKFFRLPECYIRGNNIKYLRIQDEVLSQVAKQQAQQRENRGSRFRGRGQRGRGNYGHTAPNRRGRGRGGHM | null | null | nuclear-transcribed mRNA catabolic process [GO:0000956]; P-body assembly [GO:0033962]; RNA folding [GO:0034337]; spliceosomal snRNP assembly [GO:0000387]; telomerase holoenzyme complex assembly [GO:1905323] | cytosol [GO:0005829]; Lsm1-7-Pat1 complex [GO:1990726]; Lsm2-8 complex [GO:0120115]; nucleolus [GO:0005730]; nucleus [GO:0005634]; P-body [GO:0000932]; spliceosomal complex [GO:0005681]; spliceosomal tri-snRNP complex [GO:0097526]; telomerase holoenzyme complex [GO:0005697]; U2 snRNP [GO:0005686]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]; U6 snRNP [GO:0005688] | U2 snRNA binding [GO:0030620]; U6 snRNA binding [GO:0017070] | PF01423; | 2.30.30.100; | SnRNP Sm proteins family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA. {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14356 | TOR1_SCHPO | MEYFSDLKNKNESIQLAAADQLKEFVHSSTKELSGESLARFNNDINRRIFELIHSHDSHERFGGILAIGKLIEFESEGDVTNLSRYANYLRMTLPSTDWHSMELSAKVLGHLAASGGTLAAEFVEFEVQRAFEWLQGDRQEQKRMAAILIIKALAQNSPTLVYLYISEIFQNLWTGLRDPKPLIRETAADALGASLDVVCQREAKVQLQCFNEVLLQAEHGLRQSSVEYLHGSLLAYKELFEKSGSFIREHYTEFCDLALRLREHRDNSIRRCIVFLLPTLSEYNPKKFQQRYLDSFMVYLLSHIRKDKEKSLAFEAIGRIAMAVNEAMIPYLQNILKVIRDTLTAKVREKTQYEKPVFECIGMLAAAVKLELLEDSRSLLGLIFSCELSVHLRQALVKMAENIPPLLAPIQERLLNMVSQILTGKNFEIRTNDTYTPSFTNIYSAREPDQRSKSTESIILALETLGTFNFTGYSLISFIQESVLSYLENDNSEIRIAAARTCCQVFARDPICRKTNPLAVESVAEVLEKLLTLGIADSDPKIRETVLSLLDERFDRHLAHPDNIRCLFIALNDEVFSIREIAIIIIGRLALYNPAHVMPSLRKTIIQLLSDMEYSGNSRQKEESAQLLKLLVSKARTLIKPYIQSIIHVILPKAADTSPGVSSAIISALGELASVEGEDMPVDVRGSFMKLILVNLQDQSSTLKRLASLKCLRKLCGRSGYVIQPYLDYPPLLGALIGILQSEQPTPIRREVLRTLGVLGALDPYTYLTTEEVSDDLQSSHNNAHGVPQISAAQYPSLENYAMVAVVTLIGILKDSSLSMHHSSVVQAVMHICSQMGSKSTVFLPQVVPTFLQVMQSLSASSAEFYFQQLTTLTSIIGPNIRDYVSDIFNLSKVFWESTTSLLLVILELIDAIAIALQDEFKFYLPQILSCMLKAFSLDNTSSRSVSYKVLQSFVIFGSNIEEYMHLVLPVIIRSFERDTIPLGFRKSALKCIAQLFQSVNFSDHASRIIHPLVRMLGKSNGDLRAVIMDTLCAIVSQLGYDYSIFIPMVNKVLVSHKISHPAYELLVSRLLKGEPLPKDVVVKEFKPRPSTKPFSTQDEVLTKLPVDQASLKAAWESSQKLTRDDWQDWIRRISIELLKESPSSALRSCSTLAGIYHPLARDLFNVSFLSCWDELTESNKKNLVKSIELAMNAPNISVEILQTLLNLAEYMEREDHTLPIPIKVISAHASKCNVYAKALHYTELQFVQETKEEVSISTIESLITINNHLQQSDAAVGMLQYTKEHKQFSLKETWYEKLHRWDDALAAYEHREREGDSSFEINIGKLRCYYALGDWDHLSELAQKAWVTSEQEHREAIAPLAAAAAWGLGQWNLISEYVSAMDRDPQDKEFFSAISAVHLGQYNKAYGHIERHRDILVNDLSSIIGESYNRAYGIMVKSQMLSELEEIIDYKKNMQYENNLDSLKKTWRKRLEGCQKNVDVWHNTLRFRALVLSPQDSPEMWIKLADLCRRSDRLKLSNQCLTYLMGRDPSNAYPLDSLKLLNPHVVYTYLKYLWATDQKNIAVSELEEFTSYLSSKHGYKMGDSSKLVDILASSSVSSEERSFLARCFHKLGKWKKSLQDSVNQESVRDILNCYFYATLFDKSWYKAWHSWALANFEVVGYYEQTEHGVTQDMYEQYIVPAIKGFFHSSVLNQKNSLQDILRLLNLWFKFGEHSDVAAAIVEGFSNVPMDTWLEVIPQLIARIHTSSSSVRASVHQLLSDIGRVHPQALVYSLTVSSKSTNPQQKHSAKSIMDSMLSHSDTLVRQALLVSQELIRVAILWHELWYEGLEEASQAYFSDHDISLMIDIVKPLHETLEKGPSTLSEISFAQTFGYDLRKARSYWQKFLQDGDPTELNQSWDLYYQVFRRIQKQLPRIKHLELQYVSPKLLDACDLELAVPGTYGHNKPVIRISHFHHTFEVISSKQRPRRLTIHGSDGKDYQYVLKGHEDLRQDERVMQLFGLCNTLLTTDSETFKRRLNIERYTVIPLSPNSGLLGWVPHSDTLHFLIKEFRSKRNILLNLEHRMMLQMAPDCDSLTLLQKLEVFEYVMANTDGYDLYHVLWLKSRSSEAWLDRRTSYTQSLAVMSMVGYILGLGDRHPSNLMMDRYSGKIIHIDFGDCFEVAMHREKFPEKIPFRLTRMLINAMEVSGIQGTYKITCELVMRVLRSNTESLMAVLEAFVYDPLINWRLMTKSSFGASTTLRPTSSSVEEKGRSYTHRARHADYAALSETNGVNAEGLNERSIQVLKRVSNKLTGKDFDLKEQLPVKAQVEKLIQQATAPENLCRCYVGWCSFW | 2.7.11.1 | null | meiotic cell cycle [GO:0051321]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of macroautophagy [GO:0016242]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of induction of conjugation with cellular fusion [GO:1900237]; positive regulation of transcription by RNA polymerase II [GO:0045944]; TOR signaling [GO:0031929]; TORC2 signaling [GO:0038203] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein-containing complex binding [GO:0044877] | PF11865;PF02259;PF02260;PF08771;PF00454; | 1.20.120.150;1.25.10.10;1.10.1070.11;1.25.40.10; | PI3/PI4-kinase family | PTM: Phosphorylation at Thr-1972 in the ATP-binding region by AKT1 strongly reduces kinase activity. {ECO:0000269|PubMed:24247430}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. | 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:0000305|PubMed:12805221}; 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:0000305|PubMed:12805221}; | null | null | null | null | FUNCTION: Phosphatidylinositol 3-kinase homolog, component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases (PubMed:11096119, PubMed:11409178, PubMed:15466417, PubMed:17179073). Responsible for the phosphorylation of AGC kinase gad8 at 'Ser-527' and 'Ser-546', activating gad8 kinase activity and promoting sexual development (PubMed:12805221). {ECO:0000269|PubMed:11096119, ECO:0000269|PubMed:11409178, ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:15466417, ECO:0000269|PubMed:17179073}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14368 | HSP16_SCHPO | MSLQPFFGFPPTVNDLFSDFVSYSPRLNNQIPGELSPSIDVHEGKDTVSVDVELPGVKKEDVQVHYDSGKLTISGEVVNERKNESTEGNQRWSERRFGSFSRTITIPAKIDADRIEANFSNGLLTVTLPKVEKSQTKKQIAIK | null | null | cellular response to heat [GO:0034605]; cellular response to misfolded protein [GO:0071218]; cellular response to unfolded protein [GO:0034620]; protein complex oligomerization [GO:0051259]; protein folding [GO:0006457]; response to hydrogen peroxide [GO:0042542]; response to salt stress [GO:0009651] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein aggregate center [GO:0140453] | identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein self-association [GO:0043621]; unfolded protein binding [GO:0051082] | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11452028}. Nucleus {ECO:0000269|PubMed:11452028}. | null | null | null | null | null | null | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14370 | BCA1_SCHPO | MSLMFLRRAGNIKGRNIRFALQRGSVGYSQQSSEACKNFLNTTQLRTMVQTAALHGPKPMDSSHIKVTNVKELKPLPEWKSLKFGENFTDHMLIMKWNREKGWSTPEIVPFGKLCFHPASSVFHYGFECFEGMKAFRDEKGVPRLFRPIKNAERMLSTGTRISLPSFDPAELAEIIRKFVAHENRWVPDQRGYSLYIRPTFIGTDEALGVHHCDNAMLYVIASPVGPYYSSGFKAVKLCCSEESVRAWPGGTGHYKLGGNYAPSVLPQKEAAKKGYAQILWLYGDEDYITEVGTMNCFTVWINKNGEKEIITAPLDGMILPGVTRDSILEICRERLAPKGWKITEGKYSMKEVAQASKEGRLLEVFGAGTAALVSPVKAINYKGTEYEIPMPEGQEAGPITSEISKWILDIQYGKEPNNPWSVPALP | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]; pyridoxal phosphate binding [GO:0030170] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9483807}; | null | null | null | null | FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14405 | LP9A_HYPJE | MIQKLSNLLVTALAVATGVVGHGHINDIVINGVWYQAYDPTTFPYESNPPIVVGWTAADLDNGFVSPDAYQNPDIICHKNATNAKGHASVKAGDTILFQWVPVPWPHPGPIVDYLANCNGDCETVDKTTLEFFKIDGVGLLSGGDPGTWASDVLISNNNTWVVKIPDNLAPGNYVLRHEIIALHSAGQANGAQNYPQCFNIAVSGSGSLQPSGVLGTDLYHATDPGVLINIYTSPLNYIIPGPTVVSGLPTSVAQGSSAATATASATVPGGGSGPTSRTTTTARTTQASSRPSSTPPATTSAPAGGPTQTLYGQCGGSGYSGPTRCAPPATCSTLNPYYAQCLN | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:G0R6T8}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:G0R6T8}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9370370}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:11737205, ECO:0000269|PubMed:9370370}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:11737205, PubMed:9370370). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable). Shows activity on beta-glucan and amorphous cellulose (PubMed:11737205, PubMed:9370370). Does not show beta-1-3-glucanase, beta-1,6-glucanase, mannanase, xylanase, beta-1,3-galactosidase, amylase, pectinase, nor chitinase activities (PubMed:11737205). {ECO:0000269|PubMed:11737205, ECO:0000269|PubMed:9370370, ECO:0000305}. | Hypocrea jecorina (Trichoderma reesei) |
O14417 | MAD2_SCHPO | MSSVPIRTNFSLKGSSKLVSEFFEYAVNSILFQRGIYPAEDFKVVRKYGLNMLVSVDEEVKTYIRKIVSQLHKWMFAKKIQKLILVITSKCSGEDLERWQFNVEMVDTADQFQNIGNKEDELRVQKEIQALIRQITATVTFLPQLEEQCTFNVLVYADKDSEVPTDWVDSDPRILRDAEQVQLRSFSTSMHKIDCQVAYRVNP | null | null | cell division [GO:0051301]; meiosis I spindle assembly checkpoint signaling [GO:1905318]; meiotic spindle assembly checkpoint signaling [GO:0033316]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; mitotic checkpoint complex [GO:0033597]; mitotic spindle microtubule [GO:1990498]; mitotic spindle pole body [GO:0044732]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654] | anaphase-promoting complex binding [GO:0010997] | PF02301; | 3.30.900.10; | MAD2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. It interacts with the anaphase promoting complex/cyclosome (APC/C) thereby inhibiting APC/C-dependent proteolysis, a step required for exit from mitosis. {ECO:0000269|PubMed:9461438}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14434 | ARP1_ASPFU | MVEKKPNLTLEFHDYLALKKVLFDWADSYDAKDWDRLRSIIAPTLTVDYRQIGLRKWDDMPAEDYMAMISDMDFLGDPTVKTQHLLGESWWEKISDTEVIGHHQLRAAHQVYTDSTLQTVKLKGHGHATNEHYYRKVDGVWKFAGLKPTVRWNEYQFEDVFRAAKPSV | 4.2.1.94 | null | conidium formation [GO:0048315]; melanin biosynthetic process [GO:0042438]; pigment biosynthetic process [GO:0046148]; sporulation resulting in formation of a cellular spore [GO:0030435] | endosome [GO:0005768] | scytalone dehydratase activity [GO:0030411] | PF02982; | 3.10.450.50; | Scytalone dehydratase family | null | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:26972005}. | CATALYTIC ACTIVITY: Reaction=scytalone = 1,3,8-trihydroxynaphthalene + H2O; Xref=Rhea:RHEA:24396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16945, ChEBI:CHEBI:18393; EC=4.2.1.94; Evidence={ECO:0000305|PubMed:9383199}; | null | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:9383199}. | null | null | FUNCTION: Scytalone dehydratase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21573171, PubMed:21747802, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622). {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078, ECO:0000269|PubMed:21573171, ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666, ECO:0000269|PubMed:25684622, ECO:0000269|PubMed:26972005}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
O14442 | CP51_UNCNE | MYIADILSDLLTQQTTRYGWIFMVTSIAFSIILLAVGLNVLSQLLFRRPYEPPVVFHWFPIIGSTISYGIDPYKFYFDCRAKYGDIFTFILLGKKVTVYLGLQGNNFILNGKLKDVNAEEIYTNLTTPVFGRDVVYDCPNSKLMEQKKFMKTALTIEAFHSYVTIIQNEVEAYINNCVSFQGESGTVNISKVMAEITIYTASHALQGEEVRENFDSSFAALYHDLDMGFTPINFTFYWAPLPWNRARDHAQRTVARTYMNIIQARREEKRSGENKHDIMWELMRSTYKDGTPVPDREIAHMMIALLMAGQHSSSSTSSWIMLWLAARPDIMEELYEEQLRIFGSEKPFPPLQYEDLSKLQLHQNVLKEVLRLHAPIHSIMRKVKNPMIVPGTKYVIPTSHVLISSPGCTSQDATFFPDPLKWDPHRWDIGSGKVLGNDAVDEKYDYGYGLTSTGASSPYLPFGAGRHRCIGEQFATLQLVTIMATMVRFFRFRNIDGKQGVVKTDYSSLFSMPLAPALIGWEKR | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; sterol biosynthetic process [GO:0016126] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000250|UniProtKB:P10613}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | null | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. | null | null | FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10613, ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5}. | Uncinula necator (Grape powdery mildew) |
O14463 | TRX1_SCHPO | MVKQVSDSSEFKSIVCQDKLVVVDFFATWCGPCKAIAPKFEQFSNTYSDATFIKVDVDQLSEIAAEAGVHAMPSFFLYKNGEKIEEIVGANPAKLEASIKANL | null | null | cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to reactive oxygen species [GO:0034614]; hydrogen peroxide catabolic process [GO:0042744]; L-methionine salvage from methionine sulphoxide [GO:1990355]; sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) [GO:0019379] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | antioxidant activity [GO:0016209]; protein-disulfide reductase activity [GO:0015035] | PF00085; | 3.40.30.10; | Thioredoxin family | null | null | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14467 | MBF1_YEAST | MSDWDTNTIIGSRARAGGSGPRANVARSQGQINAARRQGLVVSVDKKYGSTNTRGDNEGQRLTKVDRETDIVKPKKLDPNVGRAISRARTDKKMSQKDLATKINEKPTVVNDYEAARAIPNQQVLSKLERALGVKLRGNNIGSPLGAPKKK | null | null | maintenance of translational fidelity [GO:1990145]; positive regulation of transcription by RNA polymerase II [GO:0045944]; rescue of stalled ribosome [GO:0072344] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA binding [GO:0003677]; ribosome binding [GO:0043022]; transcription coactivator activity [GO:0003713] | PF01381;PF08523; | 1.10.260.40; | MBF1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters (PubMed:9710580). Involved in induction of the ribosome quality control (RQC) pathway; a pathway that degrades nascent peptide chains during problematic translation (PubMed:30465652, PubMed:36583309). Required to prevent stalled ribosomes from frameshifting (PubMed:30465652, PubMed:36583309). {ECO:0000269|PubMed:30465652, ECO:0000269|PubMed:36583309, ECO:0000269|PubMed:9710580}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O14470 | SSR2_SCHPO | MTLDQVRIPFLVEQTYPIIVPSYAGWFDMSKIHDIERRSNPEFFNGKSPLKTPSIYKDYRDFMINSYRLEPNEYLTVTACRRNLVGDVCAIIRVHAFLEQWGLINYQIDPETRPAFRLPPISGHVQAISNTPIVTQEMLAQHPPPSTVGGSSSQEFVKLEEKHYSPSLNAMEQTSPKEEDEKSDKVPRVDKVCFTCGVNCSQTWYHNLKNKKYDICPNCYKQGRFSSSFNSSDFLCMDAIDFNHDEEKPWSNQETLLLLEAIETYGDDWNQIALHVGSRTKEQCLIHFLQIPIEDPYRQKLQGDFSPFKKGFLPFDENENPVLSTLTYLASIVQQGMKERKQNESVKQGETSFGNSEFKNPLERVAYYALKSAAQKAKLIAAFENRQLRRLVFSLIQAQLEKLQLKMKVLEQLEKMCSLELSELDLRGKNLLLSRLSTKKMLLAFNKKLEEAVNLGGEDGLKIIDDLMSTEHAEALLTFEMPTATTVSPLSKQYPDKFRTIAL | null | null | chromatin remodeling [GO:0006338]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514] | DNA binding [GO:0003677]; histone binding [GO:0042393]; zinc ion binding [GO:0008270] | PF00249;PF04433;PF16495; | 1.10.10.60;1.10.10.10; | SMARCC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}. | null | null | null | null | null | FUNCTION: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. {ECO:0000269|PubMed:18622392}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O14490 | DLGP1_HUMAN | MKGLSGSRSHHHGVTCDSACDSLSHHSDRKPYLLSPVEHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDECALVPRTLATKANRIPANLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGPSKGSVNGGKASPDEAQAARYGKRSKSKERRAEPKARPSTSPGWWSSDDNLDGDMCIYHAPSGVMTMGRCPDRSASQYFLEAYNTISEQAVKASRSNNDVKCSTCANLPVSLDTPLLKKSAWSSTLTVSRAREVYQKASVNMDQAMVKSESCQQERSCQYLQVPQDEWTGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPMPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTVSSCITTYKKTPPPVPPRTTTKPFISITAQSSTESAQDAYMDGQGQRGDIISQSGLSNSTESLDSMKALTAAIEAANAQIHGPASQHMGNNTATVTTTTTIATVTTEDRKKDHFKKNRCLSIGIQVDDAEEPDKTGENKAPSKFQSVGVQVEEEKCFRRFTRSNSVTTAVQADLDFHDNLENSLESIEDNSCPGPMARQFSRDASTSTVSIQGSGNHYHACAADDDFDTDFDPSILPPPDPWIDSITEDPLEAVQRSVCHRDGHWFLKLLQAERDRMEGWCQQMEREERENNLPEDILGKIRTAVGSAQLLMAQKFYQFRELCEENLNPNAHPRPTSQDLAGFWDMLQLSIENISMKFDELHQLKANNWKQMDPLDKKERRAPPPVPKKPAKGPAPLIRERSLESSQRQEARKRLMAAKRAASVRQNSATESAESIEIYIPEAQTRL | null | null | chemical synaptic transmission [GO:0007268] | glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic specialization [GO:0099572] | molecular adaptor activity [GO:0060090]; protein-containing complex binding [GO:0044877] | PF03359; | null | SAPAP family | PTM: Ubiquitinated by TRIM3; leading to proteasomal degradation. {ECO:0000250|UniProtKB:P97836}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}. | null | null | null | null | null | FUNCTION: Part of the postsynaptic scaffold in neuronal cells. | Homo sapiens (Human) |
O14492 | SH2B2_HUMAN | MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY | null | null | actin cytoskeleton organization [GO:0030036]; antigen receptor-mediated signaling pathway [GO:0050851]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell homeostasis [GO:0001922]; brown fat cell differentiation [GO:0050873]; cytokine-mediated signaling pathway [GO:0019221]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399]; regulation of metabolic process [GO:0019222]; regulation of Ras protein signal transduction [GO:0046578] | actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; stress fiber [GO:0001725] | identical protein binding [GO:0042802]; SH2 domain binding [GO:0042169]; signaling adaptor activity [GO:0035591]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068] | PF00169;PF08916;PF00017; | 6.10.140.110;2.30.29.30;3.30.505.10; | SH2B adapter family | PTM: Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B-cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex. {ECO:0000250|UniProtKB:Q9JID9, ECO:0000269|PubMed:10374881, ECO:0000269|PubMed:9233773, ECO:0000269|PubMed:9989826}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9989826}. Cell membrane {ECO:0000269|PubMed:9989826}. Note=Cytoplasmic before PDGF stimulation. After PDGF stimulation, localized at the cell membrane and peripheral region. | null | null | null | null | null | FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3. {ECO:0000269|PubMed:10374881, ECO:0000269|PubMed:12400014, ECO:0000269|PubMed:15378031, ECO:0000269|PubMed:9989826}. | Homo sapiens (Human) |
