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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P13656 | CHIA_ECOLI | MKLNIFTKSMIGMGLVCSALPALAMEAWNNQQGGNKYQVIFDGKIYENAWWVSSTNCPGKAKANDATNPWRLKRTATAAEISQFGNTLSCEKSGSSSSSNSNTPASNTPANGGSATPAQGTVPSNSSVVAWNKQQGGQTWYVVFNGAVYKNAWWVASSNCPGDAKSNDASNPWRYVRAATATEISETSNPQSCTSAPQPSPDVKPAPDVKPAPDVQPAPADKSNDNYAVVAWKGQEGSSTWYVIYNGGIYKNAWWVGAANCPGDAKENDASNPWRYVRAATATEISQYGNPGSCSVKPDNNGGAVTPVDPTPETPVTPTP... | 3.2.1.14; 3.2.1.17 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576]; outer membrane-bounded periplasmic space [GO:0030288] | carbohydrate binding [GO:0030246]; chitin binding [GO:0008061]; endochitinase activity [GO:0008843]; lysozyme activity [GO:0003796] | PF02839; | 2.10.10.20;3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class II subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10760150}. Note=Secreted via the Gsp type II secretion machinery under conditions of derepressed gsp gene expression. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:10760150}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in... | null | null | null | null | FUNCTION: Bifunctional enzyme with lysozyme/chitinase activity. {ECO:0000269|PubMed:10760150}. | Escherichia coli (strain K12) |
P13658 | MBEA_ECOLX | MIVKFHARGKGGGSGPVDYLLGRERNREGATVLQGNPEEVRELIDATPFAKKYTSGVLSFAEKELPPGGREKVMASFERVLMPGLEKNQYSILWVEHQDKGRLELNFVIPNMELQTGKRLQPYYDRADRPRIDAWQTLVNHHYGLHDPNAPENRRTLTLPDNLPETKQALAEGVTRGIDALYHAGEIKGRQDVIQALTEAGLEVVRVTRTSISIADPNGGKNIRLKGAFYEQSFADGRGVREKAERESRIYRENAEQRVQEARRICKRGCDIKRDENQRRYSPVHSLDRGIAGKTPGRGERGDDAAQEGRVKAGREYGHD... | 5.6.2.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12675806}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:12675806}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:12675806}; Note=Divalent metal cation. Can use Mg(2+), Co(2+) or Ni(2+) with similar effic... | null | null | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF03432; | null | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; | null | null | null | null | FUNCTION: Relaxase involved in plasmid ColE1 conjugative mobilization and is thus essential to promote the specific transfer of the plasmid during conjugation. First catalyzes the specific cleavage of one of the DNA strands at oriT, forming a covalent 5'-phosphotyrosine intermediate. The nic site corresponds to 5'-(146... | Escherichia coli |
P13661 | BLO1_ECOLX | MKNTIHINFAIFLIIANIIYSSASASTDISTVASPLFEGTEGCFLLYDASTNAEIAQFNKAKCATQMAPDSTFKIALSLMAFDAEIIDQKTIFKWDKTPKGMEIWNSNHTPKTWMQFSVVWVSQEITQKIGLNKIKNYLKDFDYGNQDFSGDKERNNGLTEAWLESSLKISPEEQIQFLRKIINHNLPVKNSAIENTIENMYLQDLDNSTKLYGKTGAGFTANRTLQNGWFEGFIISKSGHKYVFVSALTGNLGSNLTSSIKAKKNAITILNTLNL | 3.5.2.6 | null | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | null | beta-lactamase activity [GO:0008800]; penicillin binding [GO:0008658] | PF00905; | 3.40.710.10; | Class-D beta-lactamase family | null | null | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10103}; | null | null | null | null | FUNCTION: This is an oxacillin-hydrolyzing beta-lactamase. | Escherichia coli |
P13663 | DHAS_YEAST | MAGKKIAGVLGATGSVGQRFILLLANHPHFELKVLGASSRSAGKKYVDAVNWKQTDLLPESATDIIVSECKSEFFKECDIVFSGLDADYAGAIEKEFMEAGIAIVSNAKNYRREQDVPLIVPVVNPEHLDIVAQKLDTAKAQGKPRPGFIICISNCSTAGLVAPLKPLIEKFGPIDALTTTTLQAISGAGFSPGVPGIDILDNIIPYIGGEEDKMEWETKKILAPLAEDKTHVKLLTPEEIKVSAQCNRVAVSDGHTECISLRFKNRPAPSVEQVKTCLKEYVCDAYKLGCHSAPKQTIHVLEQPDRPQPRLDRNRDSGY... | 1.2.1.11 | null | homoserine biosynthetic process [GO:0009090]; isoleucine biosynthetic process [GO:0009097]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; threonine biosynthetic process [GO:0009088] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | aspartate-semialdehyde dehydrogenase activity [GO:0004073]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein dimerization activity [GO:0046983] | PF01118;PF02774; | 3.40.50.720; | Aspartate-semialdehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; | null | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threon... | null | null | FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000250}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13667 | PDIA4_HUMAN | MRPRKAFLLLLLLGLVQLLAVAGAEGPDEDSSNRENAIEDEEEEEEEDDDEEEDDLEVKEENGVLVLNDANFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIANILKDKDPPIPVAKIDATSASVLASRFDVSGYPTIKILKKGQAVDYEGSRTQEEIVAKVREVSQPDWTPPPEVTLVLTKENFDEVVNDADIILVEFYAPWCGHCKKLAPEYEKAAKELSKRSPPIPLAKVDATAETDLAKRFDVSGYPTLKIFRKGRPYDYNGPREKYGIVDYMIEQSGPPSKEILTLKQVQEFLKDGDDVIIIGVFKGESDPAY... | 5.3.4.1 | null | chaperone-mediated protein folding [GO:0061077]; protein folding [GO:0006457]; protein secretion [GO:0009306]; response to endoplasmic reticulum stress [GO:0034976] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; melanosome [GO:0042470] | protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]; RNA binding [GO:0003723] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12643545}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:17081065}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P08003}; | null | null | null | null | null | Homo sapiens (Human) |
P13668 | STMN1_RAT | MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHVEEVRKNKESKDPADETEAD | null | null | axonogenesis [GO:0007409]; establishment of skin barrier [GO:0061436]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; intracellular signal transduction [GO:0035556]; microtubule depolymerization [GO:0007019]; mitotic cytokinesis [GO:0000281]; mitotic spindle organization [GO:0007052]; negative regula... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]; neuron projection [GO:0043005] | tubulin binding [GO:0015631] | PF00836; | 6.10.280.30; | Stathmin family | PTM: Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF (By similarity). Phosphorylation at Ser-16 is higher in the developing axons from hippocampal neurons and seems... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules (By similarity). Its phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate ... | Rattus norvegicus (Rat) |
P13670 | CHB_VIBHA | MLKHSLIAASVITTLAGCSSLQSSEQQVVNSLADNLDIQYEVLTNHGANEGLACQDMGAEWASCNKVNMTLVNQGEAVDSKDWAIYFHSIRLILDVDNEQFKISRVTGDLHKLEPTDKFDGFAAGEEVVLPLVGEYWQLFETDFMPGAFVSAPNAEPKMIASLNTEDVASFVTGLEGNNLKRTPDDNNVFANAVSRFEKNEDLATQDVSTTLLPTPMHVEAGKGKVDIADGIALPKDAFDATQFAAIQDRAEVVGVDVRGDLPVSITVVPADFTGELAKSGAYEMSIKGDGIVIKAFDQAGAFYAVQSIFGLVDSQNADS... | 3.2.1.52 | null | chitin catabolic process [GO:0006032]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan metabolic process [GO:0030203]; polysaccharide catabolic process [GO:0000272] | cell outer membrane [GO:0009279]; lysosome [GO:0005764] | beta-N-acetylglucosaminidase activity [GO:0016231]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]; polysaccharide binding [GO:0030247] | PF03173;PF03174;PF00728;PF02838; | 2.60.40.290;3.30.379.10;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 20 family | PTM: This protein is probably a lipoprotein, its processing is inhibited by globomycin. | SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; | null | PATHWAY: Glycan degradation; chitin degradation. | null | null | FUNCTION: Hydrolysis of terminal, non-reducing N-acetyl-beta-D-glucosamine residues in chitobiose and higher analogs, and in glycoproteins. | Vibrio harveyi (Beneckea harveyi) |
