Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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B2KI42 | CADH2_RHIFE | MCRIVGAPRTLLPLLAALLQASVEASGGIALCKTGFPEDVYSAVLSQDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPNLPEDSVKESQEIEEIVFPRQLMKHNGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDDDDPNTLNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYMLIIQATDTEGSPTYGLSNTATAVITVTDVNDNPPEFTAMSFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMPQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVVPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; glial cell differentiation [GO:0010001]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural crest cell development [GO:0014032]; neuronal stem cell population maintenance [GO:0097150]; regulation of axonogenesis [GO:0050770]; regulation of synaptic transmission, glutamatergic [GO:0051966]; synapse assembly [GO:0007416]; type B pancreatic cell development [GO:0003323] | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; sarcolemma [GO:0042383] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence. {ECO:0000250|UniProtKB:P15116}.; PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P15116}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P15116}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (By similarity). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15116}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. {ECO:0000250|UniProtKB:P15116}. | Rhinolophus ferrumequinum (Greater horseshoe bat) |
B2KI64 | PI4KB_RHIFE | MGDTVVAPAPLKPASESTPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLQKVKLSHGGVASSDRGTPLELVNGDGVDGEIRCLDDPPTGIREEDDETEATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYVHMDEDVGDAIKPYIVHRCRQSVDFSLQCALLLGAYSSDMHISTQRHSRGTKLRRLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVESEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGISHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEMHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | inner ear development [GO:0048839]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development. {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8}. | Rhinolophus ferrumequinum (Greater horseshoe bat) |
B2KPN7 | COMA_CONMR | MMSKLGVLLCIFLVLFPMATLQLDGDQTADRHADQRGQDLTEQQRNSKRVLKKRDWEYHAHPKPNSFWTLV | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF02950; | null | Conotoxin M superfamily | PTM: The D-Phe is essential to the structural conformation. {ECO:0000269|PubMed:18355315}.; PTM: Since conomarphin is a cysteine-free peptide, hydroxyproline plays a critical role in maintaining a restricted conformation of the peptide.; PTM: Mature peptide with hydroxylation at Pro-64 and D-amino acid at Phe-67 are described by Han and colleagues (2008), whereas the same sequence without modification is described by Fu and colleagues (2022). {ECO:0000269|PubMed:18355315, ECO:0000269|PubMed:35677566}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18355315}. | null | null | null | null | null | FUNCTION: May act as a neurotoxin. | Conus marmoreus (Marble cone) |
B2KPR3 | LAMT_CATRO | MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAIMECILTEHFGENILDPLFEIYTKNLQENFHVFDKEIRKDADLYLVLKRKGN | 2.1.1.50 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9FLN8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8}; | indole alkaloid metabolic process [GO:0035834]; methylation [GO:0032259] | null | loganate O-methyltransferase activity [GO:0030749]; metal ion binding [GO:0046872] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=loganate + S-adenosyl-L-methionine = loganin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12508, ChEBI:CHEBI:15771, ChEBI:CHEBI:18052, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.50; Evidence={ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568, ECO:0000269|PubMed:29399933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12509; Evidence={ECO:0000269|PubMed:18326827}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=315 uM for loganic acid (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29399933}; KM=15 mM for loganic acid {ECO:0000269|PubMed:18326827}; KM=742 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18326827}; Note=kcat is 0.31 sec(-1) with loganic acid as substrate (at pH 7.5 and 30 degrees Celsius). {ECO:0000269|PubMed:29399933}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:18326827}; | null | FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine and ajmalicine) biosynthesis pathway. Catalyzes the methylation of loganic acid (6S,7R) to produce loganin (PubMed:18326827, PubMed:24104568, PubMed:29399933). Weak activity with secologanic acid as substrate. Inactive on deoxyloganic, dehydrologanic, epiloganic and loganetic acid (PubMed:18326827). {ECO:0000269|PubMed:18326827, ECO:0000269|PubMed:24104568, ECO:0000269|PubMed:29399933}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
B2LT61 | TLR2_BISBI | MPRALWTAWVWAXIILSTEGASDQASSLSCDSTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLXTLKVGNSNSFTEIHEKDFTGLTFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMSTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFHDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKTGELLLTLENLNSLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISRNIINTFSKEQLDSFQQLKTLEAGGNNFICSCDFLSFTQGQQALGRVLVDWPDDYRCDSPSHVRGQRVQDARLSLSECHRAAVVSAACCALFLVLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDICYDAFVSYSERDSYWVENLMVQELEQFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTIFVLSENFVXSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPVDETQQEGFWLNLRAAIRS | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224] | Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670] | NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497] | PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. | null | null | null | null | null | FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}. | Bison bison (American bison) (Bos bison) |
B2LT62 | TLR2_CAPIB | MPRALWTAWVWAVISAFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLKQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFTALTLNRIRYLGNVETLTIRKLHIPQFFLFYDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLRNSACEHAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAIRS | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224] | Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670] | NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497] | PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. | null | null | null | null | null | FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}. | Capra ibex (Ibex) |
B2LT64 | TLR2_GIRCA | MPRALWTAWVWAVISLSTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITHVGNRDLQSCVNLKTLRLGANEIHTVEEDSFFHLRSLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYRTLGETSLFSHLSNLRTLKVGNSNSFTEIHEKDFTGLTFLEELEISARNLQIYAPKSLKSIQNISHLILHLKQPVLLLDILVDIVSSLDYLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGISEVEFDDCTHDGIGDFRALALERTRYLGNVETLTIRKLHIPQFFLFQDLSSIYSLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACEHAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLTNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTHCLPQTLEILDVSSNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISRNIINTFSKEQLDSFQQLKTLEAGGNNFICSCDFLSFMQGQQALARVLADWPDDYWCDSPSHVRGQRVRDARLTLSECHRTAVVSAVCCALFLLLLLTGVLCHRLHGLWYMKMMWAWLQAKRKPRKAPRRDICYDAFVSYSERDSYWVENLMVRELEHFDPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTIFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKVMNTKTYLEWPMDETQQEGFWLNLRAAVRS | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224] | Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670] | NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497] | PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. | null | null | null | null | null | FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}. | Giraffa camelopardalis (Giraffe) |
B2LT65 | TLR2_SHEEP | MPRALWTAWVWAVISVFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTASVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLRQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLTFRNVQFTDDSFVEVVKLFNYVSGILEVEFDDCTHDGVGDFTALTLNRIRYLGNVETLTIRKLHIPQFFLFYDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACEHAWPVLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFAQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSERDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSESFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAVPQRFCKLRKIMNTRTYLEWPTDETHREAFWLNLRAAIRS | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224] | Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670] | NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497] | PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. | null | null | null | null | null | FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}. | Ovis aries (Sheep) |
B2MVY4 | CDK4_SHEEP | MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE | 2.7.11.22 | null | cell division [GO:0051301]; cellular response to interleukin-4 [GO:0071353]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; G1/S transition of mitotic cell cycle [GO:0000082]; phosphorylation [GO:0016310]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; regulation of gene expression [GO:0010468]; regulation of type B pancreatic cell proliferation [GO:0061469]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165] | bicellular tight junction [GO:0005923]; chromatin [GO:0000785]; cyclin D1-CDK4 complex [GO:0097128]; cyclin D2-CDK4 complex [GO:0097129]; cyclin D3-CDK4 complex [GO:0097130]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}. | 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=2.7.11.22; 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=2.7.11.22; | null | null | null | null | FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}. | Ovis aries (Sheep) |
B2RH54 | FIMA1_PORG3 | MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW | null | null | cell adhesion [GO:0007155] | cell outer membrane [GO:0009279]; pilus [GO:0009289] | structural molecule activity [GO:0005198] | PF15495;PF06321; | 2.60.40.2580;2.60.40.3690; | Bacteroidetes fimbrillin superfamily, FimA/Mfa1 family | PTM: Synthesized as palmitoylated precursor (PubMed:15165251). Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (PubMed:15165251, PubMed:8778568, PubMed:9786913). {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:8778568, ECO:0000269|PubMed:9786913}. | SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:9786913}. Cell outer membrane {ECO:0000269|PubMed:15165251}. Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. {ECO:0000269|PubMed:15165251}. | null | null | null | null | null | FUNCTION: Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:12593606, PubMed:15165251, PubMed:17526848, PubMed:17675496, PubMed:20530728, PubMed:27062925, PubMed:9786913). They play an important role in the invasion of periodontal tissues (PubMed:12593606). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification (PubMed:23809984). The sequence-based classification correlates with pathogenicity (PubMed:17675496). {ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:27062925, ECO:0000269|PubMed:9786913}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG1 | MFA1_PORG3 | MKLNKMFLVGALLSLGFASCSKEGNGPDPDNAAKSYMSMTLSMPMGSARAGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYYDYAGLWEDHNTNEAVISGTQVPTLADYQLQDVTGELANALSGKFLLPNTHKSGANAASSDYKRGNTAYVLVRAKFTPKKEAFIDRGKTYSDNTAVPEYVAGEDFFVGENGQFYVSMKSVTDPKVGGVAGMKAHKYVKGKVLYYAWLNPSTTSPDSWWNSPVVRNNIYHIHIKSIKKLGFNWNPLVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDTFMSVEVTVLPWKVHSYEVDL | null | null | cell-cell adhesion [GO:0098609] | cell outer membrane [GO:0009279]; outer membrane [GO:0019867]; pilus shaft [GO:0009418] | null | PF15495; | 2.60.40.3690; | Bacteroidetes fimbrillin superfamily | null | SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277}. Cell outer membrane {ECO:0000269|PubMed:11083792, ECO:0000269|PubMed:15972485, ECO:0000305|PubMed:9786913}. Note=Probably synthesized as a palmitoylated precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (Probable). {ECO:0000305}. | null | null | null | null | null | FUNCTION: Structural subunit of the minor fimbriae (PubMed:12593606, PubMed:19589838, PubMed:24118823). These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:11083792, PubMed:12593606, PubMed:15972485, PubMed:19589838, PubMed:23809984, PubMed:24118823, PubMed:26001707, PubMed:26437277). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Mfa1 orthologs from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable). {ECO:0000269|PubMed:11083792, ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:15972485, ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277, ECO:0000305}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG2 | MFA2_PORG3 | MNKRKHMDIRRLIISLPAIMALWGGLASCDKMIYDNYDDCPRGVYVNFYSQTECAENPSYPAEVARLNVYAFDKDGILRSANVFEDVQLSAAKEWLIPLEKDGLYTIFAWGNIDDHYNIGEIKIGETTKQQVLMRLKQDGKWATNIDGTTLWYATSPVVELKNMEDGADQYIHTRANLREYTNRVTVSVDSLPHPENYEIKLASSNGSYRFDGTVAKADSTYYPGETKVVGDSTCRAFFTTLKLESGHENTLSVTHKPTGREIFRTDLVGAILSSQYAQNINLRCINDFDIRLVAHHCNCPDDTYVVVQIWINGWLIHSYEIEL | null | null | pilus assembly [GO:0009297] | cell outer membrane [GO:0009279] | null | PF08842; | 2.60.40.2090;2.60.40.2100; | Bacteroidetes fimbrillin superfamily, FimB/Mfa2 family | PTM: Palmitoylated. Palmitoylation is important for export to the outer membrane. {ECO:0000269|PubMed:27062925}.; PTM: Unlike other fimbrial subunits, does not contain a propeptide that is cleaved by gingipain. {ECO:0000269|PubMed:27062925}. | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:27062925}; Lipid-anchor {ECO:0000305|PubMed:27062925}. | null | null | null | null | null | FUNCTION: Anchoring subunit of the minor fimbriae. Regulates fimbrial length (PubMed:19589838). These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors (Probable). {ECO:0000269|PubMed:19589838, ECO:0000305}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG4 | MFA4_PORG3 | MKKYLLYASLLTSVLLFSCSKNNPSEPVEDRSIEISIRVDDFTKTGETVRYERNQGSAAERLITNLYLLLFDQSGANPAKYYIAGNTFSGGIWLPDDMKVKLDMTQSEAGERKVYVVANVDNAVKTALDAVANESDLQTVKRTTAMPWSTDIASPFLMSGNKTHDFLANRLLDNVPLVRAIAKVELNISLSEKFQIVPIIVNGSLSEFKFRYVNFDKETYVVKPTTKPDNLISSANGVWPQITDWTVWGASLNTSPAPDAGTGYTLDANGKVTALRIVTYLNERDSKGATVEVALPRVDDGTLPPPEFGPELYRLPLPDKILRNHWYKYEVEI | null | null | null | cell outer membrane [GO:0009279]; pilus [GO:0009289] | null | PF06321; | 2.60.40.2580; | Bacteroidetes fimbrillin superfamily, FimA/Mfa1 family | null | SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:26972441}. Cell outer membrane {ECO:0000269|PubMed:26437277}. Note=Targeted to the outer membrane as a palmitoylated precursor. The lipid modification is no longer present after proteolytic processing to the mature form. {ECO:0000305|PubMed:26437277, ECO:0000305|PubMed:26972441}. | null | null | null | null | null | FUNCTION: Tip subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:19589838, PubMed:26001707). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors (Probable). {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:26001707, ECO:0000305}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RID1 | DPP11_PORG3 | MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQIKIMYSAKYAASQNAYKRAIGANWAIKTRGLRQNKQAMQDRLIAWGAKQGTPRYEEAVHEIDATVAKRADLRRRYWMIEEGIIRGIEFARSPIPTEDETKALQGNDASARKEAIDKIRTRYSKFANKDYSAEVDKKVAVAMLTEYLKEIPYENLPLHLRLVKDRFAGDVQAYVDDIFARSVFGSEAQFDAFAAVPSVEKLAEDPMVLFASSVFDEYRKLYNELRPYDDPILRAQRTYIAGLLEMDGDQDQFPDANLTLRFTYGQVKGYSPRDNVYYGHQTTLDGVMEKEDPDNWEFVVDPKLKAVYERKDFGRYADRSGRMPVAFCATTHTTGGNSGSPVMNANGELIGLNFDRNWEGVGGDIQYLADYQRSIIVDIRYVLLVIDKVGGCQRLLDEMNIVP | 3.4.14.- | null | developmental cell growth [GO:0048588]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cell surface [GO:0009986] | dipeptidyl-peptidase activity [GO:0008239]; peptide binding [GO:0042277]; serine-type aminopeptidase activity [GO:0070009] | PF10459; | 2.40.10.10; | Peptidase S46 family | null | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21896480}. Note=Is exclusively cell-associated. {ECO:0000269|PubMed:21896480}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21896480}; | null | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:21896480, ECO:0000269|PubMed:23246913}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RIT0 | DPP5_PORG3 | MNKKIFSMMAASIIGSAAMTPSAGTNTGEHLTPELFMTLSRVSEMALSPDGKTAVYAVSFPDVKTNKATRELFTVNLDGSGRKQITDTESNEYAPAWMADGKRIAFMSNEGGSMQLWVMNADGTERRQLSNIEGGITGFLFSPDEKQVLFTKDIKFGKRTKDIYPDLDKATGRIITDLMYKHWDEWVETIPHPFIANATDGMITTGKDIMEGEPYEAPMKPWSGIEDFSWSPDGQNIAYASRKKTGMAYSLSTNSDIYIYNLTSGRTHNISEGMMGYDTYPKFSPDGKSIAWISMERDGYESDLKRLFVADLATGKRTHVNPTFDYNVDMIQWAPDSKGIYFLACKEAETNLWEITLKTGKIRQITQGQHDYADFSVRNDVMLAKRHSFELPDDLYRVNPKNGAAQAVTAENKAILDRLTPIACEKRWMKTTDGGNMLTWVVLPPDFDKNKKYPAILYCQGGPQNTVSQFWSFRWNLRLMAEQGYIVIAPNRHGVPGFGQKWNEQISGDYGGQNMRDYLTAVDEMKKEPYVDGDRIGAVGASYGGFSVYWLAGHHDKRFAAFIAHAGIFNLEMQYATTEEMWFANWDIGGPFWEKDNVVAQRTYATSPHKYVQNWDTPILMIHGELDFRILASQAMAAFDAAQLRGVPSEMLIYPDENHWVLQPQNALLFHRTFFGWLDRWLKK | 3.4.14.- | null | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | periplasmic space [GO:0042597] | aminopeptidase activity [GO:0004177]; dipeptidyl-peptidase activity [GO:0008239]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252] | PF07676;PF00326; | 3.40.50.1820;2.120.10.30; | Peptidase S9C family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:24398682}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=396 uM for Gly-Phe-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=688 uM for Lys-Ala-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=701 uM for Met-Leu-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=151 uM for Lys-Phe-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=296 uM for Ser-Tyr-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=146 uM for Lys-Leu-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; KM=220 uM for Lys-Val-MCA (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24398682}; Note=kcat is 5638 sec(-1) with Gly-Phe-MCA as substrate. kcat is 7577 sec(-1) with Lys-Ala-MCA as substrate. kcat is 5562 sec(-1) with Met-Leu-MCA as substrate. kcat is 744 sec(-1) with Lys-Phe-MCA as substrate. kcat is 1329 sec(-1) with Ser-Tyr-MCA as substrate. kcat is 490 sec(-1) with Lys-Leu-MCA as substrate. kcat is 299 sec(-1) with Lys-Val-MCA as substrate (at 37 degrees Celsius and pH 6.0). {ECO:0000269|PubMed:24398682}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7, using Lys-Ala-MCA as substrate. {ECO:0000269|PubMed:24398682}; | null | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Prefers Ala and hydrophobic residues except Pro at the P1 position, and has no preference for P2 residues. Shows high dipeptidyl peptidase activity toward the synthetic substrates Lys-Ala-, Gly-Phe-, Met-Leu-, and Ser-Tyr-methylcoumaryl-7-amide (MCA), and slowly hydrolyzes Val-Tyr-MCA. Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:24398682}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RKV3 | DPP7_PORG3 | MQMKLKSILLGAALLLGASGVAKADKGMWLLNELNQENLDRMRELGFTLPLDSLYSFDKPSIANAVVIFGGGCTGITVSDQGLIFTNHHCGYGAIQSQSTVDHDYLRDGFVSRTMGEELPIPGLSVKYLRKIVKVTDKVEGQLKGITDEMERLRKAQEVCQELAKKENADENQLCIVEPFYSNNEYFLIVYDVFKDVRMVFAPPSSVGKFGGDTDNWMWPRHTGDFSVFRVYAGADNRPAEYSKDNKPYKPVYFAAVSMQGYKADDYAMTIGFPGSTDRYLTSWGVEDRIENENNPRIEVRGIKQGIWKEAMSADQATRIKYASKYAQSANYWKNSIGMNRGLARLDVIGRKRAEERAFADWIRKNGKSAVYGDVLSSLEKAYKEGAKANREMTYLSETLFGGTEVVRFAQFANALATNPDAHAGILKSLDDKYKDYLPSLDRKVLPAMLDIVRRRIPADKLPDIFKNVIDKKFKGDTKKYADFVFDKSVVPYSDKFHAMLKSMDKEKFAKAIEKDPAVELSKSVIAAARAIQADAMANAYAIEKGKRLFFAGLREMYPGRALPSDANFTMRMSYGSIKGYEPQDGAWYNYHTTGKGVLEKQDPKSDEFAVQENILDLFRTKNYGRYAENGQLHIAFLSNNDITGGNSGSPVFDKNGRLIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWGQCPRLIQELKLI | 3.4.14.- | null | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cell outer membrane [GO:0009279] | dipeptidyl-peptidase activity [GO:0008239]; peptide binding [GO:0042277]; serine-type aminopeptidase activity [GO:0070009]; serine-type peptidase activity [GO:0008236] | PF10459; | 2.40.10.10; | Peptidase S46 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:11096098}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=313 uM for Ala-Ala-pNA {ECO:0000269|PubMed:11096098}; KM=441 uM for Ala-Phe-pNA {ECO:0000269|PubMed:11096098}; KM=256 uM for Gly-Ala-pNA {ECO:0000269|PubMed:11096098}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Is active against Ala-Phe-pNA over a broad pH range, from neutral to basic pH (6.5-9.0). {ECO:0000269|PubMed:11096098}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 43 degrees Celsius, using Ala-Phe-pNA as substrate. {ECO:0000269|PubMed:11096098}; | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides (PubMed:11096098, PubMed:23246913). Shows a broad specificity for both aliphatic and aromatic residues in the P1 position, with glycine or proline being not acceptable in this position (PubMed:11096098). Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), Leu-Arg-MCA and Lys-Ala-MCA to a lesser extent (PubMed:23246913). Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources (PubMed:11096098). {ECO:0000269|PubMed:11096098, ECO:0000269|PubMed:23246913}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RLK2 | KGP_PORG3 | MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSLTATQVKALTNKDKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVNMTKQITENGNYDVVITRSNYLPVIKQIQAGEPSPYQPVSNLTATTQGQKVTLKWDAPSAKKAEASREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIQEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQDWLCLSSGQLDWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKVCVNVTINPTQFNPVKNLKAQPDGGDVVLKWEAPSGKRGELLNEDFEGDAIPTGWTALDADGDGNNWDITLNEFTRGERHVLSPLRASNVAISYSSLLQGQEYLPLTPNNFLITPKVEGAKKITYKVGSPGLPQWSHDHYALCISKSGTAAADFEVIFEETMTYTQGGANLTREKDLPAGTKYVAFRHYNCTDVLGIMIDDVVITGEGEGPSYTYTVYRDGTKIQEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAIK | 3.4.22.47 | null | hemolysis in another organism [GO:0044179]; proteolysis [GO:0006508] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; cysteine-type endopeptidase activity [GO:0004197] | PF07675;PF10365;PF01364;PF03785;PF08126; | 2.60.120.200;2.60.40.3800;3.40.50.1460;2.60.40.10; | Peptidase C25 family | PTM: Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing (By similarity). {ECO:0000250|UniProtKB:P72194, ECO:0000250|UniProtKB:Q51817}. | SUBCELLULAR LOCATION: [Lys-gingipain catalytic subunit]: Secreted {ECO:0000250|UniProtKB:P72194}. | CATALYTIC ACTIVITY: Reaction=Endopeptidase with strict specificity for lysyl bonds.; EC=3.4.22.47; Evidence={ECO:0000269|PubMed:18295742, ECO:0000269|PubMed:9538207}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Activity remains high from pH 6.5 to 9.5. Loses 60% of its activity following incubation at pH 3.5 for 5 minutes. {ECO:0000269|PubMed:9538207}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Only retains 40% of activity after incubation at 60 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:9538207}; | FUNCTION: Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. {ECO:0000269|PubMed:15576324, ECO:0000269|PubMed:9538207}. | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RPY5 | GP161_MOUSE | MDFVQHALLTASRGALTMSLNSSLSYRKELSNLTATEGGEGGAVSEFIAIIIITVLVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHQEPGYTIFWQIWCALFPFLIMLVCYGFIFRVARVKARKVHCGTVVTVEEDSQRSGRKNSSTSTSSSGSRRNALQGVVYSANQCKALITILVVIGAFMVTWGPYMVVITSEALWGKNCVSPTLETWATWLSFTSAICHPLIYGLWNKTVRKELLGMCFGDRYYRESFVQRQRTSRLFSISNRITDLGLSPHLTALMAGGQSLGHSSSTGDTGFSYSQDSGTDVMLLEDGTSEDNPPQHCTCPPKRRSSVTFEDEVEQIKEAAKNSLLHVKAEVHKSLDSYAASLAKAIEAEAKINLFGEEALPGVLFTARTVPGAGFGGRRGSRTLVNQRLQLQSIKEGNVLAAEQR | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:1901621] | ciliary membrane [GO:0060170]; cilium [GO:0005929]; glial cell projection [GO:0097386]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded. | null | null | null | null | null | FUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown. {ECO:0000269|PubMed:18250320, ECO:0000269|PubMed:23332756}. | Mus musculus (Mouse) |