O14493 | CLD4_HUMAN | MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV | 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]; circadian rhythm [GO:0007623]; establishment of skin barrier [GO:0061436]; female pregnancy [GO:0007565]; positive regulation of cell migration [GO:0030335]; positive regulation of metallopeptidase activity [GO:1905050]; positive regulation of wound healing [GO:0090303]; regulation of cell morphogenesis [GO:0022604]; renal absorption [GO:0070293]; response to progesterone [GO:0032570] | apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basal plasma membrane [GO:0009925]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; chloride channel complex [GO:0034707]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | chloride channel activity [GO:0005254]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]; transmembrane signaling receptor activity [GO:0004888] | PF00822; | 1.20.140.150; | Claudin family | PTM: Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1. {ECO:0000269|PubMed:16236711}. | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250|UniProtKB:O35054}. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}. Note=CLDN4 is required for tight junction localization in the kidney. {ECO:0000250|UniProtKB:O35054}. | null | null | null | null | null | FUNCTION: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250|UniProtKB:O35054}. | Homo sapiens (Human) |
O14494 | PLPP1_HUMAN | MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP | 3.1.3.-; 3.1.3.106; 3.1.3.4; 3.6.1.75 | null | androgen receptor signaling pathway [GO:0030521]; ceramide metabolic process [GO:0006672]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of cell population proliferation [GO:0008285]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of lipid metabolic process [GO:0019216]; signal transduction [GO:0007165]; sphingolipid catabolic process [GO:0030149]; sphingosine metabolic process [GO:0006670] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | ceramide-1-phosphate phosphatase activity [GO:0106235]; diacylglycerol diphosphate phosphatase activity [GO:0000810]; lipid phosphatase activity [GO:0042577]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: N-glycosylated (PubMed:10962286, PubMed:9305923). N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity (By similarity). {ECO:0000250|UniProtKB:Q61469, ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:14527693}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:17005594}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000305|PubMed:9305923}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000305|PubMed:9305923}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000305|PubMed:9305923}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000305|PubMed:9305923}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000305|PubMed:9305923}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000305|PubMed:9607309}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000250|UniProtKB:O08564}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000250|UniProtKB:O08564}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=170 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=116 uM for N-(9Z-octadecenoyl)-ethanolamine phosphate {ECO:0000269|PubMed:9607309}; Vmax=0.54 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.5 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.3 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.32 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=41 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=33 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=29 nmol/min/mg enzyme with N-(9Z-octadecenoyl)-ethanolamine phosphate as substrate {ECO:0000269|PubMed:9607309}; | PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}. | null | null | FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:10962286, PubMed:17379599, PubMed:9305923, PubMed:9607309, PubMed:9705349). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:10962286, PubMed:12909631, PubMed:15461590, PubMed:17379599). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (PubMed:17379599). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (PubMed:12909631, PubMed:15461590). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity). {ECO:0000250|UniProtKB:O08564, ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:12909631, ECO:0000269|PubMed:15461590, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}. | Homo sapiens (Human) |
O14495 | PLPP3_HUMAN | MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIKPYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYRCRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVDIIDRNNHHNMM | 3.1.3.-; 3.1.3.4 | null | Bergmann glial cell differentiation [GO:0060020]; blood vessel development [GO:0001568]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by integrin [GO:0033631]; ceramide metabolic process [GO:0006672]; gastrulation with mouth forming second [GO:0001702]; homotypic cell-cell adhesion [GO:0034109]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of protein phosphorylation [GO:0001933]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; protein stabilization [GO:0050821]; regulation of sphingolipid mediated signaling pathway [GO:1902068]; regulation of Wnt signaling pathway [GO:0030111]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; signal transduction [GO:0007165]; sphingolipid catabolic process [GO:0030149]; sphingosine metabolic process [GO:0006670]; wound healing [GO:0042060] | adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ceramide-1-phosphate phosphatase activity [GO:0106235]; integrin binding [GO:0005178]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: N-glycosylated (PubMed:9705349). Contains high-mannose oligosaccharides (PubMed:9705349). {ECO:0000269|PubMed:9705349}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12660161, ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Basolateral cell membrane {ECO:0000269|PubMed:14527693}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Membrane raft {ECO:0000269|PubMed:17005594}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Note=Cycles between the endoplasmic reticulum and the Golgi. {ECO:0000269|PubMed:23591818}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000305|PubMed:9607309}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000269|PubMed:27694435}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000305|PubMed:9607309}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=110 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=56 uM for N-oleoyl ethanolamine phosphatidic acid {ECO:0000269|PubMed:9607309}; Vmax=0.27 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.46 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.36 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.24 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=13 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=15 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=29 nmol/min/mg enzyme with N-(9Z-octadecenoyl)-ethanolamine phosphate as substrate {ECO:0000269|PubMed:9607309}; | PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}. | null | null | FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:27694435, PubMed:9607309, PubMed:9705349). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:23591818, PubMed:27694435, PubMed:9607309). Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro-inflammatory cytokines (PubMed:27694435). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (By similarity). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers (PubMed:23591818). {ECO:0000250|UniProtKB:Q99JY8, ECO:0000269|PubMed:23591818, ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.; FUNCTION: Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta-catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth (PubMed:20123964, PubMed:21569306). Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis (PubMed:12660161, PubMed:16099422). {ECO:0000269|PubMed:12660161, ECO:0000269|PubMed:16099422, ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:21569306}. | Homo sapiens (Human) |
O14497 | ARI1A_HUMAN | MAAQVAPAAASSLGNPPPPPPSELKKAEQQQREEAGGEAAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLTEPPGGGGGGSSDGVGAPPHSAAAALPPPAYGFGQPYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPAPAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYSGGPQDGGAGKGPADMASQCWGAAAAAAAAAAASGGAQQRSHHAPMSPGSSGGGGQPLARTPQPSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGGLSYTQQIPPYGQQGPSGYGQQGQTPYYNQQSPHPQQQQPPYSQQPPSQTPHAQPSYQQQPQSQPPQLQSSQPPYSQQPSQPPHQQSPAPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPAPSTLSQQAAYPQPQSQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYSSPQPGSALSPRQPSGGQIHTGMGSYQQNSMGSYGPQGGQYGPQGGYPRQPNYNALPNANYPSAGMAGGINPMGAGGQMHGQPGIPPYGTLPPGRMSHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQETAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYSMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFNDGSDSTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPDSGMYSPSRYPPQQQQQQQQRHDSYGNQFSTQGTPSGSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSTGQGQPQQQQLPPAQPQPASQQQAAQPSPQQDVYNQYGNAYPATATAATERRPAGGPQNQFPFQFGRDRVSAPPGTNAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQSTGSAPQGPAYHGVNRTDEMLHTDQRANHEGSWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMQNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPAPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFSKVSSPAPMEGGEEEEELLGPKLEEEEEEEVVENDEEIAFSGKDKPASENSEEKLISKFDKLPVKIVQKNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKTELLPSRPHAPCPPAPRKHVTTAEGTPGTTDQEGPPPDGPPEKRITATMDDMLSTRSSTLTEDGAKSSEAIKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS | null | null | androgen receptor signaling pathway [GO:0030521]; chromatin remodeling [GO:0006338]; glucocorticoid receptor signaling pathway [GO:0042921]; intracellular estrogen receptor signaling pathway [GO:0030520]; nervous system development [GO:0007399]; nucleosome disassembly [GO:0006337]; positive regulation of cell differentiation [GO:0045597]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of T cell differentiation [GO:0045582]; regulation of G0 to G1 transition [GO:0070316]; 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]; transcription initiation-coupled chromatin remodeling [GO:0045815] | bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514] | DNA binding [GO:0003677]; nuclear receptor binding [GO:0016922]; nucleosome binding [GO:0031491]; transcription coactivator activity [GO:0003713] | PF01388;PF12031; | 1.10.150.60;1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:26614907}. | 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. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250|UniProtKB:A2BH40, ECO:0000303|PubMed:12672490, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. | Homo sapiens (Human) |
O14503 | BHE40_HUMAN | MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD | null | null | anterior/posterior pattern specification [GO:0009952]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634] | bHLH transcription factor binding [GO:0043425]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; MRF binding [GO:0043426]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837] | PF07527;PF00010; | 6.10.250.980;4.10.280.10; | null | PTM: Ubiquitinated; which may lead to proteasomal degradation. {ECO:0000269|PubMed:11278694}.; PTM: Sumoylation inhibits its ubiquitination and promotes its negative regulation of the CLOCK-BMAL1 heterodimer transcriptional activator activity. {ECO:0000269|PubMed:11278694, ECO:0000269|PubMed:21829689}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21829689}. Nucleus {ECO:0000269|PubMed:11278694, ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:28797635}. Note=Predominantly localized in the nucleus (PubMed:11278694). {ECO:0000269|PubMed:11278694}. | null | null | null | null | null | FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes (PubMed:12397359, PubMed:18411297). Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop) (PubMed:14672706). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2 (PubMed:15193144). Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes (PubMed:15560782). Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2 (PubMed:14672706). Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity (PubMed:19786558). May be involved in the regulation of chondrocyte differentiation via the cAMP pathway (PubMed:19786558). Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (PubMed:28797635). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system (PubMed:30012868). {ECO:0000269|PubMed:12397359, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15193144, ECO:0000269|PubMed:15560782, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:28797635, ECO:0000269|PubMed:30012868}. | Homo sapiens (Human) |
O14508 | SOCS2_HUMAN | MTLRCLEPSGNGGEGTRSQWGTAGSAEEPSPQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV | null | null | cellular response to hormone stimulus [GO:0032870]; growth hormone receptor signaling pathway [GO:0060396]; intracellular signal transduction [GO:0035556]; lactation [GO:0007595]; mammary gland alveolus development [GO:0060749]; negative regulation of apoptotic process [GO:0043066]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of neuron differentiation [GO:0045666]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell growth [GO:0001558]; regulation of signal transduction [GO:0009966]; response to estradiol [GO:0032355] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; growth hormone receptor binding [GO:0005131]; insulin-like growth factor receptor binding [GO:0005159]; JAK pathway signal transduction adaptor activity [GO:0008269] | PF00017;PF07525; | 3.30.505.10;1.10.750.20; | null | PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent proteasomal degradation (PubMed:31578312). Ubiquitination is dependent on its phosphorylation at Ser-52, by PKC (PubMed:31578312). Ubiquitination is stimulated by LPS (By similarity). {ECO:0000250|UniProtKB:O35717, ECO:0000269|PubMed:31578312}.; PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination and proteasomal degradation. {ECO:0000269|PubMed:31578312}. | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. | Homo sapiens (Human) |
O14511 | NRG2_HUMAN | MRQVCCSALPPPPLEKGRCSSYSDSSSSSSERSSSSSSSSSESGSSSRSSSNNSSISRPAAPPEPRPQQQPQPRSPAARRAAARSRAAAAGGMRRDPAPGFSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLDTNGKNLKKEVGKILCTDCATRPKLKKMKSQTGQVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLYVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRKQMHNHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRRETETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYNLEERRRATAPPYHDSVDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGPGPGPGADMQRSYDSYYYPAAGPGPRRGTCALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRARGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGGGSASASDDDADDADGALAAESTPFLGLRGAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPPRAKQDSAPL | null | null | animal organ development [GO:0048513]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399]; signal transduction [GO:0007165] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | growth factor activity [GO:0008083]; signaling receptor binding [GO:0005102] | PF07679;PF02158; | 2.60.40.10;2.10.25.10; | Neuregulin family | PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. | SUBCELLULAR LOCATION: [Pro-neuregulin-2, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor. | Homo sapiens (Human) |