P13671 | CO6_HUMAN | MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVM... | null | null | complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; in utero embryonic development [GO:0001701]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886] | null | PF21288;PF21195;PF00057;PF01823;PF00084;PF00090; | 3.30.60.30;2.10.70.10;4.10.400.10;2.20.100.10; | Complement C6/C7/C8/C9 family | PTM: All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cysteine residues are supposed to have disulfide linkages only within the same module. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. | Homo sapiens (Human) |
P13674 | P4HA1_HUMAN | MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPK... | 1.14.11.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:9211872}; Note=Binds 1 Fe(2+) ion per subunit.; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000305|PubMed:9211872}; | collagen fibril organization [GO:0030199] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; procollagen-proline 4-dioxygenase complex [GO:0016222] | identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-proline 4-dioxygenase activity [GO:0004656] | PF13640;PF08336; | 6.10.140.1460;2.60.120.620;1.25.40.10; | P4HA family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for 2-oxoglutarate {ECO:0000269|PubMed:9211872}; | null | null | null | FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. {ECO:0000269|PubMed:9211872}. | Homo sapiens (Human) |
P13677 | KPC2_DROME | MAAAAVATPGATVLPPSVPSAAPGAKAPAAGAGKGPGNLLEITGEANIVNYMKNRLRKGAMKRKGLEMVNGHRFGVRFFKNPTYCGHCKDFIWGFGKQGFQCEECRFNIHQKCCKFVVFKCPGKDTDFDADCAKVKHGWISTTYTTPTFCDECGLLLHGVAHQGVKCENCNLNVHHACQETVPPMCGADISEVRGKLLLYVELKGNNLKVDIKEAANLIPMDTNGFSDPYIAVQMHPDRSGRTKKKTKTIQKNLNPVFNETFTFELQPQDRDKRLLIEVWDWDRTSRNDFMGSFSFSLEELQKEPVDGWYKFLSQVEGEH... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041}; | adaptation of rhodopsin mediated signaling [GO:0016062]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; deactivation of rhodopsin mediated signaling [GO:0016059]; detection of light stimulus involved in sensory perception [GO:0050962]; female gonad development [GO:0008585]; intracellular signal t... | cytoplasm [GO:0005737]; inaD signaling complex [GO:0016027]; nucleus [GO:0005634]; rhabdomere [GO:0016028] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. This isozyme is a negative regulator of the visual transduction cascade and has been shown to be required for photoreceptor cell inactivation and light adaptation. Negative regulation is dependent on interaction with s... | Drosophila melanogaster (Fruit fly) |
P13678 | KPC3_DROME | MFTGKLQIKVCEASGLRPTDFQKRHNLTFGKLADEQLIDPYVSIDVDESHFDRATTRPKTFDPVWNEQFVHDVTNVSNINLTVFHDAALPPDDFVANCIISFEDLMQSETAVQDLWVNLEPQGKIHVIIELKNRTDKAKAEAVVEHTVAVNKEFKERAGFNRRRGAMRRRVHQVNGHKFMATFLRQPTFCSHCREFIWGIGKQGYQCQVCTLVVHKKCHLSVVSKCPGMRDEQPAKVEMVPAGQRFNVNLPHRFVVHSYKRFTFCDHCGSLLYGLIKQGLQCETCGMNVHKRCQKNVANTCGINTKQMAEILSSLGISPD... | 2.7.11.13 | null | dorsal/ventral axis specification [GO:0009950]; Golgi organization [GO:0007030]; intracellular signal transduction [GO:0035556]; lipid droplet organization [GO:0034389]; long-term memory [GO:0007616]; negative regulation of cell population proliferation [GO:0008285]; protein phosphorylation [GO:0006468]; response to et... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. | Drosophila melanogaster (Fruit fly) |