B2RQC2 | UBP42_MOUSE | MTIVDKTEPSDPSTCQNQPGSCEAVSPEDMDTGSASWGAVSSISDVSSHTLPLGPVPGAVVYSNSSVPEKSKPSPPKDQVLGDGIAPPQKVLFPSEKICLKWQQSHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQTHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVTKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTISLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRAVLNQQAYVLFYIRSHDVKNGGESAHPAHSPGQSSPRPGVSQRVVNNKQVAPGFIGPQLPSHVMKNTPHLNGTTPVKDTPSSSVSSPNGNTSVNRASPATASTSVQNWSVTRPSVIPDHPKKQKITISIHNKLPARQGQAPLNNSLHGPCLEAPSKAAPSSTITNPSAIQSTSNVPTTSTSPSEACPKPMVNGKAKVGASVLVPYGAESSEESDEESKGLAKENGVDMMAGTHSDRPEAAADDGAEASSHELQEPVLLNGANSADSDSQENSLAFDSASCQVQPELHTENLFSKLNGLPGKVTPAPLQSVPEDRILETFKLTNQAKGPAGEESWTTTGGSSPKDPVSQLEPISDEPSPLEIPEAVTNGSTQTPSTTSPLEPTISCTKEDSSVVVSAEPVEGLPSVPALCNSTGTILGDTPVPELCDPGDLTANPSQPTEAVKGDTAEKAQDSAMAEVVERLSPAPSVLTGDGCEQKLLLYLSAEGSEETEDSSRSSAVSADTMPPKPDRTTTSSCEGAAEQAAGDRGDGGHVGPKAQEPSPAKEKMSSLRKVDRGHYRSRRERSSSGEHVRDSRPRPEDHHHKKRHCYSRERPKQDRHPTNSYCNGGQHLGHGDRASPERRSLSRYSHHHSRIRSGLEQDWSRYHHLENEHAWVRERFYQDKLRWDKCRYYHDRYTPLYTARDAREWRPLHGREHDRLVQSGRPYKDSYWGRKGWELQSRGKERPHFNSPREAPSLAVPLERHLQEKAALSVQDSSHSLPERFHEHKSVKSRKRRYETLENNDGRLEKKVHKSLEKDTLEEPRVKKHKKSKKKKKSKDKHRDRESRHQQESDFSGAYSDADLHRHRKKKKKKKRHSRKSEDFIKDVEMRLPKLSSYEAGGHFRRTEGSFLLADGLPVEDSGPFREKTKHLRMESRPDRCRLSEYGQGD | 3.4.19.12 | null | cell differentiation [GO:0030154]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; spermatogenesis [GO:0007283] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF00443; | 3.90.70.10; | Peptidase C19 family | null | null | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinating enzyme which may play an important role during spermatogenesis. {ECO:0000269|PubMed:16904385}. | Mus musculus (Mouse) |
B2RQC6 | PYR1_MOUSE | MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVREAAAGNIGGQTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDLLHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGVVPQPPPSTPATTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPPRKVVEPELMGTPDGPCYPAPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVIVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF | 2.1.3.2; 3.5.1.2; 3.5.2.3; 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P27708}; Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity). {ECO:0000250|UniProtKB:P27708}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; animal organ regeneration [GO:0031100]; cellular response to epidermal growth factor stimulus [GO:0071364]; citrulline biosynthetic process [GO:0019240]; female pregnancy [GO:0007565]; glutamine metabolic process [GO:0006541]; heart development [GO:0007507]; lactation [GO:0007595]; liver development [GO:0001889]; response to amine [GO:0014075]; response to caffeine [GO:0031000]; response to cortisol [GO:0051414]; response to insulin [GO:0032868]; response to starvation [GO:0042594]; response to testosterone [GO:0033574]; UDP biosynthetic process [GO:0006225]; UTP biosynthetic process [GO:0006228]; xenobiotic metabolic process [GO:0006805] | cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; terminal bouton [GO:0043195] | amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; enzyme binding [GO:0019899]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; UTP binding [GO:0002134]; zinc ion binding [GO:0008270] | PF01979;PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729; | 3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380; | CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivity to feedback inhibition by UTP (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:P27708}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000250|UniProtKB:P07259}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:P07259}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000250|UniProtKB:P27708}; CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000250|UniProtKB:P27708}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. | null | null | FUNCTION: Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000250|UniProtKB:P27708}. | Mus musculus (Mouse) |
B2RQL2 | STOX1_MOUSE | MARPVQLAPGSLALVLSPREAGQAAGEPGGRALFRAFRRANARCFWNARLARAASRLAFLGWLRRGVLLVRAPQPCVQVLRDAWRRRALRPPRGFRITAVGDVFPVQMSPIAQCRFVPLAEVLCCAIADMNAAQVMVTQQSLLEHLIKHYPGIAVPSPDILYSTLGALIQERKIYHTGEGYFIVTPSTYFITNTPMQGNKSALLSNEGCSGPTSGTYLVSVDCCAEPTQENEALFSHCPSCQCYPDTSMCDSKDLLTAAEVTRKSQEGLEETTALTENQVVSASEDTHICVNPKPLPYTKDKGKRFGFGFLWRSLSRKEKPKAEYHSFSAQFPPEEWPVRDEDSSTKIPRDVEHALIKRINPVLTVDNLTKHTALMQKYEEQKKYNSQGTSMDILTTRHKDSSKEVIGKRQGQFAKSRRRGSSHKGRHKARSQGSELEPGNPGQEKEKQPKVPAAQPAPRTKSPSEQVHHLQGRNPAVLGSHLIYKKQINNPFQGMHLRKHSVSKGHAVQKTHGLKPTCVGPEEKPFWSAGSSDPSGVFDGEAQPPYPEQCRDKLEAGSTQVAKAPVHPVSDDFRGGPGNYPPRRVLPGPSRCCSFRESMLRPGVYHEENKDLPEVLRKSWSTCDMFLGTKEKKQALPAQRCSLDPDSSSVHAEDKTVDKILHQFQNLGLLDCPAGANRLRTHERQDGNSEELSRKALQIPEAEIVNMENEGLSDSEQDQVALSHSDPGAGDDGGCSSLCLEDDDFSETDDFCPSLPGHTQHSFAGGGTWNHLGTPAMTGKSLTDCNSKAHRLELLAIERNPWYKATGLFSNAGESPNPDLSDNPGQNSRIPWGFNYEGEPTVAHVQTPAAAAGRSLLACSTVRTTSFPVEILQESPGDRGKSPIVWRQSLPSQEMKEHFTDKLQLVKTSHGPVSAQEPQGEHLEGTENYSMTGDSGIDSPRTQSLVSTNSAILDGFKRRQHFLPNREGVQKSQNLASNSLFQLTPAINV | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to nitrosative stress [GO:0071500]; inner ear development [GO:0048839]; negative regulation of gene expression [GO:0010629]; positive regulation of cell cycle [GO:0045787]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of gene expression [GO:0010628]; positive regulation of otic vesicle morphogenesis [GO:1904120]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of mitochondrial DNA metabolic process [GO:1901858]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of mitochondrion organization [GO:0010821]; regulation of mitotic cell cycle [GO:0007346]; regulation of response to oxidative stress [GO:1902882]; regulation of transcription by RNA polymerase II [GO:0006357] | cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF10264; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25677106}. Cytoplasm {ECO:0000269|PubMed:25677106}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6ZVD7}. Note=In epithelial cells, diffusely expressed in the cytoplasm, particularly in peri-membrane cortical regions (PubMed:25677106). Concentrated at centrosomes during metaphase (By similarity). {ECO:0000250|UniProtKB:Q6ZVD7, ECO:0000269|PubMed:25677106}. | null | null | null | null | null | FUNCTION: Involved in regulating the levels of reactive oxidative species and reactive nitrogen species and in mitochondrial homeostasis in the placenta (By similarity). Required for regulation of inner ear epithelial cell proliferation via the AKT signaling pathway (PubMed:25677106). Involved in cell cycle regulation by binding to the CCNB1 promoter, up-regulating its expression and promoting mitotic entry (By similarity). Induces phosphorylation of MAPT/tau (By similarity). {ECO:0000250|UniProtKB:Q6ZVD7, ECO:0000269|PubMed:25677106}. | Mus musculus (Mouse) |
B2RQR8 | ECE2_MOUSE | MNVALHELGGGGSMVEYKRAKLRDEESPEITVEGRATRDSLEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW | 3.4.24.71 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | peptide hormone processing [GO:0016486]; protein processing [GO:0016485] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:F1N476}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:F1N476}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; Evidence={ECO:0000250|UniProtKB:P0DPD6}; | null | null | null | null | FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). {ECO:0000250|UniProtKB:P0DPD6, ECO:0000269|PubMed:12464614}. | Mus musculus (Mouse) |
B2RR83 | YTDC2_MOUSE | MSRPSSVSPRPPAPSGGGTGGGGGGSGGGGGGGGGGPASCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAENREMSKTSGRLNNGIPQVPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILRTTGYTNKEMLKYKKEKQREEKQQTTLTEWYSAQENTFKPESQRQRAVASVSEEYDLLDDGGDAVFSQLTEKDVNCLEPWLIKEMDACLSDIWLHKDVDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFTSQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSASLEFGNLDESSLVQTNGNDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAILIFLPGYDEIVGLRDRILFDDKRFADNTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNCTIADFLMKAPEPPPALIVRNAVQMLKTIDAMDAWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKRFTAGTFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFVRARGGGDIRDVNTNSENWAVVKAALVAGMYPNLVHVDRENVILTGPKEKKVRFHPTSVLSQPQYKKIPPANGQAAAIQALPTDWLIYDEMTRAHRIANIRCCSAVTPVTVLVFCGPARLASNALQEPSSFRADGIPNDSSDSEMEDRTTANLAALKLDEWLNFKLEPEAASLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSEELPLASSWRSNNSRKSTADTEFADGSTTGERVLMKSPSPALHPPQKYKDRGILHPKRSTDDRSDQSSVKSTDSSSYPSPCASPSPPSSGKGSKSPSPRPNMPIRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQDWGSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWERLPLGEKTTSD | 3.6.4.13 | null | germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; meiotic cell cycle [GO:0051321]; oocyte development [GO:0048599]; positive regulation by host of viral genome replication [GO:0044829]; response to interleukin-1 [GO:0070555]; response to tumor necrosis factor [GO:0034612]; spermatid development [GO:0007286] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein granule [GO:0035770] | 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063] | PF00270;PF21010;PF04408;PF00271;PF07717;PF01424;PF04146; | 1.20.120.1080;1.25.40.20;3.40.50.300;3.10.590.10;3.30.1370.50; | DEAD box helicase family, DEAH subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6S0}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:29360036}; | null | null | null | null | FUNCTION: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:28380054, PubMed:28809393, PubMed:29033321, PubMed:29087293, PubMed:29360036, PubMed:32470506). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:29360036). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (PubMed:29033321). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (PubMed:28809393, PubMed:29033321). {ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036, ECO:0000269|PubMed:32470506}. | Mus musculus (Mouse) |
B2RRD7 | BRPF1_MOUSE | MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDSPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHSAPASAAPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAVDCALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARRLPALSHSEGEEEEDEEEDEGKSWSSEKVKKAKAKSRIKMKKARKILAEKRAAAPVVSVPCIPPHRLSKITNRLTIQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNCEQVGRDSDDKNWALKEQLKSWQRLRHDLERARLLVELIRKREKLKRETIKIQQIAMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGIDFETGMHIPHNLAGDEVSHHTEDVEEERLVLLENQKHLPVEEQLKLLLERLDEVNASKQSVGRSRRAKMIKKEMTALRRKLAHQRETGRDGPERHGPSGRGNLTPHPAACDKDGQTDSAAEESSSQETSKGLGPNMSSTPAHEVGRRTSVLFSKKNPKTAGPPKRPGRPPKNRESQMTPSHGGSPVGPPQLPIMGSLRQRKRGRSPRPSSSSDSDSDKSTEDPPMDLPANGFSSGNQPVKKSFLVYRNDCNLPRSSSDSESSSSSSSSAASDRTSTTPSKQGRGKPSFSRGTFPEDSSEDTSGTENEAYSVGTGRGVGHSMVRKSLGRGAGWLSEDEDSPLDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKRTWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRALQHRSKVQGEQSSETSDSD | null | null | chromatin remodeling [GO:0006338]; common myeloid progenitor cell proliferation [GO:0035726]; neural tube formation [GO:0001841]; regulation of fibroblast proliferation [GO:0048145]; regulation of transcription by RNA polymerase II [GO:0006357]; vasculogenesis [GO:0001570] | cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleus [GO:0005634] | acetyltransferase activator activity [GO:0010698]; DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF00439;PF10513;PF13831;PF00855;PF13832; | 2.30.30.140;1.20.920.10;3.30.40.10; | null | PTM: Acetylated by KAT6A. {ECO:0000250|UniProtKB:P55201}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55201}. Chromosome {ECO:0000250|UniProtKB:P55201}. Cytoplasm {ECO:0000250|UniProtKB:P55201}. Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6. Localizes to transcription start sites. {ECO:0000250|UniProtKB:P55201}. | null | null | null | null | null | FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (By similarity). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (By similarity). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation (PubMed:27939640). Positively regulates the transcription of RUNX1 and RUNX2 (By similarity). {ECO:0000250|UniProtKB:P55201, ECO:0000269|PubMed:27939640}. | Mus musculus (Mouse) |
B2RRE7 | OTUD4_MOUSE | MEAAVGAPDGVDQGGVGPLEDETPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYPITYKDSSAMCQSLLYELLYEKVFKTDVSKIMMGLEASEVAEESNSEISDSEDDSCKSKSTAATDVNGFKPSGSENPKNNGNSADLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCHQVRLDHNGKLSNADIHGVHSENGLVLSEELGKKHTPKNLKPPPPESWNTVSGKKMKKPNSGQNFHSDTDYRGPKNLNKPIKAPSALPPRLQHPSSGVRQHAFSSHSTGSQSQKSSSEHKNLSRMPSQITRKPDRERAEDFDHVSRESYYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVSQSPSQNSNACVPRKSSHARDRKGSMRRADAEERKDKDSLRGHTHVDKKPEPSTLEISDDKCTRVSSPSKSKKECPSPVEQKPAEHIPLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPLPQTMSLYQDPLYPGFPCSEKGDRAIAPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVYPQNTWFQEAPPAQSESDCPCTDAHYSLHPEASVNGQMPQAEMGPPAFASPLVIPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSGKNMYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMRQNIVLPPDDKGELDLPLENLDLSKECDSVSAVDEFPDARVEGAHSLSAASVSSKHEGRVEQSSQTRKADIDLASGSSAVEGKGHPPTQILNREREPGSAEPEPKRTIQSLKEKPEKVKDPKTAADVVSPGANSVDRLQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGSSGRGGYQHVRGEESWKGQPNRSRDEGYQYHRHVRGRPYRGDRRRSGMGDGHRGQHT | 3.4.19.12 | null | DNA dealkylation involved in DNA repair [GO:0006307]; innate immune response [GO:0045087]; negative regulation of interleukin-1-mediated signaling pathway [GO:2000660]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of protein K48-linked deubiquitination [GO:1903093] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]; molecular adaptor activity [GO:0060090] | PF02338; | 3.90.70.80; | null | PTM: Phosphorylation at Ser-202 and Ser-204 activates 'Lys-63'-specific deubiquitinase activity. Induced upon stimulation with IL1B. {ECO:0000305|PubMed:29395066}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01804}. Nucleus {ECO:0000250|UniProtKB:Q01804}. Note=Primarily cytoplasmic. {ECO:0000250|UniProtKB:Q01804}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000305|PubMed:29395066}; | null | null | null | null | FUNCTION: Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators (PubMed:29395066). Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity). {ECO:0000250|UniProtKB:Q01804, ECO:0000269|PubMed:29395066}. | Mus musculus (Mouse) |
B2RS91 | RRN3_MOUSE | MAAPLLHTRLSGDVTAAASATLSASRTGLSDMLALESDFFNSPPKKTVRFGGTVTEVLLKYKKGETNDLELLKNQLSDPDIKDDQIINWLLEFRSSVMYLTKDFEQLINIILRLPWLNRSQRVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIVKEGGIDVSDSDDEDDNLPAIFDTCHRALQIITRYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISLYFPTLRREILELVIEKLLKLDVSVSRQDIEDAEEKAAQTCGGTDTTEGLFNMDEDEDTDPEKKADQEQPNQMAHPTAERLDVLLCLLLSYIEDVCRVHGKIDNNKTKDLYRDLISIFDKLLLPTHASCHVQFFMFFLCSFKLGFAEAFLEHLWKKLQDPNNPAIIRQAAANYIGSFLARAKFIPLITVKTCLDLLVNWLHMYLTNQDSGTKAFCDVALHGPFYSACQAVFYTVVFRHKQLLSGNLKQGLQYLQSLNFERIVLSQLNPLKICLPQVVNFFAAITNKYQLVFCYTIMERNSRQMLPVIRSTAGGDSVQTCTNPLDTFFPFDPCVLKRSKKFIDPIYQIWEDGSAEELQEFKKSTKKEVVEDEDDDFLKGEVPQSDTVTGLTPSSFDTHFQSPSSSVGSPPVLYIPGQSPLLTRIYD | null | null | cytoplasm organization [GO:0007028]; DNA-templated transcription initiation [GO:0006352]; fibroblast proliferation [GO:0048144]; homeostasis of number of cells [GO:0048872]; in utero embryonic development [GO:0001701]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; nucleolus organization [GO:0007000]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron projection development [GO:0010976]; regulation of DNA-templated transcription initiation [GO:2000142]; ribosome biogenesis [GO:0042254]; transcription initiation at RNA polymerase I promoter [GO:0006361] | nucleolus [GO:0005730]; nucleus [GO:0005634] | RNA polymerase binding [GO:0070063]; RNA polymerase I core binding [GO:0001042]; RNA polymerase I core promoter sequence-specific DNA binding [GO:0001164]; RNA polymerase I general transcription initiation factor activity [GO:0001181] | PF05327; | null | RRN3 family | PTM: Phosphorylated at Thr-198 by MAPK9/JNK2, which abrogates initiation complex formation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12015311}. | null | null | null | null | null | FUNCTION: Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent pre-initiation complex (PIC). {ECO:0000269|PubMed:12015311, ECO:0000269|PubMed:12646563}. | Mus musculus (Mouse) |
B2RSH2 | GNAI1_MOUSE | MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to forskolin [GO:1904322]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of synaptic transmission [GO:0050805]; positive regulation of protein localization to cell cortex [GO:1904778]; regulation of cAMP-mediated signaling [GO:0043949]; regulation of mitotic spindle organization [GO:0060236] | cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | D2 dopamine receptor binding [GO:0031749]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | PTM: Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation. {ECO:0000250|UniProtKB:P10824}.; PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. {ECO:0000250|UniProtKB:P10824}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm {ECO:0000250|UniProtKB:P10824}. Cell membrane {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane {ECO:0000250|UniProtKB:P10824}; Lipid-anchor {ECO:0000250|UniProtKB:P10824}. Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824}. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity). {ECO:0000250|UniProtKB:P10824, ECO:0000250|UniProtKB:P63096}. | Mus musculus (Mouse) |
B2RTY4 | MYO9A_HUMAN | MNINDGGRRRFEDNEHTLRIYPGAISEGTIYCPIPARKNSTAAEVIESLINKLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALENRLSGEDYRFLLREKNLDGSIHYGSLQSWLRVTEERRRMMERGFLPQPQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEDERSAFHLKQPEEYHYLNQITKKPLRQSWDDYCYDSEPDCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNICYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEHNTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEDNSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSKNAFISGMIGIDPVAVFRWAILRAFFRAMVAFREAGKRNIHRKTGHDDTAPCAILKSMDSFSFLQHPVHQRSLEILQRCKEEKYSITRKNPRTPLSDLQGMNALNEKNQHDTFDIAWNGRTGIRQSRLSSGTSLLDKDGIFANSTSSKLLERAHGILTRNKNFKSKPALPKHLLEVNSLKHLTRLTLQDRITKSLLHLHKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDVLVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPRNIIPSKFNIQDFFRKINLNPDNYQVGKTMVFLKEQERQHLQDLLHQEVLRRIILLQRWFRVLLCRQHFLHLRQASVIIQRFWRNYLNQKQVRDAAVQKDAFVMASAAALLQASWRAHLERQRYLELRAAAIVIQQKWRDYYRRRHMAAICIQARWKAYRESKRYQEQRKKIILLQSTCRGFRARQRFKALKEQRLRETKPEVGLVNIKGYGSLEIQGSDPSGWEDCSFDNRIKAIEECKSVIESNRISRESSVDCLKESPNKQQERAQSQSGVDLQEDVLVRERPRSLEDLHQKKVGRAKRESRRMRELEQAIFSLELLKVRSLGGISPSEDRRWSTELVPEGLQSPRGTPDSESSQGSLELLSYEESQKSKLESVISDEGDLQFPSPKISSSPKFDSRDNALSASNETSSAEHLKDGTMKEMVVCSSESITCKPQLKDSFISNSLPTFFYIPQQDPLKTNSQLDTSIQRNKLLENEDTAGEALTLDINRETRRYHCSGKDQIVPSLNTESSNPVLKKLEKLNTEKEERQKQLQQQNEKEMMEQIRQQTDILEKERKAFKTIEKPRIGECLVAPSSYQSKQRVERPSSLLSLNTSNKGELNVLGSLSLKDAALAQKDSSSAHLPPKDRPVTVFFERKGSPCQSSTVKELSKTDRMGTQLNVACKLSNNRISKREHFRPTQSYSHNSDDLSREGNARPIFFTPKDNMSIPLVSKEALNSKNPQLHKEDEPAWKPVKLAGPGQRETSQRFSSVDEQAKLHKTMSQGEITKLAVRQKASDSDIRPQRAKMRFWAKGKQGEKKTTRVKPTTQSEVSPLFAGTDVIPAHQFPDELAAYHPTPPLSPELPGSCRKEFKENKEPSPKAKRKRSVKISNVALDSMHWQNDSVQIIASVSDLKSMDEFLLKKVNDLDNEDSKKDTLVDVVFKKALKEFRQNIFSFYSSALAMDDGKSIRYKDLYALFEQILEKTMRLEQRDSLGESPVRVWVNTFKVFLDEYMNEFKTSDCTATKVPKTERKKRRKKETDLVEEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKYDPELSSRQFGVELSRLTSEDRTVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDPLQSVQDISKTTTCVELIVVEQMNKYKARLKDISSLEFAENKAKTRLSLIRRSMGKGRIRRGNYPGPSSPVVVRLPSVSDVSEETLTSEAAMETDITEQQQAAMQQEERVLTEQIENLQKEKEELTFEMLVLEPRASDDETLESEASIGTADSSENLNMESEYAISEKSERSLALSSLKTAGKSEPSSKLRKQLKKQQDSLDVVDSSVSSLCLSNTASSHGTRKLFQIYSKSPFYRAASGNEALGMEGPLGQTKFLEDKPQFISRGTFNPEKGKQKLKNVKNSPQKTKETPEGTVMSGRRKTVDPDCTSNQQLALFGNNEFMV | null | null | cell junction assembly [GO:0034329]; establishment of epithelial cell apical/basal polarity [GO:0045198]; intracellular signal transduction [GO:0035556]; regulation of neuron projection arborization [GO:0150011]; regulation of small GTPase mediated signal transduction [GO:0051056]; visual perception [GO:0007601] | actin filament [GO:0005884]; axonal growth cone [GO:0044295]; cytosol [GO:0005829]; membrane [GO:0016020]; synapse [GO:0045202]; unconventional myosin complex [GO:0016461] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; microfilament motor activity [GO:0000146] | PF00130;PF00612;PF00063;PF00788;PF00620; | 1.10.10.820;1.20.5.190;1.20.58.530;3.30.60.20;6.20.240.20;3.40.850.10;1.20.120.720;1.10.555.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Phosphorylated by ALPK1 following monosodium urate monohydrate (MSU)-induced inflammation. {ECO:0000269|PubMed:27169898}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}. Synapse {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell bodies, dendrites and axons with occasional hints of an enrichment near the plasma membrane. Localized at the neuromuscular junction (By similarity). {ECO:0000250|UniProtKB:Q8C170, ECO:0000250|UniProtKB:Q9Z1N3}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons. Required for the regulation of neurite branching and motor neuron axon guidance (By similarity). {ECO:0000250|UniProtKB:Q8C170, ECO:0000250|UniProtKB:Q9Z1N3}. | Homo sapiens (Human) |