O14512 | SOCS7_HUMAN | MVFRNVGRPPEEEDVEAAPEPGPSELLCPRHRCALDPKALPPGLALERTWGPAAGLEAQLAALGLGQPAGPGVKTVGGGCCPCPCPPQPPPPQPQPPAAAPQAGEDPTETSDALLVLEGLESEAESLETNSCSEEELSSPGRGGGGGGRLLLQPPGPELPPVPFPLQDLVPLGRLSRGEQQQQQQQQPPPPPPPPGPLRPLAGPSRKGSFKIRLSRLFRTKSCNGGSGGGDGTGKRPSGELAASAASLTDMGGSAGRELDAGRKPKLTRTQSAFSPVSFSPLFTGETVSLVDVDISQRGLTSPHPPTPPPPPRRSLSLLDDISGTLPTSVLVAPMGSSLQSFPLPPPPPPHAPDAFPRIAPIRAAESLHSQPPQHLQCPLYRPDSSSFAASLRELEKCGWYWGPMNWEDAEMKLKGKPDGSFLVRDSSDPRYILSLSFRSQGITHHTRMEHYRGTFSLWCHPKFEDRCQSVVEFIKRAIMHSKNGKFLYFLRSRVPGLPPTPVQLLYPVSRFSNVKSLQHLCRFRIRQLVRIDHIPDLPLPKPLISYIRKFYYYDPQEEVYLSLKEAQLISKQKQEVEPST | null | null | intracellular signal transduction [GO:0035556]; negative regulation of signal transduction [GO:0009968]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; protein ubiquitination [GO:0016567] | cytosol [GO:0005829]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; SH3 domain binding [GO:0017124] | PF00017;PF07525; | 3.30.505.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Rapidly relocalizes to the nucleus after UV irradiation. Cytoplasmic location depends upon SEPT7 presence. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:16127460}. | Homo sapiens (Human) |
O14514 | AGRB1_HUMAN | MRGQAAAPGPVWILAPLLLLLLLLGRRARAAAGADAGPGPEPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDGLRPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGGPAAGPLAPRGDVCLRDAVAGGPENCLTSLTQDRGGHGATGGWKLWSLWGECTRDCGGGLQTRTRTCLPAPGVEGGGCEGVLEEGRQCNREACGPAGRTSSRSQSLRSTDARRREELGDELQQFGFPAPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSACSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRCPEPHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAYWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLTEADEASVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLRTPLEIEFAHMYNGTTNQTCILWDETDVPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADANMEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTLKRPSLPEEEKLKLAHAKGPPTNFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKRDKAPKSSFVGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSIHIDQMPQTRLIHLSTAPEASLPARSPPSRQPPSGGPPEAPPAQPPPPPPPPPPPPQQPLPPPPNLEPAPPSLGDPGEPAAHPGPSTGPSTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKDKEVLGPDSKPEKQQTPNKRPWESLRKAHGTPTWVKKELEPLQPSPLELRSVEWERSGATIPLVGQDIIDLQTEV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic cell clearance [GO:0043277]; axonogenesis [GO:0007409]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; defense response to Gram-negative bacterium [GO:0050829]; engulfment of apoptotic cell [GO:0043652]; G protein-coupled receptor signaling pathway [GO:0007186]; innate immune response [GO:0045087]; muscle organ development [GO:0007517]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein ubiquitination [GO:0031397]; peripheral nervous system development [GO:0007422]; phagocytosis, recognition [GO:0006910]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of synapse assembly [GO:0051965]; regulation of synaptic plasticity [GO:0048167]; signal transduction [GO:0007165] | cell-cell junction [GO:0005911]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | G protein-coupled receptor activity [GO:0004930]; lipopolysaccharide binding [GO:0001530]; PDZ domain binding [GO:0030165]; phosphatidylserine binding [GO:0001786] | PF00002;PF19188;PF16489;PF01825;PF02793;PF00090; | 1.25.40.610;2.60.220.50;4.10.1240.10;1.20.1070.10;2.20.100.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved to produce vasculostatin-40 and vasculostatin-120 (PubMed:15782143, PubMed:22330140, PubMed:22333914). Vasculostatin-40 is the major form and is produced through proteolytic cleavage by MMP14 between residues 321 and 329 with cleavage likely to be between Ser-326 and Leu-327 (PubMed:22330140). {ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:22330140, ECO:0000269|PubMed:22333914}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:23782696}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12074842, ECO:0000269|PubMed:26838550}; Multi-pass membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:C0HL12}. Postsynaptic density {ECO:0000250|UniProtKB:Q3UHD1}.; SUBCELLULAR LOCATION: [Vasculostatin-120]: Secreted {ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:22330140}.; SUBCELLULAR LOCATION: [Vasculostatin-40]: Secreted {ECO:0000269|PubMed:22330140}. | null | null | null | null | null | FUNCTION: Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (PubMed:24509909). Also mediates the binding and engulfment of Gram-negative bacteria (PubMed:26838550). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (PubMed:26838550). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (PubMed:24509909). Promotes myoblast fusion (By similarity). Activates the Rho pathway in a G-protein-dependent manner (PubMed:23782696). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (PubMed:11875720). {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:Q3UHD1, ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:23782696, ECO:0000269|PubMed:24509909, ECO:0000269|PubMed:26838550}.; FUNCTION: [Vasculostatin-120]: Inhibits angiogenesis in a CD36-dependent manner. {ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:19176395}.; FUNCTION: [Vasculostatin-40]: Inhibits angiogenesis. {ECO:0000269|PubMed:22330140}. | Homo sapiens (Human) |
O14519 | CDKA1_HUMAN | MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS | null | null | cell cycle [GO:0007049]; DNA-templated DNA replication [GO:0006261]; positive regulation of protein phosphorylation [GO:0001934]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; perinuclear region of cytoplasm [GO:0048471] | DNA polymerase binding [GO:0070182] | PF09806; | 6.10.140.1300; | CDK2AP family | PTM: Phosphorylated in vitro by IKBKE at Ser-46. {ECO:0000269|PubMed:22427660}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Chromosome {ECO:0000269|PubMed:20523938}. | null | null | null | null | null | FUNCTION: Inhibitor of cyclin-dependent kinase CDK2 (By similarity). Also acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:20523938, PubMed:28977666). {ECO:0000250|UniProtKB:O35207, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666}. | Homo sapiens (Human) |
O14520 | AQP7_HUMAN | MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF | null | null | glycerol transmembrane transport [GO:0015793]; water transport [GO:0006833] | basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886] | glycerol channel activity [GO:0015254]; urea transmembrane transporter activity [GO:0015204]; water channel activity [GO:0015250] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11952783, ECO:0000269|PubMed:28042826, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:9405233}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O54794}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:27832861}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Lipid droplet {ECO:0000305|PubMed:27832861}. Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (By similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (PubMed:27832861). {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:27832861}. | null | null | null | null | null | FUNCTION: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:11952783, PubMed:30420639, PubMed:30423801, PubMed:9405233). The channel is also permeable to urea (PubMed:9405233). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity). {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:11952783, ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:9405233}. | Homo sapiens (Human) |
O14521 | DHSD_HUMAN | MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL | null | null | cellular response to hypoxia [GO:0071456]; mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; regulation of catecholamine secretion [GO:0050433]; tricarboxylic acid cycle [GO:0006099] | mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177]; ubiquinone binding [GO:0048039] | PF05328; | 1.20.1300.10; | CybS family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. | null | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. | null | null | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}. | Homo sapiens (Human) |
O14522 | PTPRT_HUMAN | MASLAALALSLLLRLQLPPLPGARAQSAAGGCSFDEHYSNCGYSVALGTNGFTWEQINTWEKPMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDTHCIDFHYYFSSRDRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFYQVIFESVSLKGHPGYIAVDEVRVLAHPCRKAPHFLRLQNVEVNVGQNATFQCIAGGKWSQHDKLWLQQWNGRDTALMVTRVVNHRRFSATVSVADTAQRSVSKYRCVIRSDGGSGVSNYAELIVKEPPTPIAPPELLAVGATYLWIKPNANSIIGDGPIILKEVEYRTTTGTWAETHIVDSPNYKLWHLDPDVEYEIRVLLTRPGEGGTGPPGPPLTTRTKCADPVHGPQNVEIVDIRARQLTLQWEPFGYAVTRCHSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEGRMESEELVVQTEEDVPGAVPLESIQGGPFEEKIYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTRIATKISAPSMPEYDTDTPLNETDTTITVMLKPAQSRGAPVSVYQLVVKEERLQKSRRAADIIECFSVPVSYRNASSLDSLHYFAAELKPANLPVTQPFTVGDNKTYNGYWNPPLSPLKSYSIYFQALSKANGETKINCVRLATKGASTQNSNTVEPEKQVDNTVKMAGVIAGLLMFIIILLGVMLTIKRRRNAYSYSYYLKLAKKQKETQSGAQREMGPVASADKPTTKLSASRNDEGFSSSSQDVNGFTDGSRGELSQPTLTIQTHPYRTCDPVEMSYPRDQFQPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGNTAIPVCEFRSLYYNISRLDPQTNSSQIKDEFQTLNIVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF | 3.1.3.48 | null | cell adhesion [GO:0007155]; cellular response to interleukin-6 [GO:0071354]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell migration [GO:0030336]; negative regulation of receptor signaling pathway via STAT [GO:1904893]; peptidyl-tyrosine dephosphorylation [GO:0035335]; peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [GO:1990264]; protein dephosphorylation [GO:0006470]; regulation of synapse organization [GO:0050807]; signal transduction [GO:0007165]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cell surface [GO:0009986]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839] | alpha-actinin binding [GO:0051393]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; delta-catenin binding [GO:0070097]; gamma-catenin binding [GO:0045295]; protein homodimerization activity [GO:0042803]; protein phosphatase binding [GO:0019903]; protein tyrosine phosphatase activity [GO:0004725]; STAT family protein binding [GO:0097677]; thiolester hydrolase activity [GO:0016790]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00041;PF00629;PF00102; | 2.60.120.200;2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2B subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: May be involved in both signal transduction and cellular adhesion in the CNS. | Homo sapiens (Human) |
O14523 | C2C2L_HUMAN | MDPGWGQRDVGWAALLILFAASLLTVFAWLLQYARGLWLARARGDRGPGPALAGEPAGSLRELGVWRSLLRLRATRAGAAEEPGVRGLLASLFAFKSFRENWQRAWVRALNEQACRNGSSIQIAFEEVPQLPPRASISHVTCVDQSEHTMVLRCQLSAEEVRFPVSVTQQSPAAVSMETYHVTLTLPPTQLEVNLEEIPGEGLLISWAFTDRPDLSLTVLPKLQARERGEEQVELSTIEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPMMPQAQPAIPRPNRLFLRQLRASHLGNELEGTEELCCVAELDNPMQQKWTKPARAGSEVEWTEDLALDLGPQSRELTLKVLRSSSCGDTELLGQATLPVGSPSRPLSRRQLCPLTPGPGKALGPAATMAVELHYEEGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTIVTTVTTVQSRPRIDGKLDSPSRSPSKVEVTEKTTTVLSESSGPSNTSHSSSRDSHLSNGLDPVAETAIRQLTEPSGRVAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASVQDDAGTSGGPSSPPSDPPAMSPGPLDALSSPTSVQEADETTRSDISERPSVDDIESETGSTGALETRSLKDHKVSFLRSGTKLIFRRRPRQKEAGLSQSHDDLSNATATPSVRKKAGSFSRRLIKRFSFKSKPKANGNPSPQL | null | null | positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774] | cortical endoplasmic reticulum [GO:0032541]; cytoplasmic side of apical plasma membrane [GO:0098592]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; plasma membrane [GO:0005886] | insulin binding [GO:0043559]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol transfer activity [GO:0008526] | PF00168;PF18696; | null | null | PTM: Phosphorylation at the C-terminus acidifies the protein and leads to disassociation from the acidic cell membrane. Reassociates with the cell membrane upon dephosphorylation. {ECO:0000269|PubMed:28209843}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28209843}; Single-pass membrane protein {ECO:0000269|PubMed:28209843}. Cell membrane {ECO:0000269|PubMed:28209843}; Peripheral membrane protein {ECO:0000269|PubMed:28209843}. Note=Localizes to sites of contact between the endoplasmic reticulum and the cell membrane (PubMed:28209843). Embedded into the endoplasmic reticulum membrane via its N-terminal transmembrane domain and associates with cell membrane via its C-terminus (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane and localizes to the reticular endoplasmic reticulum (PubMed:28209843). Reassociates with cell membrane upon dephosphorylation (PubMed:28209843). {ECO:0000269|PubMed:28209843}. | null | null | null | null | null | FUNCTION: Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (PubMed:28209843). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (PubMed:28209843). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (PubMed:28209843). Positively regulates insulin secretion in response to glucose: phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (PubMed:28209843). {ECO:0000269|PubMed:28209843}. | Homo sapiens (Human) |
O14524 | NEMP1_HUMAN | MAGGMKVAVSPAVGPGPWGSGVGGGGTVRLLLILSGCLVYGTAETDVNVVMLQESQVCEKRASQQFCYTNVLIPKWHDIWTRIQIRVNSSRLVRVTQVENEEKLKELEQFSIWNFFSSFLKEKLNDTYVNVGLYSTKTCLKVEIIEKDTKYSVIVIRRFDPKLFLVFLLGLMLFFCGDLLSRSQIFYYSTGMTVGIVASLLIIIFILSKFMPKKSPIYVILVGGWSFSLYLIQLVFKNLQEIWRCYWQYLLSYVLTVGFMSFAVCYKYGPLENERSINLLTWTLQLMGLCFMYSGIQIPHIALAIIIIALCTKNLEHPIQWLYITCRKVCKGAEKPVPPRLLTEEEYRIQGEVETRKALEELREFCNSPDCSAWKTVSRIQSPKRFADFVEGSSHLTPNEVSVHEQEYGLGSIIAQDEIYEEASSEEEDSYSRCPAITQNNFLT | null | null | erythrocyte enucleation [GO:0043131]; erythrocyte maturation [GO:0043249]; nuclear membrane organization [GO:0071763] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | null | PF10225; | null | NEMP family | PTM: Phosphorylation may regulate its interaction with RAN-GTP. {ECO:0000250|UniProtKB:Q6ZQE4}. | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}. | null | null | null | null | null | FUNCTION: Together with EMD, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). Required for female fertility (By similarity). Essential for normal erythropoiesis (By similarity). Required for efficient nuclear envelope opening and enucleation during the late stages of erythroblast maturation (By similarity). {ECO:0000250|UniProtKB:Q6ZQE4, ECO:0000269|PubMed:32923640}. | Homo sapiens (Human) |
O14525 | ASTN1_HUMAN | MALAGLCALLACCWGPAAVLATAAGDVDPSKELECKLKSITVSALPFLRENDLSIMHSPSASEPKLLFSVRNDFPGEMVVVDDLENTELPYFVLEISGNTEDIPLVRWRQQWLENGTLLFHIHHQDGAPSLPGQDPTEEPQHESAEEELRILHISVMGGMIALLLSILCLVMILYTRRRWCKRRRVPQPQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDLRHHLQRECMNGGEDFASQVTRTLDSLQGCNEKSGMDLTPGSDNAKLSLMNKYKDNIIATSPVDSNHQQATLLSHTSSSQRKRINNKARAGSAFLNPEGDSGTEAENDPQLTFYTDPSRSRRRSRVGSPRSPVNKTTLTLISITSCVIGLVCSSHVNCPLVVKITLHVPEHLIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWAMDLCARRLLDPCEHQCDPETGRREHRAAGECLCYEGYMKDPVHKHLCIRNEWGTNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELAINPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSKDNGGCSKNFRCISDRKLDSTGCVCPSGLSPMKDSSGCYDRHIGVDCSDGFNGGCEQLCLQQMAPFPDDPTLYNILMFCGCIEDYKLGVDGRSCQLITETCPEGSDCGESRELPMNQTLFGEMFFGYNNHSKEVAAGQVLKGTFRQNNFARGLDQQLPDGLVVATVPLENQCLEEISEPTPDPDFLTGMVNFSEVSGYPVLQHWKVRSVMYHIKLNQVAISQALSNALHSLDGATSRADFVALLDQFGNHYIQEAIYGFEESCSIWYPNKQVQRRLWLEYEDISKGNSPSDESEERERDPKVLTFPEYITSLSDSGTKHMAAGVRMECHSKGRCPSSCPLCHVTSSPDTPAEPVLLEVTKAAPIYELVTNNQTQRLLQEATMSSLWCSGTGDVIEDWCRCDSTAFGADGLPTCAPLPQPVLRLSTVHEPSSTLVVLEWEHSEPPIGVQIVDYLLRQEKVTDRMDHSKVETETVLSFVDDIISGAKSPCAMPSQVPDKQLTTISLIIRCLEPDTIYMFTLWGVDNTGRRSRPSDVIVKTPCPVVDDVKAQEIADKIYNLFNGYTSGKEQQTAYNTLLDLGSPTLHRVLYHYNQHYESFGEFTWRCEDELGPRKAGLILSQLGDLSSWCNGLLQEPKISLRRSSLKYLGCRYSEIKPYGLDWAELSRDLRKTCEEQTLSIPYNDYGDSKEI | null | null | locomotory behavior [GO:0007626]; neuron cell-cell adhesion [GO:0007158]; neuron migration [GO:0001764] | clathrin-coated vesicle [GO:0030136]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; perikaryon [GO:0043204] | null | PF18411;PF19743;PF19441; | 2.10.25.10; | Astrotactin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61137}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q61137}. Perikaryon {ECO:0000250|UniProtKB:Q61137}. Endosome {ECO:0000250|UniProtKB:Q61137}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q61137}. Note=Detected close to the anterior pole and at the base of the leading process in migrating neurons. Is internalized from the membrane via clathrin-coated vesicles and endosomes, and recycled to the anterior pole of the migrating cell. {ECO:0000250|UniProtKB:Q61137}. | null | null | null | null | null | FUNCTION: Neuronal adhesion molecule that is required for normal migration of young postmitotic neuroblasts along glial fibers, especially in the cerebellum. Required for normal rate of migration of granule cells during brain development and for normal cerebellum development. {ECO:0000250|UniProtKB:Q61137}. | Homo sapiens (Human) |
