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 | MCRIVGAPRTLLPLLAALLQASVEASGGIALCKTGFPEDVYSAVLSQDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPNLPEDSVKESQEIEEIVFPRQLMKHNGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDDDDPNTLNGMLRYRILSQAPSTPSPNM... | 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 [... | 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:0005... | 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 ce... | 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:P151... | 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... | Rhinolophus ferrumequinum (Greater horseshoe bat) |
B2KI64 | PI4KB_RHIFE | MGDTVVAPAPLKPASESTPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLQKVKLSHGGVASSDRGTPLELVNGDGVDGEIRCLDDPPTGIREEDDETEATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYVHMDEDVGDAIKPYIVHRCRQSVDFSLQCALLLGAYSSDMHISTQRHSRGTKLRRLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVESEDEELSSSTESIDNSFSSPV... | 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:Q9... | 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|... | 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 traffickin... | 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 de... | 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 | MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAI... | 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}; Physiolo... | 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 su... | 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.... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
B2LT61 | TLR2_BISBI | MPRALWTAWVWAXIILSTEGASDQASSLSCDSTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLXTLKVGNSNSFTEIHEKDFTGLTFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMSTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIP... | 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 b... | 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 secr... | Bison bison (American bison) (Bos bison) |
B2LT62 | TLR2_CAPIB | MPRALWTAWVWAVISAFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLKQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFTALTLNRIRYLGNVETLTIRKLHIP... | 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 b... | 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 secr... | Capra ibex (Ibex) |
B2LT64 | TLR2_GIRCA | MPRALWTAWVWAVISLSTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITHVGNRDLQSCVNLKTLRLGANEIHTVEEDSFFHLRSLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYRTLGETSLFSHLSNLRTLKVGNSNSFTEIHEKDFTGLTFLEELEISARNLQIYAPKSLKSIQNISHLILHLKQPVLLLDILVDIVSSLDYLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGISEVEFDDCTHDGIGDFRALALERTRYLGNVETLTIRKLHIP... | 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 b... | 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 secr... | Giraffa camelopardalis (Giraffe) |
B2LT65 | TLR2_SHEEP | MPRALWTAWVWAVISVFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTASVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLRQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLTFRNVQFTDDSFVEVVKLFNYVSGILEVEFDDCTHDGVGDFTALTLNRIRYLGNVETLTIRKLHIP... | 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 b... | 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 secr... | 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:00163... | 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 regula... | 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 membra... | 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-[p... | 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... | Ovis aries (Sheep) |
B2RH54 | FIMA1_PORG3 | MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNS... | 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:87785... | 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 proc... | 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, P... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG1 | MFA1_PORG3 | MKLNKMFLVGALLSLGFASCSKEGNGPDPDNAAKSYMSMTLSMPMGSARAGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYY... | 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 pal... | 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... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG2 | MFA2_PORG3 | MNKRKHMDIRRLIISLPAIMALWGGLASCDKMIYDNYDDCPRGVYVNFYSQTECAENPSYPAEVARLNVYAFDKDGILRSANVFEDVQLSAAKEWLIPLEKDGLYTIFAWGNIDDHYNIGEIKIGETTKQQVLMRLKQDGKWATNIDGTTLWYATSPVVELKNMEDGADQYIHTRANLREYTNRVTVSVDSLPHPENYEIKLASSNGSYRFDGTVAKADSTYYPGETKVVGDSTCRAFFTTLKLESGHENTLSVTHKPTGREIFRTDLVGAILSSQYAQNINLRCINDFDIRLVAHHCNCPDDTYVVVQIWINGWLIHSY... | 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 fac... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RHG4 | MFA4_PORG3 | MKKYLLYASLLTSVLLFSCSKNNPSEPVEDRSIEISIRVDDFTKTGETVRYERNQGSAAERLITNLYLLLFDQSGANPAKYYIAGNTFSGGIWLPDDMKVKLDMTQSEAGERKVYVVANVDNAVKTALDAVANESDLQTVKRTTAMPWSTDIASPFLMSGNKTHDFLANRLLDNVPLVRAIAKVELNISLSEKFQIVPIIVNGSLSEFKFRYVNFDKETYVVKPTTKPDNLISSANGVWPQITDWTVWGASLNTSPAPDAGTGYTLDANGKVTALRIVTYLNERDSKGATVEVALPRVDDGTLPPPEFGPELYRLPLPDK... | 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... | 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 a... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RID1 | DPP11_PORG3 | MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQI... | 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 ... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RIT0 | DPP5_PORG3 | MNKKIFSMMAASIIGSAAMTPSAGTNTGEHLTPELFMTLSRVSEMALSPDGKTAVYAVSFPDVKTNKATRELFTVNLDGSGRKQITDTESNEYAPAWMADGKRIAFMSNEGGSMQLWVMNADGTERRQLSNIEGGITGFLFSPDEKQVLFTKDIKFGKRTKDIYPDLDKATGRIITDLMYKHWDEWVETIPHPFIANATDGMITTGKDIMEGEPYEAPMKPWSGIEDFSWSPDGQNIAYASRKKTGMAYSLSTNSDIYIYNLTSGRTHNISEGMMGYDTYPKFSPDGKSIAWISMERDGYESDLKRLFVADLATGKRTHV... | 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:243... | 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... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RKV3 | DPP7_PORG3 | MQMKLKSILLGAALLLGASGVAKADKGMWLLNELNQENLDRMRELGFTLPLDSLYSFDKPSIANAVVIFGGGCTGITVSDQGLIFTNHHCGYGAIQSQSTVDHDYLRDGFVSRTMGEELPIPGLSVKYLRKIVKVTDKVEGQLKGITDEMERLRKAQEVCQELAKKENADENQLCIVEPFYSNNEYFLIVYDVFKDVRMVFAPPSSVGKFGGDTDNWMWPRHTGDFSVFRVYAGADNRPAEYSKDNKPYKPVYFAAVSMQGYKADDYAMTIGFPGSTDRYLTSWGVEDRIENENNPRIEVRGIKQGIWKEAMSADQATRI... | 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 synthet... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RLK2 | KGP_PORG3 | MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGE... | 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 o... | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
B2RPY5 | GP161_MOUSE | MDFVQHALLTASRGALTMSLNSSLSYRKELSNLTATEGGEGGAVSEFIAIIIITVLVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHQEPGYTIFWQIWCALFPFLIMLVCYGFIFRVARVKARKVHCGTVVTVEEDSQRSGRKNSSTSTSSSGSRRNALQGVVYSANQCKALITILVVIGAFMVTWGPYMVVITSEALWGKNCVSPT... | 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... | 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 pro... | Mus musculus (Mouse) |
B2RQC2 | UBP42_MOUSE | MTIVDKTEPSDPSTCQNQPGSCEAVSPEDMDTGSASWGAVSSISDVSSHTLPLGPVPGAVVYSNSSVPEKSKPSPPKDQVLGDGIAPPQKVLFPSEKICLKWQQSHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQTHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVTKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTISLKRFA... | 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 | MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSN... | 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;... | '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... | 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]; gl... | 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 oli... | 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... | 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)-dihydrooro... | 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-d... | Mus musculus (Mouse) |
B2RQL2 | STOX1_MOUSE | MARPVQLAPGSLALVLSPREAGQAAGEPGGRALFRAFRRANARCFWNARLARAASRLAFLGWLRRGVLLVRAPQPCVQVLRDAWRRRALRPPRGFRITAVGDVFPVQMSPIAQCRFVPLAEVLCCAIADMNAAQVMVTQQSLLEHLIKHYPGIAVPSPDILYSTLGALIQERKIYHTGEGYFIVTPSTYFITNTPMQGNKSALLSNEGCSGPTSGTYLVSVDCCAEPTQENEALFSHCPSCQCYPDTSMCDSKDLLTAAEVTRKSQEGLEETTALTENQVVSASEDTHICVNPKPLPYTKDKGKRFGFGFLWRSLSRKEK... | 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]; p... | 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:... | 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 ... | Mus musculus (Mouse) |
B2RQR8 | ECE2_MOUSE | MNVALHELGGGGSMVEYKRAKLRDEESPEITVEGRATRDSLEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDE... | 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). {EC... | Mus musculus (Mouse) |