B2RU80 | PTPRB_MOUSE | MLRHGALTALWITLSVVQTGVAEQVKCNFTLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIRIDNFTYGCNPKDLQAGTVYNFRIVSLDGEESTLVLQTDPLPPARFEVNREKTASTTLQVRWTPSSGKVSWYEVQLFDHNNQKIQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVSGEKRSFPVYINGSTVPSPVKDLGISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVTMASGLQNSRWKLVRTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISGELSAEKSAAGRTVPEKVRNLVSYNEIWMKSFTVNWTPPAGDWEHYRIVLFNESLVLLNTTVGKEETHYALDGLELIPGRQYEIEVIVESGNLRNSERCQGRTVPLAVLQLRVKHANETSLGITWRAPLGEWEKYIISLMDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLKQSSSIKGRTVPAQVTDLHVNNQGMTSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVSGVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSGNYASHSFTEERTVPDKVQGISVSNSARSDYLKVSWVHATGDFDHYEVTIKNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQYEASEQGTGRTIPEPVKDLTLLNRSTEDLHVTWSRANGDVDQYEVQLLFNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDRLMVTWSPGGGDVDSYVVSAFRQDEKVDSQTIPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVAANAYSSNSLTVSWQKALGVAERYDILLLNENGLLLSNVSEPATARQHKFEDLTPGKKYKMQILTVSGGLFSKESQAEGRTVPAAVTNLRITENSSRYLSFGWTASEGELSWYNIFLYNPDRTLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPAAVNHLKGSHRNTTDSLWFSWSPASGDFDFYELILYNPNGTKKENWKEKDVTEWRFQGLVPGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKTYSKPISGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDSTITMIDRPPQPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFAVVVREADSMDELKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAESPDSSSKSFNIKLGAEMDSLGGKCDPSQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSMPITTESEPLFGVIEGVSAGLFLIGMLVALVAFFICRQKASHSRERPSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRAKKLRNEQENPLFPIYENVNPEYHRDAIYSRH | 3.1.3.48 | null | angiogenesis [GO:0001525]; dephosphorylation [GO:0016311]; glial cell migration [GO:0008347]; peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [GO:1990264] | membrane [GO:0016020]; receptor complex [GO:0043235] | cadherin binding [GO:0045296]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF18861;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 3 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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: Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin. {ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:16514057, ECO:0000269|PubMed:17360632, ECO:0000269|PubMed:19015309, ECO:0000269|PubMed:19451274}. | Mus musculus (Mouse) |
B2RUJ5 | APBA1_MOUSE | MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI | null | null | chemical synaptic transmission [GO:0007268]; establishment of localization in cell [GO:0051649]; gamma-aminobutyric acid secretion [GO:0014051]; glutamate secretion [GO:0014047]; in utero embryonic development [GO:0001701]; intracellular protein transport [GO:0006886]; locomotory behavior [GO:0007626]; multicellular organism growth [GO:0035264]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685] | amyloid-beta binding [GO:0001540]; PDZ domain binding [GO:0030165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | PF00595;PF00640; | 2.30.42.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Golgi apparatus. | null | null | null | null | null | FUNCTION: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity). Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (PubMed:10846156). {ECO:0000250, ECO:0000269|PubMed:10846156}. | Mus musculus (Mouse) |
B2RUP2 | UN13D_MOUSE | MATHLSHPQRRPLLRQAIKIRRRRVRDLQDPPPQATQEVQVQSHHFSPEERDLLYEEALYTVLHRLGQPEPNHVKEASELLSYLQEAFQVQPEEHQQMLRRVRELEKPVFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVAEGSPVSRRRQKAVVKHTIPEEETHRTQVKSQTLNPVWDETFILEFEDIANASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWFPLEPCTETYPDRGQCHLQFQFIHKRRATAASRSQPSYTVHFHLLQQLVSHEVTQHQAGSTSWDASLSPQAVTILFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQREELATSFTSLLAYGLSLIRKFRSVFPLSVSDSPSRLQSLLRVLVQMCKMKAFGELCPDSAPLSQLVSEALRMGTVEWFHLMQQHHQPMVQGILEAGKALLNLVQDVMGDLYQCRRTWNKIFHNVLKIDLFSMAFLELQWLVAKRVQDHTVAAGNLVSPDIGESLFQLYVSLKELCQLGPVPSDSREVLALDGFHRWFQPAIPSWLQKTYSVALERVQRAVQMDTLVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSAVQKDQSQAADMLCVVVNNMEQLRLIIDKLPTQLAWEALEQRVGAVLEEGQLQNTLHAQLQGALAGLGHEIRTGVRTLAEQLEVGIATHIQKLIGVKESVLPEDAILPLMKFLEVKLCYMNTNLVQENFSSLLTLLWTHTLTVLVEVASSQRSSSLASGRLKVALQNLEVCFHAEGCGLPPEALHTDTFQALQNDLELQAASSRELIQKYFCSRIQQQAETTSERLGAVTVKVSYRASEQRLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPEVAPRETQKHKKELHPLFDETFEFLVPAEPCQKAWACLLLTVLDHDRLGADDLEGEAFLPLCRVPGLTDCAEPGEAPQMRLPLTYPAPNGDPILRLLESRKGDREAQAFVKLRRQRAKQASQHAP | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | defense response to virus [GO:0051607]; dense core granule priming [GO:0061789]; establishment of localization in cell [GO:0051649]; germinal center formation [GO:0002467]; granuloma formation [GO:0002432]; natural killer cell degranulation [GO:0043320]; phagocytosis [GO:0006909]; positive regulation of regulated secretory pathway [GO:1903307]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of mast cell degranulation [GO:0043304]; secretion [GO:0046903] | cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; recycling endosome [GO:0055037]; Weibel-Palade body [GO:0033093] | metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF00168;PF06292; | 1.10.357.50;1.20.58.1100;2.60.40.150; | Unc-13 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Lysosome {ECO:0000269|PubMed:18354201}. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis (By similarity). Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000250, ECO:0000269|PubMed:18354201}. | Mus musculus (Mouse) |
B2RUR8 | OTU7B_MOUSE | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVSAALSDFEQLRQVHAGNLSPPFSGGSTCPKTPEKGGSDREPTRPSRPILQRQDDVIQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSSEHPLEMPICAFQLPDLTVYKEDFRSFIERDLIEQSMLVALEQAGRLNWWVSMDSTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYALMEKGVEKEALRRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGSNGASGGGVESSEEPVYESLEEFHVFVLAHVLKRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKESAKEQAVIPLTDSEHKLLPLHFAVDPGKGWEWGKDDNDNVRLASIILSLEVKLHLLHSYMNVKWIPLSSDSQAPLAQPESPTASAGDEPRSTPESGESDKESVGSSSLGNEGSRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGPKPGGLGSGSGISSGTETLEKKKKNNTLKSWKGGKEEAAGDGPVSEKPPSESVGNGGSKYSQEVMQSLSTMRIAMQGEGKYIFVGTLKMGHRHQYQEEMIQRYLADAEERFLAEQKQKEVERKIMNGGLVSGPPPAKKPEPDGGEDQPSDSPAEPKAMAFSTAYPGGFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPSYATFPRQYPGRPYPHQDNIPALEPGKDGVHRGALLPPQFRVADSYSNGYREPPEPDGWAGAPRGLPPTQTKCKQPNCSFYGHPETNNLCSCCYREELRRREREPGGELLAHRF | 3.4.19.12 | null | adaptive immune response [GO:0002250]; in utero embryonic development [GO:0001701]; mucosal immune response [GO:0002385]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein K11-linked deubiquitination [GO:0035871]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type peptidase activity [GO:0008234]; DNA binding [GO:0003677]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; zinc ion binding [GO:0008270] | PF02338;PF01754; | 1.20.5.4770;1.10.8.10; | Peptidase C64 family | PTM: Phosphorylated by EGFR. {ECO:0000250|UniProtKB:Q6GQQ9}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6GQQ9}. Nucleus {ECO:0000250|UniProtKB:Q6GQQ9}. Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q6GQQ9}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23334419}; | null | null | null | null | FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B (PubMed:23334419). Negatively regulates mucosal immunity against infections (PubMed:23334419). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B (PubMed:26903241). Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (PubMed:26903241). Mediates deubiquitination of EGFR (By similarity). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains. Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure. Hydrolyzes both linear and branched forms of polyubiquitin (By similarity). {ECO:0000250|UniProtKB:Q6GQQ9, ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}. | Mus musculus (Mouse) |
B2RUY7 | VWC2L_HUMAN | MALHIHEACILLLVIPGLVTSAAISHEDYPADEGDQISSNDNLIFDDYRGKGCVDDSGFVYKLGERFFPGHSNCPCVCALDGPVCDQPECPKIHPKCTKVEHNGCCPECKEVKNFCEYHGKNYKILEEFKPSPCEWCRCEPSNEVHCVVADCAVPECVNPVYEPEQCCPVCKNGPNCFAGTTIIPAGIEVKVDECNICHCHNGDWWKPAQCSKRECQGKQTV | null | null | negative regulation of BMP signaling pathway [GO:0030514]; positive regulation of neuron differentiation [GO:0045666] | AMPA glutamate receptor complex [GO:0032281]; extracellular space [GO:0005615]; synapse [GO:0045202] | null | null | 6.20.200.20; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Synapse {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in neurogenesis. May play a role in bone differentiation and matrix mineralization. {ECO:0000250}. | Homo sapiens (Human) |
B2RUZ4 | SMIM1_HUMAN | MQPQESHVHYSRWEDGSRDGVSLGAVSSTEEASRCRRISQRLCTGKLGIAMKVLGGVALFWIIFILGYLTGYYVHKCK | null | null | null | cell surface [GO:0009986]; plasma membrane [GO:0005886] | protein homodimerization activity [GO:0042803] | PF15875; | null | SMIM1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26452714}; Single-pass type II membrane protein {ECO:0000269|PubMed:26452714}. | null | null | null | null | null | FUNCTION: Regulator of red blood cell formation. {ECO:0000250|UniProtKB:B3DHH5}. | Homo sapiens (Human) |
B2RVY9 | TM182_MOUSE | MRLNVAVFFGALFGALGVLLFLVAFGSDYWLLATEVGRCSGEQNIENITFHHEGFFWRCWFSGVVEENNSNIWKFWYTNQPPSKNCTHAYLSPYPFMRGEHNSTSYDSAIIYRGFWAVLLLLGVVAALTASFLIICAAPFSSHFLYKAGGGSYIASGVLFSLVVILYVIWVQAVADMESYRALRMRDCWEFTPSILYGWSFFLAPAGVFFSLLAGLLFLVVGRHIQIHH | null | null | muscle organ development [GO:0007517]; myotube cell development involved in skeletal muscle regeneration [GO:0014906]; myotube differentiation involved in skeletal muscle regeneration [GO:0014908]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast fusion [GO:1901740] | plasma membrane [GO:0005886] | null | PF13903; | 1.20.140.150; | TMEM182 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0A1D5NY17}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1 (PubMed:34427057). Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis (PubMed:34427057). {ECO:0000269|PubMed:34427057}. | Mus musculus (Mouse) |
B2RW38 | CFA58_MOUSE | MTEDKAEKVMPEETAFEEIEKDFQEVLSELSGDKSLEKFRTEYEKLHSIMKKSYENEKRLMAKCRELNAEIVVNSAKVATALKLSQDDQTTIASLKKEIEKAWKMVDSAYDKEQKAKETILALKEEIVNLTKLVEQGSGLSMDQDSNIRDLLKFKEEVTKERDQLLSEVVKLRENLAQTIEKQQAAEHAKEEAEMAISQFQQEIQHRQNEASRESRKKEKLEKELRQIQTDMDGRQAEIKAMQQYMHKSKEELQRLEQQLKEQKILNERAAKEVEQFQMRNAKLQQENDQHTLTCEQLSQENQQKALELKAKEDEIHQMRLDLGKLNKIREQIHKKLHQLDDQKAEVEQQKDTLKNQILGLEREVESSKKQAELDKKAMEELLRERDILNKNMLKAVSATQKQVDLVKLHEQAKKNLEEEIQNYKDEAQKQRKIIFQLEKERDRYINEASDLTQRVLANMEDIKVREIQIFDYRKKIAESETKLKQQQNLYEAVRSDRNLYSKNLVEAQDEITEMKRKLKIMTHQVDQLKEEISAKEAALVKLHLEQQRIEKEKETLKAELQKLRQQALETKHFIEKQEVEERKLLRIIAEADGERVRQKKELDQVISERDILGSQLVRRNDELALLYEKIKIQQSVLNKGETQYNQRVEDMRILKLEIKKLRREKGILARSVANVEELRQELYHMQREFLKERTRCRALEEELENPMNVHRWRKLEASDPSTFELIQKIHTLQKRLISKTEEVVEKELLLQEKEKLYVELKHILARQPGPEAAEQLQIYRHTLREKTKQLKVLSSELNMYESQSQEYKYEIERLGNELMSLKKKYLAQKRKELVLKNKDRMSMNNIFSETKKSVPRFTGGGFPLHQATKVKF | null | null | cilium assembly [GO:0060271]; flagellated sperm motility [GO:0030317]; Notch signaling pathway [GO:0007219]; protein localization to motile cilium [GO:0120229]; sperm axoneme assembly [GO:0007288]; sperm flagellum assembly [GO:0120316]; sperm mitochondrial sheath assembly [GO:0120317] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225] | null | PF21771; | null | CFAP58 family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:A8HUA1}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:32791035}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:31904090}. Note=Localized to the entire flagellum and predominantly concentrated in the midpiece. Co-localizes with ODFP2 at the centrosome. {ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:32791035}. | null | null | null | null | null | FUNCTION: Has an essential role in the assembly and organization of the sperm flagellar axoneme (PubMed:32791035). Required for the elongation of the primary cilium and sperm flagellar midpiece via modulation of the Notch signaling pathway (PubMed:31904090). {ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:32791035}. | Mus musculus (Mouse) |
B2RWS6 | EP300_MOUSE | MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQAMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGIGSSGPNQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQPLKMGMMNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVPGGGMPSMGQQPTPSVQQPGLVTPVAAGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQSILTGAPVGLGNPSSLGVGQQSTPSLSTVSQIDPSSIERAYAALGLPYQVNQIPPQPQVQAKNQQSQPSGQSPQGMRSVNNMSASPMGVNGGVGVQTPNLLSDSMLHSTINSQNPMMSENAGVASLGPLPTAAQPSSTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAPGMGPVPMNTGSNMGQQPTGMTTNGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGNQPPPATAIPTPVPTPPAIPPGPQPPSLHPSSRQTPTPPTHLPPQVQPSLPAAPSADQSQQQPRSQQSTAVSVPTPTAPLLPPQPSTPLSQPAVSIEGQVSNPPSTSSTEVNSQTIPEKQPSQEVKMESKMEVDKPEPADAQPEDTKEAKGEDVKVEPTEMEERGPELKTDGKEEEEQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLKKTARTRKENKLSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDILKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIACPAPNSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTTGPVSQGKAPGQVTPPTPPQTAQAPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANPNPQPLPGQPGMTQGQPGLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQQLQPPMGAMSPQAQQMNMNHNTMPSQFRDILRRQMMQQQGAGPGIGPGMANQFQQPQGIGYPPQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSSDNADLNSNLSQSTLDIH | 2.3.1.-; 2.3.1.48 | null | animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; B cell differentiation [GO:0030183]; behavioral defense response [GO:0002209]; canonical NF-kappaB signal transduction [GO:0007249]; cartilage development [GO:0051216]; cell cycle [GO:0007049]; cellular response to interleukin-1 [GO:0071347]; cellular response to leucine [GO:0071233]; cellular response to nutrient levels [GO:0031669]; cellular response to UV [GO:0034644]; chromatin remodeling [GO:0006338]; circadian rhythm [GO:0007623]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; heart development [GO:0007507]; internal protein amino acid acetylation [GO:0006475]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; learning or memory [GO:0007611]; lung development [GO:0030324]; macrophage derived foam cell differentiation [GO:0010742]; megakaryocyte development [GO:0035855]; multicellular organism growth [GO:0035264]; N-terminal peptidyl-lysine acetylation [GO:0018076]; negative regulation of autophagy [GO:0010507]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of miRNA metabolic process [GO:2000629]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine butyrylation [GO:0140067]; peptidyl-lysine crotonylation [GO:0140066]; peptidyl-lysine propionylation [GO:0061921]; platelet formation [GO:0030220]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of axon extension [GO:0045773]; positive regulation of cell growth [GO:0030307]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of cell size [GO:0045793]; positive regulation of cellular response to hypoxia [GO:1900039]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of glycoprotein biosynthetic process [GO:0010560]; positive regulation of hydrogen peroxide-mediated programmed cell death [GO:1901300]; positive regulation of muscle atrophy [GO:0014737]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein secretion [GO:0050714]; positive regulation of proteolysis [GO:0045862]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of sarcomere organization [GO:0060298]; positive regulation of T-helper 17 cell lineage commitment [GO:2000330]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of translation [GO:0045727]; protein acetylation [GO:0006473]; protein destabilization [GO:0031648]; protein modification process [GO:0036211]; protein stabilization [GO:0050821]; protein-DNA complex assembly [GO:0065004]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of angiotensin metabolic process [GO:0060177]; regulation of glycolytic process [GO:0006110]; regulation of mitochondrion organization [GO:0010821]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tubulin deacetylation [GO:0090043]; response to calcium ion [GO:0051592]; response to dexamethasone [GO:0071548]; response to estrogen [GO:0043627]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle tissue development [GO:0007519]; somitogenesis [GO:0001756]; swimming [GO:0036268]; thigmotaxis [GO:0001966]; transcription by RNA polymerase II [GO:0006366]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; cytosol [GO:0005829]; histone acetyltransferase complex [GO:0000123]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667] | acetylation-dependent protein binding [GO:0140033]; acetyltransferase activity [GO:0016407]; antigen binding [GO:0003823]; beta-catenin binding [GO:0008013]; bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase activity [GO:0004402]; histone butyryltransferase activity [GO:0140069]; histone crotonyltransferase activity [GO:0140068]; histone H2B acetyltransferase activity [GO:0044013]; histone H3K122 acetyltransferase activity [GO:0140908]; histone H3K18 acetyltransferase activity [GO:0043993]; histone H3K27 acetyltransferase activity [GO:0044017]; histone H4 acetyltransferase activity [GO:0010485]; histone lactyltransferase activity [GO:0120301]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468]; mitogen-activated protein kinase binding [GO:0051019]; NF-kappaB binding [GO:0051059]; nuclear androgen receptor binding [GO:0050681]; nuclear glucocorticoid receptor binding [GO:0035259]; p53 binding [GO:0002039]; peptide 2-hydroxyisobutyryltransferase activity [GO:0106226]; peptide-lysine-N-acetyltransferase activity [GO:0061733]; peroxisome proliferator activated receptor binding [GO:0042975]; pre-mRNA intronic binding [GO:0097157]; promoter-specific chromatin binding [GO:1990841]; protein antigen binding [GO:1990405]; protein kinase binding [GO:0019901]; protein propionyltransferase activity [GO:0061920]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]; STAT family protein binding [GO:0097677]; transcription coactivator activity [GO:0003713]; transcription coactivator binding [GO:0001223]; transcription coregulator binding [GO:0001221]; zinc ion binding [GO:0008270] | PF00439;PF09030;PF08214;PF02172;PF06001;PF02135;PF00569; | 2.10.110.40;3.30.60.90;1.20.920.10;1.10.246.20;1.10.1630.10;1.20.1020.10;3.30.40.10; | null | PTM: Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706. {ECO:0000250|UniProtKB:Q09472}.; PTM: Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. {ECO:0000250|UniProtKB:Q09472}.; PTM: Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 (By similarity). {ECO:0000250|UniProtKB:Q09472}.; PTM: Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 (By similarity). {ECO:0000250|UniProtKB:Q09472}.; PTM: Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation. {ECO:0000250|UniProtKB:Q09472}.; PTM: Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG (By similarity). Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity (By similarity). {ECO:0000250|UniProtKB:Q09472}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09472}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00311, ECO:0000269|PubMed:19324970}. Note=In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus. Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q09472}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:27105113}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:27105113}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; Evidence={ECO:0000269|PubMed:28576496, ECO:0000305|PubMed:28883095}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence={ECO:0000269|PubMed:28576496, ECO:0000305|PubMed:28883095}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-methyl-L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-N(6)-methyl-L-lysyl-[histone]; Xref=Rhea:RHEA:77775, Rhea:RHEA-COMP:9846, Rhea:RHEA-COMP:18984, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61929, ChEBI:CHEBI:197459; Evidence={ECO:0000250|UniProtKB:Q09472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77776; Evidence={ECO:0000250|UniProtKB:Q09472}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-butanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53912, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13708, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:137955; Evidence={ECO:0000269|PubMed:27105113}; CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q09472}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + propanoyl-CoA = CoA + H(+) + N(6)-propanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54020, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:138019; Evidence={ECO:0000250|UniProtKB:Q09472}; CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:Q09472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; Evidence={ECO:0000250|UniProtKB:Q09472}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + lactoyl-CoA = CoA + H(+) + N(6)-lactoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:61996, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:16001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57382, ChEBI:CHEBI:145324; Evidence={ECO:0000250|UniProtKB:Q09472}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997; Evidence={ECO:0000250|UniProtKB:Q09472}; | null | null | null | null | FUNCTION: Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (By similarity). Also able to acetylate histone lysine residues that are already monomethylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (By similarity). Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (By similarity). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1, SIRT2 or STAT3 (PubMed:28576496, PubMed:28883095). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (By similarity). Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis (By similarity). Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (By similarity). Acetylates HDAC1 leading to its inactivation and modulation of transcription (By similarity). Acetylates 'Lys-247' of EGR2 (PubMed:28576496). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (By similarity). Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium (By similarity). Promotes cardiac myocyte enlargement (By similarity). Can also mediate transcriptional repression (By similarity). Acetylates FOXO1 and enhances its transcriptional activity (By similarity). Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (By similarity). Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (By similarity). Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter (By similarity). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:14645221, PubMed:9512516). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (By similarity). Acetylates MEF2D (By similarity). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (PubMed:25200183). Acetylates PCK1 and promotes PCK1 anaplerotic activity (By similarity). Acetylates RXRA and RXRG (By similarity). Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (By similarity). Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:18486321, PubMed:24216764). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively (PubMed:27105113). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (By similarity). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:27105113). Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (By similarity). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:20810990, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:27105113, ECO:0000269|PubMed:28576496, ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:9512516, ECO:0000305|PubMed:20955178}. | Mus musculus (Mouse) |