O14526 | FCHO1_HUMAN | MSYFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLLRKFAESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTCPEVDEEGFTVRPDVTQNSTAEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAERLQSEEQVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPAPADPTAREGLAAPPRRLRSRKVSCPLTRSNGDLSRSLSPSPLGSSAASTALERPSFLSQTGHGVSRGPSPVVLGSQDALPIATAFTEYVHAYFRGHSPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPLTNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGVDLELVGSGYRMSLVKRRFATGMYLVSC | null | null | clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; positive regulation of T cell activation [GO:0050870]; T cell receptor signaling pathway [GO:0050852] | clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | AP-2 adaptor complex binding [GO:0035612] | PF00611;PF10291; | 1.20.1270.60; | FCHO family | null | SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:32098969}; Peripheral membrane protein {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}; Cytoplasmic side {ECO:0000305|PubMed:17617719, ECO:0000305|PubMed:20448150}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. According to PubMed:17617719 it may also dynamically associate with Golgi/TGN membranes. | null | null | null | null | null | FUNCTION: Functions in an early step of clathrin-mediated endocytosis (PubMed:30822429). Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. Involved in the regulation of T-cell poliferation and activation (PubMed:30822429, PubMed:32098969). Affects TCR clustering upon receptor triggering and modulates its internalisation, playing a role in TCR-dependent T-cell activation (PubMed:32098969). {ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:30822429, ECO:0000269|PubMed:32098969}. | Homo sapiens (Human) |
O14529 | CUX2_HUMAN | MAANVGSMFQYWKRFDLRRLQKELNSVASELSARQEESEHSHKHLIELRREFKKNVPEEIREMVAPVLKSFQAEVVALSKRSQEAEAAFLSVYKQLIEAPDPVPVFEAARSLDDRLQPPSFDPSGQPRRDLHTSWKRNPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLACCSPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKFLLEKPSLLASPEEDPSEDDSIKDSLGTEQSYPSPQQLPPPPGPEDPLSPSPGQPLLGPSLGPDGTRTFSLSPFPSLASGERLMMPPAAFKGEAGGLLVFPPAFYGAKPPTAPATPAPGPEPLGGPEPADGGGGGAAGPGAEEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEPFIKMKQFLSDEQNVLALRTIQVRQRGSITPRIRTPETGSDDAIKSILEQAKKEIESQKGGEPKTSVAPLSIANGTTPASTSEDAIKSILEQARREMQAQQQALLEMEVAPRGRSVPPSPPERPSLATASQNGAPALVKQEEGSGGPAQAPLPVLSPAAFVQSIIRKVKSEIGDAGYFDHHWASDRGLLSRPYASVSPSLSSSSSSGYSGQPNGRAWPRGDEAPVPPEDEAAAGAEDEPPRTGELKAEGATAEAGARLPYYPAYVPRTLKPTVPPLTPEQYELYMYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLSDQLGQAVGQQPGASQASPTEPRSSPSPPPSPTEPEKSSQEPLSLSLESSKENQQPEGRSSSSLSGKMYSGSQAPGGIQEIVAMSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREPFVRMQLWLNDPHNVEKLRDMKKLEKKAYLKRRYGLISTGSDSESPATRSECPSPCLQPQDLSLLQIKKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEPDLDPSGGPGILPPGHSHPDPTPQSPDSETEDQKPTVKELELQEGPEENSTPLTTQDKAQVRIKQEQMEEDAEEEAGSQPQDSGELDKGQGPPKEEHPDPPGNDGLPKVAPGPLLPGGSTPDCPSLHPQQESEAGERLHPDPLSFKSASESSRCSLEVSLNSPSAASSPGLMMSVSPVPSSSAPISPSPPGAPPAKVPSASPTADMAGALHPSAKVNPNLQRRHEKMANLNNIIYRVERAANREEALEWEF | null | null | cellular response to organic substance [GO:0071310]; cognition [GO:0050890]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of gene expression [GO:0010628]; positive regulation of synapse assembly [GO:0051965]; regulation of transcription by RNA polymerase II [GO:0006357]; short-term memory [GO:0007614] | chromatin [GO:0000785]; extracellular exosome [GO:0070062]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF02376;PF00046; | 1.10.10.60;1.10.260.40; | CUT homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}. | null | null | null | null | null | FUNCTION: Transcription factor involved in the control of neuronal proliferation and differentiation in the brain. Regulates dendrite development and branching, dendritic spine formation, and synaptogenesis in cortical layers II-III. Binds to DNA in a sequence-specific manner. {ECO:0000250|UniProtKB:P70298}. | Homo sapiens (Human) |
O14530 | TXND9_HUMAN | MEADASVDMFSKVLEHQLLQTTKLVEEHLDSEIQKLDQMDEDELERLKEKRLQALRKAQQQKQEWLSKGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLGSSDILNYSGNLMEPPFQNQKKFGTNFTKLEKKTIRGKKYDSDSDDD | null | null | microtubule cytoskeleton organization [GO:0000226] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; midbody [GO:0030496]; nucleus [GO:0005634] | cadherin binding [GO:0045296] | PF00085; | 3.40.30.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CQ79}. Nucleus {ECO:0000250|UniProtKB:Q9CQ79}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CQ79}. Midbody {ECO:0000250|UniProtKB:Q9CQ79}. Note=Co-localizes with beta-tubulin in the centrosome. {ECO:0000250|UniProtKB:Q9CQ79}. | null | null | null | null | null | FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. {ECO:0000269|PubMed:16415341}. | Homo sapiens (Human) |
O14531 | DPYL4_HUMAN | MSFQGKKSIPRITSDRLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPVNPDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFVTPGAGRFVPRKTFPDFVYKRIKARNRLAEIHGVPRGLYDGPVHEVMVPAKPGSGAPARASCPGKISVPPVRNLHQSGFSLSGSQADDHIARRTAQKIMAPPGGRSNITSLS | null | null | nervous system development [GO:0007399] | cytosol [GO:0005829] | filamin binding [GO:0031005]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides [GO:0016812] | PF01979; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, Hydantoinase/dihydropyrimidinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14543 | SOCS3_HUMAN | MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFPSPPTEPSSEVPEQPSAQPLPGSPPRRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL | null | null | branching involved in labyrinthine layer morphogenesis [GO:0060670]; cellular response to interleukin-17 [GO:0097398]; cellular response to leukemia inhibitory factor [GO:1990830]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of tyrosine phosphorylation of STAT protein [GO:0042532]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; placenta blood vessel development [GO:0060674]; positive regulation of cell differentiation [GO:0045597]; protein ubiquitination [GO:0016567]; T-helper 17 cell lineage commitment [GO:0072540] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; miRNA binding [GO:0035198]; phosphotyrosine residue binding [GO:0001784]; protein kinase inhibitor activity [GO:0004860]; protein tyrosine kinase inhibitor activity [GO:0030292] | PF00017; | 3.30.505.10;1.10.750.20; | null | PTM: Phosphorylated on tyrosine residues after stimulation by the cytokines, IL-2, EPO or IGF1. | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15601820). {ECO:0000250|UniProtKB:O35718, ECO:0000269|PubMed:15601820}. | Homo sapiens (Human) |
O14544 | SOCS6_HUMAN | MKKISLKTLRKSFNLNKSKEETDFMVVQQPSLASDFGKDDSLFGSCYGKDMASCDINGEDEKGGKNRSKSESLMGTLKRRLSAKQKSKGKAGTPSGSSADEDTFSSSSAPIVFKDVRAQRPIRSTSLRSHHYSPAPWPLRPTNSEETCIKMEVRVKALVHSSSPSPALNGVRKDFHDLQSETTCQEQANSLKSSASHNGDLHLHLDEHVPVVIGLMPQDYIQYTVPLDEGMYPLEGSRSYCLDSSSPMEVSAVPPQVGGRAFPEDESQVDQDLVVAPEIFVDQSVNGLLIGTTGVMLQSPRAGHDDVPPLSPLLPPMQNNQIQRNFSGLTGTEAHVAESMRCHLNFDPNSAPGVARVYDSVQSSGPMVVTSLTEELKKLAKQGWYWGPITRWEAEGKLANVPDGSFLVRDSSDDRYLLSLSFRSHGKTLHTRIEHSNGRFSFYEQPDVEGHTSIVDLIEHSIRDSENGAFCYSRSRLPGSATYPVRLTNPVSRFMQVRSLQYLCRFVIRQYTRIDLIQKLPLPNKMKDYLQEKHY | null | null | defense response [GO:0006952]; intracellular signal transduction [GO:0035556]; negative regulation of signal transduction [GO:0009968]; negative regulation of T cell activation [GO:0050868]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; proteasomal protein catabolic process [GO:0010498]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of growth [GO:0040008] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; phosphatidylinositol 3-kinase complex [GO:0005942] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935] | PF00017;PF07525; | 3.30.505.10;1.10.750.20; | null | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor. {ECO:0000250, ECO:0000269|PubMed:21030588}. | Homo sapiens (Human) |
O14556 | G3PT_HUMAN | MSKRDIVLTNVTVVQLLRQPCPVTRAPPPPEPKAEVEPQPQPEPTPVREEIKPPPPPLPPHPATPPPKMVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK | 1.2.1.12 | null | flagellated sperm motility [GO:0030317]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; positive regulation of glycolytic process [GO:0045821] | cytosol [GO:0005829]; nucleus [GO:0005634] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PRU10009}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14558 | HSPB6_HUMAN | MEIPVPVQPSWLRRASAPLPGLSAPGRLFDQRFGEGLLEAELAALCPTTLAPYYLRAPSVALPVAQVPTDPGHFSVLLDVKHFSPEEIAVKVVGEHVEVHARHEERPDEHGFVAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQAAPASAQAPPPAAAK | null | null | chaperone-mediated protein folding [GO:0061077]; negative regulation of apoptotic process [GO:0043066]; positive regulation of angiogenesis [GO:0045766]; protein refolding [GO:0042026]; response to heat [GO:0009408] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082] | PF00525;PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8195168}.; PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:P97541, ECO:0000250|UniProtKB:Q5EBG6, ECO:0000305|PubMed:26443497}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Secreted {ECO:0000269|PubMed:22427880}. Note=Translocates to nuclear foci during heat shock. {ECO:0000269|PubMed:19464326}. | null | null | null | null | null | FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. {ECO:0000269|PubMed:14717697, ECO:0000269|PubMed:19845507, ECO:0000269|PubMed:20843828, ECO:0000269|PubMed:22427880, ECO:0000305, ECO:0000305|PubMed:22794279}. | Homo sapiens (Human) |
O14559 | RHG33_HUMAN | MVARSTDSLDGPGEGSVQPLPTAGGPSVKGKPGKRLSAPRGPFPRLADCAHFHYENVDFGHIQLLLSPDREGPSLSGENELVFGVQVTCQGRSWPVLRSYDDFRSLDAHLHRCIFDRRFSCLPELPPPPEGARAAQMLVPLLLQYLETLSGLVDSNLNCGPVLTWMELDNHGRRLLLSEEASLNIPAVAAAHVIKRYTAQAPDELSFEVGDIVSVIDMPPTEDRSWWRGKRGFQVGFFPSECVELFTERPGPGLKADADGPPCGIPAPQGISSLTSAVPRPRGKLAGLLRTFMRSRPSRQRLRQRGILRQRVFGCDLGEHLSNSGQDVPQVLRCCSEFIEAHGVVDGIYRLSGVSSNIQRLRHEFDSERIPELSGPAFLQDIHSVSSLCKLYFRELPNPLLTYQLYGKFSEAMSVPGEEERLVRVHDVIQQLPPPHYRTLEYLLRHLARMARHSANTSMHARNLAIVWAPNLLRSMELESVGMGGAAAFREVRVQSVVVEFLLTHVDVLFSDTFTSAGLDPAGRCLLPRPKSLAGSCPSTRLLTLEEAQARTQGRLGTPTEPTTPKAPASPAERRKGERGEKQRKPGGSSWKTFFALGRGPSVPRKKPLPWLGGTRAPPQPSGSRPDTVTLRSAKSEESLSSQASGAGLQRLHRLRRPHSSSDAFPVGPAPAGSCESLSSSSSSESSSSESSSSSSESSAAGLGALSGSPSHRTSAWLDDGDELDFSPPRCLEGLRGLDFDPLTFRCSSPTPGDPAPPASPAPPAPASAFPPRVTPQAISPRGPTSPASPAALDISEPLAVSVPPAVLELLGAGGAPASATPTPALSPGRSLRPHLIPLLLRGAEAPLTDACQQEMCSKLRGAQGPLGPDMESPLPPPPLSLLRPGGAPPPPPKNPARLMALALAERAQQVAEQQSQQECGGTPPASQSPFHRSLSLEVGGEPLGTSGSGPPPNSLAHPGAWVPGPPPYLPRQQSDGSLLRSQRPMGTSRRGLRGPAQVSAQLRAGGGGRDAPEAAAQSPCSVPSQVPTPGFFSPAPRECLPPFLGVPKPGLYPLGPPSFQPSSPAPVWRSSLGPPAPLDRGENLYYEIGASEGSPYSGPTRSWSPFRSMPPDRLNASYGMLGQSPPLHRSPDFLLSYPPAPSCFPPDHLGYSAPQHPARRPTPPEPLYVNLALGPRGPSPASSSSSSPPAHPRSRSDPGPPVPRLPQKQRAPWGPRTPHRVPGPWGPPEPLLLYRAAPPAYGRGGELHRGSLYRNGGQRGEGAGPPPPYPTPSWSLHSEGQTRSYC | null | null | protein transport [GO:0015031]; regulation of dendritic spine morphogenesis [GO:0061001]; response to toxic substance [GO:0009636]; small GTPase-mediated signal transduction [GO:0007264] | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; fibrillar center [GO:0001650]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | GTPase activator activity [GO:0005096]; phosphatidylinositol binding [GO:0035091]; protein kinase binding [GO:0019901] | PF00620;PF14604; | 3.30.1520.10;1.10.555.10;2.30.30.40; | PX domain-containing GAP family | null | null | null | null | null | null | null | FUNCTION: May be involved in several stages of intracellular trafficking. Could play an important role in the regulation of glucose transport by insulin. May act as a downstream effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose transport (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14561 | ACPM_HUMAN | MASRVLSAYVSRLPAAFAPLPRVRMLAVARPLSTALCSAGTQTRLGTLQPALVLAQVPGRVTQLCRQYSDMPPLTLEGIQDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE | null | null | [2Fe-2S] cluster assembly [GO:0044571]; aerobic respiration [GO:0009060]; fatty acid biosynthetic process [GO:0006633]; iron-sulfur cluster assembly [GO:0016226]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; protein lipoylation [GO:0009249]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | iron-sulfur cluster assembly complex [GO:1990229]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | acyl binding [GO:0000035]; acyl carrier activity [GO:0000036]; calcium ion binding [GO:0005509]; fatty acid binding [GO:0005504]; mitochondrial large ribosomal subunit binding [GO:0140978] | PF00550; | 1.10.1200.10; | Acyl carrier protein (ACP) family | PTM: Phosphopantetheinylation at Ser-112 is essential for interactions with LYR motif-containing proteins. {ECO:0000269|PubMed:31664822}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:28892042}. | null | null | null | null | null | FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity) (PubMed:27626371). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (PubMed:27626371). Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:31664822). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). {ECO:0000250|UniProtKB:P52505, ECO:0000250|UniProtKB:Q9H1K1, ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:31664822}. | Homo sapiens (Human) |
O14569 | C56D2_HUMAN | MALSAETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLMTEALLVFSPESSLLHSLSRKGRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLVTRHGQAGLLAVLWAGLQCSGGVGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSASLLLGMCSLWFTASVTGAAWYLAVLCPVLTSLVIMNQVSNAYLYRKRIQP | 7.2.1.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:19734123, ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}; Note=Binds 2 heme b groups non-covalently. {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}; | ascorbate homeostasis [GO:0140576] | cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; vesicle [GO:0031982] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; transmembrane ascorbate ferrireductase activity [GO:0140571]; transmembrane monodehydroascorbate reductase activity [GO:0140575] | PF03188; | 1.20.120.1770; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. | CATALYTIC ACTIVITY: Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-ascorbate(out) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; Evidence={ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525; Evidence={ECO:0000305|PubMed:23641721}; CATALYTIC ACTIVITY: Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) + monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3; Evidence={ECO:0000250|UniProtKB:Q9WUE3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404; Evidence={ECO:0000250|UniProtKB:Q9WUE3}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7 for the electron donation reaction to monodehydroascorbate reaction (PubMed:23641721). Optimum pH is around 6.5 for re-reduction reaction process of the oxidized heme with ascorbate (PubMed:23641721). {ECO:0000269|PubMed:23641721}; | null | FUNCTION: Transmembrane reductase that may use ascorbate as an electron donor in the cytoplasm and transfer electrons across endoplasmic reticulum membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in the lumen of that compartment. {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}. | Homo sapiens (Human) |
O14576 | DC1I1_HUMAN | MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTASVAIEGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA | null | null | transport along microtubule [GO:0010970]; vesicle transport along microtubule [GO:0047496] | cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; kinetochore [GO:0000776]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; spindle pole [GO:0000922]; vesicle [GO:0031982] | cytoskeletal motor activity [GO:0003774]; dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; spectrin binding [GO:0030507] | PF11540;PF00400; | 2.130.10.10; | Dynein intermediate chain family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19229290}. | null | null | null | null | null | FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores. | Homo sapiens (Human) |