B2RR83 | YTDC2_MOUSE | MSRPSSVSPRPPAPSGGGTGGGGGGSGGGGGGGGGGPASCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAENREMSKTSGRLNNGIPQVPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDS... | 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... | 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)-co... | Mus musculus (Mouse) |
B2RRD7 | BRPF1_MOUSE | MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDSPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHSAPASAAPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCL... | 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 similari... | Mus musculus (Mouse) |
B2RRE7 | OTUD4_MOUSE | MEAAVGAPDGVDQGGVGPLEDETPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYPITYKDSSAMCQSLLYELLYEKVFKTDVSKIMMGLEASEVAEESNSEISDSEDDSCKSKSTAATDVNGFKPSGSENPKNNGNSADLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCHQVRLDHNGKLSNADIHGVHSENGLVLSEELG... | 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 deubiqui... | 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 recep... | Mus musculus (Mouse) |
B2RS91 | RRN3_MOUSE | MAAPLLHTRLSGDVTAAASATLSASRTGLSDMLALESDFFNSPPKKTVRFGGTVTEVLLKYKKGETNDLELLKNQLSDPDIKDDQIINWLLEFRSSVMYLTKDFEQLINIILRLPWLNRSQRVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIVKEGGIDVSDSDDEDDNLPAIFDTCHRALQIITRYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISLYFPTLRREILELVIEKLLKLDVSVSRQDIEDAEEKAAQTCGGTDTTEGLFNMDEDEDTDPEKKADQEQPNQMAHPTAERLDVLLCLLL... | 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 intr... | 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 | MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIY... | 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 regulat... | 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 act... | 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, centr... | 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 ... | Mus musculus (Mouse) |
B2RTY4 | MYO9A_HUMAN | MNINDGGRRRFEDNEHTLRIYPGAISEGTIYCPIPARKNSTAAEVIESLINKLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALENRLSGEDYRFLLREKNLDGSIHYGSLQSWLRVTEERRRMMERGFLPQPQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL... | 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 hin... | 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, E... | Homo sapiens (Human) |
B2RU80 | PTPRB_MOUSE | MLRHGALTALWITLSVVQTGVAEQVKCNFTLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIRIDNFTYGCNPKDLQAGTVYNFRIVSLDGEESTLVLQTDPLPPARFEVNREKTASTTLQVRWTPSSGKVSWYEVQLFDHNNQKIQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVSGEKRSFPVYINGSTVPSPVKDLGISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVTMASGLQNSRWKLVRTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDS... | 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... | Mus musculus (Mouse) |
B2RUJ5 | APBA1_MOUSE | MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGL... | 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 or... | 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-co... | 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 ... | Mus musculus (Mouse) |
B2RUP2 | UN13D_MOUSE | MATHLSHPQRRPLLRQAIKIRRRRVRDLQDPPPQATQEVQVQSHHFSPEERDLLYEEALYTVLHRLGQPEPNHVKEASELLSYLQEAFQVQPEEHQQMLRRVRELEKPVFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVAEGSPVSRRRQKAVVKHTIPEEETHRTQVKSQTLNPVWDETFILEFEDIANASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWFPLEPCTETYPDRGQCHLQFQFIHKRRATAASRSQPSYTVHFHLLQQLVSHEVTQHQAGST... | 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 secre... | 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 vesicl... | 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-co... | Mus musculus (Mouse) |
B2RUR8 | OTU7B_MOUSE | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVSAALSDFEQLRQVHAGNLSPPFSGGSTCPKTPEKGGSDREPTRPSRPILQRQDDVIQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSSEHPLEMPICAFQLPDLTVYKEDFRSFIERDLIEQSMLVALEQAGRLNWWVSMDSTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYALMEKGVEKEALRRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGSNGASGGGVESSEEPVYESLEEFHVFVLAHVLKRPIVVVADTMLRD... | 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:... | 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... | 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 | MTEDKAEKVMPEETAFEEIEKDFQEVLSELSGDKSLEKFRTEYEKLHSIMKKSYENEKRLMAKCRELNAEIVVNSAKVATALKLSQDDQTTIASLKKEIEKAWKMVDSAYDKEQKAKETILALKEEIVNLTKLVEQGSGLSMDQDSNIRDLLKFKEEVTKERDQLLSEVVKLRENLAQTIEKQQAAEHAKEEAEMAISQFQQEIQHRQNEASRESRKKEKLEKELRQIQTDMDGRQAEIKAMQQYMHKSKEELQRLEQQLKEQKILNERAAKEVEQFQMRNAKLQQENDQHTLTCEQLSQENQQKALELKAKEDEIHQMR... | 