P13679 | SC11C_CANLF | MVRAGAVGTHLPASGLDIFGDLRKMNKRQLYYQVLNFAMIVSSALMIWKGLIVLTGSESPIVVVLSGSMEPAFHRGDLLFLTNFREDPIRAGEIVVFKVEGRDIPIVHRVIKVHEKDNGDIKFLTKGDNNEVDDRGLYKEGQNWLEKKDVVGRARGFLPYVGMVTIIMNDYPKFKYALLAVMGAYVLLKRES | 3.4.21.89 | null | signal peptide processing [GO:0006465] | endoplasmic reticulum membrane [GO:0005789]; signal peptidase complex [GO:0005787] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00717; | 2.10.109.10; | Peptidase S26B family | PTM: May undergo processing at the N-terminus. {ECO:0000250|UniProtKB:Q9BY50}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}; Single-pass type II membrane protein {ECO:0000269|PubMed:8444896}. | CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000269|PubMed:14559916, ECO:0000269|PubMed:3511473}; | null | null | null | null | FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:14559916, PubMed:3511473, PubMed:8444896). Specifically cleaves N-terminal signal peptides th... | Canis lupus familiaris (Dog) (Canis familiaris) |
P13681 | PP11_SCHPO | MSNPDVDLDSIIDRLLEVRGSRPGRQVQLSEDEIRFLCNKAREIFISQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLEVICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFTMHGGLSPDLNSMDQIQRIMRPTDVPDTGLLCDLLWSDPDKDLTGWGDNDRGVSFTFGPDVVSRFLHKHDMDLVCRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAEKKQRYGYQGSSQNWHMTPPRK... | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | cell division [GO:0051301]; chromosome segregation [GO:0007059]; co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; deactivation of mitotic spindle assembly checkpoint [GO:1902426]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; ... | cell cortex of growing cell tip [GO:1902716]; cell cortex of non-growing cell tip [GO:0140472]; cell division site [GO:0032153]; cell tip [GO:0051286]; CENP-A containing chromatin [GO:0061638]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; DPS complex [GO:1990567]; euchromatin [GO:0000791]; mRNA... | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; RNA polymerase II CTD heptapeptide repeat T4 phosphatase activity [GO:0180005] | PF00149;PF16891; | 3.60.21.10; | PPP phosphatase family, PP-1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P13682 | ZNF35_HUMAN | MTAELREAMALAPWGPVKVKKEEEEEENFPGQASSQQVHSENIKVWAPVQGLQTGLDGSEEEEKGQNISWDMAVVLKATQEAPAASTLGSYSLPGTLAKSEILETHGTMNFLGAETKNLQLLVPKTEICEEAEKPLIISERIQKADPQGPELGEACEKGNMLKRQRIKREKKDFRQVIVNDCHLPESFKEEENQKCKKSGGKYSLNSGAVKNPKTQLGQKPFTCSVCGKGFSQSANLVVHQRIHTGEKPFECHECGKAFIQSANLVVHQRIHTGQKPYVCSKCGKAFTQSSNLTVHQKIHSLEKTFKCNECEKAFSYSSQ... | null | null | cellular response to retinoic acid [GO:0071300]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283] | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA bindin... | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. Involved in cell differentiation and/or proliferation. | Homo sapiens (Human) |
P13686 | PPA5_HUMAN | MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASGKSLFKTRLP... | 3.1.3.2 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per subunit.; | bone morphogenesis [GO:0060349]; bone resorption [GO:0045453]; defense response to Gram-positive bacterium [GO:0050830]; dephosphorylation [GO:0016311]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of interleukin-12 pro... | cytosol [GO:0005829]; lysosome [GO:0005764]; membrane [GO:0016020] | acid phosphatase activity [GO:0003993]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198] | PF00149; | 3.60.21.10; | Metallophosphoesterase superfamily, Purple acid phosphatase family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; | null | null | null | null | FUNCTION: Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias. | Homo sapiens (Human) |