B2RX12 | MRP3_MOUSE | MDRLCGSGELGSKFWDSNLSIYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWVDLFYSFHGLIHGSSPAPVFFVTPLVVGITMLLATLLIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSALAEGKILDPFRFTTFYIYFALVFCALILSCFKEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQQNQASRSQTATAEPKIPGEDAVLLKPRPKSKQPSFLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHEAALQNANEEVLLLEDTLSTHTDLTDNEPAIYEVRKQFMREMSSLSSEGEVQNRTMPKKHTNSLEKEALVTKTKETGALIKEEIAETGNVKLSVYWDYAKSMGLCTTLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA | 7.6.2.-; 7.6.2.2; 7.6.2.3 | null | bile acid and bile salt transport [GO:0015721]; canalicular bile acid transport [GO:0015722]; leukotriene transport [GO:0071716]; monoatomic anion transmembrane transport [GO:0098656]; transmembrane transport [GO:0055085]; xenobiotic transmembrane transport [GO:0006855] | basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; glucuronoside transmembrane transporter activity [GO:0015164]; icosanoid transmembrane transporter activity [GO:0071714] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:16225954}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Basal cell membrane {ECO:0000250|UniProtKB:O15438}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. | CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000250|UniProtKB:O88563}; CATALYTIC ACTIVITY: Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; Evidence={ECO:0000250|UniProtKB:O88563}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) + phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H(+) + phosphate + taurochenodeoxycholate 3-sulfate(out); Xref=Rhea:RHEA:66176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:166912, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66177; Evidence={ECO:0000250|UniProtKB:O88563}; CATALYTIC ACTIVITY: Reaction=(4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66180, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:229704, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=(4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:229706, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66193; Evidence={ECO:0000250|UniProtKB:O15438}; | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (PubMed:15814571, PubMed:16225954). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:O15438, ECO:0000269|PubMed:15814571, ECO:0000269|PubMed:16225954}. | Mus musculus (Mouse) |
B2RX14 | TUT4_MOUSE | MEEPKTSKNENHEPKKNIICEESKAVKIISNQTLKPRNDKSEIGTSSLNRNSSKKTKQNDICIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPNLPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQKTPRSPLEPENVPSLLLKENVKQTESQQTGKKLTSSFVSMDKRKSEALQGEKSALENSSLSQKQQTQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDVNIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSAGNDMACLTTDLLAALGKVEPVFTPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWEYNSSSATEKNLIADENKAKADEPKDDTKKTETDNQSNAAKAKHGKSPLTLEAPNQVPLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQKKGGNKSTMDPKKKEKGKLSSKKPVKSDCSATNCCILGESAEKIHMERGQPAKHDETEFTSQRCIVDNDSLLVNELGLANHGQDSSSLSTASGGSDLKQKSAEKQGDLTPSETSLKKELSQCICIGTPDGAESAGTDCRSNLEMDSSHQIVCNNVSATSCNCKATEVTSDLVDEDNLPSQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPVIPVLQEIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWTSKCIAIEDPFDLNHNLGAGVSRKMTNFIMKAFINGRKLFGTPFYPLIGREAEYFFDSRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKRLKKKDSEEEKEGNEEEKDSRDLLDSRDLRCFICGDAGHVRRECPEVKMARQRNSSVAAAQLVRNLVNAQQVAGSAQQQSDQSIRTRQSSECSDSPSYSPQPQPFPQNSPQPSALPPPPSQPGSQPKLGPPQQGGQPPHQVQMPLYNFPQSPPAHYSPMHSMGLLPMHPLQIPAPSWPIHGPMLHSAPGSTPSNIGLNDPSIIFAQPAARPMAIPSPSHDGHWPRTVAPNSLVNNGAVGNSEPRFRGLNPPIPWEHAPRHFPLVPASWPYGLHQNFMHQGNPRFQPKPFYAQADRCATRRCRERCPHPPRGNVSE | 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | interleukin-6-mediated signaling pathway [GO:0070102]; miRNA catabolic process [GO:0010587]; miRNA metabolic process [GO:0010586]; oocyte maturation [GO:0001556]; polyuridylation-dependent mRNA catabolic process [GO:1990074]; positive regulation of interleukin-6 production [GO:0032755]; pre-miRNA processing [GO:0031054]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; retrotransposon silencing by mRNA destabilization [GO:0141008]; RNA 3' uridylation [GO:0071076]; RNA 3'-end processing [GO:0031123]; stem cell population maintenance [GO:0019827] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; nucleus [GO:0005634] | miRNA binding [GO:0035198]; RNA uridylyltransferase activity [GO:0050265]; uridylyltransferase activity [GO:0070569]; zinc ion binding [GO:0008270] | PF01909;PF03828;PF19088;PF00098; | 1.10.1410.10;3.30.460.10;4.10.60.10; | DNA polymerase type-B-like family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAX3}. Cytoplasm {ECO:0000269|PubMed:19703396}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q5TAX3}. Note=Mainly cytoplasmic (PubMed:19703396). Translocates into the cytoplasm following treatment of the cell with LPS. Co-enriched in cytoplasmic foci with MOV10. {ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:19701194}; | null | null | null | null | FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:28792939). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (PubMed:28792939). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (By similarity). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (PubMed:19703396). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:28671666). Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (By similarity). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP (By similarity). Does not play a role in replication-dependent histone mRNA degradation (By similarity). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:22898984, PubMed:28671666, PubMed:28792939). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:28671666, ECO:0000269|PubMed:28792939}. | Mus musculus (Mouse) |
B2RX88 | CSPP1_MOUSE | MADSLDEFIEEQKAKLAKDKAELESDPPYMEMKGKASEKLSENSKILISMAKENIPPSSQQQPKGPLGIEYGLSLPLGEDYEQKKHKLKEELRQDYRRYLTQGITQAKRKKNFLSTGETDPSTLGVSLPIDERLSAKERLKLERNREYNQFLRGKAESTEKVRQVEKNIEPKSQRNKNPISQGKSDLPLQIQTAYTHSEGPWLSRQEEGLYRQLDGEIELRSRRPLKQTKEEVGISGAEHPSLSGSAGVPERRARRANGERVLDRQHCRADRDPGVSEDMDERFRFESDFDRRLLRVYTNGRPHGSRRGYVDGDDVPEEPNTQISAAENKSVHCNGPPRSADLDITSPFAGMLFGGEDRELTKRRKEKYRQELLEQIAEQQKKKRREKDLAFGITTSGVQDPEKSPDRLKQFSLTPRHFEEMPPERPRVAFQTPPPPFSAPSSPSVPPVHSAPSHNEDLHSGLGSTLGELAHPRVLPVPLNPPPPPLLAPPASNYRTPYDDAYYFYGARNTLDPNIVYYGSGMIGGQPAPHVSAPVTHQVAPPAVNTVGQNEQKVLSDGLRNSGLVFEDKPKPSTQSLQSYQEALQEQIREREARRKKERLEKEEYEAKLEAEMRIYNPWGKGGGGAPLRDAKGNLITDLNRMHRQNIDAYHNPDARTYEDKRAVVSIDQNLATSNAENLEDSANKNSGPLQTQSSPFARGNTFGEPLSELQIKQQELYKNFLRFQIEEKRQREEAEREKLRVAEEKEEKRLAEQRARIQQEYEEEQERRREKEEEQRLKNEELIRLAEERRKEAERKKKEEEEKHNLQLQHYYERENIIGDETKHLRQPSPVVPALQNKIASKLQRPPSVDTIISSFIHESSMSRAQSPPVPARKNQLRAEEEKKNVIMELSEMRKQLRSEERRLQGRLLHLDSDDEIPMRKRERNPMDIFDMARHRVQAPVRRPSPKGLDATTFQNIHDFNELRERDSDTRVDLRLMYPDPPRDHHTLEIQQQALLREQQKRLNRIKMRRDAGADLDTICTDNAQGRRMPRDDTNDFLKNSLLESDSAFIGAYGETYPVIEDNAFPPPSQLPSARERRRNKLKGLDFDSSRLHTPQDGLSLKSISSVNVDQVRMRNEDRMRRLTEQQKKPTNTDDEGSLVDPDDIMRHLSDDGRNSAATEPWLRPGTSESLKRFMAEHLNEEQHKGPGKPGTFTWQGLSAAHA | null | null | positive regulation of cell division [GO:0051781]; positive regulation of cytokinesis [GO:0032467] | centriolar satellite [GO:0034451]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; spindle [GO:0005819]; spindle pole [GO:0000922] | null | null | null | null | PTM: Phosphorylated. Phosphorylation increases in colcemide-treated cells (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19129481}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19129481}. Note=Associated with mitotic spindles. {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in cell-cycle-dependent microtubule organization. {ECO:0000250}. | Mus musculus (Mouse) |
B2RXA7 | CP26C_MOUSE | MISWGLSCLSVLGAAGTTLLCAGLLLGLAQQLWTLRWTLSRDWASTLPLPKGSMGWPFFGETLHWLVQGSRFHSSRRERYGTVFKTHLLGRPVIRVSGAENVRTILLGEHRLVRSQWPQSAHILLGSHTLLGAVGEPHRQRRKVLARVFSRSSLEQFVPRLQGALRREVRSWCAAQRPVAVYQAAKALTFRMAARILLGLQLDEARCTELAHTFEQLVENLFSLPLDVPFSGLRKGIRARDQLYEHLDEAVAEKLQEKQTAEPGDALLLIINSARELGHEPSVQELKELAVELLFAAFFTTASASTSLILLLLQHPAAITKIQQELSAQGLGRACTCTPRASGSPPDCGCEPDLSLAMLGRLRYVDCVVKEVLRLLPPVSGGYRTALRTFELDGYQIPKGWSVMYSIRDTHETAAVYRSPPEGFDPERFGVESGDARGSGGRFHYIPFGGGARSCLGQELAQAVLQLLAVELVRTARWELATPAFPVMQTVPIVHPVDGLLLFFHPLPTSGAGDGLPF | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305|PubMed:17067568}; | anterior/posterior pattern specification [GO:0009952]; central nervous system development [GO:0007417]; neural crest cell development [GO:0014032]; organelle fusion [GO:0048284]; retinoic acid catabolic process [GO:0034653]; sterol metabolic process [GO:0016125] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; retinoic acid 4-hydroxylase activity [GO:0008401]; retinoic acid binding [GO:0001972] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000305|PubMed:12915310, ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000305|PubMed:12915310, ECO:0000305|PubMed:15911617}; CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178; Evidence={ECO:0000305|PubMed:12915310, ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985; Evidence={ECO:0000305|PubMed:12915310, ECO:0000305|PubMed:15911617}; CATALYTIC ACTIVITY: Reaction=all-trans-4-hydroxyretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-oxoretinoate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75851, 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:134178, ChEBI:CHEBI:134186; Evidence={ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75852; Evidence={ECO:0000305|PubMed:15911617}; CATALYTIC ACTIVITY: Reaction=9-cis-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = 9-cis-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75847, 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:78630, ChEBI:CHEBI:139253; Evidence={ECO:0000250|UniProtKB:Q6V0L0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75848; Evidence={ECO:0000250|UniProtKB:Q6V0L0}; CATALYTIC ACTIVITY: Reaction=9-cis-4-hydroxyretinoate + O2 + reduced [NADPH--hemoprotein reductase] = 9-cis-4-oxoretinoate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75855, 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:139253, ChEBI:CHEBI:139254; Evidence={ECO:0000250|UniProtKB:Q6V0L0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75856; Evidence={ECO:0000250|UniProtKB:Q6V0L0}; CATALYTIC ACTIVITY: Reaction=all-trans-4-hydroxy-13,14-dihydroretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-oxo-13,14-dihydroretinoate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75859, 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:194184, ChEBI:CHEBI:194478; Evidence={ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75860; Evidence={ECO:0000305|PubMed:15911617}; CATALYTIC ACTIVITY: Reaction=all-trans-13,14-dihydroretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxy-13,14-dihydroretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75863, 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:194183, ChEBI:CHEBI:194478; Evidence={ECO:0000305|PubMed:15911617}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75864; Evidence={ECO:0000305|PubMed:15911617}; | null | null | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (Probable) (PubMed:15911617). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the oxidation of atRA primarily at C-4 (Probable). Oxidation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination, thereby contributes to the regulation of atRA homeostasis and signaling. Able to metabolize other RAs such as 9-cis with high efficiency (By similarity). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). Shares sequence similarity with other CYP26 family members, but has higher affinity to 9-cis-RA and is much less sensitive to the inhibitory effects of ketoconazole (By similarity). In cooperation with Cyp26a1, contributes to the CNS patterning and the development of regions of higher visual acuity (PubMed:15531370, PubMed:17067568). {ECO:0000250|UniProtKB:Q6V0L0, ECO:0000269|PubMed:15531370, ECO:0000269|PubMed:15911617, ECO:0000269|PubMed:17067568, ECO:0000305|PubMed:12915310, ECO:0000305|PubMed:15531370, ECO:0000305|PubMed:15872003, ECO:0000305|PubMed:15911617}. | Mus musculus (Mouse) |
B2RXE2 | SL9A5_MOUSE | MLSAALLLLPGLPLAGAGATEEPTQESGPLGEPPPGLALFRWQWHEVEAPYLVALWILVASLAKIVFHLSRKVTSLVPESCLLILLGLVLGGIVLAVAKKAEYQLEPGTFFLFLLPPIVLDSGYFMPSRLFFDNLGAILTYAVVGTLWNAFTTGVALWGLQQAGLVAPRVQAGLLDFLLFGSLISAVDPVAVLAVFEEVHVNQTLFIIIFGESLLNDAVTVVLYKVCNSFVEMGSANVQATDYLKGVASLFVVSLGGAAVGLVFAFLLALTTRFTKRVRIIEPLLVFLLAYAAYLTAEMASLSAILAVTMCGLGCKKYVEANISHKSRTAVKYTMKTLASCAETVIFMLLGISAVDSSKWAWDSGLVLGTLFFILFFRALGVVLQTWALNQFRLVPLDKIDQVVMSYGGLRGAVAFALVILLDRTKVPAKDYFVATTIVVVFFTVIVQGLTIKPLVKWLRVKRSDYHKPTLNQELHEHTFDHILAAVEDVVGHHGYHYWRDRWEQFDKKYLSQLLMRRSAYRIRDQIWDVYYRLNIRDAISFVDQGGHVLSSTGLTLPSMPSRNSVAETSVTNLLRESGSGACLDLQVIDTVRSGRDREDAVMHHLLCGGLYKPRRRYKASCGRHFISEDAQERQDKEIFQQNMKRRLESFKSTKHNICFTKSKPRPRKTSHKKKDGVANPEATNGKPPRDLGFQDTAAVILTVESEEEEESDSSETEKEDDEGIIFVARATSEVLQEGKVSGSLEVCPSPRIIPPSPTCAEKELPWKSGQGDLAVYVSSETTKIVPVDMQTGWNQSISSLESLASPPCTQPPTLTRLPPHPLVTEEPQVPIDLSSDPRSSFAFPPSLAKAGRSRSESSADIPQQELQPLMGHKDHTHLSPGTANSHWCIQFNRGGRL | null | null | potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814] | dendritic spine membrane [GO:0032591]; focal adhesion [GO:0005925]; neuron spine [GO:0044309]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; recycling endosome membrane [GO:0055038]; synapse [GO:0045202] | arrestin family protein binding [GO:1990763]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Phosphorylated by PRKAA2; promotes its accumulation at the cell surface. Phosphorylated by CSNK2A1 in a manner favoring its beta-arrestin binding and endocytosis. {ECO:0000250|UniProtKB:Q14940}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14940}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q14940}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q14940}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q14940}; Multi-pass membrane protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q14940}. Note=Cycles between recycling endosome and plasma membrane in response to diverse stimuli. Its internalization is clathrin- and beta-arrestin dependent and its plasma membrane insertion from the recycling endosomes requires phosphoinositide 3-kinase (PIK3CA) and SCAMP2. {ECO:0000250|UniProtKB:Q14940}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q14940}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29421; Evidence={ECO:0000250|UniProtKB:Q14940}; | null | null | null | null | FUNCTION: Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry. Responsible for regulating intracellular pH homeostasis, in particular in neural tissues. Acts as a negative regulator of dendritic spine growth. Plays a role in postsynaptic remodeling and signaling. Can also contribute to organellar pH regulation, with consequences for receptor tyrosine kinase trafficking. {ECO:0000250|UniProtKB:Q14940}. | Mus musculus (Mouse) |
B2RXF5 | ZBT42_HUMAN | MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDRPAGSRDTVRLNGDIVTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLQEKDRSLDPGNPAPGAEPAQPPCPWPVWTADLCPAARKAKLPPFGVKAALPPRASGPPPCQVPEESDQALDLSLKSGPRQERVHPPCVLQTPLCSQRQPGAQPLVKDERDSLSEQEESSSSRSPHSPPKPPPVPAAKGLVVGLQPLPLSGEGSRELELGAGRLASEDELGPGGPLCICPLCSKLFPSSHVLQLHLSAHFRERDSTRARLSPDGVAPTCPLCGKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHTVVHTREKPHACRWCERRFTQSGDLYRHVRKFHCGLVKSLLV | null | null | muscle organ development [GO:0007517]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872] | PF00651;PF00096;PF13894; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family, ZBTB18 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q811H0}. Nucleus {ECO:0000269|PubMed:21193930}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q811H0}. Note=In skeletal myofibers, highly enriched in subsynaptic nuclei at the neuromuscular junctions. {ECO:0000250|UniProtKB:Q811H0}. | null | null | null | null | null | FUNCTION: Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. {ECO:0000250|UniProtKB:Q811H0}. | Homo sapiens (Human) |
B2RXH2 | KDM4E_HUMAN | MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL | 1.14.11.66 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:21914792}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:21914792}; | chromatin remodeling [GO:0006338]; regulation of gene expression [GO:0010468] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; metal ion binding [GO:0046872] | PF02373;PF02375; | 2.60.120.650; | JHDM3 histone demethylase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence={ECO:0000305|PubMed:21914792}; | null | null | null | null | FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. {ECO:0000269|PubMed:21914792}. | Homo sapiens (Human) |
B2RXS4 | PLXB2_MOUSE | MALPLWALTFLGLTGLGLSLRSRKPESFRSETELNHLAVDEVTGVVYVGAVNALYQLSADLHVQQHVVTGPFMDNKKCTPPIEASQCHEAVLTDNFNQLLLLDPPGKRLVECGSLFKGICALRAMSNISVRLFYEDGSGEKSFVASNDERVATVGLVTSTRPDGERVLFVGKGNGPHDNGIIVSTRLLDRAEGREAFEAYSDHTTFKAGYLSTNTQQFVAAFEDDFYVFFVFNHQDKHPAKNRTLLARMCKDDPSYYSYVEMDLQCQDPSDPQDSAFGTCLAASVATSGAGRALYAVFSRDGRSTGGPGAGLCVFPLDKVREKIEANRNACYTGAREAGRTIFYKPFHGEIQCGGHLIGASESFPCGSEHLPYPLGSRDGLVATAVLHRGGLNLTAVTVTAENDHTVAFLGTSDGRILKVYLAPDGTSAEYGSIPVDINKKIKQDLALSGNLSSLYAMTQDKVFRLPVQECLSYVTCAQCRDSQDPYCGWCVIEGRCTRKSECSRAEETGHWLWSREKSCVAITDAFPQNMSRRAQGEVRLSVSPLPTLTEDDELLCLFGDSPPHPARVEDDTVICNSPSSIPSTPPGQDHVDVSIQLLLKSGSVFLTSHQYPFYDCREAMSLVENLPCISCASNRWTCQWDLQYYECREASPNPEEGIIRAHMEDNCPQFLAPDPLVIPMNHETEVTFQGKNLETVKVSSLYVGSELLNFEETVTMHESDTFSFRTPKLSHDGNETLPLHLYVKSFGKNIDSKLQVTLYNCSFGRSDCSLCLAADPAYRCVWCRGQNRCVYEALCSNVTSECPPPVITRIQPETGPLGGGILVTIHGSNLGVKADDVKKITVAGQNCAFEPRGYSVSTRIVCAIEASEMPFTGGIEVDVNGKLGHSPPHVQFTYQQPQPLSVEPRQGPQAGGTTLTINGTHLDTGSKEDVRVTLNDVPCEVTKFGAQLQCVTGQQLAPGQVTLEIYYGGSRVPSPGISFTYCENPMIRAFEPLRSFVSGGRSINVTGQGFSLIQKFAMVVIAEPLRSWRRRRREAGALERVTVEGMEYVFYNDTKVVFLSPAVPEEPEAYNLTVLIRMDGHCAPLRTEAGVFEYVADPTFENFTGGVKKQVNKLIHARGTNLNKAMTLEEAEAFVGAERCIMKTLTETDLYCEPPEVQPPPKRRQKRDTAHNLPEFIVKFGSREWVLGRVEYDTRASDVPLSLILPLVMVPMVFIIVVSIYCYWRKSQQAEREYEKIKSQLEGLEESVRDRCKKEFTDLMIEMEDQTNDVHEAGIPTLDYKTYTDRVFFLPSKDGDKDVMITGKLDIPESRRPIVEQALYQFSNLLNSKSFLINFIHTLENQREFSARAKVYFASLLTVALHGKLEYYTDIMRTLFLELMEQYVVAKNPKLMLRRSETVVERMLSNWMSICLYQYLKDSAGEPLYKLFKAIKHQVEKGPVDAVQKKAKYTLNDTGLLGDDVEYAPLTVSVIVQDEGIDAIPVKVLNCDTISQVKEKIIDQVYRTQPCSCWPKPDSVVLEWRPGSTAQILSDLDLTSQREGRWKRINTLMHYNVRDGATLILSKVGVSQQPEDSQQDLPGERHALLEEENRVWHLVRPTDEVDEGKSKRGSMKEKERTKAITEIYLTRLLSVKGTLQQFVDNFFQSVLAPGHAVPPAVKYFFDFLDEQAEKHDIRDEDTIHIWKTNSLPLRFWVNILKNPHFIFDVHVHEVVDASLSVIAQTFMDACTRTEHKLSRDSPSNKLLYAKEISTYKKMVEDYYKGIRQMVQVSDQDMNTHLAEISRAHTDSLNTLVALHQLYQYTQKYYDEIINALEEDPAAQKMQLAFRLQQIAAALENKVTDL | null | null | brain development [GO:0007420]; excitatory synapse assembly [GO:1904861]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell adhesion [GO:0007162]; neural tube closure [GO:0001843]; neuroblast proliferation [GO:0007405]; positive regulation of axonogenesis [GO:0050772]; positive regulation of neuron projection development [GO:0010976]; positive regulation of translation [GO:0045727]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; regulation of GTPase activity [GO:0043087]; regulation of neuron migration [GO:2001222]; regulation of protein phosphorylation [GO:0001932]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287] | collagen-containing extracellular matrix [GO:0062023]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21966369}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling (PubMed:17554007). Plays a role in glutamatergic synapse development and is required for SEMA4A-mediated excitatory synapse development (PubMed:29981480). Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248' (PubMed:17554007). Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development (PubMed:19948886). Regulates the migration of cerebellar granule cells in the developing brain (PubMed:21122816). Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton (By similarity). Plays a role in axon guidance, invasive growth and cell migration (By similarity). May modulate the activity of RAC1 and CDC42 (PubMed:21966369). Down-regulates macrophage migration in wound-healing assays (in vitro) (PubMed:21966369). {ECO:0000250|UniProtKB:O15031, ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:19948886, ECO:0000269|PubMed:21122816, ECO:0000269|PubMed:21966369, ECO:0000269|PubMed:29981480}. | Mus musculus (Mouse) |