O14578 | CTRO_HUMAN | MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFEECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATGDIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGGDLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDFGSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGRSPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFFSKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPNIFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGTPARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV | 2.7.11.1 | null | actomyosin structure organization [GO:0031032]; generation of neurons [GO:0048699]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; negative regulation of hippo signaling [GO:0035331]; neuron apoptotic process [GO:0051402]; phosphorylation [GO:0016310]; positive regulation of cytokinesis [GO:0032467] | actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine kinase inhibitor activity [GO:0030291]; scaffold protein binding [GO:0097110]; SH3 domain binding [GO:0017124]; transcription coactivator binding [GO:0001223] | PF00780;PF00169;PF00069;PF00433; | 1.10.287.1490;1.20.5.340;3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | 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: Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:27453578}. | Homo sapiens (Human) |
O14579 | COPE_HUMAN | MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPERDVERDVFLYRAYLAQRKFGVVLDEIKPSSAPELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFLLMAASIYLHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDEDATLTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHMAQGRWEAAEGLLQEALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYQAKENDFDRLVLQYAPSA | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein localization to axon [GO:0099612]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890] | COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; transport vesicle [GO:0030133] | structural molecule activity [GO:0005198] | PF04733; | 1.25.40.10; | COPE family | PTM: Phosphorylated by PKA.; PTM: Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation. {ECO:0000269|PubMed:17721809}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}. | null | null | null | null | null | FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14593 | RFXK_HUMAN | MELTQPAEDLIQTQQTPASELGDPEDPGEEAADGSDTVVLSLFPCTPEPVNPEPDASVSSPQAGSSLKHSTTLTNRQRGNEVSALPATLDSLSIHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKVQQVIENHILKLFQSNLVPADPE | null | null | positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of transcription by RNA polymerase II [GO:0045944]; Ras protein signal transduction [GO:0007265]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; intercellular bridge [GO:0045171]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; histone deacetylase binding [GO:0042826] | PF12796; | 1.25.40.20; | null | PTM: Phosphorylated by RAF1. {ECO:0000250|UniProtKB:Q9Z205}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z205}. Nucleus {ECO:0000250|UniProtKB:Q9Z205}. | null | null | null | null | null | FUNCTION: Activates transcription from class II MHC promoters. Activation requires the activity of the MHC class II transactivator/CIITA. May regulate other genes in the cell. RFX binds the X1 box of MHC-II promoters (PubMed:10072068, PubMed:10725724, PubMed:9806546). May also potentiate the activation of RAF1 (By similarity). {ECO:0000250|UniProtKB:Q9Z205, ECO:0000269|PubMed:10072068, ECO:0000269|PubMed:10725724, ECO:0000269|PubMed:9806546}.; FUNCTION: Isoform 2 is not involved in the positive regulation of MHC class II genes. {ECO:0000269|PubMed:10072068}. | Homo sapiens (Human) |
O14594 | NCAN_HUMAN | MGAPFVWALGLLMLQMLLFVAGEQGTQDITDASERGLHMQKLGSGSVQAALAELVALPCLFTLQPRPSAARDAPRIKWTKVRTASGQRQDLPILVAKDNVVRVAKSWQGRVSLPSYPRRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRSYGRRNPQELYDVYCFARELGGEVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGFPSPAERFDAYCFRAHHPTSQHGDLETPSSGDEGEILSAEGPPVRELEPTLEEEEVVTPDFQEPLVSSGEEETLILEEKQESQQTLSPTPGDPMLASWPTGEVWLSTVAPSPSDMGAGTAASSHTEVAPTDPMPRRRGRFKGLNGRYFQQQEPEPGLQGGMEASAQPPTSEAAVNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPHPTPISTEANRVEAHGEATATAPPSPAAETKVYSLPLSLTPTGQGGEAMPTTPESPRADFRETGETSPAQVNKAEHSSSSPWPSVNRNVAVGFVPTETATEPTGLRGIPGSESGVFDTAESPTSGLQATVDEVQDPWPSVYSKGLDASSPSAPLGSPGVFLVPKVTPNLEPWVATDEGPTVNPMDSTVTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKVGVPAMSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLPVTLGIEDFELEVLAGSPGVESFWEEVASGEEPALPGTPMNAGAEEVHSDPCENNPCLHGGTCNANGTMYGCSCDQGFAGENCEIDIDDCLCSPCENGGTCIDEVNGFVCLCLPSYGGSFCEKDTEGCDRGWHKFQGHCYRYFAHRRAWEDAEKDCRRRSGHLTSVHSPEEHSFINSFGHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKGTVLCGPPPAVENASLIGARKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVCTKPRRSHRMRRHHHHHQHHHQHHHHKSRKERRKHKKHPTEDWEKDEGNFC | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; perineuronal net [GO:0072534]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; hyaluronic acid binding [GO:0005540] | PF00008;PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;2.10.25.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458}. | null | null | null | null | null | FUNCTION: May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid. | Homo sapiens (Human) |
O14595 | CTDS2_HUMAN | MEHGSIITQARREDALVLTKQGLVSKSSPKKPRGRNIFKALFCCFRAQHVGQSSSSTELAAYKEEANTIAKSDLLQCLQYQFYQIPGTCLLPEVTEEDQGRICVVIDLDETLVHSSFKPINNADFIVPIEIEGTTHQVYVLKRPYVDEFLRRMGELFECVLFTASLAKYADPVTDLLDRCGVFRARLFRESCVFHQGCYVKDLSRLGRDLRKTLILDNSPASYIFHPENAVPVQSWFDDMADTELLNLIPIFEELSGAEDVYTSLGQLRAP | 3.1.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per monomer.; | negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of protein phosphorylation [GO:0001933]; protein dephosphorylation [GO:0006470] | nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; RNA polymerase II CTD heptapeptide repeat phosphatase activity [GO:0008420] | PF03031; | 3.40.50.1000; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | 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; 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; | null | null | null | null | FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas. {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}. | Homo sapiens (Human) |
O14607 | UTY_HUMAN | MKSCAVSLTTAAVAFGDEAKKMAEGKASRESEEESVSLTVEEREALGGMDSRLFGFVRLHEDGARTKTLLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKRCSNTSTLAARIKFLQNGSDNWNGGQSLSHHPVQQVYSLCLTPQKLQHLEQLRANRDNLNPAQKHQLEQLESQFVLMQQMRHKEVAQVRTTGIHNGAITDSSLPTNSVSNRQPHGALTRVSSVSQPGVRPACVEKLLSSGAFSAGCIPCGTSKILGSTDTILLGSNCIAGSESNGNVPYLQQNTHTLPHNHTDLNSSTEEPWRKQLSNSAQGLHKSQSSCLSGPNEEQPLFSTGSAQYHQATSTGIKKANEHLTLPSNSVPQGDADSHLSCHTATSGGQQGIMFTKESKPSKNRSLVPETSRHTGDTSNGCADVKGLSNHVHQLIADAVSSPNHGDSPNLLIADNPQLSALLIGKANGNVGTGTCDKVNNIHPAVHTKTDHSVASSPSSAISTATPSPKSTEQRSINSVTSLNSPHSGLHTVNGEGLGKSQSSTKVDLPLASHRSTSQILPSMSVSICPSSTEVLKACRNPGKNGLSNSCILLDKCPPPRPPTSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWRCESNRSHTTIAKYAQYQASSFQESLREENEKRTQHKDHSDNESTSSENSGRRRKGPFKTIKFGTNIDLSDNKKWKLQLHELTKLPAFARVVSAGNLLTHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNNLNFLMSSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNVGPLTACQYKLAVERYEWNKLKSVKSPVPMVHLSWNMARNIKVSDPKLFEMIKYCLLKILKQYQTLREALVAAGKEVIWHGRTNDEPAHYCSICEVEVFNLLFVTNESNTQKTYIVHCHDCARKTSKSLENFVVLEQYKMEDLIQVYDQFTLALSLSSSS | 1.14.11.68 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; | heart development [GO:0007507]; regulation of gene expression [GO:0010468] | MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654] | chromatin DNA binding [GO:0031490]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF02373;PF21322;PF21326;PF13432;PF13181; | 1.20.58.1370;2.10.110.20;2.60.120.650;1.25.40.10; | UTX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.68; Evidence={ECO:0000269|PubMed:24798337}; | null | null | null | null | FUNCTION: Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity. {ECO:0000269|PubMed:24798337}. | Homo sapiens (Human) |
O14610 | GBGT2_HUMAN | MAQDLSEKDLLKMEVEQLKKEVKNTRIPISKAGKEIKEYVEAQAGNDPFLKGIPEDKNPFKEKGGCLIS | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602] | heterotrimeric G-protein complex [GO:0005834] | G-protein beta-subunit binding [GO:0031681]; GTPase activity [GO:0003924] | PF00631; | 4.10.260.10; | G protein gamma family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | Homo sapiens (Human) |
O14613 | BORG1_HUMAN | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTMVEGPEEDGTFDLPFQFTRTATVCGRELPDGPSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLETPQPSPQEGGSVDIWRIPETGSPNSGLTPESGAEEPFLSNASSLLSLHVDLGPSILDDVLQIMDQDLDSMQIPT | null | null | actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; cellular response to type II interferon [GO:0071346]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of pseudopodium assembly [GO:0031274]; regulation of cell shape [GO:0008360]; Rho protein signal transduction [GO:0007266] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096]; opioid peptide activity [GO:0001515]; small GTPase binding [GO:0031267] | PF14957;PF00786; | null | BORG/CEP family | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:11035016}; Peripheral membrane protein {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11035016}. | null | null | null | null | null | FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}. | Homo sapiens (Human) |
O14617 | AP3D1_HUMAN | MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRIGYLAASQSFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQYITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSALLDSAHLLASSTQRNGICEVLYAAAWICGEFSEHLQEPHHTLEAMLRPRVTTLPGHIQAVYVQNVVKLYASILQQKEQAGEAEGAQAVTQLMVDRLPQFVQSADLEVQERASCILQLVKHIQKLQAKDVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPLSDSESEDERPRAVFHEEEQRRPKHRPSEADEEELARRREARKQEQANNPFYIKSSPSPQKRYQDTPGVEHIPVVQIDLSVPLKVPGLPMSDQYVKLEEERRHRQKLEKDKRRKKRKEKEKKGKRRHSSLPTESDEDIAPAQQVDIVTEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPIQKHRNTETSKSPEKDVPMVEKKSKKPKKKEKKHKEKERDKEKKKEKEKKKSPKPKKKKHRKEKEERTKGKKKSKKQPPGSEEAAGEPVQNGAPEEEQLPPESSYSLLAENSYVKMTCDIRGSLQEDSQVTVAIVLENRSSSILKGMELSVLDSLNARMARPQGSSVHDGVPVPFQLPPGVSNEAQYVFTIQSIVMAQKLKGTLSFIAKNDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMSSIKVDGIRMSFQNLLAKICFHHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGENSVSVDGKCSDSTLLSNLLEEMKATLAKC | null | null | anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; clathrin-coated vesicle cargo loading, AP-3-mediated [GO:0035654]; endosome to melanosome transport [GO:0035646]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; intracellular transport [GO:0046907]; melanosome assembly [GO:1903232]; melanosome organization [GO:0032438]; neurotransmitter receptor transport, postsynaptic endosome to lysosome [GO:0098943]; platelet dense granule organization [GO:0060155]; positive regulation of NK T cell differentiation [GO:0051138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to membrane [GO:0072657]; protein targeting to vacuole [GO:0006623]; synaptic vesicle budding from endosome [GO:0016182]; synaptic vesicle coating [GO:0016183]; synaptic vesicle membrane organization [GO:0048499]; synaptic vesicle recycling [GO:0036465]; vesicle-mediated transport [GO:0016192]; zinc ion import into lysosome [GO:0140916] | AP-3 adaptor complex [GO:0030123]; axon cytoplasm [GO:1904115]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; postsynapse [GO:0098794]; presynaptic endosome [GO:0098830]; terminal bouton [GO:0043195] | null | PF01602;PF06375; | 1.25.10.10;3.30.450.50; | Adaptor complexes large subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. Involved in process of CD8+ T-cell and NK cell degranulation (PubMed:26744459). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (By similarity). {ECO:0000250|UniProtKB:O54774, ECO:0000269|PubMed:26744459}. | Homo sapiens (Human) |
O14618 | CCS_HUMAN | MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAIFRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL | null | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0007744|PDB:2RSQ}; Note=Binds 2 copper ions per subunit. {ECO:0007744|PDB:2RSQ}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10677207}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10677207}; | cellular response to oxidative stress [GO:0034599]; protein maturation by copper ion transfer [GO:0015680]; removal of superoxide radicals [GO:0019430]; superoxide metabolic process [GO:0006801] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | cadherin binding [GO:0045296]; copper ion binding [GO:0005507]; protein-disulfide reductase activity [GO:0015035]; superoxide dismutase copper chaperone activity [GO:0016532] | PF00403;PF00080; | 3.30.70.100;2.60.40.200; | Cu-Zn superoxide dismutase family | PTM: Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241. {ECO:0000269|PubMed:20154138}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9726962}. | null | null | null | null | null | FUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1). | Homo sapiens (Human) |
O14625 | CXL11_HUMAN | MSVKGMAIALAVILCATVVQGFPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell-cell signaling [GO:0007267]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; inflammatory response [GO:0006954]; neutrophil chemotaxis [GO:0030593]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; regulation of cell population proliferation [GO:0042127]; signal transduction [GO:0007165]; T cell chemotaxis [GO:0010818] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses. | Homo sapiens (Human) |
O14627 | CDX4_HUMAN | MYGSCLLEKEAGMYPGTLMSPGGDGTAGTGGTGGGGSPMPASNFAAAPAFSHYMGYPHMPSMDPHWPSLGVWGSPYSPPREDWSVYPGPSSTMGTVPVNDVTSSPAAFCSTDYSNLGPVGGGTSGSSLPGQAGGSLVPTDAGAAKASSPSRSRHSPYAWMRKTVQVTGKTRTKEKYRVVYTDHQRLELEKEFHCNRYITIQRKSELAVNLGLSERQVKIWFQNRRAKERKMIKKKISQFENSGGSVQSDSDSISPGELPNTFFTTPSAVRGFQPIEIQQVIVSE | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; blood vessel development [GO:0001568]; cell differentiation [GO:0030154]; labyrinthine layer development [GO:0060711]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | 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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF04731;PF00046; | 1.10.10.60; | Caudal homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | null | Homo sapiens (Human) |
O14628 | ZN195_HUMAN | MTLLTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWNVKRQEAADGHPEMGFHHATQACLELLGSSDLPASASQSAGITGVNHRAQPGLNVSVDKFTALCSPGVLQTVKWFLEFRCIFSLAMSSHFTQDLLPEQGIQDAFPKRILRGYGNCGLDNLYLRKDWESLDECKLQKDYNGLNQCSSTTHSKIFQYNKYVKIFDNFSNLHRRNISNTGEKPFKCQECGKSFQMLSFLTEHQKIHTGKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYKCQECNNVIKTCSVLTKNRIYAGGEHYRCEEFGKVFNQCSHLTEHEHGTEEKPCKYEECSSVFISCSSLSNQQMILAGEKLSKCETWYKGFNHSPNPSKHQRNEIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECGKAYTQSSHLSEHRRIHTGEKPYQCEECGKVFRTCSSLSNHKRTHSEEKPYTCEECGNIFKQLSDLTKHKKTHTGEKPYKCDECGKNFTQSSNLIVHKRIHTGEKPYKCEECGRVFMWFSDITKHKKTHTGEKPYKCDECGKNFTQSSNLIVHKRIHTGEKPYKCEKCGKAFTQFSHLTVHESIHT | null | null | regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF01352;PF00096;PF13912; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
O14633 | LCE2B_HUMAN | MSCQQNQQQCQPPPKCPPKCTPKCPPKCPPKCLPQCPAPCSPAVSSCCGPISGGCCGPSSGGCCNSGAGGCCLSHHRPRLFHRRRHQSPDCCESEPSGGSGCCHSSGGCC | null | null | epidermis development [GO:0008544]; keratinization [GO:0031424] | null | identical protein binding [GO:0042802] | PF14672; | null | LCE family | null | null | null | null | null | null | null | FUNCTION: Precursors of the cornified envelope of the stratum corneum. | Homo sapiens (Human) |