P13688 | CEAM1_HUMAN | MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTE... | null | null | angiogenesis [GO:0001525]; bile acid and bile salt transport [GO:0015721]; blood vessel development [GO:0001568]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cellular response to insulin stimulus [GO:0032869]; common myeloid progenitor... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; cell junction [GO:0030054]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; extracellular exosome [GO:0070062]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microvillus membrane [GO:00315... | actin binding [GO:0003779]; bile acid transmembrane transporter activity [GO:0015125]; calmodulin binding [GO:0005516]; filamin binding [GO:0031005]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein p... | PF00047;PF13895;PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, CEA family | PTM: [Isoform 1]: Phosphorylated on serine and tyrosine (By similarity). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:15467833, PubMed:18424730, PubMed:7478590). Phosphorylated at Ser-508; mediates activity. Phosphoryla... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:P16573}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junctio... | null | null | null | null | null | FUNCTION: [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its co... | Homo sapiens (Human) |
P13689 | ABP1_MAIZE | MAPDLSELAAAAAARGAYLAGVGVAVLLAASFLPVAESSCVRDNSLVRDISQMPQSSYGIEGLSHITVAGALNHGMKEVEVWLQTISPGQRTPIHRHSCEEVFTVLKGKGTLLMGSSSLKYPGQPQEIPFFQNTTFSIPVNDPHQVWNSDEHEDLQVLVIISRPPAKIFLYDDWSMPHTAAVLKFPFVWDEDCFEAAKDEL | null | null | auxin-activated signaling pathway [GO:0009734]; cytokinesis by cell plate formation [GO:0000911]; positive regulation of cell division [GO:0051781]; positive regulation of cell size [GO:0045793]; positive regulation of DNA endoreduplication [GO:0032877]; unidimensional cell growth [GO:0009826] | endoplasmic reticulum lumen [GO:0005788] | auxin binding [GO:0010011]; zinc ion binding [GO:0008270] | PF02041; | 2.60.120.10; | null | PTM: Glycosylated. {ECO:0000269|PubMed:12065401, ECO:0000269|PubMed:2555179}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:2555179}. | null | null | null | null | null | FUNCTION: Receptor for the plant hormone auxin. {ECO:0000303|PubMed:2555179}. | Zea mays (Maize) |
P13693 | TCTP_HUMAN | MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC | null | null | calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; regulation of apoptotic process [GO:0042981]; response to virus [GO:0009615] | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; multivesicular body [GO:0005771]; nucleus [GO:0005634]; spindle pole [GO:0000922] | calcium ion binding [GO:0005509]; RNA binding [GO:0003723] | PF00838; | null | TCTP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9059837}. | null | null | null | null | null | FUNCTION: Involved in calcium binding and microtubule stabilization (PubMed:12167714, PubMed:15162379, PubMed:15958728). Acts as a negative regulator of TSC22D1-mediated apoptosis, via interaction with and destabilization of TSC22D1 protein (PubMed:18325344). {ECO:0000269|PubMed:12167714, ECO:0000269|PubMed:15162379, E... | Homo sapiens (Human) |
P13697 | MAOX_RAT | MDPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLKIHGLLPPCIVNQEIQVLRVIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSNVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANLNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLIVMAMEKE... | 1.1.