B2RXV4 | FLVC1_MOUSE | MARPDDEVGPAVAPGHPLGKGYLPVPKGAPDGEARLVPQNGPEALNGGPGLGPLIAGAQGGPQALIAAEEETQARLLPAGDGEDVPCPACPPRTALSPRRFVVLLIFSLYSLVNAFQWIQYSSISNVFEDFYEVSPLHINWLSMVYMVAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCGSVQRHLFWVTMLGQILCSVAQVFILGLPSPVASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPALGTQNSTGLLAHTQNNTDLLAHNINTMFYGTAFISTFLFFLTIIAFKEKPPLPPSQAQAVLRDSPPEEYSYKSSIWNLCRNIPFVLLLVSYGIMTGAFYSISTLLNQIILTYYVGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYVLSFIGMLIFTFTLNLGYIIVVFFTGGILGFFMTGYLPLGFEFAVEITYPESEGMSSGLLNTAAQILGIFFTLAQGKITTDYNSPEAGNIFLCAWMFVGIILTALIKSDLRRHNINTGLTNIDVKAVPVDSRVDPKPKVMVSIQSESSL | null | null | blood vessel development [GO:0001568]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal system morphogenesis [GO:0048704]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; head morphogenesis [GO:0060323]; heme export [GO:0097037]; heme transport [GO:0015886]; in utero embryonic development [GO:0001701]; limb morphogenesis [GO:0035108]; mitochondrial transport [GO:0006839]; multicellular organism growth [GO:0035264]; regulation of organ growth [GO:0046620]; spleen development [GO:0048536] | membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | heme binding [GO:0020037]; heme transmembrane transporter activity [GO:0015232] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Feline leukemia virus subgroup C receptor (TC 2.A.1.28.1) family | PTM: N-Glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane {ECO:0000269|PubMed:23187127}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with HADHA. {ECO:0000269|PubMed:23187127}. | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=heme b(in) = heme b(out); Xref=Rhea:RHEA:75443, ChEBI:CHEBI:60344; Evidence={ECO:0000305|PubMed:23187127}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75444; Evidence={ECO:0000305|PubMed:23187127}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=heme b(in) = heme b(out); Xref=Rhea:RHEA:75443, ChEBI:CHEBI:60344; Evidence={ECO:0000305|PubMed:23187127}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75444; Evidence={ECO:0000305|PubMed:23187127}; | null | null | null | null | FUNCTION: [Isoform 1]: Heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythropoiesis, a process in which heme synthesis intensifies. Possibly export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. The molecular mechanism of heme transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated. {ECO:0000250|UniProtKB:Q9Y5Y0, ECO:0000269|PubMed:18258918, ECO:0000269|PubMed:23187127}.; FUNCTION: [Isoform 2]: Heme transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation. {ECO:0000269|PubMed:23187127}. | Mus musculus (Mouse) |
B2RXZ1 | PNDC1_MOUSE | MDVGADEFEQSLPLLQELVAGADFVGLDIEFTGLRSNLSRPQQISLFDLPSEWYLKTRQSVQQFTICQIGLSMFSSIEGESNKYVAHSCNFFLFPTTFGILDSEFSFQASSVQFLNQYGFDYNKFLKNGIPYMNEEQEKKIKHSILRGNWRVRSSLDKDQIKVVIDKVTQWLDLAEEGDQMTLPGIAGFQAFEVQLVLRQALPNIWTVLKEEWVIVKKVSQPQRWYLEHASCDQVSCWKEQILLSARGFSVFFQMLVKAQKPLVGHNMMMDLLHLHEKFFRPLPESYDQFKQNIHSLFPVLIDTKNVTKDIWKELRFPRVSNLLEVYEVLSSNLNPTKDSGPVIIHARQCKKYAETKCPHEAAYDAFLCGSVLLKVAHLLLQRVHGNGAVHEPAFPQYLDVLAPYVNQVNLIRAGVPKINFSGPDYPSIRPPVLILTVKRWPGVSEQQVYREFQNLCKFDVRRFTRSQFLLLTNKFKDARSVLKEYRNHPTLQVSLYRSWRHSPNITCLLQVCSIVTTWAMIAFLLGRPMP | 3.1.13.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8NA58}; | blastocyst formation [GO:0001825]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; piRNA processing [GO:0034587]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723] | PF04857; | 3.30.420.10; | CAF1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27515512}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NA58}. Note=Localizes mainly in the endoplasmic reticulum. {ECO:0000269|PubMed:27515512}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000269|PubMed:27515512}; | null | null | null | null | FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails (PubMed:27515512). Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development (PubMed:27515512). May act as a regulator of multipotency in embryonic stem cells (PubMed:27515512). Is a critical factor for proper spermatogenesis, involved in pre-piRNAs processing to generate mature piRNAs (By similarity). {ECO:0000250|UniProtKB:Q8NA58, ECO:0000269|PubMed:27515512}. | Mus musculus (Mouse) |
B2RY04 | DOCK5_MOUSE | MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEATVEDGGQHETVIPGELPLVQELTNTLREWAVIWRKLYVNNKVTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTVALFRAHEVASKRIEEKIQEEKSILQNLDLRGQAIFSTVHTYGLYVNFKNFVCNIGEDAELFIALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSTDLIRPRISLVCQIVRVGRMELKEGKKHTCGLRRPFGVAVMDISDIVHGKVDDEEKQHFIPFQQIAMETYIRQRQLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHLVDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVFDEEGNLLEKAIHPGAGYEGVSEYKSVVYYQVKQPCWYETVKVFIAIEEVTRCHIRFTFRHRSSQESRDKSERAFGVAFVKLMNADGTTLQDGRHDLVVYKGDNKKMEDAKYYLTLPGTKAELEEKELQASKNPSVFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEVDGGEIVKFLQDTLDALFNIMMEMSDNETYDFLVFDALVFIISLIGDIKFQHFNPVLETYIYKHFSATLAHVKLSKVLNFYVANAEDPSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQSEDGDEFNDSIRQLFLAFNTLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPMELSVLFCKFIQSIPDNQLVRQKLNCMTKIVESSLFQQAECREVLLPLLTDQLSGQLDDHSTKPDHEASSQLLSNILEVLDRTDVGPTSAHVQLIMERLLRRINRTVIGMSRQSPHIGSFVACMIAVLRQMEDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAINQFAEVLTKSFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSEAKRNKIVKKYGDMRKEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNLSGNGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLANSGEAFAFLVSSLLENLLDYRTIIIHDESKENRMSCTVNVLNFYKDKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQRDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGSLLKKRALFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYLQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFSYSRPFRKGEKDPENEFATMWIERTTYRTAYTFPGILKWFEAKEISVEEISPLENAIETMELTNERVSNCVQQHAWDHSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQIPLLTEGIRIHGEKLTEQLKPLHARLSSCFRELKEKVEKLYGVITLPPSMTERKPSRAGSMVLPYILSSTLRRLSVTSVASSVISTSSNSSDNASSRPGSDGSILEPLFERRASSGARVEDLPPKEDSENRISKFKRKDWNLSKSQVIAEKAPEPDVMSPGKKTQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLTASVPPPPPPKSKPYESSQRNSAEIAPPLPVRRDSKAPPPPPPKARKSGILSSEPGSQ | null | null | bone remodeling [GO:0046849]; cell migration [GO:0016477]; myoblast fusion [GO:0007520]; negative regulation of vascular associated smooth muscle contraction [GO:1904694]; podosome assembly [GO:0071800]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; Rac protein signal transduction [GO:0016601] | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; podosome [GO:0002102] | GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF06920;PF20422;PF20421;PF14429;PF16172;PF00018; | 1.20.58.740;1.25.40.410;2.60.40.150;1.20.1270.350;2.30.30.40; | DOCK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18396277}. Cell membrane {ECO:0000250|UniProtKB:Q9H7D0}. Cell projection, podosome {ECO:0000269|PubMed:27505886}. Note=Associated with the edge of the plasma membrane in intestinal epithelial cells spreading on type IV collagen. {ECO:0000250|UniProtKB:Q9H7D0}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP (PubMed:18396277). Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (By similarity). {ECO:0000250|UniProtKB:Q9H7D0, ECO:0000269|PubMed:18396277}. | Mus musculus (Mouse) |
B2RY50 | ODAD2_MOUSE | MGVALTRLAQWTAAGYETGTLEITPLNESILNEITKFVESFSYKYPQEAKFVFVEPLEWKTYLEPSAFELGYVVSATTAESEETGKDGQPLLFLSVPYIKVRSFGQLSQLLSIATDSKLQEAQACIEANRDPVVKILGPDYNEMKEDPTRLTLLDTIIKDKETYMKRKVAILLKQLDLHLLNHSLKYISLEISLNPGTFKKDIELLKRFSGKGEQTVLESIEYTSDYEFSNGCRAPPWRQIQGEICYVLVKPHDMETLCLTCSTEGVFLNGGKTEEEGEINYERKGEIYKDLVTCLKDKSPVFSENMSKHEIRFTEEQQKDNQIFEKPKTEDGHSSVAGSEKSKIEKISFGKSPMTKRLEPSLNWRVTVDYKDHKSSIKDSQEEKQGKLEKSSSVSVAPSRAQSHRKGGEKVEETVSESSSESEEDEEPPDHRQEANADLPSEYWQIQKLVKYLKGGNQTATVIALCSMRDFNLAQETCQLAIRDVGGLEVLINLLDTDEVKCKIGSLKILKEISHNPQIRRNIVDLGGLPIMVNILDSPHKSLKCLSAETIANVAKFKRARRAVRQHGGITKLVALLDCGQNSTEPTQPSLYETRDVEVARCGALALWSCSKSHSNKEAIRKAGGIPLLARLLKTSHENMLIPVVGTLQECASEENYRAAIKAERIIENLVKNLNSENEQLQEHCAMAIYQCAEDEETRDLVRLHGGLKPLASLLNNTDNKERLAAVTGAIWKCSISKENVIKFREYKAIETLVGLLTDQPEEVLVNVVGALGECCQEYENRVLVRKCGGIQPLVNLLVGINQALLVNVTKAVGACAVEPESMAIIDRLDGVRLLWSLLKNPHPDVKASAAWALCPCIENAKDAGEMVRSFVGGLELVVNLLKSDNKEVLASVCAAITNIAKDQENLAVITDHGVVPLLSKLANTNNDKLRRHLAEAISRCCMWGRNRVAFGEHKAVAPLVRYLKSNDTNVHRATAQALYQLSEDADNCITMHENGAVKLLLDMVGSPDQDLQEAAAGCISNIRRLALATEKARYN | null | null | cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; outer dynein arm assembly [GO:0036158]; regulation of cilium beat frequency [GO:0003356]; ventricular system development [GO:0021591] | axoneme [GO:0005930]; ciliary base [GO:0097546] | null | PF00514;PF13646; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q5T2S8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5T2S8}. | null | null | null | null | null | FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule (By similarity). Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (PubMed:23849778). {ECO:0000250|UniProtKB:E1B8W3, ECO:0000269|PubMed:23849778}. | Mus musculus (Mouse) |
B2RY71 | DNAI3_MOUSE | MAPKPPKSPKGQKKGKKNMKQQLLVPEEEEPMNMESMGHPEIYPLVLTTKTQEIFNCRVDEDMTDEQTYKLIKKEDILADLQNRAAVSDFHPVKKIVREYPGEELLLVYDKDFKYGLNFYLIGTEDGKENFLKPPEVPEEQEEPKEHVQEDVYVYNPPVSKPWVSLGSEKEIEEESVQESGKRVTYMISRKRSEFGAPVTFSDQNASSVKDAYIECTSYPEKNYTLSQVEKDVGLQVIAEVKDTSTQTKWAFPKNATTQYYPREFSEEEKSLIGKSKSLVDFFNNVSTSVEVALQQNEIMNTFIDDWKNLAEEESTFGDKTDTHLKEYQSFTDLHNTMEKMITCVSWHPTIFGLIVVSVAVRLSYEERVQNSGRLLLQPSLLLFWSFSDPIHPQLMLESPDDIFCFEFCPSDPNIIAGGCINGQIVLWDITAHADRIENIKTGGHRSKKTSLKPMFLLEPDSNKESMYIRHCAVSSIENGHRKVITDIHWLPDSFEINRMGSVFENRSGINCQLVTCSADCTICFWDIRPQKPAVTAAAAASAATTATNNANSQQSPVEKKKEENIDIPFDVPSTFLHLDLSWKPLSRLKLSKGDTSLDHCPTKLSLGEDPFLCKIQGTSSIHIILRDKMLSQIKMVKTSEINPYQNLEAGIANILKPIEDFCTKFFVGTEEGEVIYTDWKMERDSDTGRLMAKKPVSLYTVHDGAVHTIQRSPFFNDIVLTVGGWNVAIWKEEVMTGPLLQTCCGPKRYTAGHWSLTRPGVFYIGREDGNVDIWDLLEKTHEPAQSQNICITMITYIKPWTFSSKQQFIAVADYYGTLHILEIPWTLSHPSLNEVSSVNYYFEREVRHLEYVQQRKEIREQEKIDMALELVKKKAKIYQKTKEQMEAELKLEYESYLDLEKSVLFALGLSKVSEKKSYLDSH | null | null | cilium movement involved in cell motility [GO:0060294]; inner dynein arm assembly [GO:0036159]; negative regulation of Arp2/3 complex-mediated actin nucleation [GO:0034316]; negative regulation of cell migration [GO:0030336]; positive regulation of osteoblast differentiation [GO:0045669] | axonemal dynein complex [GO:0005858]; cytoplasm [GO:0005737]; inner dynein arm [GO:0036156] | Arp2/3 complex binding [GO:0071933]; dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503] | null | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWG1}. | null | null | null | null | null | FUNCTION: Acts as a negative regulator of cell migration, invasion, and metastasis downstream of p53/TP53, through inhibition of Arp2/3 complex-mediated actin polymerization (By similarity). Via its association with the multisubunit axonemal dynein complex, is potentially involved in the regulation of cilia function (PubMed:30060180). May play a role in osteogenesis of dental tissue-derived mesenchymal stem cells (PubMed:25498833). {ECO:0000250|UniProtKB:Q8IWG1, ECO:0000269|PubMed:25498833, ECO:0000269|PubMed:30060180}. | Mus musculus (Mouse) |
B2RYF7 | WASH1_RAT | MTAVKTQHSLAGQVYAVPLIQPDLRREEAIQQVADALQYLQNISGDIFSRISQRVELSRRQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPEHLQEYNSVFTGALDPGLQRRPRYRIQSKHRPLDERALQEKLKYFPVCVSTKSEPEDEAEEGLGGLPSNISSISSLLLFNTTENLYKKYVFLDPLAGAVTKTHTMLGTEEEKLFDAPLSISKREQLEQPAPENYFYVPGLGQVPEIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPAFHTEVAEPFQPEREDGALLAPPPPPPPPPPPPPPAPTAVVSAPQPPMSPDVVTVTGKVAREEDSGSGEAHSASVQGAPKEVVDPSSGRATLLESIRQAGGIGKAKLRSVKERKLEKKKQKEQEQVRATSQGGDLMSDLFNKLVMRRKGISGKGPGTGTSEGPGGAFSRMSDSIPPLPPPQQPAGDEDEDDWES | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; dendritic cell antigen processing and presentation [GO:0002468]; early endosome to late endosome transport [GO:0045022]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; endosome to plasma membrane protein transport [GO:0099638]; exocytosis [GO:0006887]; extracellular matrix disassembly [GO:0022617]; low-density lipoprotein particle clearance [GO:0034383]; meiotic spindle assembly [GO:0090306]; negative regulation of autophagy [GO:0010507]; oocyte maturation [GO:0001556]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of cell migration [GO:0030335]; positive regulation of cholesterol import [GO:1904109]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of pseudopodium assembly [GO:0031274]; protein localization to cell surface [GO:0034394]; protein targeting to lysosome [GO:0006622]; regulation of actin filament polymerization [GO:0030833]; regulation of immune response [GO:0050776]; regulation of protein ubiquitination [GO:0031396]; retrograde transport, endosome to Golgi [GO:0042147]; T cell proliferation [GO:0042098] | autophagosome [GO:0005776]; BLOC-1 complex [GO:0031083]; centrosome [GO:0005813]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; exocyst [GO:0000145]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; late endosome [GO:0005770]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; ubiquitin protein ligase binding [GO:0031625] | PF11945; | null | WASH1 family | PTM: Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly. {ECO:0000250|UniProtKB:A8K0Z3}. | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2. Localized to Salmonella typhimurium entry sites (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8}. | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in cytokinesis and following polar body extrusion during oocyte meiotic maturation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity. {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}. | Rattus norvegicus (Rat) |
B2RYG6 | OTUB1_RAT | MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHVFPEGSEPKVYLLYRPGHYDILYK | 3.4.19.12 | null | adaptive immune response [GO:0002250]; cellular response to interleukin-1 [GO:0071347]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; negative regulation of double-strand break repair [GO:2000780]; positive regulation of TORC1 signaling [GO:1904263]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; deNEDDylase activity [GO:0019784]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase inhibitor activity [GO:0055105] | PF10275; | 3.30.200.60;1.20.1300.20; | Peptidase C65 family | PTM: Phosphorylation at Tyr-26 by SRC and SRMS promotes deubiquitination of RPTOR via a non-catalytic process. {ECO:0000250|UniProtKB:Q96FW1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19343716}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q96FW1}; | null | null | null | null | FUNCTION: Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (By similarity). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (By similarity). Acts via its interaction with RNF128/GRAIL (By similarity). Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (By similarity). Deubiquitinates estrogen receptor alpha (ESR1) (By similarity). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (By similarity). Not able to cleave di-ubiquitin (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (By similarity). {ECO:0000250|UniProtKB:Q96FW1}.; FUNCTION: Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain. Acts as a regulator of mTORC1 and mTORC2 complexes. When phosphorylated at Tyr-26, acts as an activator of the mTORC1 complex by mediating deubiquitination of RPTOR via a non-catalytic process: acts by binding and inhibiting the activity of the ubiquitin-conjugating enzyme E2 (UBE2D1/UBCH5A, UBE2W/UBC16 and UBE2N/UBC13), thereby preventing ubiquitination of RPTOR. Can also act as an inhibitor of the mTORC1 and mTORC2 complexes in response to amino acids by mediating non-catalytic deubiquitination of DEPTOR. {ECO:0000250|UniProtKB:Q96FW1}. | Rattus norvegicus (Rat) |
B2RYM5 | BRCC3_RAT | MAVPVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDVRSESKFAHAGSDVCTVPEKVDSIRVVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSVQAQKSSDYERIEIPVHVVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQREKEELMAELRSLE | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7, ECO:0000250|UniProtKB:P46736}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; cellular response to ionizing radiation [GO:0071479]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; response to ionizing radiation [GO:0010212]; response to X-ray [GO:0010165] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]; spindle pole [GO:0000922]; ubiquitin ligase complex [GO:0000151] | cysteine-type deubiquitinase activity [GO:0004843]; enzyme regulator activity [GO:0030234]; K63-linked deubiquitinase activity [GO:0061578]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity). {ECO:0000250|UniProtKB:P46736, ECO:0000250|UniProtKB:P46737}. | Rattus norvegicus (Rat) |
B2RYN7 | SPAST_RAT | MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRFSRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMVSGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV | 5.6.1.1 | null | anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cytokinetic process [GO:0032506]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; exit from mitosis [GO:0010458]; membrane fission [GO:0090148]; metabolic process [GO:0008152]; microtubule bundle formation [GO:0001578]; microtubule severing [GO:0051013]; mitotic cytokinesis [GO:0000281]; mitotic spindle disassembly [GO:0051228]; nuclear membrane reassembly [GO:0031468]; positive regulation of cytokinesis [GO:0032467]; positive regulation of microtubule depolymerization [GO:0031117]; protein hexamerization [GO:0034214]; protein homooligomerization [GO:0051260] | axon [GO:0030424]; axon cytoplasm [GO:1904115]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle pole [GO:0000922] | alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; beta-tubulin binding [GO:0048487]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568] | PF00004;PF17862;PF09336; | 1.10.8.60;3.40.50.300;1.20.58.80; | AAA ATPase family, Spastin subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021}. | CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021}; | null | null | null | null | FUNCTION: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}. | Rattus norvegicus (Rat) |
B2RYR0 | RN168_RAT | MAAPKNSIPSLAECQCGICMEILVEPVTLPCNHTLCNPCFQSTVEKANLCCPFCRRRVSSWTRYHTRRNSLVNTDLWEIIQKHYAKECKLRISGQESKEIVDEYQPVRLLSKPGELRREYEEEISKVEAERQASKEEENKASEEYIQRLLAEEEEEEKRRTERRRSEMEEQLRGDEELARRLSTSINSNYERNILASPLSSRKSDPVTNKSQKKNTNKQKNFGDIQRYLSPKSKPGTAWACKTEHGEDMCKSKETDSSDTKSPVLQDTDVEESMPTHSPQTCPETQGQGPEPLTEMPVPWLCARNAEQCLEGKAEAVSTNPDDSCIVNDGGPRAIVSNSKEAAVKPPTKIENEEYSVSGVTQLTGGNGVPTESRVYDLLVGKEISERENQESVFEEVMDPCFSAKRRKIFITSSLDQEETEVNFTQKLIDLEHMLFERHKQEEQDRLLALQLQKEADKEKMVPNRQKGSPDQYQLRTSSPPDGLLNGQRKNVKDRNSPKQTADRSKSQRSRKGEYWETFESTWKGSVNGTKMPTPRKDSCNVSKRACPLQHRSAQKSILQMFQR | 2.3.2.27 | null | cellular response to UV [GO:0034644]; DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand break repair via nonhomologous end joining [GO:0006303]; epigenetic regulation of gene expression [GO:0040029]; isotype switching [GO:0045190]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of DNA repair [GO:0045739]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; regulation of protein localization [GO:0032880]; response to ionizing radiation [GO:0010212]; ubiquitin-dependent protein catabolic process [GO:0006511] | DNA repair complex [GO:1990391]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of double-strand break [GO:0035861]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; histone H2AK15 ubiquitin ligase activity [GO:0140858]; histone ubiquitin ligase activity [GO:0140852]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]; ubiquitin binding [GO:0043130]; ubiquitin-protein transferase activity [GO:0004842] | PF00097; | 3.30.40.10; | RNF168 family | PTM: Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs). {ECO:0000255|HAMAP-Rule:MF_03066}.; PTM: Ubiquitinated. {ECO:0000255|HAMAP-Rule:MF_03066}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03066}. Note=Localizes to double-strand breaks (DSBs) sites of DNA damage. {ECO:0000255|HAMAP-Rule:MF_03066}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000255|HAMAP-Rule:MF_03066}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|HAMAP-Rule:MF_03066}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066}. | Rattus norvegicus (Rat) |