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 predom... | 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 | MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQAMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGIGSSGPNQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQPLKMGMMNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVPGGGMPSMGQQPTPSVQQPGLVTPV... | 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]; cell... | 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 bi... | 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|UniProtK... | 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}; P... | 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 'Ly... | Mus musculus (Mouse) |
B2RX12 | MRP3_MOUSE | MDRLCGSGELGSKFWDSNLSIYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWVDLFYSFHGLIHGSSPAPVFFVTPLVVGITMLLATLLIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSALAEGKILDPFRFTTFYIYFALVFCALILSCFKEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQQNQASRSQTATAEPKIPGEDAVLLKPRPKSKQPSFLRALVRTFTSSLLMSACFNLIQ... | 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 t... | 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:O15... | 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-... | Mus musculus (Mouse) |
B2RX14 | TUT4_MOUSE | MEEPKTSKNENHEPKKNIICEESKAVKIISNQTLKPRNDKSEIGTSSLNRNSSKKTKQNDICIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPNLPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQKTPRSPLEPENVPSLLLKENVKQTESQQTGKKLTSSFVSMDKRKSEALQGEKSALENSSLSQKQQTQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYT... | 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... | 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 cyto... | 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 transcr... | Mus musculus (Mouse) |
B2RX88 | CSPP1_MOUSE | MADSLDEFIEEQKAKLAKDKAELESDPPYMEMKGKASEKLSENSKILISMAKENIPPSSQQQPKGPLGIEYGLSLPLGEDYEQKKHKLKEELRQDYRRYLTQGITQAKRKKNFLSTGETDPSTLGVSLPIDERLSAKERLKLERNREYNQFLRGKAESTEKVRQVEKNIEPKSQRNKNPISQGKSDLPLQIQTAYTHSEGPWLSRQEEGLYRQLDGEIELRSRRPLKQTKEEVGISGAEHPSLSGSAGVPERRARRANGERVLDRQHCRADRDPGVSEDMDERFRFESDFDRRLLRVYTNGRPHGSRRGYVDGDDVPEEP... | 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 | MISWGLSCLSVLGAAGTTLLCAGLLLGLAQQLWTLRWTLSRDWASTLPLPKGSMGWPFFGETLHWLVQGSRFHSSRRERYGTVFKTHLLGRPVIRVSGAENVRTILLGEHRLVRSQWPQSAHILLGSHTLLGAVGEPHRQRRKVLARVFSRSSLEQFVPRLQGALRREVRSWCAAQRPVAVYQAAKALTFRMAARILLGLQLDEARCTELAHTFEQLVENLFSLPLDVPFSGLRKGIRARDQLYEHLDEAVAEKLQEKQTAEPGDALLLIINSARELGHEPSVQELKELAVELLFAAFFTTASASTSLILLLLQHPAAIT... | 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:57... | 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 i... | Mus musculus (Mouse) |
B2RXE2 | SL9A5_MOUSE | MLSAALLLLPGLPLAGAGATEEPTQESGPLGEPPPGLALFRWQWHEVEAPYLVALWILVASLAKIVFHLSRKVTSLVPESCLLILLGLVLGGIVLAVAKKAEYQLEPGTFFLFLLPPIVLDSGYFMPSRLFFDNLGAILTYAVVGTLWNAFTTGVALWGLQQAGLVAPRVQAGLLDFLLFGSLISAVDPVAVLAVFEEVHVNQTLFIIIFGESLLNDAVTVVLYKVCNSFVEMGSANVQATDYLKGVASLFVVSLGGAAVGLVFAFLLALTTRFTKRVRIIEPLLVFLLAYAAYLTAEMASLSAILAVTMCGLGCKKYVE... | 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... | 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... | Mus musculus (Mouse) |
B2RXF5 | ZBT42_HUMAN | MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDRPAGSRDTVRLNGDIVTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLQEKDRSLDPGNPAPGAEPAQPPCPWPVWTADLCPAARKAKLPPFGVKAALPPRASGPPPCQVPEESDQALDLSLKSGPRQERVHPPCVLQTPLCSQRQPGAQPLVKDERDSLSEQEESSSSRSPHSPPKPPPVPAAKGLVVGLQPLPLSGEGSRELELGAGRLASEDELGPGGPLCICPLCSKLFPSSHVLQLHLSAHFRER... | 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 | MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDP... | 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:168... | 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 | MALPLWALTFLGLTGLGLSLRSRKPESFRSETELNHLAVDEVTGVVYVGAVNALYQLSADLHVQQHVVTGPFMDNKKCTPPIEASQCHEAVLTDNFNQLLLLDPPGKRLVECGSLFKGICALRAMSNISVRLFYEDGSGEKSFVASNDERVATVGLVTSTRPDGERVLFVGKGNGPHDNGIIVSTRLLDRAEGREAFEAYSDHTTFKAGYLSTNTQQFVAAFEDDFYVFFVFNHQDKHPAKNRTLLARMCKDDPSYYSYVEMDLQCQDPSDPQDSAFGTCLAASVATSGAGRALYAVFSRDGRSTGGPGAGLCVFPLDKV... | 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:0050... | 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 ... | Mus musculus (Mouse) |