O14638 | ENPP3_HUMAN | MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFDASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCLQRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTLMPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLSSKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERISTLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRNLHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGGGNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLNHLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEITATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPTVPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEEFRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHYFVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVRDVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI | 3.1.4.1; 3.6.1.9 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:29717535}; Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:29717535}; | ATP metabolic process [GO:0046034]; basophil activation involved in immune response [GO:0002276]; negative regulation of inflammatory response [GO:0050728]; negative regulation of mast cell activation involved in immune response [GO:0033007]; negative regulation of mast cell proliferation [GO:0070667]; nucleoside triphosphate catabolic process [GO:0009143]; phosphate ion homeostasis [GO:0055062]; phosphate-containing compound metabolic process [GO:0006796]; pyrimidine nucleotide metabolic process [GO:0006220] | apical plasma membrane [GO:0016324]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471] | calcium ion binding [GO:0005509]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; phosphodiesterase I activity [GO:0004528]; zinc ion binding [GO:0008270] | PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylated. N-glycosylation is necessary for normal transport to the cell membrane, but is not the apical targeting signal. {ECO:0000250|UniProtKB:P97675}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11342463}; Single-pass type II membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15072822}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15072822}. Note=Detected at the cell surface of basophils (PubMed:11342463). Detected at the apical plasma membrane of bile duct cells (PubMed:15072822). Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells. {ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:15072822}. | CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000269|PubMed:11342463}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:29717535}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61.5 uM for ATP; KM=120.3 uM for UTP; KM=120.2 uM for CTP; KM=123.7 uM for GTP; | null | null | null | FUNCTION: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (PubMed:29717535). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity). Has also alkaline phosphodiesterase activity (PubMed:11342463). {ECO:0000250|UniProtKB:Q6DYE8, ECO:0000269|PubMed:11342463, ECO:0000269|PubMed:29717535}. | Homo sapiens (Human) |
O14639 | ABLM1_HUMAN | MPAFLGLKCLGKLCSSEKSKVTSSERTSARGSNRKRLIVEDRRVSGTSFTAHRRATITHLLYLCPKDYCPRGRVCNSVDPFVAHPQDPHHPSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGEYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKETTFSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGAPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPRTLSPTPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQSKSSEDIIKFSKFPAAQAPDPSETPKIETDHWPGPPSFAVVGPDMKRRSSGREEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKESRERSSLLASRYDSPINSASHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILREVDRTRLERHLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF | null | null | animal organ morphogenesis [GO:0009887]; cilium assembly [GO:0060271]; cytoskeleton organization [GO:0007010]; lamellipodium assembly [GO:0030032]; visual perception [GO:0007601] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; stress fiber [GO:0001725] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; metal ion binding [GO:0046872] | PF16182;PF00412;PF02209; | 2.10.110.10;1.10.950.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the cytoskeleton. {ECO:0000250}. | null | null | null | null | null | FUNCTION: May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269|PubMed:9245787}. | Homo sapiens (Human) |
O14640 | DVL1_HUMAN | MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNREEAARTNGHPRGDRRRDVGLPPDSASTALSSELESSSFVDSDEDGSTSRLSSSTEQSTSSRLIRKHKRRRRKQRLRQADRASSFSSITDSTMSLNIVTVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTVPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAVTRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAVVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSLLKHGFLRHTVNKITFSEQCYYVFGDLCSNLATLNLNSGSSGTSDQDTLAPLPHPAAPWPLGQGYPYQYPGPPPCFPPAYQDPGFSYGSGSTGSQQSEGSKSSGSTRSSRRAPGREKERRAAGAGGSGSESDHTAPSGVGSSWRERPAGQLSRGSSPRSQASATAPGLPPPHPTTKAYTVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; canonical Wnt signaling pathway [GO:0060070]; cochlea morphogenesis [GO:0090103]; collateral sprouting [GO:0048668]; convergent extension involved in neural plate elongation [GO:0022007]; cytoplasmic microtubule organization [GO:0031122]; dendrite morphogenesis [GO:0048813]; dendritic spine morphogenesis [GO:0060997]; heart looping [GO:0001947]; intracellular signal transduction [GO:0035556]; negative regulation of protein phosphorylation [GO:0001933]; neural tube development [GO:0021915]; neuromuscular junction development [GO:0007528]; neurotransmitter secretion [GO:0007269]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of neuron projection arborization [GO:0150012]; positive regulation of neuron projection development [GO:0010976]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein localization to presynapse [GO:1905386]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prepulse inhibition [GO:0060134]; presynapse assembly [GO:0099054]; protein localization to microtubule [GO:0035372]; protein localization to nucleus [GO:0034504]; protein stabilization [GO:0050821]; receptor clustering [GO:0043113]; regulation of DNA-templated transcription [GO:0006355]; regulation of postsynapse organization [GO:0099175]; regulation of protein localization [GO:0032880]; regulation of synaptic vesicle exocytosis [GO:2000300]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]; social behavior [GO:0035176]; synapse organization [GO:0050808]; synaptic vesicle exocytosis [GO:0016079]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071] | clathrin-coated vesicle [GO:0030136]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; lateral plasma membrane [GO:0016328]; microtubule [GO:0005874]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; Wnt signalosome [GO:1990909] | beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; small GTPase binding [GO:0031267] | PF00610;PF02377;PF00778;PF12316;PF00595; | 2.30.42.10;2.40.240.130;1.10.10.10; | DSH family | PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localizes at the cell membrane upon interaction with frizzled family members. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). | Homo sapiens (Human) |
O14641 | DVL2_HUMAN | MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHTDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM | null | null | canonical Wnt signaling pathway [GO:0060070]; cochlea morphogenesis [GO:0090103]; convergent extension involved in neural plate elongation [GO:0022007]; heart development [GO:0007507]; heart looping [GO:0001947]; intracellular signal transduction [GO:0035556]; neural tube closure [GO:0001843]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of neuron projection arborization [GO:0150012]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization [GO:0008104]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; segment specification [GO:0007379]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071] | aggresome [GO:0016235]; apical part of cell [GO:0045177]; clathrin-coated endocytic vesicle [GO:0045334]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lateral plasma membrane [GO:0016328]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; protein-macromolecule adaptor activity [GO:0030674]; small GTPase binding [GO:0031267] | PF00610;PF02377;PF00778;PF12316;PF00595; | 2.30.42.10;2.40.240.130;1.10.10.10; | DSH family | PTM: Phosphorylated by CSNK1D (PubMed:21422228, PubMed:9192851). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (PubMed:25805136). {ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:9192851}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q60838}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q60838}; Cytoplasmic side {ECO:0000250|UniProtKB:Q60838}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q60838}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q60838}. Nucleus {ECO:0000269|PubMed:25805136}. Note=Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity). Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136). {ECO:0000250|UniProtKB:Q60838, ECO:0000269|PubMed:25805136}. | null | null | null | null | null | FUNCTION: Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. {ECO:0000250|UniProtKB:Q60838, ECO:0000269|PubMed:19252499}. | Homo sapiens (Human) |
O14645 | IDLC_HUMAN | MIPPADSLLKYDTPVLVSRNTEKRSPKARLLKVSPQQPGPSGSAPQPPKTKLPSTPCVPDPTKQAEEILNAILPPREWVEDTQLWIQQVSSTPSTRMDVVHLQEQLDLKLQQRQARETGICPVRRELYSQCFDELIREVTINCAERGLLLLRVRDEIRMTIAAYQTLYESSVAFGMRKALQAEQGKSDMERKIAELETEKRDLERQVNEQKAKCEATEKRESERRQVEEKKHNEEIQFLKRTNQQLKAQLEGIIAPKK | null | null | sperm flagellum assembly [GO:0120316] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dynein axonemal particle [GO:0120293]; dynein complex [GO:0030286]; filopodium [GO:0030175]; motile cilium [GO:0031514]; sperm flagellum [GO:0036126] | dynein heavy chain binding [GO:0045504] | PF10211; | null | Inner dynein arm light chain family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:27120127}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:31178125}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6GN86}. Cytoplasm {ECO:0000269|PubMed:36792588}. | null | null | null | null | null | FUNCTION: Involved in sperm flagellum assembly. {ECO:0000269|PubMed:36792588}. | Homo sapiens (Human) |
O14646 | CHD1_HUMAN | MNGHSDEESVRNSSGESSQSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSESGSQSESESDTSRENKVQAKPPKVDGAEFWKSSPSILAVQRSAILKKQQQQQQQQQHQASSNSGSEEDSSSSEDSDDSSSEVKRKKHKDEDWQMSGSGSPSQSGSDSESEEEREKSSCDETESDYEPKNKVKSRKPQNRSKSKNGKKILGQKKRQIDSSEEDDDEEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEEEEFETIERFMDCRIGRKGATGATTTIYAVEADGDPNAGFEKNKEPGEIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETKRWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALISKKFQACIDEYFSRNQSKTTPFKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWTHHQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSALQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIFSQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETHENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEDQRRRLEEEERQKELEEIYMLPRMRNCAKQISFNGSEGRRSRSRRYSGSDSDSISEGKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGELVHNGCIKALKDSSSGTERTGGRLGKVKGPTFRISGVQVNAKLVISHEEELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSNLLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKKEALSGAGSSKRRKARAKKNKAMKSIKVKEEIKSDSSPLPSEKSDEDDDKLSESKSDGRERSKKSSVSDAPVHITASGEPVPISEESEELDQKTFSICKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLKEYTNPEQIKQWRKNLWIFVSKFTEFDARKLHKLYKHAIKKRQESQQNSDQNSNLNPHVIRNPDVERLKENTNHDDSSRDSYSSDRHLTQYHDHHKDRHQGDSYKKSDSRKRPYSSFSNGKDHRDWDHYKQDSRYYSDREKHRKLDDHRSRDHRSNLEGSLKDRSHSDHRSHSDHRLHSDHRSSSEYTHHKSSRDYRYHSDWQMDHRASSSGPRSPLDQRSPYGSRSPFEHSVEHKSTPEHTWSSRKT | 3.6.4.12 | null | chromatin remodeling [GO:0006338]; nucleosome organization [GO:0034728]; positive regulation by host of viral transcription [GO:0043923]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; methylated histone binding [GO:0035064] | PF18375;PF13907;PF00385;PF00271;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40201}. Cytoplasm {ECO:0000250|UniProtKB:P40201}. Note=Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis. {ECO:0000250|UniProtKB:P40201}. | 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=3.6.4.12; | null | null | null | null | FUNCTION: ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250|UniProtKB:P40201, ECO:0000269|PubMed:18042460, ECO:0000269|PubMed:28866611}. | Homo sapiens (Human) |
O14647 | CHD2_HUMAN | MMRNKDKSQEEDSSLHSNASSHSASEEASGSDSGSQSESEQGSDPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNIKEEASSGSESGSPKRRGQRQLKKQEKWKQEPSEDEQEQGTSAESEPEQKKVKARRPVPRRTVPKPRVKKQPKTQRGKRKKQDSSDEDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSDDLIEMTGEGVDEQQDNSETIEKVLDSRLGKKGATGASTTVYAIEANGDPSGDFDTEKDEGEIQYLIKWKGWSYIHSTWESEESLQQQKVKGLKKLENFKKKEDEIKQWLGKVSPEDVEYFNCQQELASELNKQYQIVERVIAVKTSKSTLGQTDFPAHSRKPAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSRNNSKTIPTRECKALKQRPRFVALKKQPAYLGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGTRGSTSGFLNIVMELKKCCNHCYLIKPPEENERENGQEILLSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRMDTTGRTILENNSGRSNSNPFNKEELTAILKFGAEDLFKELEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQFKVANFATMEDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYMLPRIRSSTKKAQTNDSDSDTESKRQAQRSSASESETEDSDDDKKPKRRGRPRSVRKDLVEGFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCVSAMQEYEEQLKENASEGKGPGKRRGPTIKISGVQVNVKSIIQHEEEFEMLHKSIPVDPEEKKKYCLTCRVKAAHFDVEWGVEDDSRLLLGIYEHGYGNWELIKTDPELKLTDKILPVETDKKPQGKQLQTRADYLLKLLRKGLEKKGAVTGGEEAKLKKRKPRVKKENKVPRLKEEHGIELSSPRHSDNPSEEGEVKDDGLEKSPMKKKQKKKENKENKEKQMSSRKDKEGDKERKKSKDKKEKPKSGDAKSSSKSKRSQGPVHITAGSEPVPIGEDEDDDLDQETFSICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYSDQEHIKLWRRNLWIFVSKFTEFDARKLHKLYKMAHKKRSQEEEEQKKKDDVTGGKKPFRPEASGSSRDSLISQSHTSHNLHPQKPHLPASHGPQMHGHPRDNYNHPNKRHFSNADRGDWQRERKFNYGGGNNNPPWGSDRHHQYEQHWYKDHHYGDRRHMDAHRSGSYRPNNMSRKRPYDQYSSDRDHRGHRDYYDRHHHDSKRRRSDEFRPQNYHQQDFRRMSDHRPAMGYHGQGPSDHYRSFHTDKLGEYKQPLPPLHPAVSDPRSPPSQKSPHDSKSPLDHRSPLERSLEQKNNPDYNWNVRKT | 3.6.4.12 | null | DNA damage response [GO:0006974]; gene expression [GO:0010467]; hematopoietic stem cell differentiation [GO:0060218]; muscle organ development [GO:0007517]; nucleosome organization [GO:0034728]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF18375;PF13907;PF00385;PF00271;PF00176; | 2.40.50.40;6.10.140.1440;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binds to myogenic gene promoters. {ECO:0000250}. | 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=3.6.4.12; | null | null | null | null | FUNCTION: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14649 | KCNK3_HUMAN | MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPELIERQRLELRQQELRARYNLSQGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTLVRYLLHRAKKGLGMRRADVSMANMVLIGFFSCISTLCIGAAAFSHYEHWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTRNGQAGGGGGGGSAHTTDTASSTAAAGGGGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEQSHSSPGGGGRYSDTPSRRCLCSGAPRSAISSVSTGLHSLSTFRGLMKRRSSV | null | null | cellular response to hypoxia [GO:0071456]; cellular response to zinc ion [GO:0071294]; chemical synaptic transmission [GO:0007268]; cochlea development [GO:0090102]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to xenobiotic stimulus [GO:0009410]; stabilization of membrane potential [GO:0030322] | plasma membrane [GO:0005886]; synapse [GO:0045202] | monoatomic ion channel activity [GO:0005216]; open rectifier potassium channel activity [GO:0005252]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; S100 protein binding [GO:0044548] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. {ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:9312005}. | Homo sapiens (Human) |
O14653 | GOSR2_HUMAN | MDPLFQQTHKQVHEIQSCMGRLETADKQSVHIVENEIQASIDQIFSRLERLEILSSKEPPNKRQNARLRVDQLKYDVQHLQTALRNFQHRRHAREQQERQREELLSRTFTTNDSDTTIPMDESLQFNSSLQKVHNGMDDLILDGHNILDGLRTQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCVVMFLVVQYLT | null | null | intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF12352; | 1.20.58.400; | GOSR2 family | null | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:21549339}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:9349823}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35165}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000250|UniProtKB:O35165}. | null | null | null | null | null | FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000269|PubMed:9349823}. | Homo sapiens (Human) |