B2RZ55 | SIR7_RAT | MAAGGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESEDLVTELQGRSRRREGLKRRQEEVCDDPEELRRKVRELAGAVRSARHLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRPVSAADLSEAEPTLTHMSITQLHKHKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCIPNREYVRVFDVTERTALHRHLTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASKADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMDELGLEIPVYNRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEPPPGDQSAPLASATPILGGWFGRGCAKRAKRKKAA | 2.3.1.-; 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9NXA8}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8}; | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; homologous chromosome pairing at meiosis [GO:0007129]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of rRNA processing [GO:2000234]; positive regulation of transcription by RNA polymerase I [GO:0045943]; protein deacetylation [GO:0006476]; protein deglutarylation [GO:0061698]; protein depropionylation [GO:0106230]; R-loop processing [GO:0062176]; regulation of DNA repair [GO:0006282]; regulation of mitochondrion organization [GO:0010821]; regulation of protein export from nucleus [GO:0046825]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901836]; retrotransposon silencing [GO:0010526]; rRNA transcription [GO:0009303]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleolus organizer region [GO:0005731]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent protein deacetylase activity [GO:0034979]; protein methyltransferase activity [GO:0008276]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-propionyllysine depropionylase activity [GO:0106231]; protein-succinyllysine desuccinylase activity [GO:0036055] | PF02146; | 2.20.28.200;3.40.50.1220; | Sirtuin family, Class IV subfamily | PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9NRC8}.; PTM: Methylation at Arg-390 by PRMT6 inhibits the H3K18Ac histone deacetylase activity, promoting mitochondria biogenesis and maintaining mitochondria respiration. {ECO:0000250|UniProtKB:Q9NRC8}.; PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains. Deubiquitinated by USP7, inhibiting the H3K18Ac histone deacetylase activity and regulating gluconeogenesis. Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO7; leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q9NRC8}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NRC8}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NRC8}. Chromosome {ECO:0000250|UniProtKB:Q9NRC8}. Cytoplasm {ECO:0000250|UniProtKB:Q9NRC8}. Note=Mainly localizes in the nucleolus and nucleoplasm. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis. In response to stress, released from nucleolus to nucleoplasm. Associated with chromatin. In response to DNA damage, recruited to DNA double-strand breaks (DSBs) sites. Located close to the nuclear membrane when in the cytoplasm. {ECO:0000250|UniProtKB:Q9NRC8}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000250|UniProtKB:Q9NRC8, ECO:0000255|PROSITE-ProRule:PRU00236}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47665; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47669; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015; Evidence={ECO:0000250|UniProtKB:Q8BKJ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501; Evidence={ECO:0000250|UniProtKB:Q8BKJ9}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-decanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-decanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:70631, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:17932, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:143222, ChEBI:CHEBI:189688; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70632; Evidence={ECO:0000250|UniProtKB:Q9NRC8}; | null | null | null | null | FUNCTION: NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context. Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes. Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53. Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex. Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region. In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription. Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis. Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex. Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65. Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation. Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II. Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (By similarity). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51. Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases. In addition to protein deacetylase activity, also acts as a protein-lysine deacylase (By similarity). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (By similarity). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina. Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (By similarity). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity). {ECO:0000250|UniProtKB:Q8BKJ9, ECO:0000250|UniProtKB:Q9NRC8}. | Rattus norvegicus (Rat) |
B2TWL8 | HCHA_SHIB3 | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) |
B2UP57 | H2018_AKKM8 | MARPLPILGGILLSFSPPAEATAQYSIIPEPSRTELRQETAKTLQLLSDQEVPTLETDAYRLTVTPQGAHLASGGREGRIYGLATLRQLRDQLAGQPEGIPCGVITDKPRYPWRGLMVDPARHFIPAADLKKFVDMMAYYKFNRLHLHLTDNQGWRLPVPGYPKLKSVASRREESFGDGIPHEGMYTKQELKELVAYCAARGIDVIPEIDMPGHNQALHAAYPEFFCFPKPDMNVRTTAGNSKELVCPQKPEVWKFYASVFNELKDIFPSGIVHLGGDEAPTELWEKCPLCREARTRAAMKDEQEQMKAFFAKTAALLAKNGQTPQFWYEGNAGIYHPGETVYAWRQGQALQSIEKTKKAGLNLIMASSEYCYLDFPQIQGQRNWGWMKTTTLQKCYDLDPAFGKPEKEAGHIRGVHAPVWAERLPDLNHLLYRAYPRACAIAEAGWSPMGVRSWENFRRKLADHRQFILKRFNYDMERTQGNEPAFRWENNK | 3.2.1.52 | null | chitobiose catabolic process [GO:0052781]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan metabolic process [GO:0030203]; polysaccharide catabolic process [GO:0000272] | lysosome [GO:0005764]; membrane [GO:0016020] | beta-N-acetylgalactosaminidase activity [GO:0032428]; beta-N-acetylglucosaminidase activity [GO:0016231]; metal ion binding [GO:0046872]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00728;PF02838; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:29304441, ECO:0000269|PubMed:30846208}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.031 mM for pNP-beta-GlcNAc (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:30846208}; KM=0.52 mM for pNP-beta-GlcNAc (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:29304441}; KM=0.11 mM for pNP-beta-GalNAc (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:29304441}; Vmax=79.99 umol/min/mg enzyme with pNP-beta-GlcNAc as substrate (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:30846208}; Vmax=44 umol/min/mg enzyme with pNP-beta-GlcNAc as substrate (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:29304441}; Note=kcat is 1.01 sec(-1) and kcat/KM is 34.34 mM(-1)sec(-1) with pNP-beta-GlcNAc as substrate. {ECO:0000269|PubMed:30846208}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. The activity drops sharply below pH 4.5 and above pH 5.5. {ECO:0000269|PubMed:29304441}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains more than 90% of activity after 96 hours of incubation at 37 degrees Celsius and after 12 hours of incubation at 42 degrees Celsius. {ECO:0000269|PubMed:29304441}; | FUNCTION: Hydrolyzes terminal GlcNAc residues from terminally unbranched N-glycans and from chitobiose. Hydrolyzes beta-1,6-linked N-acetylglucosamine and beta-1,4-linked N-acetylgalactosamine from pNP-alpha-GalNAc[beta1,3Gal]beta1,6GlcNAc and pNP-beta-GlcNAc-beta1,4-GalNAc substrates, respectively, as well as beta-1,2-linked N-acetylglucosamine units from the non-reducing end of N-glycans. Hydrolyzes GlcNAc residues linked to alpha1,3- or alpha1,6-mannose branch, but has low activity on substrates with more than one GlcNAc residue on one of the mannose branches. Releases terminal GlcNAc moieties from the N-glycopeptide Gly-Glu-Asn-(GlcNAc2Man3GlcNAc2)-Arg with high efficiency. Has moderate hydrolytic activity on the chitobiose moiety of N-glycopeptide substrate Gly-Glu-Asn-(GlcNAc2)-Arg. Does not hydrolyze GlcNAc residues from N-glycan structures bearing a bisecting GlcNAc moiety (beta1,4-linked GlcNAc to the beta1,4-linked core mannose) (PubMed:29304441). Potentially capable of cleaving the specific glycoside linkages in the process of mucin degradation in human intestinal tract (Probable). Hydrolyzes synthetic substrate pNP-beta-GlcNAc with high activity and pNP-beta-GalNAc to a lesser extent (PubMed:29304441, PubMed:30846208). Does not hydrolyze pNP-beta-glucose, pNP-beta-galactose, pNP-alpha-glucose, pNP-alpha-galactose, pNP-alpha-GlcNAc or pNP-alpha-fucose (PubMed:29304441). {ECO:0000269|PubMed:29304441, ECO:0000269|PubMed:30846208, ECO:0000305}. | Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) |
B2ZFP3 | SMAL1_DANRE | MSVSLTPEQQRRIEENRKKALARRAERQAQIADPGPAQNKHTQSGTTGGPAKNNQHFASDRGQSGAPTRQTQLIDINAACTKTAPPTSITAASTASSFYGQAGKPSTGEKRPPKPPEPAANIPAKKPAVYLRGRCVSHSENRFRVEVGYHADLILVFKSIPSKNYDPATKMWNFSLEDYQMLMEQVAHLPSISLKPLEGMEGLNISASTCRPKDAAAMAALMRLCQGWQKPGATIKGKCVLVSRSRLEVDIGYQADVIGIFKQMPSKSYDMKTRKWTFLLEDYGKLMADLNELPTVETEPLPHAVLQSFSSQFEKTQSQAPVPPEADLSHIDPQLTRSLMPFQRDGVNFAVSREGRLLLADDMGLGKTVQAICIAAYYRSEWPLLVVAPSSVRFTWAEAFRRWLPSVKPDSINVVVKGKDSLRSGLINIISYDLLNKMDKQPPSSPFNVIIMDESHFLKNMKTARCRAALPLLKTAKRVILLSGTPAMSRPAELYTQIQAVRPALFPRFHDFGTRYCDAKQLPWGWDYSSSSNLTELKLLLEESLMLRRLKSEVLSQLPAKQRKVVTVTTDGINSRTKAALNAAARELAKGYHNKSQEKEALLVFFNHTAEAKIRAIMEYISDMLECGREKFLVFAHHKLVLDSITKELGEKSISFIRIDGSTPSAERQLLCERFQASQQSCVAVLSITAANMGLTLHSAALVVFAELFWNPGVLIQAEDRVHRIGQTSNVDIHYLVAKGTADDYLWPMIQAKMNVLEQVGLSESNISENAESASFHSRDRQQLTITEMFQRSFDEDEMLALMDQDP | 3.6.4.- | null | angiogenesis [GO:0001525]; cartilage development [GO:0051216]; developmental growth [GO:0048589]; DNA repair [GO:0006281]; embryonic body morphogenesis [GO:0010172]; hemopoiesis [GO:0030097]; mitotic cell cycle [GO:0000278]; regulation of transcription by RNA polymerase II [GO:0006357]; replication fork processing [GO:0031297] | nuclear replication fork [GO:0043596]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; ATP-dependent DNA/DNA annealing activity [GO:0036310]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787] | PF07443;PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family, SMARCAL1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B2ZRS9 | CNL_CLINE | MSITPGTYNITNVAYTNRLIDLTGSNPAENTLIIGHHLNKTPSGYGNQQWTLVQLPHTTIYTMQAVNPQSYVRVRDDNLVDGAALVGSQQPTPVSIESAGNSGQFRIKIPNLGLALTLPSDANSTPIVLGEVDETSTNQLWAFESVSAV | null | null | null | null | carbohydrate binding [GO:0030246]; protein homodimerization activity [GO:0042803] | PF14200; | 2.80.10.50; | null | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:19100814}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-6.5. Retains more than 70% of the maximum agglutinating activity over the pH range 5-9. {ECO:0000269|PubMed:19100814}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Unchanged hemagglutinating activity after 30 minutes incubation at temperatures up to 50 degrees Celsius, then at higher temperatures activity decreases. 14% of the initial activity is retained even after heating at 100 degrees Celsius. {ECO:0000269|PubMed:19100814}; | FUNCTION: Lectin specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). Specific also for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Agglutinates human blood group A, AB, B and O erythrocytes with a strong preference for group A. Agglutinates bovine erythrocytes with a very low specificity (PubMed:19100814, PubMed:22298779). Binds carbohydrates bivalently, which is required for its biological activity (PubMed:22298779). Exhibits insecticidal activity against the fruit fly D.melanogaster, mosquito A.aegypti, and amoebozoa A.castellanii. Has anti-nutritional activity against Colorado potato beetle L.decemlineata, and against worm C.elegans (PubMed:21486374, PubMed:21556921). Has antiproliferative activity against human leukemic T-cells (PubMed:19100814). Has an immunostimulatory effect on human antigen-presenting dendritic cells, which are subsequently able to induce efficient T-cell immune responses (PubMed:22044067). {ECO:0000269|PubMed:19100814, ECO:0000269|PubMed:21486374, ECO:0000269|PubMed:21556921, ECO:0000269|PubMed:22044067, ECO:0000269|PubMed:22298779}. | Clitocybe nebularis (Clouded agaric) (Lepista nebularis) |
B2ZX90 | FAS1_ORYSJ | MEGGKLLGVAHPEPANNIDADLRYDLGQSRMQVDGPVVLNRSAELEPSDSMAIDDVPVEASSQPAPAKQSPALMDTIVEVQKQLKRKRASSGPALAAADKDALVAGCCQELEGLLEYYREVSGHRMQFEVGNLSTNAAIGCLLEESSLGLSKLVDEIYEKLKGMEGVSATSVRSSVLLIGQRMMYGQSSPDADVLEDESETALWCWEVRDLKVIPLRMRGPLSTRRTARKKIHERITAIYSTLSVLEAPGAEAQVNDMRKASLKLSKALNLEGIKSLVERATQKSNIERGAKNTGSTAKEPMQEMVKSNNDTGIIENVDDSQLQKNTSTNEKDTQKAQKQVEKELKQKEKEEARMRKQQKKQQEEALREQKRREKEEAEMKKQQRKQEEEAQKEQKRREKEEAETRKQQKKQQEEAEKEQKRREKEAVQLKKQLAIQKQASMMERFFKNKKDSEKLEKPGGKDSGVQTTDPCTTNKEVVPLVTSIIDSSFSQKENWALEDLRRLQISGWQKLSSYNRSSRWGIRNKPKKEAFKELKLQKTSDNMLEEILSPNEDTCHNLSQENEPDKSANDVDMLPAVELQFHGTNHANPLPTRSIKRKLLQFDKSNRPAYYGTWRKKSAVVGPRCPLKMDPDLDYEVDSDDEWEEEDPGESLSDCEKDNDEVMEEDSKITDEESEDSFFVPDGYLSDNEGIQIESLLDDKDEASSSPPDQCAEVEEFRALLRQQKVLNTLTEQALRKSQPLVISNLTHEKAELLTAGDLKGTSKIEQLCLQVLSMRICPGGATIDLPVIDSSSANAEETNQLNVKSSPAAASAIPDTDLAEIVKVIGSCRDGINKLVESLHQKFPNVSKSQLKNKVREISEFVDNRWQVKKEVLSKLGLSSSPASSKKPKSIATYFSKRCLPPEEAILASPELRLKSKTTQNVNGDTDIPRINLLPSSQ | null | null | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; mitotic cell cycle phase transition [GO:0044772]; nucleosome assembly [GO:0006334]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; root meristem growth [GO:0010449]; vegetative meristem growth [GO:0010448] | CAF-1 complex [GO:0033186]; nucleus [GO:0005634] | null | PF21796;PF12253; | null | CHAF1A family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Required for several aspects of development, including apical meristem maintenance by regulating the durations of the S- and G2-phases of the cell cycle through its chromatin assembly activity. {ECO:0000269|PubMed:18538315}. | Oryza sativa subsp. japonica (Rice) |
B2ZXD5 | GPHR_CRIGR | MSFLIDSSIMVTSQILFFGFGWLFFMRQLFKDYEVRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIQLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAVARRTMFQRGEVQNKPSGLWGMLKSVTASAPGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVLDRVGKTDPVTRGIEITVNYLGIQFDVKFWSQHISFILVGIIIVSSIRGLLITLTKFFYAISSSKSSNVIVLLLAQIMGMYFVSSVLLIRMSMPPEYRTIITQVLGELQFNFYHRWFDVIFLVSALSSILFLYLAHKQAPEKHMAP | null | null | intracellular pH reduction [GO:0051452]; protein transport [GO:0015031]; response to abscisic acid [GO:0009737]; T cell differentiation [GO:0030217] | Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; monoatomic ion channel complex [GO:0034702] | abscisic acid binding [GO:0010427]; voltage-gated monoatomic anion channel activity [GO:0008308] | PF12430;PF12537; | null | Golgi pH regulator (TC 1.A.38) family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P0CG08}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000250|UniProtKB:P0CG08}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P0CG08}; CATALYTIC ACTIVITY: Reaction=bromide(in) = bromide(out); Xref=Rhea:RHEA:75383, ChEBI:CHEBI:15858; Evidence={ECO:0000250|UniProtKB:P0CG08}; CATALYTIC ACTIVITY: Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, ChEBI:CHEBI:17051; Evidence={ECO:0000250|UniProtKB:P0CG08}; | null | null | null | null | FUNCTION: Voltage-gated channel that enables the transfer of anions such as iodide, chloride, bromide and fluoride which may function in counter-ion conductance and participates in Golgi acidification (PubMed:18794847). Plays a role in lymphocyte development, probably by acting as a RABL3 effector in hematopoietic cells (By similarity). {ECO:0000250|UniProtKB:Q8BS95, ECO:0000269|PubMed:18794847}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
B2ZZS9 | WDR55_ORYLA | MAAPPEHAATGSEQTDPPETNSEPDLSQPEPADSDADEPVGPKIRETPEDIRLEAIANTVALHPSRDVLVCGDVDGDVYAYAYSCTEGETRELWSSGHHLKSCRQVRFSADGLKLYSVSRDKAVHQLDVERGQLVSRIRGAHAAAINSLLLVDENILATGDDRGTLKVWDMRKGEAFMDLKHHDDYISDIAVDQAKRILLTTSGDGTMGVFNIKRRRFELLSEFQSGDLTSVALMKRGKKVVCGSSEGTVYIFNWNGFGATSDRFAVKAESVDCIVPITDSIMCTASMDGYIRAINLLPNRVIGCIGQHVGEPIEEINKSWDSRFLVSCAHDQLIKFWEISNLQKTTVSDYRKRKKKDGRMKSLTKKALGDNDFFSGLVEETEKKEEEEEEEEDSDSDSD | null | null | chordate pharynx development [GO:0160093]; eye development [GO:0001654]; head development [GO:0060322]; liver development [GO:0001889]; rRNA processing [GO:0006364]; spleen development [GO:0048536]; thymus development [GO:0048538] | nucleolus [GO:0005730] | null | PF00400; | 2.130.10.10; | WD repeat WDR55 family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18769712}. | null | null | null | null | null | FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis, including thymus development. {ECO:0000269|PubMed:18769712}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
B3A003 | LYS3_CRAVI | MNGLFLFCVATTAALAYGSDAPCTNSGGVCQDDHLACHNGHYQSGLCTGGAHRRCCLTSASHTGSFSTGIVSQQCLQCICNVESGCKAIGCHFDVNSDSCGYFQIKEGYWHDCGSPGSSWRSCANDLACASKCVQAYMSRYIGFSGCSHSCESYARIHNGGPAGCKHTNTLGYWSHVHAQGCSHNSK | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | extracellular region [GO:0005576] | lysozyme activity [GO:0003796] | PF05497; | 1.10.530.10; | Glycosyl hydrolase 22 family, Type-I lysozyme subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|PubMed:20633278}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:20633278}; | null | FUNCTION: Has antibacterial activity against the Gram-negative bacterium E.coli. No antibacterial activity detected against the Gram-negative bacterium V.vulnificus. {ECO:0000269|PubMed:20633278}. | Crassostrea virginica (Eastern oyster) |
B3A0M2 | SLS4_TRYBB | MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNIHTIAWIRFITSYALLLLFRSAVIVMTSLPAPDDLCQDPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWWPCCGANSREVTEDSQPVMVAFKSEELDEMNGVLEGRQKKHGGVGDGESLMFKCGAYV | 2.7.8.-; 2.7.8.27 | null | ceramide biosynthetic process [GO:0046513]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139] | ceramide cholinephosphotransferase activity [GO:0047493]; kinase activity [GO:0016301]; sphingomyelin synthase activity [GO:0033188] | PF14360; | null | Sphingomyelin synthase family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18699867}; Multi-pass membrane protein {ECO:0000269|PubMed:18699867}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin; Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815, ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27; Evidence={ECO:0000269|PubMed:18699867, ECO:0000269|PubMed:20457606, ECO:0000269|PubMed:21899277}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766; Evidence={ECO:0000269|PubMed:18699867, ECO:0000269|PubMed:20457606, ECO:0000269|PubMed:21899277}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767; Evidence={ECO:0000269|PubMed:21899277}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphinganine = a 1,2-diacyl-sn-glycerol + an N-acylsphinganine-1-phosphocholine; Xref=Rhea:RHEA:44620, ChEBI:CHEBI:17815, ChEBI:CHEBI:31488, ChEBI:CHEBI:57643, ChEBI:CHEBI:67090; Evidence={ECO:0000305|PubMed:18699867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44621; Evidence={ECO:0000305|PubMed:18699867}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + an N-acylsphing-4-enine 1-phosphoethanolamine; Xref=Rhea:RHEA:36079, ChEBI:CHEBI:17815, ChEBI:CHEBI:52639, ChEBI:CHEBI:64612, ChEBI:CHEBI:73203; Evidence={ECO:0000269|PubMed:20457606, ECO:0000269|PubMed:21899277, ECO:0000305|PubMed:18699867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36080; Evidence={ECO:0000269|PubMed:20457606, ECO:0000269|PubMed:21899277, ECO:0000305|PubMed:18699867}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + an N-acylsphinganine = a 1,2-diacyl-sn-glycerol + an N-acylsphinganine-1-phosphoethanolamine; Xref=Rhea:RHEA:42136, ChEBI:CHEBI:17815, ChEBI:CHEBI:31488, ChEBI:CHEBI:64612, ChEBI:CHEBI:78655; Evidence={ECO:0000305|PubMed:18699867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42137; Evidence={ECO:0000305|PubMed:18699867}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + an N-acylsphing-4-enine-(1D-myo-inositol); Xref=Rhea:RHEA:73683, ChEBI:CHEBI:17815, ChEBI:CHEBI:52639, ChEBI:CHEBI:57880, ChEBI:CHEBI:192974; Evidence={ECO:0000269|PubMed:19545591}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73684; Evidence={ECO:0000269|PubMed:19545591}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-acylsphinganine = a 1,2-diacyl-sn-glycerol + an N-acylsphinganine-(1D-myo-inositol); Xref=Rhea:RHEA:33475, ChEBI:CHEBI:17815, ChEBI:CHEBI:31488, ChEBI:CHEBI:57880, ChEBI:CHEBI:64941; Evidence={ECO:0000305|PubMed:19545591}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33476; Evidence={ECO:0000305|PubMed:19545591}; | null | null | null | null | FUNCTION: Bifunctional sphingomyelin (SM)/ethanolamine phosphorylceramide (EPC) synthase with minimal inositol phosphorylceramide (IPC) synthase activity (PubMed:18699867, PubMed:19545591, PubMed:20457606, PubMed:21899277). Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors (PubMed:21899277). SM is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphoryl headgroup from a 1,2-diacyl-sn-glycero-3-phosphocholine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) with release of 1,2-diacyl-sn-glycerol (PubMed:18699867). Also catalyzes the reverse reaction, production of ceramide from sphingomyelin (PubMed:21899277). EPC is synthesized by transferring phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF (PubMed:18699867). The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide (PubMed:18699867). {ECO:0000269|PubMed:18699867, ECO:0000269|PubMed:19545591, ECO:0000269|PubMed:20457606, ECO:0000269|PubMed:21899277, ECO:0000303|PubMed:18699867}. | Trypanosoma brucei brucei |
B3A0N3 | PA2B3_BOTMA | DLWQWGQMILKETGKLPFSYYTAYGCYCGWGGRGGKPKADTDRCCFVHDC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P59071}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P59071}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in modulation of transmission of nerve impulse in another organism [GO:0044487]; fatty acid biosynthetic process [GO:0006633]; phospholipid catabolic process [GO:0009395]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|Ref.1}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that causes irreversible neuromuscular blockade in chick biventer cervicis muscle preparations. The neuromuscular blockade is mediated by inhibitory action at the presynaptic motor nerve endings. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|Ref.1}. | Bothrops marajoensis (Marajo lancehead) |
B3A0S5 | XYNA_FUSO4 | AASGLEAAMKAAGKQYFGTALTVRNDQGEIDIINNKNEIGSITPENAMKWEAIQPNRGQFNWGPADQHAAAATSRGYELRCHTLVWHSQLPSWVANGNWNNQTLQAVMRDHINAVMGRYRGKCTHWDVVNEALNEDGTYRDSVFLRVIGEAYIPIAFRMALAADPTTKLYYNDYNLEYGNAKTEGAKRIARLVKSYGLRIDGIGLQAHMTSESTPTQNTPTPSRAKLASVLQGLADLGVDVAYTELDIRMNTPATQQKLQTNADAYARIVGSCMDVKRCVGITVWGISDKYSWVPGTFPGEGSALLWNDNFQKKPSYTSTLNTINRR | 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00331; | 3.20.20.80; | Glycosyl hydrolase 10 (cellulase F) family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:9291571}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:9291571}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=1.22 mmol/min/mg enzyme {ECO:0000269|PubMed:9291571}; | PATHWAY: Glycan degradation; xylan degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:9291571}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:9291571}; | FUNCTION: Catalyzes the hydrolysis of the internal glycosidic bonds in heteroxylans, releasing mainly xylobiose and xylotriose. Most active on oat-spelt xylan. {ECO:0000269|PubMed:9291571}. | Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) |