B2RXV4 | FLVC1_MOUSE | MARPDDEVGPAVAPGHPLGKGYLPVPKGAPDGEARLVPQNGPEALNGGPGLGPLIAGAQGGPQALIAAEEETQARLLPAGDGEDVPCPACPPRTALSPRRFVVLLIFSLYSLVNAFQWIQYSSISNVFEDFYEVSPLHINWLSMVYMVAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCGSVQRHLFWVTMLGQILCSVAQVFILGLPSPVASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPALGTQNSTGLLAHTQNNTDLLAHNINTMFYGTAFISTFLFFLTIIAFKEKPPLPPSQAQAVLRDSP... | 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 embryon... | 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); Xre... | 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 ... | Mus musculus (Mouse) |
B2RXZ1 | PNDC1_MOUSE | MDVGADEFEQSLPLLQELVAGADFVGLDIEFTGLRSNLSRPQQISLFDLPSEWYLKTRQSVQQFTICQIGLSMFSSIEGESNKYVAHSCNFFLFPTTFGILDSEFSFQASSVQFLNQYGFDYNKFLKNGIPYMNEEQEKKIKHSILRGNWRVRSSLDKDQIKVVIDKVTQWLDLAEEGDQMTLPGIAGFQAFEVQLVLRQALPNIWTVLKEEWVIVKKVSQPQRWYLEHASCDQVSCWKEQILLSARGFSVFFQMLVKAQKPLVGHNMMMDLLHLHEKFFRPLPESYDQFKQNIHSLFPVLIDTKNVTKDIWKELRFPRV... | 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 ... | Mus musculus (Mouse) |
B2RY04 | DOCK5_MOUSE | MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEATVEDGGQHETVIPGELPLVQELTNTLREWAVIWRKLYVNNKVTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTVALFRAHEVASKRIEEKIQEEKSILQNLDLRGQAIFSTVHTYGLYVNFKNFVCNIGEDAELFIALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSTDLIRPRISLVCQIVRVGRMELKEGKKHTCGLRR... | 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 c... | 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|UniP... | Mus musculus (Mouse) |
B2RY50 | ODAD2_MOUSE | MGVALTRLAQWTAAGYETGTLEITPLNESILNEITKFVESFSYKYPQEAKFVFVEPLEWKTYLEPSAFELGYVVSATTAESEETGKDGQPLLFLSVPYIKVRSFGQLSQLLSIATDSKLQEAQACIEANRDPVVKILGPDYNEMKEDPTRLTLLDTIIKDKETYMKRKVAILLKQLDLHLLNHSLKYISLEISLNPGTFKKDIELLKRFSGKGEQTVLESIEYTSDYEFSNGCRAPPWRQIQGEICYVLVKPHDMETLCLTCSTEGVFLNGGKTEEEGEINYERKGEIYKDLVTCLKDKSPVFSENMSKHEIRFTEEQQK... | 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:... | Mus musculus (Mouse) |
B2RY71 | DNAI3_MOUSE | MAPKPPKSPKGQKKGKKNMKQQLLVPEEEEPMNMESMGHPEIYPLVLTTKTQEIFNCRVDEDMTDEQTYKLIKKEDILADLQNRAAVSDFHPVKKIVREYPGEELLLVYDKDFKYGLNFYLIGTEDGKENFLKPPEVPEEQEEPKEHVQEDVYVYNPPVSKPWVSLGSEKEIEEESVQESGKRVTYMISRKRSEFGAPVTFSDQNASSVKDAYIECTSYPEKNYTLSQVEKDVGLQVIAEVKDTSTQTKWAFPKNATTQYYPREFSEEEKSLIGKSKSLVDFFNNVSTSVEVALQQNEIMNTFIDDWKNLAEEESTFGDK... | 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 (P... | Mus musculus (Mouse) |
B2RYF7 | WASH1_RAT | MTAVKTQHSLAGQVYAVPLIQPDLRREEAIQQVADALQYLQNISGDIFSRISQRVELSRRQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPEHLQEYNSVFTGALDPGLQRRPRYRIQSKHRPLDERALQEKLKYFPVCVSTKSEPEDEAEEGLGGLPSNISSISSLLLFNTTENLYKKYVFLDPLAGAVTKTHTMLGTEEEKLFDAPLSISKREQLEQPAPENYFYVPGLGQVPEIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPAFHTEVAEPFQPEREDGALLAPPPPPPPPPPPPPPAPTA... | 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 tran... | 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:... | 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... | 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 ... | 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-linke... | 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 t... | 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]; p... | 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 ... | 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|UniPr... | 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 targ... | Rattus norvegicus (Rat) |
B2RYN7 | SPAST_RAT | MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRFSRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMVSGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQ... | 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]; m... | 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:... | 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:... | 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... | Rattus norvegicus (Rat) |
B2RYR0 | RN168_RAT | MAAPKNSIPSLAECQCGICMEILVEPVTLPCNHTLCNPCFQSTVEKANLCCPFCRRRVSSWTRYHTRRNSLVNTDLWEIIQKHYAKECKLRISGQESKEIVDEYQPVRLLSKPGELRREYEEEISKVEAERQASKEEENKASEEYIQRLLAEEEEEEKRRTERRRSEMEEQLRGDEELARRLSTSINSNYERNILASPLSSRKSDPVTNKSQKKNTNKQKNFGDIQRYLSPKSKPGTAWACKTEHGEDMCKSKETDSSDTKSPVLQDTDVEESMPTHSPQTCPETQGQGPEPLTEMPVPWLCARNAEQCLEGKAEAVSTN... | 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];... | 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 bi... | 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-d... | Rattus norvegicus (Rat) |