O14654 | IRS4_HUMAN | MASCSFTRDQATRRLRGAAAAAAAALAAVVTTPLLSSGTPTALIGTGSSCPGAMWLSTATGSRSDSESEEEDLPVGEEVCKRGYLRKQKHGHRRYFVLKLETADAPARLEYYENARKFRHSVRAAAAAAAAAASGAAIPPLIPPRRVITLYQCFSVSQRADARYRHLIALFTQDEYFAMVAENESEQESWYLLLSRLILESKRRRCGTLGAQPDGEPAALAAAAAAEPPFYKDVWQVIVKPRGLGHRKELSGVFRLCLTDEEVVFVRLNTEVASVVVQLLSIRRCGHSEQYFFLEVGRSTVIGPGELWMQVDDCVVAQNMHELFLEKMRALCADEYRARCRSYSISIGAHLLTLLSARRHLGLVPLEPGGWLRRSRFEQFCHLRAIGDGEDEMLFTRRFVTPSEPVAHSRRGRLHLPRGRRSRRAVSVPASFFRRLAPSPARPRHPAEAPNNGARLSSEVSGSGSGNFGEEGNPQGKEDQEGSGGDYMPMNNWGSGNGRGSGGGQGSNGQGSSSHSSGGNQCSGEGQGSRGGQGSNGQGSGGNQCSRDGQGTAGGHGSGGGQRPGGGHGSGGGQGPGDGHGSGGGKNSGGGKGSGSGKGSDGDGERGKSLKKRSYFGKLTQSKQQQMPPPPPPPPPPPPAGGTGGKGKSGGRFRLYFCVDRGATKECKEAKEVKDAEIPEGAARGPHRARAFDEDEDDPYVPMRPGVATPLVSSSDYMPMAPQNVSASKKRHSRSPFEDSRGYMMMFPRVSPPPAPSPPKAPDTNKEDDSKDNDSESDYMFMAPGAGAIPKNPRNPQGGSSSKSWSSYFSLPNPFRSSPLGQNDNSEYVPMLPGKFLGRGLDKEVSYNWDPKDAASKPSGEGSFSKPGDGGSPSKPSDHEPPKNKAKRPNRLSFITKGYKIKPKPQKPTHEQREADSSSDYVNMDFTKRESNTPAPSTQGLPDSWGIIAEPRQSAFSNYVNVEFGVPFPNPANDLSDLLRAIPRANPLSLDSARWPLPPLPLSATGSNAIEEEGDYIEVIFNSAMTPAMALADSAIRYDAETGRIYVVDPFSECCMDISLSPSRCSEPPPVARLLQEEEQERRRPQSRSQSFFAAARAAVSAFPTDSLERDLSPSSAPAVASAAEPTLALSQVVAAASALAAAPGIGAAAAAAGFDSASARWFQPVANAADAEAVRGAQDVAGGSNPGAHNPSANLARGDNQAGGAAAAAAAPEPPPRSRRVPRPPEREDSDNDDDTHVRMDFARRDNQFDSPKRGR | null | null | insulin receptor signaling pathway [GO:0008286]; signal transduction [GO:0007165] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | insulin receptor binding [GO:0005158]; phosphatidylinositol 3-kinase binding [GO:0043548] | PF02174; | 2.30.29.30; | null | PTM: Phosphorylated on tyrosine residues in response to both insulin and IGF1 signaling. Phosphorylated on Tyr-921 in response to FGF2 signaling. Phosphorylation of Tyr-921 is required for GRB2, phospholipase C-gamma and phosphatidylinositol 3-kinase interaction. {ECO:0000269|PubMed:15316024, ECO:0000269|PubMed:9261155, ECO:0000269|PubMed:9553137}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9553137}; Peripheral membrane protein {ECO:0000269|PubMed:9553137}; Cytoplasmic side {ECO:0000269|PubMed:9553137}. | null | null | null | null | null | FUNCTION: Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. {ECO:0000269|PubMed:10531310, ECO:0000269|PubMed:10594015, ECO:0000269|PubMed:12639902, ECO:0000269|PubMed:17408801, ECO:0000269|PubMed:9553137}. | Homo sapiens (Human) |
O14656 | TOR1A_HUMAN | MKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIILNAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHALSVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEERVFSDKGCKTVFTKLDYYYDD | 3.6.4.- | null | cell adhesion [GO:0007155]; chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated protein folding [GO:0061077]; ERAD pathway [GO:0036503]; intermediate filament cytoskeleton organization [GO:0045104]; neuron projection development [GO:0031175]; nuclear envelope organization [GO:0006998]; nuclear membrane organization [GO:0071763]; organelle organization [GO:0006996]; positive regulation of synaptic vesicle endocytosis [GO:1900244]; protein deneddylation [GO:0000338]; protein localization to nucleus [GO:0034504]; regulation of dopamine uptake involved in synaptic transmission [GO:0051584]; regulation of protein localization to cell surface [GO:2000008]; response to oxidative stress [GO:0006979]; synaptic vesicle membrane organization [GO:0048499]; synaptic vesicle transport [GO:0048489]; wound healing, spreading of cells [GO:0044319] | cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; secretory granule [GO:0030141]; synaptic vesicle [GO:0008021] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894]; misfolded protein binding [GO:0051787]; unfolded protein binding [GO:0051082] | PF21376;PF06309; | 3.40.50.300; | ClpA/ClpB family, Torsin subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:10871631, ECO:0000269|PubMed:15147511, ECO:0000269|PubMed:17037984}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:29053766}. Nucleus membrane {ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:29053766}; Peripheral membrane protein {ECO:0000305}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasm, cytoskeleton. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}. | 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; Evidence={ECO:0000269|PubMed:23569223}; | null | null | null | null | FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues. {ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24930953}. | Homo sapiens (Human) |
O14657 | TOR1B_HUMAN | MLRAGWLRGAAALALLLAARVVAAFEPITVGLAIGAASAITGYLSYNDIYCRFAECCREERPLNASALKLDLEEKLFGQHLATEVIFKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLHPKGLKSNFVHLFVSTLHFPHEQKIKLYQDQLQKWIRGNVSACANSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGVSYRKAIFIFLSNAGGDLITKTALDFWRAGRKREDIQLKDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYRHVKMCVRAEMRARGSAIDEDIVTRVAEEMTFFPRDEKIYSDKGCKTVQSRLDFH | 3.6.4.- | null | chaperone cofactor-dependent protein refolding [GO:0051085]; endoplasmic reticulum organization [GO:0007029]; nuclear membrane organization [GO:0071763]; protein localization to nucleus [GO:0034504]; response to unfolded protein [GO:0006986] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894] | PF21376;PF06309; | 3.40.50.300; | ClpA/ClpB family, Torsin subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:15147511}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}. | 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; Evidence={ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}; | null | null | null | null | FUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}. | Homo sapiens (Human) |
O14662 | STX16_HUMAN | MATRRLTDAFLLLRNNSIQNRQLLAEQVSSHITSSPLHSRSIAAELDELADDRMALVSGISLDPEAAIGVTKRPPPKWVDGVDEIQYDVGRIKQKMKELASLHDKHLNRPTLDDSSEEEHAIEITTQEITQLFHRCQRAVQALPSRARACSEQEGRLLGNVVASLAQALQELSTSFRHAQSGYLKRMKNREERSQHFFDTSVPLMDDGDDNTLYHRGFTEDQLVLVEQNTLMVEEREREIRQIVQSISDLNEIFRDLGAMIVEQGTVLDRIDYNVEQSCIKTEDGLKQLHKAEQYQKKNRKMLVILILFVIIIVLIVVLVGVKSR | null | null | endocytic recycling [GO:0032456]; intracellular protein transport [GO:0006886]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905] | PF05739;PF00804; | 1.20.58.70; | Syntaxin family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein.; SUBCELLULAR LOCATION: [Isoform C]: Cytoplasm. | null | null | null | null | null | FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}. | Homo sapiens (Human) |
O14669 | TMG2_HUMAN | MRGHPSLLLLYMALTTCLDTSPSEETDQEVFLGPPEAQSFLSSHTRIPRANHWDLELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYIYNGKGGRGRVDVASLAVGLTGGILLIVLAGLGAFWYLRWRQHRGQQPCPQEAGLISPLSPLNPLGPPTPLPPPPPPPPGLPTYEQALAASGVHDAPPPPYTSLRRPH | null | null | null | extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509] | PF00594; | 4.10.740.10; | null | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:17502622}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17502622}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | null | Homo sapiens (Human) |
O14672 | ADA10_HUMAN | MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR | 3.4.24.81 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:29224781}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:29224781}; | adherens junction organization [GO:0034332]; amyloid precursor protein catabolic process [GO:0042987]; cell-cell signaling [GO:0007267]; cochlea development [GO:0090102]; constitutive protein ectodomain proteolysis [GO:0051089]; epidermal growth factor receptor ligand maturation [GO:0038004]; extracellular matrix disassembly [GO:0022617]; in utero embryonic development [GO:0001701]; integrin-mediated signaling pathway [GO:0007229]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte activation [GO:0042117]; negative regulation of cell adhesion [GO:0007162]; negative regulation of gene expression [GO:0010629]; Notch signaling pathway [GO:0007219]; pore complex assembly [GO:0046931]; 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 T cell chemotaxis [GO:0010820]; postsynapse organization [GO:0099173]; protein catabolic process at postsynapse [GO:0140249]; protein phosphorylation [GO:0006468]; protein processing [GO:0016485]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of Notch signaling pathway [GO:0008593]; regulation of postsynapse organization [GO:0099175]; regulation of vasculature development [GO:1901342]; response to tumor necrosis factor [GO:0034612] | adherens junction [GO:0005912]; axon [GO:0030424]; cell surface [GO:0009986]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle [GO:0005798]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; pore complex [GO:0046930]; postsynaptic density [GO:0014069]; specific granule membrane [GO:0035579]; synaptic membrane [GO:0097060]; tertiary granule membrane [GO:0070821]; tetraspanin-enriched microdomain [GO:0097197] | endopeptidase activity [GO:0004175]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; metalloendopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902945]; metallopeptidase activity [GO:0008237]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; signaling receptor binding [GO:0005102] | PF21299;PF00200;PF13574; | 3.40.390.10;4.10.70.10; | null | PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20624979, ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:24990881, ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:29430990, ECO:0000269|PubMed:30463011}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:12475894}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:12475894}. Cell projection, axon {ECO:0000250|UniProtKB:O35598}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35598}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011}. Cytoplasm {ECO:0000269|PubMed:30463011}. Note=Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (PubMed:12475894). During long term depression, it is recruited to the cell membrane by DLG1 (PubMed:23676497). The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane (PubMed:30463011). The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11 (PubMed:30463011). {ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:30463011}. | CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905, ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900, ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:29224781, ECO:0000269|PubMed:29430990, ECO:0000269|PubMed:37516108, ECO:0000305|PubMed:24990881}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for substrate (in complex with TSPAN15) {ECO:0000269|PubMed:37516108}; | null | null | null | FUNCTION: Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed:11786905, PubMed:12475894, PubMed:20592283, PubMed:24990881, PubMed:26686862, PubMed:28600292, PubMed:31792032). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed:26686862, PubMed:28600292, PubMed:31792032, PubMed:34739841, PubMed:37516108). Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:11786905, PubMed:26686862, PubMed:29224781, PubMed:34739841). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE-cadherin/CDH5 in endothelial cells (PubMed:28600292). {ECO:0000250|UniProtKB:O35598, ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905, ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900, ECO:0000269|PubMed:24990881, ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:26876177, ECO:0000269|PubMed:28600292, ECO:0000269|PubMed:29224781, ECO:0000269|PubMed:31792032, ECO:0000269|PubMed:34739841, ECO:0000269|PubMed:37516108}.; FUNCTION: (Microbial infection) Promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting formation of toxin pores. {ECO:0000269|PubMed:20624979, ECO:0000269|PubMed:30463011}. | Homo sapiens (Human) |
O14678 | ABCD4_HUMAN | MAVAGPAPGAGARPRLDLQFLQRFLQILKVLFPSWSSQNALMFLTLLCLTLLEQFVIYQVGLIPSQYYGVLGNKDLEGFKTLTFLAVMLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHRLYFRGRAYYTLNVLRDDIDNPDQRISQDVERFCRQLSSMASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPAELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLRETLLDMSLKSQDCEILGESEWGLDTPPGWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWELMRIKVE | 7.6.2.8 | null | cellular response to leukemia inhibitory factor [GO:1990830]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; fatty acid beta-oxidation [GO:0006635]; long-chain fatty acid import into peroxisome [GO:0015910]; peroxisome organization [GO:0007031]; transmembrane transport [GO:0055085]; very long-chain fatty acid catabolic process [GO:0042760] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; identical protein binding [GO:0042802]; long-chain fatty acid transporter activity [GO:0005324] | PF06472;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27456980}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:22922874, ECO:0000269|PubMed:25535791, ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511, ECO:0000269|PubMed:33845046}; Multi-pass membrane protein {ECO:0000255}. Note=Targeted by LMBRD1 lysosomal chaperone to the lysosomal membrane. {ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511}. | CATALYTIC ACTIVITY: Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216; EC=7.6.2.8; Evidence={ECO:0000269|PubMed:33845046, ECO:0000305|PubMed:28572511, ECO:0000305|PubMed:31467407}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17874; Evidence={ECO:0000305|PubMed:33845046}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=426 uM for cobalamin {ECO:0000269|PubMed:33845046}; Vmax=667 pmol/min/mg enzyme toward cobalamin {ECO:0000269|PubMed:33845046}; Vmax=11.8 nmol/min/mg enzyme toward ATP {ECO:0000269|PubMed:31467407}; | null | null | null | FUNCTION: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner (PubMed:22922874, PubMed:28572511, PubMed:31467407, PubMed:33845046). Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane (PubMed:27456980). Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to transport cobalamin across the lysosomal membrane (PubMed:25535791). {ECO:0000269|PubMed:22922874, ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511, ECO:0000269|PubMed:31467407, ECO:0000269|PubMed:33845046, ECO:0000303|PubMed:25535791}. | Homo sapiens (Human) |
O14681 | EI24_HUMAN | MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTSAEKFPSPHPSPAKLKATAGH | null | null | apoptotic process [GO:0006915]; macroautophagy [GO:0016236]; negative regulation of cell growth [GO:0030308] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nuclear membrane [GO:0031965] | importin-alpha family protein binding [GO:0061676] | PF07264; | null | EI24 family | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:21154811}; Multi-pass membrane protein {ECO:0000269|PubMed:21154811}. Cytoplasm {ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O14682 | ENC1_HUMAN | MSVSVHENRKSRASSGSINIYLFHKSSYADSVLTHLNLLRQQRLFTDVLLHAGNRTFPCHRAVLAACSRYFEAMFSGGLKESQDSEVNFDNSIHPEVLELLLDYAYSSRVIINEENAESLLEAGDMLEFQDIRDACAEFLEKNLHPTNCLGMLLLSDAHQCTKLYELSWRMCLSNFQTIRKNEDFLQLPQDMVVQLLSSEELETEDERLVYESAINWISYDLKKRYCYLPELLQTVRLALLPAIYLMENVAMEELITKQRKSKEIVEEAIRCKLKILQNDGVVTSLCARPRKTGHALFLLGGQTFMCDKLYLVDQKAKEIIPKADIPSPRKEFSACAIGCKVYITGGRGSENGVSKDVWVYDTLHEEWSKAAPMLVARFGHGSAELKHCLYVVGGHTAATGCLPASPSVSLKQVEHYDPTINKWTMVAPLREGVSNAAVVSAKLKLFAFGGTSVSHDKLPKVQCYDQCENRWTVPATCPQPWRYTAAAVLGNQIFIMGGDTEFSACSAYKFNSETYQWTKVGDVTAKRMSCHAVASGNKLYVVGGYFGIQRCKTLDCYDPTLDVWNSITTVPYSLIPTAFVSTWKHLPS | null | null | negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; positive regulation of neuron projection development [GO:0010976]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; protein ubiquitination [GO:0016567] | chromatin [GO:0000785]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; neuronal cell body [GO:0043025]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | actin binding [GO:0003779] | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | null | PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination. {ECO:0000269|PubMed:15983046}. | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:19424503}. Cytoplasm {ECO:0000269|PubMed:19424503}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19424503}. | null | null | null | null | null | FUNCTION: Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin-mediated proteasomal degradation mechanism. {ECO:0000269|PubMed:19424503}. | Homo sapiens (Human) |