B3BM80 | CDIA4_ECO5C | MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAKFKEYALSGRELTSSMISNREIQLAIPADTTKTQWAEINRAIEYGKSQGVKVTVTQVK | 3.1.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23236156}; Note=Bind 1 Zn(2+) per subunit. {ECO:0000269|PubMed:23236156}; | null | null | deoxyribonuclease I activity [GO:0004530]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF21111;PF21483;PF04829; | 3.40.1350.110;6.10.140.1810; | null | null | SUBCELLULAR LOCATION: Target cell, target cell cytoplasm {ECO:0000305|PubMed:25174572}. Note=Toxin translocation into the target cell depends on the proton motive force of the target cell, but not on tolA or tonB. {ECO:0000269|PubMed:25174572}. | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:21829394, PubMed:25174572). The C-terminal 289 residues (the CT fragment) has a strong DNase activity in the presence of Zn(2+), completely degrading supercoiled and linear plasmids, and inhibits growth. In the presence of Mg(2+) it nicks dsDNA (PubMed:23236156). Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI-o11-EC869, but not by non-cognate immunity proteins from other toxin-immunity modules or other strains of E.coli (PubMed:21829394). Gains access to the cytoplasm of target cells by using integral inner membrane protein YciB (PubMed:26305955). {ECO:0000269|PubMed:21829394, ECO:0000269|PubMed:23236156, ECO:0000269|PubMed:25174572, ECO:0000269|PubMed:26305955}.; FUNCTION: Expression of this locus confers protection against other bacteria carrying the locus. {ECO:0000269|PubMed:21829394}. | Escherichia coli O157:H7 (strain EC869) |
B3DH20 | DAA11_DANRE | MVRISEDLIRRRAEHNNGEIFSLEELSLHQQDIQRIEHIHKWCRDLKILYLQNNLIPKIENVGRLKKLEYLNLALNNIEVIENLEGCESLQKLDLTVNFVGRLSSVETLKHNLHLKELYLVGNPCAEYQGYRQYVVATVPQLQSLDGKEISRAERIQALQELDAVRTRVLQQETKYLEEREKQKSNANEHPEINQSLSESQNGTQQYPESSSKTHTEAEDEEREFWEKPCPFTPESRLEAHRHLEEKRRANEKEKEKPKTKTPRTLITPDGRVLNVNEPKLDFSLFEDENNCLLLDLHVYRHMDSSLLDVDVQPMYVRVTVKGKVFQLVLPAEVKPDSSSAQRSQTTGHLLLILPLANEDVKPKKRTIRPTSVTSNQNNKKDTRAAPRRELLEVDPGLAGSLANIVPKGQESSHNPQRCGLEERPVSKDFVDDPEVPPLM | null | null | axonemal dynein complex assembly [GO:0070286]; cerebrospinal fluid circulation [GO:0090660]; cilium assembly [GO:0060271]; cilium movement involved in cell motility [GO:0060294]; convergent extension involved in gastrulation [GO:0060027]; determination of left/right symmetry [GO:0007368]; dorsal/ventral pattern formation [GO:0009953]; embryonic heart tube morphogenesis [GO:0003143]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; heart jogging [GO:0003146]; heart looping [GO:0001947]; motile cilium assembly [GO:0044458]; outer dynein arm assembly [GO:0036158]; pronephros development [GO:0048793]; protein localization to cilium [GO:0061512]; protein localization to motile cilium [GO:0120229] | cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular region [GO:0005576] | null | PF14580; | 3.80.10.10; | TilB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18539122}. Dynein axonemal particle {ECO:0000305|PubMed:18539122}. Cell projection, cilium {ECO:0000269|PubMed:18539122}. Note=Localized to cytoplasmic puncta in ciliated cells. In the semicircular canal, localized to kinocilia. | null | null | null | null | null | FUNCTION: Plays a crucial role in regulating cilia motility in pronephric tubules, cloaca and neural tube. Required for establishing left-right asymmetry of the body plan; controls cell fate and convergent extension (CE) movements during gastrulation, respectively, via the Wnt and the planar cell polarity (PCP) signaling pathways. Required for the proper development of renal glomeruli and tubules. {ECO:0000269|PubMed:18539122, ECO:0000269|PubMed:19395640}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DIV9 | KL40A_DANRE | MASMSVDPVTEPRMYQQTLLQDGLCDLLDANKFVDCILKIKDKEFPCHRLVLAATSPYFKAMFLSDLEESKKREIVLKDIEPGVMGMILRYIYTSDINLTEQNVQDIFMAANMYQIPSIFSVCVSYLQQKLVLSNCLAIFRLGLLLDCPRLAMEARDFICDRYLLIIRDQDFHQLGPSELAAIITCDSLNVEREESVFESLMDWVEYDTDERTKELPELLHCVRFRLMPTSYFKEKVEGHRLIRTNQELKKELQLIKDAQKGLLHRVKRSSHRKEGKSAEFESDDDDEDGLLPGILNDNPRFGMFQSDLILMINDAGTVAYDVGANECFVASSSTEIPKNHCSLVTKENQIFVVGGLRYNEENKDQPFSSYFLQFDPMSSEWLGMPSLPNPRCLFGLVEAENSIYVVGGKELKEGERALDSVMIYDRQSFKWGESDPLPYAVYGHGIVSHKGLVYVIGGKTESKKCLRRVCVYDPSKFEWKDLAPMKTARSLFGTAVHKNKIYVVTGVTDNGLTSTVEVYDIASNSWSEFVDFPQERSSLNLVELGGFLYAIGGFAMMPNETTEKLEPTEMNDIWKFDEEENCWNGILREIRYAAGATVLGVRLNTLRLTKI | null | null | muscle structure development [GO:0061061]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; skeletal muscle fiber development [GO:0048741]; skeletal muscle fiber differentiation [GO:0098528]; swimming [GO:0036268] | A band [GO:0031672]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; I band [GO:0031674] | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | KLHL40 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}. | null | null | null | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (By similarity). Required for skeletal muscle development (PubMed:23746549). {ECO:0000250|UniProtKB:Q9D783, ECO:0000269|PubMed:23746549}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DJT0 | SART3_DANRE | MAATGNEEQTLLPDIEEEAEGMEREMESEDDEEEGMGVEHSEEEDEEDTSEDERENEAEIQRLEEQLSINAFDYNCHVDLIKLLRQEGKLHRLRKARQKMSELFPLTEEIWLDWLKDEIRITEDESDREKVYELFERAIKDYVCPEIWLEYVQYSIGGMGAQGGIERVRSIFERALTAVGLHMTKGASIWEAYREFEIVILSTVQPPPGTVPSQEQQELLSAQLERIHTLFRRQLAVPLMDMEGTYAEYSDWADDGVPETVTHQYRRALQQMEKGKPYEEALLVSEPPKLAEYQSYIDFEIKEGDPARVQIIFERALAENCLVPDLWIKYTTYLDRQLKIKDLVLSAHERAVRNCPWTMGLWKSYLLALERHGADHQTVKDVFEKALNAGFIQATDYVEIWQSYLDYLRRRVDFSKEWSRELDELRAAFSRSLEYLKQDVEERFSESGDLSCTLMQIWARIEALHCKNMQKARELWDSIMTKGNAKYANMWLEYYNLERSYGDAAHCRKALHRAVQCTSDYPEHVCDVLLNFERVEGSLEDWDAAVQKTETKLNRVCEQRARVAEKEALHARQEEEKAEQRRKVKADKKAQKKGQKANRTGDKRKAEDDDEEEWGEEAELPSKRLRGEDDFDSTVTEELMETESGLFGRRAPPARKTEPPGFRKNQQGAPEPQRQPHDMPKEQRKDENCVFVSNLTFNMEDPEGKLRTLFQGCGTIQQVRPVFTAKGTFRGYCYVQFEDRLAVPEALKMDRQEVDGRPMYVSPCVDKNKNPDFKVFKYKTSMEKHKIFISGLPYSATKETLEDLCKEHGTIRAIRIVTNRSGKSKGLAYVEFEDEAQASQAVLKMDGTMLENFTLSVAISNPPGRRMKDEAAPSRFLGAAMPRQLQGARGKGRTQISLLPRSLYRQSTPDAKAENGTISAPHATVTDGETSLDTQTKSLSNEDFARMLLKK | null | null | exocrine pancreas development [GO:0031017]; hematopoietic stem cell homeostasis [GO:0061484]; lymphocyte differentiation [GO:0030098]; mRNA splicing, via spliceosome [GO:0000398]; nucleosome assembly [GO:0006334]; regulation of hematopoietic stem cell proliferation [GO:1902033]; regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902253]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]; thymus development [GO:0048538]; transcription elongation-coupled chromatin remodeling [GO:0140673] | ASAP complex [GO:0061574]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | histone binding [GO:0042393]; U6 snRNA binding [GO:0017070] | PF16605;PF00076; | 3.30.70.330;1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q15020}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q15020}. Nucleus speckle {ECO:0000250|UniProtKB:Q15020}. Cytoplasm {ECO:0000250|UniProtKB:Q15020}. | null | null | null | null | null | FUNCTION: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:17416673). May also function as a substrate targeting factor for deubiquitinases and mediate the deubiquitination of components of the spliceosome and histones (By similarity). {ECO:0000250|UniProtKB:Q15020, ECO:0000269|PubMed:17416673}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DK56 | PTPRU_DANRE | MNTCAFLLILAVQIHADSVEGPTAGCTFDEDSDPSLCEFSQGEEDDFDWQLFRAHASPHSTSDLLRGSYMMVNSSQHAAGQRAQLLLQTLSENDTHCVQFSYFLYSRDGHSPGALRVYVRVNGGPLGIPVWNVSGSRGRQWHQVELAVSTFWPNEYQILLEATVDRKGYIAVDDILLLNYPCYKAPHFSRLGDVEVNAGQNATFQCVAAGRPSEAEKFLLERHNGEVSSGGSVKHLGRNRFAVSFQLEDVQKPEQDLYRCVTQSSRGSGVSNFAELIVKVPPSPIAPPQLLRAGSTYLIIQLNTNSILGDGPIIRREIEYRASLAPWSEILGVNMVTYKLWHLDPDTEYHISVLLTRPGEGGTGPPGPPLISRTKCAEPMRALRGLRASEIQSRQLTLQWEVPAFNLTRCHTYSVSLCYRYTTAGGGGGHNTTVRECLAVEHNTSRFTLRDLPPFHTIQIRLALANTEGKKEGKEVMFQTEEDIPGGIAPESLTFTPLEDMIFLKWEEPVEPNGLITQYEISYQSIESSDPGINVPGPRRTVSKLKNETYHMFSNLHPGTTYLISVRARTAKGFGQTALTEITTNISAPTFDYGDMPSPLSETENTITVLLRPAQGRGAPVSTYQVVVEEEAGRKVKRELGIQDCFPIPTSHGEAQARGAPHYYTAELPPSSLSEATPFTVGDNHTYNGYWNSPLDPRKNYLVYFQAMSNFRGETRINCIRIARKAACKDHQRALEVTQRSEEMGLILGVCAGGLVVLILLLGAIIIIIKKGRDYYSYSYYPRKPGNMNKTPITYRQEKSNMMGSMERSFTDQSTLQEDERMALSFMDTHTCSTRSDPRSSMNESSSLLGGSPRRQCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFDGWDINKKKDKTKGRHDTLMGYDRHRVKLHPLLGDPNSDYINANYIDGYHRSNHFIATQGPKQETVYDFWRMVWQENCFSIVMITKLVEVGRVKCCKYWPDESEMYGDIKITLLKTETLAEYTVRTFALERRGYSAKHEVCQFHFTSWPEHGVPYHATGLLAFIRRVKTSTPLDAGPVVVHCSVGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLCGETAIPVNEFALAYKEMLRVDSQSNSSQLREEFQTLNSVTPHLDVEECSIALLPRNREKNRSMDVLPPDRALAFLVTTEGESNNYINAALMDSFHRPAAFIVTPHPLPGTTSDFWRLVFDYGCTSVVMLNQLNQSNSAWPCVQYWPEPGLQQYGPMQVEFLSMSADEDIITRLFRVKNVTRLQEGQLVVCQFQFLRWSAYRDVPDSKKAFLNLLASVQKWQRECGEGRTVVHCLNGGGRSGTYCASNILMEMIQYQNIVDVFYAVKTLRNAKPNMVETLEQYRFCYELVLEYLDCLEVR | 3.1.3.48 | null | cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; dephosphorylation [GO:0016311]; somite specification [GO:0001757] | anchoring junction [GO:0070161]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein tyrosine phosphatase activity [GO:0004725] | 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: Cell junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. Functions in somitogenesis. Functions as a regulator of the biochemical clock responsible for the segmentation of the presomitic mesoderm. {ECO:0000269|PubMed:15226256}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DL84 | PLK4_XENTR | MAGSIGERREDFKVLNLLGKGSFACVYRAQSINTGIDVAIKMIDKKAMQKVGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLILEMCHNGEMNRFLKNRKKPFSEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLSSDMNIKIADFGLATQLKMPNEKHFTMCGTPNYIAPEIATRSAHGLESDVWSLGCMLYTFLVGRPPFDTDTVKNTLNKIVLADYEMPDFVSREAKDLIFQLLRKNPADRLSLSSVLDHAFMTGFSNVQSKVMGAVEDSIDSGHATISTGFTGSSGVSISGRFQEKRILSGPSLPNKVNIFQFKDKHPAERSNGGSFHNTQRENNDFSEGNGRKTVACEDRPHSRYLRRAHSSDRSGTSQSQTYGKPSSFSERCHSVEMLAKPSNLKGYCTSSPPKSYGDIPQMFTDERSLERHTSPPVKEKTPSEFMCPAKQITPRSGDKCQAETVQQWFGAMQLNGKFKNTPDTSSVSNMGGDFYSQQTMQNGAPQYAWNDVKRKKDTDSSVESVLRGISKLPSGQHKAEKSQFGEQSKARVPQQAFGSSTLRSIISPLNAERLKPIRQKTKNAVVSILETGEVCMEFLKEQNSQERVKEVLRISCDGNLIYVYHPNEGKGFPLVERPPSPPENMRSYTFDSLPEKYWKKYQYAAKFIQLVRSKMPKVTYYTRYAKCMLMENGPNADFEVCFYDGAKIHKTPDLIRVIEKSGKSYTVEGSRLSTLSDQVRSYVNHANESHCVCLSLESAINTEEKKGENISLFPITFGRRPAITESPRTQLTVDSARERKDEQSSANRVLHSSATSPPQIPNINPSLISYEGSVFSATTAQPSPPTSNTLKTHAPDRAQVLKSVFVENVGWASQLNSGAVWVQFNDGSQLVVQPGVSSIIYTAPNGQITRHGENDKLPEYIKSKLQCLSSILMLFASSSSH | 2.7.11.21 | null | centriole replication [GO:0007099]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of centriole replication [GO:0046601] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). {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=2.7.11.21; 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=2.7.11.21; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as sass6, cenpj/cpap, ccp110, cep135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (By similarity). {ECO:0000250|UniProtKB:O00444}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B3DLB3 | ANM2_XENTR | MSTSGCSSEKSDFQDSTEGEEEEDTQSENLCMREYVVIRDYMAADATQLSLCFGDKVLLLSAVTQDWWWVKHNGICGYVPASYLHDALNDQEDTEVDDPWQDEEYYGSYKTLKLHLEMLSDVPRTTAYKEVILRNSSSLCGKHILDLGCGTGIISFFCAKLAQPEAVYAVEASEIAEQTRRLVKQNGISNLVHVIRQRAEELQLPTKVDILVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSASKEYANKVLFWDNPYQLDFSLLKPLAAKEFFARPKPDYVLQPEDCLSEPCILLHLNLKTLQLAELERMNSDFTFFVHTDGLLHGFTAWFSVQFQNLEEQGQLELNTGPFSPLTHWKHTLFMLDEPLQVQKGDKISGSVVFQRNSVWRRHMSVTLSWVINGKLTMQNVSQQWQAILA | 2.1.1.319 | null | developmental cell growth [GO:0048588]; methylation [GO:0032259]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of androgen receptor signaling pathway [GO:0060765] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | histone H3 methyltransferase activity [GO:0140938]; histone H3R8 methyltransferase activity [GO:0140592]; histone methyltransferase activity [GO:0042054]; nuclear estrogen receptor binding [GO:0030331]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-containing complex binding [GO:0044877] | PF13649;PF14604; | 2.70.160.11;2.30.30.40;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; Evidence={ECO:0000250|UniProtKB:P55345}; | null | null | null | null | FUNCTION: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation. Involved in embryonic dorsal development. {ECO:0000250}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B3DMA2 | ACD11_RAT | MEMDVTRDTVEVLPQHKFDIRSLEAYLNQHLPGFGSDHRAVLTVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKVQKALFSVGFPVPKPLLYCSNASIIGTEFYVMEHVQGRIFRDFSIPGVSPAERAAIYVSLVETLAWLHSLDIHSLGLDRYGTGVGYCKRQVSTWTKQYQASAHQSIPAMDQLSTWLMRNLPDSDNEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPLSDLAHLSLFYFWPRTLPMINRGSHIQENTGIPLMEELISIYCRRRGIDPNLPNWNFFMALSFFKLAGIAQGVYSRYLMGNNSSEDSFLTANTVQPLAETGLQLSRRTLSTVPPQADAKSRLFAQSRRGQEVLTRVKQFMKQHVFPAEKEVAEYYAQNGNSAEKWEHPLVIEKLKEMAKAEGLWNLFLPAVSGLSQVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEQQKQQWLEPLLRGDITSVFCMTEPNVSSSDATNMECSIQRDGGSYIVHGKKWWSSGAGNPKCKIAVVLGRTESPSVSRHKVHSMILVPMDTPGVELIRPLSVFGYMDNVHGGHWEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRSVGLAERILQIMCDRAVQREAFGKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTLGSAAARKEIAMIKVAAPKAVCKIADRAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMELQDQARQLKARM | 1.3.8.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q709F0}; | fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539] | cytoplasm [GO:0005737]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660]; long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991]; very-long-chain fatty acyl-CoA dehydrogenase activity [GO:0017099] | PF00441;PF02770;PF02771;PF01636; | 3.90.1200.10;1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14561759}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q709F0}. | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65059, ChEBI:CHEBI:74692; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:64868, ChEBI:CHEBI:74281; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:90118, ChEBI:CHEBI:90119; Evidence={ECO:0000250|UniProtKB:Q709F0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221; Evidence={ECO:0000250|UniProtKB:Q709F0}; | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q709F0}. | null | null | FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain. {ECO:0000250|UniProtKB:Q709F0}. | Rattus norvegicus (Rat) |
B3DNN5 | CDC16_ARATH | MREEEIEKIRGVVRDCVSKHLYSSAIFFADKVAALTNDPSDIYMQAQALFLGRHYRRAFHLLNASKIVLRDLRFRYLAAKCLEELKEWDQCLLMLGDAKVDDDGIVYDAKDGNVIDFDKDGEDREINISSAICFLRGKAYGALQNRSQARQWYKAAIKADPLCYEALECLIESHMLTSEEESSLLSSLQFSPEDGWLSSFYSCLIKKYDKESTVELKFKKLENETSGSVSGSSMITLANNTDLLACKAEYYHQCCEYQKCFELTAALLEKDPFHLKCTLVHLAAAMELGNSNELYLMACNLVKDYPSKALSWFAVGCYYYCIKKYAEARRYFSKATGIDGSFSPARIGYGNSFAAQEEGDQAMSAYRTAARLFPGCHLPTLYIGMEYMRTHSYKLADQFFMQAKAICPSDPLVYNELGVVAYHMKEYGKAVRWFEKTLAHIPSALTESWEPTVVNLAHAYRKLRKDREAISYYERALTLSTKSLSTYSGLAYTYHLQGNFSAAISYYHKALWLKPDDQFCTEMLNVALMDECQNGVDSKVELC | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle [GO:0007049]; cell division [GO:0051301]; phloem or xylem histogenesis [GO:0010087]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein ubiquitination [GO:0016567]; regulation of DNA endoreduplication [GO:0032875] | anaphase-promoting complex [GO:0005680]; cytoplasm [GO:0005737] | null | PF12895;PF00515;PF13432;PF13176;PF13181; | 1.25.40.10; | APC6/CDC16 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. {ECO:0000269|PubMed:14675450, ECO:0000269|PubMed:19336465}. | Arabidopsis thaliana (Mouse-ear cress) |
B3EWF4 | LTX2A_LACTA | MKVLVIIALCLVAFQSALSKKIENFESYIEDLKSEARECIPLYNDCTAFKYNNNCCKDPEKKYQYKCSCIVCKEGKEQCTCQRKETVESMMKCVRFVKKVGEKVIEKVG | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | null | null | Neurotoxin 19 (CSTX) family, 11 (latartoxin) subfamily | PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23088912}.; PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:27287558}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23088912, ECO:0000269|PubMed:27287558}. | null | null | null | null | null | FUNCTION: Insect toxin. Causes paralysis in larvae of C.vicina by depolarizing membranes at the neuromuscular junction. {ECO:0000269|PubMed:23088912}. | Lachesana tarabaevi (Spider) |
B3EWF5 | LTX2B_LACTA | MKVLVIIALCFFILQTALSEDKYESFESYVEDLKSGNMKGEARECIPLYNDCKEFKYNNNCCKDPEKKYQYKCSCIMCEGGEEQCTCQRKETVENMMKCVRFVKKVVEKVG | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | null | null | Neurotoxin 19 (CSTX) family, 11 (latartoxin) subfamily | PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23088912}.; PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:27287558}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23088912, ECO:0000269|PubMed:27287558}. | null | null | null | null | null | FUNCTION: Insect toxin. {ECO:0000269|PubMed:23088912}. | Lachesana tarabaevi (Spider) |
B3EWF6 | LTX2C_LACTA | MKVLVITALCFILLQNVLGEDTYEDLQNYIENLINENQDEARECVPLENDCTKLKYSNPCCKDEKKKYQYKCSCIVDKTEQCTCQRKETVEKMMKGMKYIKNLGKKIG | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | null | null | Neurotoxin 19 (CSTX) family, 11 (latartoxin) subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:23088912}.; PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E). {ECO:0000303|PubMed:27287558}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23088912, ECO:0000269|PubMed:27287558}. | null | null | null | null | null | FUNCTION: Insect toxin. {ECO:0000269|PubMed:23088912}. | Lachesana tarabaevi (Spider) |
B3EWF8 | 3SX1_MICMP | MKTLLLTLVVVTIVCLDLGNSLKCYVSREGKTQTCPEGEKLCEKYAVSYFHDGRWRYRYECTSACHRGPYNVCCSTDLCNK | null | null | envenomation resulting in modulation of process in another organism [GO:0035738]; modulation of process of another organism [GO:0035821]; negative regulation of signaling receptor activity [GO:2000272] | extracellular space [GO:0005615] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | 2.10.60.10; | Snake three-finger toxin family, Short-chain subfamily | PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:22677806}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22677806}. | null | null | null | null | null | FUNCTION: Snake venom neurotoxin that blocks neuromuscular transmission on both avian and mouse nerve-muscle preparations, presenting a postsynaptic action through the nicotinic acetylcholine receptor (nAChR). Reversibly inhibits twitches in mouse phrenic nerve diaphragm and irreversibly in chick biventer cervicis muscle. Has no cytotoxic activity towards C2C12 cells up to 180 ug/ml. {ECO:0000269|PubMed:22677806}. | Micrurus mipartitus (Red-tailed coral snake) |
B3EWH0 | TXPR2_ALOMR | AKACTPLLHDCSHDRHSCCRGDMFKYVCDCFYPEGEDKTEVCSCQQPKSHKIAEKIIDKAKTTL | null | null | null | extracellular region [GO:0005576] | calcium channel inhibitor activity [GO:0019855]; toxin activity [GO:0090729] | PF10530; | null | Neurotoxin 19 (CSTX) family, 05 (U4-Lctx) subfamily | PTM: Amidation at Leu-64 is not mandatory for activity on P2RX3. {ECO:0000269|PubMed:22842000}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22842000}. | null | null | null | null | null | FUNCTION: Enhances the high-affinity desensitization of human P2RX3 purinoceptors (PubMed:22842000). At 50 nM, the toxin decreases the IC(50) for ambient ATP from 2.67 nM to 0.77 nM in human P2RX3 (PubMed:22842000). {ECO:0000269|PubMed:22842000}. | Alopecosa marikovskyi (Wolf spider) (Lycosa kazakhstanicus) |
B3EWH2 | AON_AZEFE | DNWWPKPPHQGPRPPRPRPKP | null | null | null | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: In vitro, reversibly blocks human muscle-type nicotinic acetylcholine receptors (nAChR) alpha-1-beta-1-epsilon-delta/CHRNA1-CHRNB1-CHRNE-CHRND (EC(50)=0.44 uM) and alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND (EC(50)=1.56 uM). Binds to nAChR from T.californica (IC(50)=0.03-0.18 uM), human neuronal nAChR alpha-7/CHRNA7 (IC(50)=22 uM) and acetylcholine-binding proteins (AChBP) from L.stagnalis (IC(50)=63 uM) and A.californica (IC(50)=230 uM). {ECO:0000269|PubMed:22613724}. | Azemiops feae (Fea's viper) |
B3EWP6 | PA2_LACMR | HLLQFGDLINKIARRNGILYYSFYGCYCGLGGRGRPQDATDRCCFVHDCCYGKVTGCDPK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P20249}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P20249}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in induction of edema in another organism [GO:0044398]; envenomation resulting in positive regulation of platelet aggregation in another organism [GO:0044478]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26145564}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:26145564}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.404 mM for 4-nitro-3-(octanoyloxy) benzoic acid {ECO:0000269|PubMed:26145564}; | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that displays mild but significant inhibition of mouse platelet aggregation induced by ADP and collagen (PubMed:26145564). In vivo, induces edema in the foot pads and gastrocnemius muscles of mice but shows no myonecrotic or myotoxic activity (PubMed:26145564). PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:26145564). {ECO:0000269|PubMed:26145564}. | Lachesis muta rhombeata (Bushmaster) |
B3EWR1 | LEC1_MYTGA | MTFAKQSCFNSIILLSIATSYFKIGHKISELGNRIEKMTTFLIKHKASGKFLHPKGGSSNPANDTNLVLHSDIHERMYFQFDVVDERWGYIKHAASGKIVHPLGGKADPPNETKLVLHQDRHDRALFAMDFFNDNIIHKAGKYVHPKGGSTNPPNETLTVMHGDKHGAMEFIFVSPKNKDKRVLVYV | null | null | killing of cells of another organism [GO:0031640] | null | galactose binding [GO:0005534] | null | 2.80.10.50; | null | null | null | null | null | null | null | null | FUNCTION: Alpha-D-galactose-binding lectin (PubMed:23093409, PubMed:27187419, PubMed:27321048). Binds D-GalNAc, but not glucose or its derivatives (PubMed:27321048). Has hemagglutinating activity towards rabbit erythrocytes (PubMed:23093409, PubMed:27321048). Agglutinates bacteria. Has bacteriostatic activity on both Gram-positive and Gram-negative bacteria including B.subtilis, S.aureus, E.coli and V.parahaemolyticus, respectively (PubMed:27187419). Has a dose-dependent cytotoxic effect on the human globotriaosylceramide (Gb3)-expressing Epstein-Barr virus (EBV)-positive Burkitt's lymphoma (Raji) cell line (PubMed:23093409, PubMed:27321048). Has dose-dependent cytotoxic effect on another Burkitt's lymphoma (Ramos) cell line, which does not possess the EBV genome, but also expresses Gb3. Binds to Gb3 in these cells leading to phosphorylation of MEK1/2, ERK1/2, JNK and p38 kinase, activation of caspase-9/3 and to expression of p21 and tumor necrosis factor (TNF)-alpha (PubMed:26694420). No cytotoxic effect on the human chronic myelogenous leukemia (K-562) cell line, which does not express Gb3 (PubMed:23093409, PubMed:26694420). May be involved in innate immunity acting as an antibacterial or antifungal agent (PubMed:26694420, PubMed:27321048). May be a pattern recognition receptor (PRR) involved in recognition of glycans found on parasitic or symbiotic microorganisms (PubMed:27187419). {ECO:0000269|PubMed:23093409, ECO:0000269|PubMed:26694420, ECO:0000269|PubMed:27187419, ECO:0000269|PubMed:27321048}. | Mytilus galloprovincialis (Mediterranean mussel) |