B2RZ55 | SIR7_RAT | MAAGGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESEDLVTELQGRSRRREGLKRRQEEVCDDPEELRRKVRELAGAVRSARHLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRPVSAADLSEAEPTLTHMSITQLHKHKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCIPNREYVRVFDVTERTALHRHLTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASKADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVM... | 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 tr... | 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]; ... | 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 chain... | 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.... | 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=... | 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... | 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:00... | 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 prote... | Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) |
B2UP57 | H2018_AKKM8 | MARPLPILGGILLSFSPPAEATAQYSIIPEPSRTELRQETAKTLQLLSDQEVPTLETDAYRLTVTPQGAHLASGGREGRIYGLATLRQLRDQLAGQPEGIPCGVITDKPRYPWRGLMVDPARHFIPAADLKKFVDMMAYYKFNRLHLHLTDNQGWRLPVPGYPKLKSVASRREESFGDGIPHEGMYTKQELKELVAYCAARGIDVIPEIDMPGHNQALHAAYPEFFCFPKPDMNVRTTAGNSKELVCPQKPEVWKFYASVFNELKDIFPSGIVHLGGDEAPTELWEKCPLCREARTRAAMKDEQEQMKAFFAKTAALLAK... | 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:00... | 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... | Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) |
B2ZFP3 | SMAL1_DANRE | MSVSLTPEQQRRIEENRKKALARRAERQAQIADPGPAQNKHTQSGTTGGPAKNNQHFASDRGQSGAPTRQTQLIDINAACTKTAPPTSITAASTASSFYGQAGKPSTGEKRPPKPPEPAANIPAKKPAVYLRGRCVSHSENRFRVEVGYHADLILVFKSIPSKNYDPATKMWNFSLEDYQMLMEQVAHLPSISLKPLEGMEGLNISASTCRPKDAAAMAALMRLCQGWQKPGATIKGKCVLVSRSRLEVDIGYQADVIGIFKQMPSKSYDMKTRKWTFLLEDYGKLMADLNELPTVETEPLPHAVLQSFSSQFEKTQSQA... | 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:... | 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 ... | 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:1910081... | 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... | Clitocybe nebularis (Clouded agaric) (Lepista nebularis) |
B2ZX90 | FAS1_ORYSJ | MEGGKLLGVAHPEPANNIDADLRYDLGQSRMQVDGPVVLNRSAELEPSDSMAIDDVPVEASSQPAPAKQSPALMDTIVEVQKQLKRKRASSGPALAAADKDALVAGCCQELEGLLEYYREVSGHRMQFEVGNLSTNAAIGCLLEESSLGLSKLVDEIYEKLKGMEGVSATSVRSSVLLIGQRMMYGQSSPDADVLEDESETALWCWEVRDLKVIPLRMRGPLSTRRTARKKIHERITAIYSTLSVLEAPGAEAQVNDMRKASLKLSKALNLEGIKSLVERATQKSNIERGAKNTGSTAKEPMQEMVKSNNDTGIIENVDD... | 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 ass... | Oryza sativa subsp. japonica (Rice) |
B2ZXD5 | GPHR_CRIGR | MSFLIDSSIMVTSQILFFGFGWLFFMRQLFKDYEVRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIQLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAVARRTMFQRGEVQNKPSGLWGMLKSVTASAPGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVLDRVGKTDPVT... | 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) =... | 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 cell... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
B2ZZS9 | WDR55_ORYLA | MAAPPEHAATGSEQTDPPETNSEPDLSQPEPADSDADEPVGPKIRETPEDIRLEAIANTVALHPSRDVLVCGDVDGDVYAYAYSCTEGETRELWSSGHHLKSCRQVRFSADGLKLYSVSRDKAVHQLDVERGQLVSRIRGAHAAAINSLLLVDENILATGDDRGTLKVWDMRKGEAFMDLKHHDDYISDIAVDQAKRILLTTSGDGTMGVFNIKRRRFELLSEFQSGDLTSVALMKRGKKVVCGSSEGTVYIFNWNGFGATSDRFAVKAESVDCIVPITDSIMCTASMDGYIRAINLLPNRVIGCIGQHVGEPIEEINKS... | 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 | MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNIHTIAWIRFITSYALLLLFRSAVIVMTSLPAPDDLCQDPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWWPCCGANSREVTE... | 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,... | 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 wi... | 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:0... | 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-p... | Bothrops marajoensis (Marajo lancehead) |
B3A0S5 | XYNA_FUSO4 | AASGLEAAMKAAGKQYFGTALTVRNDQGEIDIINNKNEIGSITPENAMKWEAIQPNRGQFNWGPADQHAAAATSRGYELRCHTLVWHSQLPSWVANGNWNNQTLQAVMRDHINAVMGRYRGKCTHWDVVNEALNEDGTYRDSVFLRVIGEAYIPIAFRMALAADPTTKLYYNDYNLEYGNAKTEGAKRIARLVKSYGLRIDGIGLQAHMTSESTPTQNTPTPSRAKLASVLQGLADLGVDVAYTELDIRMNTPATQQKLQTNADAYARIVGSCMDVKRCVGITVWGISDKYSWVPGTFPGEGSALLWNDNFQKKPSYTST... | 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 | MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAK... | 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). T... | Escherichia coli O157:H7 (strain EC869) |