O14684 | PTGES_HUMAN | MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL | 1.11.1.-; 2.5.1.18; 5.3.99.3 | COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:12460774, ECO:0000269|PubMed:12672824, ECO:0000269|PubMed:18682561, ECO:0000269|PubMed:27684486}; | cell population proliferation [GO:0008283]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of prostaglandin secretion [GO:0032308]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]; regulation of fever generation [GO:0031620]; regulation of inflammatory response [GO:0050727]; sensory perception of pain [GO:0019233]; signal transduction [GO:0007165] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471] | glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; prostaglandin-D synthase activity [GO:0004667]; prostaglandin-E synthase activity [GO:0050220] | PF01124; | 1.20.120.550; | MAPEG family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:16439136, ECO:0000269|PubMed:18682561, ECO:0000269|PubMed:27684486}; Multi-pass membrane protein {ECO:0000303|PubMed:18682561}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10869354}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000269|PubMed:10869354}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12460774, ECO:0000269|PubMed:12672824, ECO:0000269|PubMed:16439136, ECO:0000269|PubMed:18682561, ECO:0000269|PubMed:26755582, ECO:0000269|PubMed:27684486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894; Evidence={ECO:0000305|PubMed:10377395, ECO:0000305|PubMed:12460774, ECO:0000305|PubMed:12672824, ECO:0000305|PubMed:16439136}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin E2; Xref=Rhea:RHEA:53324, ChEBI:CHEBI:85166, ChEBI:CHEBI:137172; Evidence={ECO:0000269|PubMed:12244105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325; Evidence={ECO:0000305|PubMed:12244105}; CATALYTIC ACTIVITY: Reaction=prostaglandin G2 = (15S)-15-hydroperoxy-prostaglandin E2; Xref=Rhea:RHEA:64364, ChEBI:CHEBI:82629, ChEBI:CHEBI:152564; Evidence={ECO:0000269|PubMed:12672824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365; Evidence={ECO:0000305|PubMed:12672824}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:12672824, ECO:0000269|PubMed:27684486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51221; Evidence={ECO:0000305|PubMed:27684486}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:12244105}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for glutathione {ECO:0000269|PubMed:12460774}; KM=160 uM for prostaglandin H2 (at 37 degrees) {ECO:0000269|PubMed:12672824}; KM=71 uM for glutathione (at 37 degrees) {ECO:0000269|PubMed:12672824}; KM=160 uM for prostaglandin G2 (at 37 degrees) {ECO:0000269|PubMed:12672824}; KM=14 uM for prostaglandin H2 {ECO:0000269|PubMed:12460774}; KM=130 uM for prostaglandin H2 {ECO:0000269|PubMed:16439136}; Vmax=170 umol/min/mg enzyme with prostaglandin H2 as substrate {ECO:0000269|PubMed:12672824}; Note=kcat is 50 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 75 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 21 sec(-1) for glutathione as substrate (PubMed:12672824). {ECO:0000269|PubMed:12672824}; | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:10869354}. | null | null | FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:10377395, PubMed:10869354, PubMed:12244105, PubMed:12460774, PubMed:12672824, PubMed:18682561). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2 (PubMed:12244105, PubMed:12672824). In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (PubMed:12672824). {ECO:0000250|UniProtKB:Q9JM51, ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12460774, ECO:0000269|PubMed:12672824, ECO:0000269|PubMed:18682561}. | Homo sapiens (Human) |
O14686 | KMT2D_HUMAN | MDSQKLAGEDKDSEPAADGPAASEDPSATESDLPNPHVGEVSVLSSGSPRLQETPQDCSGGPVRRCALCNCGEPSLHGQRELRRFELPFDWPRCPVVSPGGSPGPNEAVLPSEDLSQIGFPEGLTPAHLGEPGGSCWAHHWCAAWSAGVWGQEGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLLCPEHSEGAAYLEEARCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPECKVCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKACRVCRACGAGSAELNPNSEWFENYSLCHRCHKAQGGQTIRSVAEQHTPVCSRFSPPEPGDTPTDEPDALYVACQGQPKGGHVTSMQPKEPGPLQCEAKPLGKAGVQLEPQLEAPLNEEMPLLPPPEESPLSPPPEESPTSPPPEASRLSPPPEELPASPLPEALHLSRPLEESPLSPPPEESPLSPPPESSPFSPLEESPLSPPEESPPSPALETPLSPPPEASPLSPPFEESPLSPPPEELPTSPPPEASRLSPPPEESPMSPPPEESPMSPPPEASRLFPPFEESPLSPPPEESPLSPPPEASRLSPPPEDSPMSPPPEESPMSPPPEVSRLSPLPVVSRLSPPPEESPLSPPPEESPTSPPPEASRLSPPPEDSPTSPPPEDSPASPPPEDSLMSLPLEESPLLPLPEEPQLCPRSEGPHLSPRPEEPHLSPRPEEPHLSPQAEEPHLSPQPEEPCLCAVPEEPHLSPQAEGPHLSPQPEELHLSPQTEEPHLSPVPEEPCLSPQPEESHLSPQSEEPCLSPRPEESHLSPELEKPPLSPRPEKPPEEPGQCPAPEELPLFPPPGEPSLSPLLGEPALSEPGEPPLSPLPEELPLSPSGEPSLSPQLMPPDPLPPPLSPIITAAAPPALSPLGELEYPFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGSPVGPASPILMEPLPPQCSPLLQHSLVPQNSPPSQCSPPALPLSVPSPLSPIGKVVGVSDEAELHEMETEKVSEPECPALEPSATSPLPSPMGDLSCPAPSPAPALDDFSGLGEDTAPLDGIDAPGSQPEPGQTPGSLASELKGSPVLLDPEELAPVTPMEVYPECKQTAGQGSPCEEQEEPRAPVAPTPPTLIKSDIVNEISNLSQGDASASFPGSEPLLGSPDPEGGGSLSMELGVSTDVSPARDEGSLRLCTDSLPETDDSLLCDAGTAISGGKAEGEKGRRRSSPARSRIKQGRSSSFPGRRRPRGGAHGGRGRGRARLKSTASSIETLVVADIDSSPSKEEEEEDDDTMQNTVVLFSNTDKFVLMQDMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECIVCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVSCMQCGAASPGFHCEWQNSYTHCGPCASLVTCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSCQPYVVKPVAPVAPPELVPMKVKEPEPQYFRFEGVWLTETGMALLRNLTMSPLHKRRQRRGRLGLPGEAGLEGSEPSDALGPDDKKDGDLDTDELLKGEGGVEHMECEIKLEGPVSPDVEPGKEETEESKKRKRKPYRPGIGGFMVRQRKSHTRTKKGPAAQAEVLSGDGQPDEVIPADLPAEGAVEQSLAEGDEKKKQQRRGRKKSKLEDMFPAYLQEAFFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESRGLEGKADTPGPEDGGVKASPVPSDPEKPGTPGEGMLSSDLDRISTEELPKMESKDLQQLFKDVLGSEREQHLGCGTPGLEGSRTPLQRPFLQGGLPLGNLPSSSPMDSYPGLCQSPFLDSRERGGFFSPEPGEPDSPWTGSGGTTPSTPTTPTTEGEGDGLSYNQRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINKVQKQAESQINKQTKVGDIARKTDRPALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGLSTSADGFLKPPAGSVPGPDSPGELFLKLPPQVPAQVPSQDPFGLAPAYPLEPRFPTAPPTYPPYPSPTGAPAQPPMLGASSRPGAGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLAVPESPGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPNLGFVDSPSSGTHLGGLELKTPDVFKAPLTPRASQVEPQSPGLGLRPQEPPPAQALAPSPPSHPDIFRPGSYTDPYAQPPLTPRPQPPPPESCCALPPRSLPSDPFSRVPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFKAGSLAHTSLGAGGFPAALPAGPAGELHAKVPSGQPPNFVRSPGTGAFVGTPSPMRFTFPQAVGEPSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTNYTVATGNFHPSGSPLGPSSGSTGESYGLSPLRPPSVLPPPAPDGSLPYLSHGASQRSGITSPVEKREDPGTGMGSSLATAELPGTQDPGMSGLSQTELEKQRQRQRLRELLIRQQIQRNTLRQEKETAAAAAGAVGPPGSWGAEPSSPAFEQLSRGQTPFAGTQDKSSLVGLPPSKLSGPILGPGSFPSDDRLSRPPPPATPSSMDVNSRQLVGGSQAFYQRAPYPGSLPLQQQQQQLWQQQQATAATSMRFAMSARFPSTPGPELGRQALGSPLAGISTRLPGPGEPVPGPAGPAQFIELRHNVQKGLGPGGTPFPGQGPPQRPRFYPVSEDPHRLAPEGLRGLAVSGLPPQKPSAPPAPELNNSLHPTPHTKGPTLPTGLELVNRPPSSTELGRPNPLALEAGKLPCEDPELDDDFDAHKALEDDEELAHLGLGVDVAKGDDELGTLENLETNDPHLDDLLNGDEFDLLAYTDPELDTGDKKDIFNEHLRLVESANEKAEREALLRGVEPGPLGPEERPPPAADASEPRLASVLPEVKPKVEEGGRHPSPCQFTIATPKVEPAPAANSLGLGLKPGQSMMGSRDTRMGTGPFSSSGHTAEKASFGATGGPPAHLLTPSPLSGPGGSSLLEKFELESGALTLPGGPAASGDELDKMESSLVASELPLLIEDLLEHEKKELQKKQQLSAQLQPAQQQQQQQQQHSLLSAPGPAQAMSLPHEGSSPSLAGSQQQLSLGLAGARQPGLPQPLMPTQPPAHALQQRLAPSMAMVSNQGHMLSGQHGGQAGLVPQQSSQPVLSQKPMGTMPPSMCMKPQQLAMQQQLANSFFPDTDLDKFAAEDIIDPIAKAKMVALKGIKKVMAQGSIGVAPGMNRQQVSLLAQRLSGGPSSDLQNHVAAGSGQERSAGDPSQPRPNPPTFAQGVINEADQRQYEEWLFHTQQLLQMQLKVLEEQIGVHRKSRKALCAKQRTAKKAGREFPEADAEKLKLVTEQQSKIQKQLDQVRKQQKEHTNLMAEYRNKQQQQQQQQQQQQQQHSAVLALSPSQSPRLLTKLPGQLLPGHGLQPPQGPPGGQAGGLRLTPGGMALPGQPGGPFLNTALAQQQQQQHSGGAGSLAGPSGGFFPGNLALRSLGPDSRLLQERQLQLQQQRMQLAQKLQQQQQQQQQQQHLLGQVAIQQQQQQGPGVQTNQALGPKPQGLMPPSSHQGLLVQQLSPQPPQGPQGMLGPAQVAVLQQQHPGALGPQGPHRQVLMTQSRVLSSPQLAQQGQGLMGHRLVTAQQQQQQQQHQQQGSMAGLSHLQQSLMSHSGQPKLSAQPMGSLQQLQQQQQLQQQQQLQQQQQQQLQQQQQLQQQQLQQQQQQQQLQQQQQQQLQQQQQQLQQQQQQQQQQFQQQQQQQQMGLLNQSRTLLSPQQQQQQQVALGPGMPAKPLQHFSSPGALGPTLLLTGKEQNTVDPAVSSEATEGPSTHQGGPLAIGTTPESMATEPGEVKPSLSGDSQLLLVQPQPQPQPSSLQLQPPLRLPGQQQQQVSLLHTAGGGSHGQLGSGSSSEASSVPHLLAQPSVSLGDQPGSMTQNLLGPQQPMLERPMQNNTGPQPPKPGPVLQSGQGLPGVGIMPTVGQLRAQLQGVLAKNPQLRHLSPQQQQQLQALLMQRQLQQSQAVRQTPPYQEPGTQTSPLQGLLGCQPQLGGFPGPQTGPLQELGAGPRPQGPPRLPAPPGALSTGPVLGPVHPTPPPSSPQEPKRPSQLPSPSSQLPTEAQLPPTHPGTPKPQGPTLEPPPGRVSPAAAQLADTLFSKGLGPWDPPDNLAETQKPEQSSLVPGHLDQVNGQVVPEASQLSIKQEPREEPCALGAQSVKREANGEPIGAPGTSNHLLLAGPRSEAGHLLLQKLLRAKNVQLSTGRGSEGLRAEINGHIDSKLAGLEQKLQGTPSNKEDAAARKPLTPKPKRVQKASDRLVSSRKKLRKEDGVRASEALLKQLKQELSLLPLTEPAITANFSLFAPFGSGCPVNGQSQLRGAFGSGALPTGPDYYSQLLTKNNLSNPPTPPSSLPPTPPPSVQQKMVNGVTPSEELGEHPKDAASARDSERALRDTSEVKSLDLLAALPTPPHNQTEDVRMESDEDSDSPDSIVPASSPESILGEEAPRFPHLGSGRWEQEDRALSPVIPLIPRASIPVFPDTKPYGALGLEVPGKLPVTTWEKGKGSEVSVMLTVSAAAAKNLNGVMVAVAELLSMKIPNSYEVLFPESPARAGTEPKKGEAEGPGGKEKGLEGKSPDTGPDWLKQFDAVLPGYTLKSQLDILSLLKQESPAPEPPTQHSYTYNVSNLDVRQLSAPPPEEPSPPPSPLAPSPASPPTEPLVELPTEPLAEPPVPSPLPLASSPESARPKPRARPPEEGEDSRPPRLKKWKGVRWKRLRLLLTIQKGSGRQEDEREVAEFMEQLGTALRPDKVPRDMRRCCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIRAKCMFFKDKTMLCPMHKIKGPCEQELSSFAVFRRVYIERDEVKQIASIIQRGERLHMFRVGGLVFHAIGQLLPHQMADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGENNGRPEFVIKVIEQGLEDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNYLFRYGRHPLMELPLMINPTGCARSEPKILTHYKRPHTLNSTSMSKAYQSTFTGETNTPYSKQFVHSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWMN | 2.1.1.364 | null | beta-catenin-TCF complex assembly [GO:1904837]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; oocyte growth [GO:0001555]; oogenesis [GO:0048477]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; response to estrogen [GO:0043627] | MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; histone binding [GO:0042393]; histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]; histone H3K4 trimethyltransferase activity [GO:0140999]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713] | PF05965;PF05964;PF00628;PF00856;PF13771;PF13832; | 3.30.160.360;1.10.30.10;2.170.270.10;3.30.40.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23508102}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; Evidence={ECO:0000269|PubMed:25561738}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265; Evidence={ECO:0000305|PubMed:25561738}; | null | null | null | null | FUNCTION: Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17500065, PubMed:25561738). Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (PubMed:16603732). {ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:25561738}. | Homo sapiens (Human) |
O14713 | ITBP1_HUMAN | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | null | null | activation of protein kinase B activity [GO:0032148]; biomineral tissue development [GO:0031214]; blood vessel diameter maintenance [GO:0097746]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; myoblast migration [GO:0051451]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of protein binding [GO:0032091]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein targeting to membrane [GO:0090315]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; Notch signaling pathway [GO:0007219]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; receptor clustering [GO:0043113]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of GTPase activity [GO:0043087]; regulation of integrin-mediated signaling pathway [GO:2001044]; tube formation [GO:0035148] | cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; membrane [GO:0016020]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726] | GDP-dissociation inhibitor activity [GO:0005092]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901] | PF10480; | 6.20.360.10; | null | PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction. {ECO:0000269|PubMed:9281591, ECO:0000269|PubMed:9813144, ECO:0000269|PubMed:9867804}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium. Cell projection, ruffle. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in a integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen. | null | null | null | null | null | FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292, ECO:0000269|Ref.19}. | Homo sapiens (Human) |
O14717 | TRDMT_HUMAN | MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGITLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLENVKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPGQVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHRKNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSYIEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGFPEKITVKQRYRLLGNSLNVHVVAKLIKILYE | 2.1.1.204 | null | response to amphetamine [GO:0001975]; tRNA methylation [GO:0030488]; tRNA modification [GO:0006400]; tRNA stabilization [GO:0036416] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | RNA binding [GO:0003723]; tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA methyltransferase activity [GO:0008175] | PF00145; | 3.90.120.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16424344}. | CATALYTIC ACTIVITY: Reaction=cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42956, Rhea:RHEA-COMP:10299, Rhea:RHEA-COMP:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.204; Evidence={ECO:0000269|PubMed:16424344}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42957; Evidence={ECO:0000269|PubMed:16424344}; | null | null | null | null | FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp) (PubMed:16424344). Has higher activity on tRNA(Asp) modified with queuosine at position 34 (PubMed:30093495). {ECO:0000269|PubMed:16424344, ECO:0000269|PubMed:30093495}. | Homo sapiens (Human) |
O14727 | APAF_HUMAN | MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic process [GO:0006915]; cardiac muscle cell apoptotic process [GO:0010659]; cell differentiation [GO:0030154]; cellular response to transforming growth factor beta stimulus [GO:0071560]; forebrain development [GO:0030900]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; nervous system development [GO:0007399]; neural tube closure [GO:0001843]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; regulation of apoptotic DNA fragmentation [GO:1902510]; regulation of apoptotic process [GO:0042981]; response to G1 DNA damage checkpoint signaling [GO:0072432]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584] | apoptosome [GO:0043293]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; secretory granule lumen [GO:0034774] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166] | PF21296;PF17908;PF00619;PF00931;PF00400; | 1.25.40.370;1.10.533.10;1.10.8.430;3.40.50.300;1.10.10.10;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12804598}. | null | null | null | null | null | FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis. {ECO:0000269|PubMed:10393175, ECO:0000269|PubMed:12804598}. | Homo sapiens (Human) |
O14730 | RIOK3_HUMAN | MDLVGVASPEPGTAAAWGPSKCPWAIPQNTISCSLADVMSEQLAKELQLEEEAAVFPEVAVAEGPFITGENIDTSSDLMLAQMLQMEYDREYDAQLRREEKKFNGDSKVSISFENYRKVHPYEDSDSSEDEVDWQDTRDDPYRPAKPVPTPKKGFIGKGKDITTKHDEVVCGRKNTARMENFAPEFQVGDGIGMDLKLSNHVFNALKQHAYSEERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYGGSMEDEKEDSKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALSERELFNAVSGLNITADNEADFLAEIEALEKMNEDHVQKNGRKAASFLKDDGDPPLLYDE | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | cellular response to dsDNA [GO:1990786]; cellular response to dsRNA [GO:0071359]; cellular response to virus [GO:0098586]; chromosome segregation [GO:0007059]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; maturation of SSU-rRNA [GO:0030490]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of MDA-5 signaling pathway [GO:0039534]; negative regulation of protein-containing complex assembly [GO:0031333]; phosphorylation [GO:0016310]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728] | cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688] | ATP binding [GO:0005524]; caspase binding [GO:0089720]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF01163; | 1.10.510.10; | Protein kinase superfamily, RIO-type Ser/Thr kinase family | PTM: Autophosphorylated (in vitro). {ECO:0000269|PubMed:19557502}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22418843}. | 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: Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses. May act as an adapter protein essential for the recruitment of TBK1 to IRF3 (PubMed:24807708). Phosphorylates IFIH1 on 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and resulting in attenuated IFIH1-signaling (PubMed:25865883). Can inhibit CASP10 isoform 7-mediated activation of the NF-kappaB signaling pathway (PubMed:19557502). May play a role in the biogenesis of the 40S ribosomal subunit. Involved in the processing of 21S pre-rRNA to the mature 18S rRNA (PubMed:22418843). {ECO:0000269|PubMed:19557502, ECO:0000269|PubMed:22418843, ECO:0000269|PubMed:24807708, ECO:0000269|PubMed:25865883}. | Homo sapiens (Human) |
O14732 | IMPA2_HUMAN | MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHLVEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK | 3.1.3.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17068342}; | inositol biosynthetic process [GO:0006021]; inositol metabolic process [GO:0006020]; phosphate-containing compound metabolic process [GO:0006796]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; response to lithium ion [GO:0010226]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17068342}. | CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000269|PubMed:17068342}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 mM for myo-inositol 1-monophosphate {ECO:0000269|PubMed:17068342}; | PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:17068342}; | null | FUNCTION: Can use myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain. {ECO:0000269|PubMed:17068342}. | Homo sapiens (Human) |
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.