B3EWR6 | AMP_ECHCG | MGKGSSGGGAWWAFLLLAGVLLAVAATAAGAEEDVATEVAAAADRDPKEDLRWCRKGCQWQYGQDTRQRKECERDCRQRHREQEQDADEEDGSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGDDDVAVDACEGADRCRERCERRHRGDWQGKQRCLMECRRREQEEDVDDRCPCPCRRQCERHGDPATRQRCVEACQRRREEERRHGGGDADEEGSRGGRCERKCRRHSDWQTRQRCLQQCEQRERQEEGGRDDAGDGKDTYCADRCQSMCRQRHRGDREMQRRCARKCEREEGCPRRRDATADADEAEEDDGNDRCSQQCQHHRDPDRKQQCMRECRRHQGRSDDDDTRAGEDDS | null | null | defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | null | PF14861; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28794}. | null | null | null | null | null | FUNCTION: [Antimicrobial peptide 1]: Has antifungal activity. Inhibits spore germination of F.graminearum (EC(50)=4.5 uM), F.oxysporum (EC(50)=8.5 uM), F.solani (EC(50)=4.0 uM), F.verticillioides (EC(50)=8.1 uM), P.infestans (EC(50)=16.3 uM), P.betae (EC(50)=6.0 uM), P.debaryanum (EC(50)=12.0 uM), P.ultimatum (EC(50)=14.4 uM), B.sorokiniana (EC(50)=18.2 uM), A.alternata (EC(50)=16.0 uM) and A.solani (EC(50)=14.0 uM). Does not destroy spores but rather inhibits hyphal growth during germination. Does not affect spore germination in A.niger, C.graminicola, D.maydis and T.album. Does not inhibit trypsin. {ECO:0000269|PubMed:21561864}.; FUNCTION: [Antimicrobial peptide 2]: Inhibits spore germination of P.infestans with an IC(50) of 24 uM (PubMed:22940285). EcAMP2 has no activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger at concentration up to 32 uM (PubMed:24275143). Has no antibacterial activity (PubMed:22940285, PubMed:24275143). {ECO:0000269|PubMed:22940285}.; FUNCTION: [Antimicrobial peptide 2.1]: Inhibit spore germination of P.infestans with an IC(50) of 24 uM (PubMed:22940285). EcAMP2 has no activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger at concentration up to 32 uM (PubMed:24275143). Has no antibacterial activity (PubMed:22940285, PubMed:24275143). {ECO:0000269|PubMed:22940285}.; FUNCTION: [Antimicrobial peptide 3]: Has antifungal activity. Inhibits spore germination of F.graminearum (IC(50)=5.5 uM), F.oxysporum (IC(50)=9.6 uM), B.sorokiniana (IC(50)=15.0 uM) and A.niger (IC(50)=22.4 uM). Has antibacterial activity. Inhibits P.syringae (MIC=4.5 uM), C.michiganensis (MIC=2.1 uM) and E.carotovora (MIC=9.8 uM). Does not inhibit trypsin. {ECO:0000269|PubMed:24275143}. | Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli) |
B3EWR7 | HBAC_OPHSE | SLSDKDKTFVKAFWGKLKGKADDVGAEALARMFGAFPATKSYFAHWPDLSAGSGPVKKHGKIIMAGVGDAVDKIDNLVSGLSKLSDLHATKLRIDXXXXXXXXXXXLVTLAANFPADFTPELHVSLDKFFAAVGAALSDKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | PTM: Acetylated on Ser-1. {ECO:0000269|PubMed:23632627}. | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the gills to various peripheral tissues. {ECO:0000305|PubMed:23632627}. | Ophisurus serpens (Serpent eel) (Muraena serpens) |
B3EX61 | PI4KB_SORAR | MGDTAVEPAPLKPASEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVRLLHGAVAVSKRGTALELVNGDGVDTEIRCLDDPPAQIREEEDEMGATVTSGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPALNTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVENEDEPIRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAAFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTNVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEMHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFRRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMNMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | inner ear development [GO:0048839]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development. {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8}. | Sorex araneus (Eurasian common shrew) (European shrew) |
B3EY95 | SCACT_ACEAC | MTERIRNVALRSKVCPAETASELIKHGDVVGTSGFTGAGYPKEVPKALAQRMEAAHDRGEKYQISLITGASTGPQLDGELAKANGVYFRSPFNTDATMRNRINAGETEYFDNHLGQVAGRAVQGNYGKFNIALVEATAITEDGGIVPTSSVGNSQTFLNLAEKVIIEVNEWQNPMLEGIHDIWDGNVSGVPTRDIVPIVRADQRVGGPVLRVNPDKIAAIVRTNDRDRNAPFAAPDETAKAIAGYLLDFFGHEVKQNRLPPSLLPLQSGVGNVANAVLEGLKEGPFENLVGYSEVIQDGMLAMLDSGRMRIASASSFSLSPEAAEEINNRMDFFRSKIILRQQDVSNSPGIIRRLGCIAMNGMIEADIYGNVNSTRVMGSKMMNGIGGSGDFARSSYLSIFLSPSTAKGGKISAIVPMAAHVDHIMQDAQIFVTEQGLADLRGLSPVQRAREIISKCAHPDYRPMLQDYFDRALKNSFGKHTPHLLTEALSWHQRFIDTGTMLPS | 2.8.3.18 | null | acetate catabolic process [GO:0045733]; acetyl-CoA biosynthetic process from acetate [GO:0019427]; succinyl-CoA catabolic process [GO:1901289] | null | acetate CoA-transferase activity [GO:0008775]; acetyl-CoA hydrolase activity [GO:0003986]; transferase activity [GO:0016740] | PF13336;PF02550; | 3.40.1080.20;3.40.1080.10; | Acetyl-CoA hydrolase/transferase family | null | null | CATALYTIC ACTIVITY: Reaction=acetate + succinyl-CoA = acetyl-CoA + succinate; Xref=Rhea:RHEA:35711, ChEBI:CHEBI:30031, ChEBI:CHEBI:30089, ChEBI:CHEBI:57288, ChEBI:CHEBI:57292; EC=2.8.3.18; Evidence={ECO:0000269|PubMed:18502856, ECO:0000269|PubMed:23030530, ECO:0000269|Ref.3}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 mM for acetate {ECO:0000269|PubMed:18502856}; KM=22.1 mM for succinyl-CoA {ECO:0000269|PubMed:18502856}; KM=22.3 mM for acetyl-CoA {ECO:0000269|PubMed:18502856}; KM=0.9 mM for succinate {ECO:0000269|PubMed:18502856}; KM=130 mM for acetoacetate {ECO:0000269|PubMed:18502856}; Note=kcat is 280 sec(-1) with acetate. kcat is 201 sec(-1) with succinyl-CoA. kcat is 75 sec(-1) with acetyl-CoA. kcat is 36.5 sec(-1) with acetoacetate. kcat is 70.9 sec(-1) with succinate. {ECO:0000269|PubMed:18502856}; | PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis. {ECO:0000269|PubMed:18502856, ECO:0000269|Ref.3}. | null | null | FUNCTION: Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA and succinate. Required for growth on acetic acid and for resistance to high levels of acetic acid. Has also low activity with acetoacetate as substrate. {ECO:0000269|PubMed:18502856, ECO:0000269|PubMed:23030530, ECO:0000269|Ref.1, ECO:0000269|Ref.3}. | Acetobacter aceti |
B3F211 | IBP2B_DANRE | MSLALLCSLLLVHGSLGEIVFRCPSCTAERQAACPKLTTSCEIVREPGCGCCPVCARQKGELCGVYTTRCGSGLRCYPSANSELPLEQLIQGLGRCENKVDLEPTMTNQESAAHSGEVNGTRSPPMKKPGKDYQYIKEIAVNKHHNNKRTRMYNTQDDPKTPHPKQSQCQQELDKVLENISRMAFHDNKGPLENLYDLKFPNCDKTGQYNLKQCHMSTHGQRGECWCVNPYTGVQIPSSDKVRGDPNCSQYYGGPELEPPTAQQK | null | null | negative regulation of cell population proliferation [GO:0008285]; negative regulation of developmental growth [GO:0048640]; negative regulation of DNA replication [GO:0008156]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; sprouting angiogenesis [GO:0002040] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. {ECO:0000269|PubMed:19081843}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3FK34 | PHUZ_BP201 | MPVKVCLIFAGGTGMNVATKLVDLGEAVHCFDTCDKNVVDVHRSVNVTLTKGTRGAGGNRKVILPLVRPQIPALMDTIPEADFYIVCYSLGGGSGSVLGPLITGQLADRKASFVSFVVGAMESTDNLGNDIDTMKTLEAIAVNKHLPIVVNYVPNTQGRSYESINDEIAEKIRKVVLLVNQNHGRLDVHDVANWVRFTDKHNYLIPQVCELHIETTRKDAENVPEAISQLSLYLDPSKEVAFGTPIYRKVGIMKVDDLDVTDDQIHFVINSVGVVEIMKTITDSKLEMTRQQSKFTQRNPIIDADDNVDEDGMVV | 3.6.5.- | null | establishment of localization [GO:0051234] | host cell cytoplasm [GO:0030430] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802] | null | 3.40.50.1440; | FtsZ family, PhuZ subfamily | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:22726436, ECO:0000269|PubMed:25429514}. Note=In infected host cells forms a spindle-like structure emanating from each cell pole. {ECO:0000269|PubMed:24631461, ECO:0000269|PubMed:25429514, ECO:0000269|PubMed:28813669}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:22726436}; | null | null | null | null | FUNCTION: A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication (PubMed:22726436, PubMed:25429514, PubMed:28082593, PubMed:28813669, PubMed:31199917). The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell (PubMed:28082593, PubMed:28813669). Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell (PubMed:31199917). Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell (PubMed:22726436, PubMed:25429514, PubMed:28082593, PubMed:28813669, PubMed:31199917). Filaments have a three-stranded intertwined achitecture and form a spindle-like cytoskeleton within the infected cell (PubMed:24631461). Has GTPase activity (PubMed:22726436). Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin. In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic (PubMed:25429514). Both capsid movement and DNA rotation probably require treadmilling (Probable). {ECO:0000269|PubMed:22726436, ECO:0000269|PubMed:24631461, ECO:0000269|PubMed:25429514, ECO:0000269|PubMed:28082593, ECO:0000269|PubMed:28813669, ECO:0000269|PubMed:31199917, ECO:0000305|PubMed:31199917}. | Pseudomonas phage 201phi2-1 (Pseudomonas chlororaphis phage 201phi2-1) |
B3G515 | GPER1_DANRE | MEEQTTNVIQIYVNGTEQFNASFDFNITDVKESTDTYEFYIIGLFLSCLYTIFLFPIGFIGNILILVVNLNHRERMTIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYVALTSSMSSSPLRTMQHAKLSCSLIWMASILATLLPFTIVQTQHTGEVHFCFANVFEIQWLEVTIGFLIPFSIIGLCYSLIVRTLMRAQKHKGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSKRTDTTLWHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKRKASWSVVYRFCNHTLDLQIPVRSESEV | null | null | apoptotic process [GO:0006915]; brain development [GO:0007420]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; heart contraction [GO:0060047]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oocyte maturation [GO:1900194]; positive regulation of embryonic development [GO:0040019]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of ovarian follicle development [GO:2000354]; regulation of vitellogenesis [GO:1903186] | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; recycling endosome [GO:0055037] | G protein-coupled estrogen receptor activity [GO:0038054]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:19228597}; Multi-pass membrane protein {ECO:0000269|PubMed:19228597}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane. {ECO:0000250}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Binds 17-beta-estradiol (E2) in plasma membranes with high affinity and displays rapid kinetics of association and dissociation. {ECO:0000269|PubMed:19228597}; | null | null | null | FUNCTION: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. Specifically induces apoptosis and reduces proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19228597, ECO:0000269|PubMed:23583372}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3GNI6 | SEP11_RAT | MAVAVGRPSNEELRNLSLSGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQFPTDEETVAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVMRVKEKEAELKEAEKELHEKFDLLKRTHQEEKKKVEDKKKELEEEVSNFQKKKAAAQLLQSQAQQSGAQQTKKDKDKKNPWLCTE | null | null | cilium assembly [GO:0060271]; cytoskeleton-dependent cytokinesis [GO:0061640]; regulation of synapse organization [GO:0050807] | axon [GO:0030424]; cell division site [GO:0032153]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; microtubule cytoskeleton [GO:0015630]; postsynapse [GO:0098794]; postsynaptic specialization of symmetric synapse [GO:0099629]; septin complex [GO:0031105]; septin ring [GO:0005940]; stress fiber [GO:0001725] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse. Cell projection, dendritic spine. Cell projection, axon. Note=Partly colocalizes with stress fibers. Association with microtubules not observed in embryonic fibroblasts. In cultured hippocampal neurons, localizes to 54% of GABAergic and 25% of glutamatergic synapses. Frequently present at the base of dendritic protrusions and at the bifurcation points of the dendritic branches. Expressed at low levels in the axons of mature cultured hippocampal neurons. In embryonic fibroblasts, associated with actin stress fibers. | null | null | null | null | null | FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity. {ECO:0000269|PubMed:19380581, ECO:0000305}. | Rattus norvegicus (Rat) |
B3GS44 | LRE_ARATH | MELILLFFFLMALLVSLSSSSSISDGVFESQTSVSGRNLRHAKKKCEVNFEYMDYKVLTKRCKGPAFPAKECCSAFKEFACPYVSQINDMNSDCAQTMFSYMNIYGNYPTGLFANECRERKDGLVCPLPPLYSHNLNASTADSTPRFISLLISAATAVFALLVLT | null | null | double fertilization forming a zygote and endosperm [GO:0009567]; pollen tube guidance [GO:0010183]; pollen tube reception [GO:0010483]; synergid death [GO:0010198] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27081182}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:27081182}. Note=Localized to the filiform apparatus of the synergid cell. {ECO:0000269|PubMed:27081182}. | null | null | null | null | null | FUNCTION: Female gametophyte-specific component of the signaling pathway required for fertilization. Required for reception of the pollen tube by the female gametophyte (PubMed:19028964, PubMed:26052747, PubMed:27081182). Acts specifically at the synergid cell surface for pollen tube reception (PubMed:26052747, PubMed:27081182). Plays a role in double fertilization and early seed development (PubMed:20163554). Component of the FER-regulated Rho GTPase signaling complex. Acts as a chaperone and coreceptor for FER. Required for localization of FER to the plasma membrane (PubMed:26052747). {ECO:0000269|PubMed:19028964, ECO:0000269|PubMed:20163554, ECO:0000269|PubMed:26052747, ECO:0000269|PubMed:27081182}. | Arabidopsis thaliana (Mouse-ear cress) |
B3GSH5 | ASMT_RAT | MAPGREGELDRDFRVLMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLRGAGDGSYTNSALSSTFLVSGSPQSQRCMLLYLAGTTYGCWAHLAAGVREGRNQYSRAVGISAEDPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQEAARLYPGSSVCVFDLPDVIAAARTHFLSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRPGGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFPRLQLRRPGGPYHAMLARRGPRPGIITGVGSNTTGTGSFVTGIRRDVPGARSDAAGTGSGTGNTGSGIMLQGETLESEVSAPQAGSDVGGAGNEPRSGTLKQGDWK | 2.1.1.4 | null | lipid metabolic process [GO:0006629]; male gonad development [GO:0008584]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; negative regulation of male gonad development [GO:2000019] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF16864;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378, ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.4; Evidence={ECO:0000269|PubMed:8930356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15574; Evidence={ECO:0000305|PubMed:8930356}; | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. {ECO:0000305|PubMed:8930356}. | null | null | FUNCTION: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). {ECO:0000269|PubMed:8930356}. | Rattus norvegicus (Rat) |
B3H4Y2 | STMP3_ARATH | MGLKMSSNALLLSLFLLLLCLFSEIGGSETTHWKIVEEPVRGQIATPPSLTCGGQRLGGPQPRLSPCPRPRPRPRPRTGS | null | null | response to ethylene [GO:0009723]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | apoplast [GO:0048046]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; secretory vesicle [GO:0099503] | LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612] | null | null | Serine rich endogenous peptide (SCOOP) phytocytokine family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Endoplasmic reticulum {ECO:0000269|PubMed:31001913}. Golgi apparatus {ECO:0000269|PubMed:31001913}. Note=Observed in a reticular pattern and a perinuclear ring (PubMed:31001913). The precursor of STMP3 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP3 in the apoplasm (PubMed:31001913). {ECO:0000269|PubMed:31001913}. | null | null | null | null | null | FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. {ECO:0000250|UniProtKB:B3H7I1}. | Arabidopsis thaliana (Mouse-ear cress) |
B3H5A8 | RVE7_ARATH | MLCFVRFQAGFVRIIVAARKRFRYFLMAAEDRSEELSSNVENGSCNSNEGINPETSSHWIENVVKVRKPYTVTKQREKWSEEEHDRFLEAIKLYGRGWRQIQEHIGTKTAVQIRSHAQKFFSKMAQEADSRSEGSVKAIVIPPPRPKRKPAHPYPRKSPVPYTQSPPPNLSAMEKGTKSPTSVLSSFGSEDQVNRCSSPNSCTSDIQSIGATSIDKKNNYTTSKQPFKDDSDIGSTPISSITLFGKIVLVAEESHKPSSYNDDDLKQMTCQENHYSGMLVDTNLSLGVWETFCTGSNAFGSVTEASENLEKSAEPISSSWKRLSSLEKQGSCNPVNASGFRPYKRCLSEREVTSSLTLVASDEKKSQRARIC | null | null | chromatin remodeling [GO:0006338]; circadian rhythm [GO:0007623]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; histone binding [GO:0042393]; transcription coactivator activity [GO:0003713] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14523250}. | null | null | null | null | null | FUNCTION: Transcription factor involved in phytochrome A-mediated cotyledon opening. Controlled by the central oscillator mediated by LHY and CCA1. Part of a regulatory circadian feedback loop. Regulates its own expression. {ECO:0000269|PubMed:14523250}. | Arabidopsis thaliana (Mouse-ear cress) |
B3H5A9 | PCEP6_ARATH | MKLSVYIILSILFISTVFYEIQFTEARQLRKTDDQDHDDHHFTVGYTDDFGPTSPGNSPGIGHKMKENEENAGGYKDDFEPTTPGHSPGVGHAVKNNEPNA | null | null | cellular response to nitrogen starvation [GO:0006995]; nitrate import [GO:1902025]; regulation of leaf morphogenesis [GO:1901371]; regulation of root development [GO:2000280]; root development [GO:0048364] | apoplast [GO:0048046] | hormone activity [GO:0005179] | null | null | C-terminally encoded plant signaling peptide (CEP) family | PTM: The mature small signaling peptide is generated by proteolytic processing of the longer precursor. {ECO:0000269|PubMed:25324386}. | SUBCELLULAR LOCATION: [C-terminally encoded peptide 6.2]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 6.1]: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25324386}. Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}. | null | null | null | null | null | FUNCTION: Extracellular signaling peptide that represses primary root growth rate. Modulates leaf morphology (PubMed:24179096). Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways (PubMed:25324386). {ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386}. | Arabidopsis thaliana (Mouse-ear cress) |
B3H5J1 | GLV10_ARATH | MSSIHVASMILLLFLFLHHSDSRHLDNVHITASRFSLVKDQNVVSSSTSKEPVKVSRFVPGPLKHHHRRPPLLFADYPKPSTRPPRHN | null | null | cell differentiation [GO:0030154]; lateral root development [GO:0048527]; positive regulation of cell population proliferation [GO:0008284]; regulation of asymmetric cell division [GO:0009786]; regulation of lateral root development [GO:2000023]; regulation of root meristem growth [GO:0010082]; regulation of root morphogenesis [GO:2000067]; root system development [GO:0022622] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615] | growth factor activity [GO:0008083] | null | null | RGF family | null | SUBCELLULAR LOCATION: [GLV10p]: Secreted {ECO:0000305|PubMed:22307643}.; SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:22307643}. Note=The precursor is detected in the endoplasmic reticulum probably during its processing. {ECO:0000269|PubMed:22307643}. | null | null | null | null | null | FUNCTION: [GLV10p]: Signaling peptide (root growth factor) that maintains the postembryonic root stem cell niche (PubMed:20798316). Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (PubMed:22307643, PubMed:23370719). {ECO:0000269|PubMed:20798316, ECO:0000269|PubMed:22307643, ECO:0000269|PubMed:23370719}. | Arabidopsis thaliana (Mouse-ear cress) |
B3H5K9 | NEDD1_ARATH | MMSNLVEPSWRLLAASGGDTVKLFDVSADSGDPCVLSYTPSPGCAVNSVKWNHTNLVVASTGEDKKISLWRKNGQSLGTVPVTGKDGGDSAEECLSAISFSKKGSRYICSGGTGQIVKIWDLQRKLCIKKLKGHTSTITGVMYNCKDEHLASVSVGGDLIVHNLASGARATELKDPNGQVLRLLDYSRSSRHLLVTAGDDGTVHLWDTTGRSPKMSWLKQHSAPTAGVCFSPSNEKIIASVGMDKKLYTYDSGSRRSSSCIAYEAPFSSLAFGDNGYILVAGTSNGRVVFYDIRGKPQPVTVLHAFSNSEDVTSLSWQTSKPVIVNEKNYTSEMALLGSTVEDSVVIPDPLPSTTPSASQSAMAPGSRGVSASTVNASSVEQTPNRNHLWPSGPLGRLHALRANDSYNDDMGVFSPIIDVSSVEKWADSEGYNNKDHLVVDNKPSSLLFPSSSKGYSFGDNGSKEHPIFDWKPSSTSKQDDPRAAFSSFGSITPTASSKSEDSALTPPEAWGGDKFSEKFNQLANEKFSDKFSHLHAPSRLAVSSTGASTSGSMFSSSRDFPLSHGQTNFANASLEFPRIRDFSSTFETSSTQTDNNLPSSPLFTKGITAPGNIDSLRLSPNFTRRFSTYAERISTTSSFSDGASLSLGGSPKIKKTGSETREEVLNHLLARPETVVATEAGAMPLMNQGGLKQSQTDQQQVMGSSNFTLQLFQRTLEGTLDSFQNSIHDDVRNLHIEILRQFHMHEMEMSKVLSSILENQAEQMKELKLLRKENQELRQRL | null | null | cell plate assembly [GO:0000919]; embryo sac development [GO:0009553]; pollen development [GO:0009555]; positive regulation of cytokinesis [GO:0032467]; regulation of microtubule nucleation [GO:0010968]; regulation of mitotic spindle organization [GO:0060236]; regulation of phragmoplast microtubule organization [GO:2000694] | kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; microtubule organizing center [GO:0005815]; nuclear envelope [GO:0005635]; phragmoplast [GO:0009524] | gamma-tubulin complex binding [GO:0140496] | PF00400; | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:25438942}. Note=First detected in prophase on the nuclear envelope, where it appeared to cap the future spindle poles. Later detected along kinetochore microtubules (MTs) of the metaphase spindle, with more prominent signals toward the poles. In anaphase, detected with the shortening kinetochore fibers. In the developing phragmoplast, localized mainly toward the minus end of MTs. {ECO:0000269|PubMed:19383896}. | null | null | null | null | null | FUNCTION: Regulates microtubules organization in a centrosome-independent manner. Required for the spindle to be positioned correctly and for the function of gamma-tubulin in organizing phragmoplast microtubules (PubMed:19383896). Component of active gamma-tubulin ring complexes (gamma-TuRCs) associated with cortical microtubules in interphase cells (PubMed:25438942). Mediates gamma-TuRC recruitment to the nucleation sites and is important for determining the ratio of branched to parallel nucleation (PubMed:25438942). May mediate the localization of GCP2 and GCP3 to the nuclear envelope (PubMed:19383896). {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}. | Arabidopsis thaliana (Mouse-ear cress) |
B3H5Q2 | GLV8_ARATH | MKKWSYAKLMTSALLLVFLSIILLAFHGGSRGDNHLYDHVAIGTKDILMGRKLKDLKPKTESLKMINPKKKNGFEYSDQVSSDLSRQEVFVDMMARDYQGPKPRSKPLKNN | null | null | regulation of asymmetric cell division [GO:0009786]; regulation of lateral root development [GO:2000023]; regulation of root meristem growth [GO:0010082]; regulation of root morphogenesis [GO:2000067]; root hair cell development [GO:0080147]; root hair initiation [GO:0048766] | extracellular region [GO:0005576] | growth factor activity [GO:0008083] | null | null | RGF family | PTM: The tyrosine sulfation is critical for the function of the peptide. {ECO:0000250|UniProtKB:Q3E880}. | SUBCELLULAR LOCATION: [GLV8p]: Secreted {ECO:0000250|UniProtKB:Q3E880}. | null | null | null | null | null | FUNCTION: [GLV8p]: Signaling peptide (root growth factor) that promotes root hairs formation and growth (PubMed:23370719). Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (By similarity). {ECO:0000250|UniProtKB:Q93VK8, ECO:0000269|PubMed:23370719}. | Arabidopsis thaliana (Mouse-ear cress) |
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