B3DH20 | DAA11_DANRE | MVRISEDLIRRRAEHNNGEIFSLEELSLHQQDIQRIEHIHKWCRDLKILYLQNNLIPKIENVGRLKKLEYLNLALNNIEVIENLEGCESLQKLDLTVNFVGRLSSVETLKHNLHLKELYLVGNPCAEYQGYRQYVVATVPQLQSLDGKEISRAERIQALQELDAVRTRVLQQETKYLEEREKQKSNANEHPEINQSLSESQNGTQQYPESSSKTHTEAEDEEREFWEKPCPFTPESRLEAHRHLEEKRRANEKEKEKPKTKTPRTLITPDGRVLNVNEPKLDFSLFEDENNCLLLDLHVYRHMDSSLLDVDVQPMYVRVT... | 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 formati... | 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) signali... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DIV9 | KL40A_DANRE | MASMSVDPVTEPRMYQQTLLQDGLCDLLDANKFVDCILKIKDKEFPCHRLVLAATSPYFKAMFLSDLEESKKREIVLKDIEPGVMGMILRYIYTSDINLTEQNVQDIFMAANMYQIPSIFSVCVSYLQQKLVLSNCLAIFRLGLLLDCPRLAMEARDFICDRYLLIIRDQDFHQLGPSELAAIITCDSLNVEREESVFESLMDWVEYDTDERTKELPELLHCVRFRLMPTSYFKEKVEGHRLIRTNQELKKELQLIKDAQKGLLHRVKRSSHRKEGKSAEFESDDDDEDGLLPGILNDNPRFGMFQSDLILMINDAGTVA... | 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 | MAATGNEEQTLLPDIEEEAEGMEREMESEDDEEEGMGVEHSEEEDEEDTSEDERENEAEIQRLEEQLSINAFDYNCHVDLIKLLRQEGKLHRLRKARQKMSELFPLTEEIWLDWLKDEIRITEDESDREKVYELFERAIKDYVCPEIWLEYVQYSIGGMGAQGGIERVRSIFERALTAVGLHMTKGASIWEAYREFEIVILSTVQPPPGTVPSQEQQELLSAQLERIHTLFRRQLAVPLMDMEGTYAEYSDWADDGVPETVTHQYRRALQQMEKGKPYEEALLVSEPPKLAEYQSYIDFEIKEGDPARVQIIFERALAEN... | 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 signal... | 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 ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DK56 | PTPRU_DANRE | MNTCAFLLILAVQIHADSVEGPTAGCTFDEDSDPSLCEFSQGEEDDFDWQLFRAHASPHSTSDLLRGSYMMVNSSQHAAGQRAQLLLQTLSENDTHCVQFSYFLYSRDGHSPGALRVYVRVNGGPLGIPVWNVSGSRGRQWHQVELAVSTFWPNEYQILLEATVDRKGYIAVDDILLLNYPCYKAPHFSRLGDVEVNAGQNATFQCVAAGRPSEAEKFLLERHNGEVSSGGSVKHLGRNRFAVSFQLEDVQKPEQDLYRCVTQSSRGSGVSNFAELIVKVPPSPIAPPQLLRAGSTYLIIQLNTNSILGDGPIIRREIEY... | 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. {E... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3DL84 | PLK4_XENTR | MAGSIGERREDFKVLNLLGKGSFACVYRAQSINTGIDVAIKMIDKKAMQKVGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLILEMCHNGEMNRFLKNRKKPFSEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLSSDMNIKIADFGLATQLKMPNEKHFTMCGTPNYIAPEIATRSAHGLESDVWSLGCMLYTFLVGRPPFDTDTVKNTLNKIVLADYEMPDFVSREAKDLIFQLLRKNPADRLSLSSVLDHAFMTGFSNVQSKVMGAVEDSIDSGHATISTGFTGSSGVSISGRFQEKRILSGPSLPNK... | 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, ... | 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-[p... | 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 overexpres... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B3DLB3 | ANM2_XENTR | MSTSGCSSEKSDFQDSTEGEEEEDTQSENLCMREYVVIRDYMAADATQLSLCFGDKVLLLSAVTQDWWWVKHNGICGYVPASYLHDALNDQEDTEVDDPWQDEEYYGSYKTLKLHLEMLSDVPRTTAYKEVILRNSSSLCGKHILDLGCGTGIISFFCAKLAQPEAVYAVEASEIAEQTRRLVKQNGISNLVHVIRQRAEELQLPTKVDILVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSASKEYANKVLFWDNPYQLDFSLLKPLAAKEFFARPKPDYVLQPEDCLSEPCILLHLNLKTLQLA... | 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 tr... | 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 act... | 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:... | 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 | MEMDVTRDTVEVLPQHKFDIRSLEAYLNQHLPGFGSDHRAVLTVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKVQKALFSVGFPVPKPLLYCSNASIIGTEFYVMEHVQGRIFRDFSIPGVSPAERAAIYVSLVETLAWLHSLDIHSLGLDRYGTGVGYCKRQVSTWTKQYQASAHQSIPAMDQLSTWLMRNLPDSDNEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPLSDLAHLSLFYFWPRTLPMINRGSHIQENTGIPLMEELISIYCRRRGIDPNLPNWNFFMALSFFKLAGIAQ... | 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:CHEB... | 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 | MREEEIEKIRGVVRDCVSKHLYSSAIFFADKVAALTNDPSDIYMQAQALFLGRHYRRAFHLLNASKIVLRDLRFRYLAAKCLEELKEWDQCLLMLGDAKVDDDGIVYDAKDGNVIDFDKDGEDREINISSAICFLRGKAYGALQNRSQARQWYKAAIKADPLCYEALECLIESHMLTSEEESSLLSSLQFSPEDGWLSSFYSCLIKKYDKESTVELKFKKLENETSGSVSGSSMITLANNTDLLACKAEYYHQCCEYQKCFELTAALLEKDPFHLKCTLVHLAAAMELGNSNELYLMACNLVKDYPSKALSWFAVGCYYY... | 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:003... | 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 degr... | 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 musc... | 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 nAC... | 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]; negativ... | 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 catalyze... | 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 G... | Mytilus galloprovincialis (Mediterranean mussel) |
B3EWR6 | AMP_ECHCG | MGKGSSGGGAWWAFLLLAGVLLAVAATAAGAEEDVATEVAAAADRDPKEDLRWCRKGCQWQYGQDTRQRKECERDCRQRHREQEQDADEEDGSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGDDDVAVDACEGADRCRERCERRHRGDWQGKQRCLMECRRREQEEDVDDRCPCPCRRQCERHGDPATRQRCVEACQRRREEERRHGGGDADEEGSRGGRCERKCRRHSDWQTRQRCLQQCEQRERQEEGGRDDAGDGKDTYCADRCQSMCRQRHRGDREMQRRCARKCEREEGCPRRRDATADADEAEEDDGND... | 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)=1... | 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 | MGDTAVEPAPLKPASEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVRLLHGAVAVSKRGTALELVNGDGVDTEIRCLDDPPAQIREEEDEMGATVTSGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPALNTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVENEDEPIRLAPEREFIKSLMAI... | 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:Q9... | 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|... | 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 traffickin... | Sorex araneus (Eurasian common shrew) (European shrew) |
B3EY95 | SCACT_ACEAC | MTERIRNVALRSKVCPAETASELIKHGDVVGTSGFTGAGYPKEVPKALAQRMEAAHDRGEKYQISLITGASTGPQLDGELAKANGVYFRSPFNTDATMRNRINAGETEYFDNHLGQVAGRAVQGNYGKFNIALVEATAITEDGGIVPTSSVGNSQTFLNLAEKVIIEVNEWQNPMLEGIHDIWDGNVSGVPTRDIVPIVRADQRVGGPVLRVNPDKIAAIVRTNDRDRNAPFAAPDETAKAIAGYLLDFFGHEVKQNRLPPSLLPLQSGVGNVANAVLEGLKEGPFENLVGYSEVIQDGMLAMLDSGRMRIASASSFSLS... | 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|PubMe... | 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 (e... | Pseudomonas phage 201phi2-1 (Pseudomonas chlororaphis phage 201phi2-1) |
B3G515 | GPER1_DANRE | MEEQTTNVIQIYVNGTEQFNASFDFNITDVKESTDTYEFYIIGLFLSCLYTIFLFPIGFIGNILILVVNLNHRERMTIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYVALTSSMSSSPLRTMQHAKLSCSLIWMASILATLLPFTIVQTQHTGEVHFCFANVFEIQWLEVTIGFLIPFSIIGLCYSLIVRTLMRAQKHKGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSKRTDTTLWHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKL... | 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 cyc... | 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 [G... | 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:0... | 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 proli... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B3GNI6 | SEP11_RAT | MAVAVGRPSNEELRNLSLSGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQFPTDEETVAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQ... | 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 ... | 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 synaps... | 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:... | Arabidopsis thaliana (Mouse-ear cress) |
B3GSH5 | ASMT_RAT | MAPGREGELDRDFRVLMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLRGAGDGSYTNSALSSTFLVSGSPQSQRCMLLYLAGTTYGCWAHLAAGVREGRNQYSRAVGISAEDPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQEAARLYPGSSVCVFDLPDVIAAARTHFLSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRPGGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNL... | 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-... | 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... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
B3H5A8 | RVE7_ARATH | MLCFVRFQAGFVRIIVAARKRFRYFLMAAEDRSEELSSNVENGSCNSNEGINPETSSHWIENVVKVRKPYTVTKQREKWSEEEHDRFLEAIKLYGRGWRQIQEHIGTKTAVQIRSHAQKFFSKMAQEADSRSEGSVKAIVIPPPRPKRKPAHPYPRKSPVPYTQSPPPNLSAMEKGTKSPTSVLSSFGSEDQVNRCSSPNSCTSDIQSIGATSIDKKNNYTTSKQPFKDDSDIGSTPISSITLFGKIVLVAEESHKPSSYNDDDLKQMTCQENHYSGMLVDTNLSLGVWETFCTGSNAFGSVTEASENLEKSAEPISSSW... | 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, a... | 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|Pu... | 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 morph... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
B3H5K9 | NEDD1_ARATH | MMSNLVEPSWRLLAASGGDTVKLFDVSADSGDPCVLSYTPSPGCAVNSVKWNHTNLVVASTGEDKKISLWRKNGQSLGTVPVTGKDGGDSAEECLSAISFSKKGSRYICSGGTGQIVKIWDLQRKLCIKKLKGHTSTITGVMYNCKDEHLASVSVGGDLIVHNLASGARATELKDPNGQVLRLLDYSRSSRHLLVTAGDDGTVHLWDTTGRSPKMSWLKQHSAPTAGVCFSPSNEKIIASVGMDKKLYTYDSGSRRSSSCIAYEAPFSSLAFGDNGYILVAGTSNGRVVFYDIRGKPQPVTVLHAFSNSEDVTSLSWQTS... | 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:200... | 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}.... | 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 m... | 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 div... | Arabidopsis thaliana (Mouse-ear cress) |
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