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P48163}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P48163}; Note=Divalent metal cations. Prefers magnesium or manganese. {ECO:0000250|UniProtKB:P48163}; | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; protein homotetramerization [GO:0051289]; pyruvate metabolic process [GO:0006090]; regulation of NADP metabolic process [GO:1902031]; response to hormone [GO:0009725] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; malic enzyme activity [GO:0004470]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxaloacetate decarboxylase activity [GO:0008948] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2416344}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; Evidence={ECO:0000269|PubMed:2416344}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254; Evidence={ECO:0... | null | null | null | null | FUNCTION: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate. {ECO:0000269|PubMed:2416344}. | Rattus norvegicus (Rat) |
P13699 | NCAP_LASSJ | MSASKEIKSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEVSNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKSILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMGNLSSQQLDQRRALLNMIGMSGGNQGARAGRDGVVRVWDVKNAELLNNQFGTMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSDLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGACMLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPGERNPYENILYKICLSGDGWPYI... | 3.1.13.- | null | negative stranded viral RNA replication [GO:0039689]; RNA-templated viral transcription [GO:0039696]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity [GO:0039724]; symbiont-mediated suppression of host cytoplasmic pattern recognition rece... | helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | 3'-5' exonuclease activity [GO:0008408]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF17290;PF00843; | 6.10.250.1200;3.30.420.410;1.10.150.550; | Arenaviridae nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04085}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04085}. | null | null | null | null | null | FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in... | Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV) |
P13705 | MSH3_MOUSE | MPRGKSASGGSTAAGPGPGRQTVLSRFFRSAGSLRSSASSTEPAEKVTEGDSRKRSLGNGGPTKKKARKVPEKEEENISVASHHPEAKKCLRPRIVLKSLEKLKEFCCDSALPQNRVQTEALRERLEVLPRCTDFEDITLQRAKNAVLSEDSKSQANQKDSQFGPCPEVFQKTSDCKPFNKRSKSVYTPLELQYLDMKQQHKDAVLCVECGYKYRFFGEDAEIAARELNIYCHLDHNFMTASIPTHRLFVHVRRLVAKGYKVGVVKQTETAALKAIGDNKSSVFSRKLTALYTKSTLIGEDVNPLIRLDDSVNIDEVMTD... | null | null | mismatch repair [GO:0006298]; mitotic recombination [GO:0006312]; somatic recombination of immunoglobulin gene segments [GO:0016447] | MutSbeta complex [GO:0032302]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; centromeric DNA binding [GO:0019237]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; mismatched DNA binding [GO:0030983] | PF01624;PF05188;PF05192;PF00488; | 1.10.1420.10;3.40.1170.10;3.30.420.110;3.40.50.300; | DNA mismatch repair MutS family, MSH3 subfamily | null | null | null | null | null | null | null | FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-d... | Mus musculus (Mouse) |
P13706 | GPDA_DROME | MADKVNVCIVGSGNWGSAIAKIVGANAAALPEFEERVTMFVYEELIDGKKLTEIINETHENVKYLKGHKLPPNVVAVPDLVEAAKNADILIFVVPHQFIPNFCKQLLGKIKPNAIAISLIKGFDKAEGGGIDLISHIITRHLKIPCAVLMGANLANEVAEGNFCETTIGCTDKKYGKVLRDLFQANHFRVVVVDDADAVEVCGALKNIVACGAGFVDGLKLGDNTKAAVIRLGLMEMIRFVDVFYPGSKLSTFFESCGVADLITTCYGGRNRRVSEAFVTSGKTIEELEKEMLNGQKLQGPPTAEEVNYMLKNKGLEDKF... | 1.1.1.8 | null | ethanol metabolic process [GO:0006067]; flight behavior [GO:0007629]; glycerol-3-phosphate biosynthetic process [GO:0046167]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerophospholipid metabolic process [GO:0006650]; glycolytic process [GO:0006096]; NAD... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]; M band [GO:0031430]; nucleus [GO:0005634]; Z disc [GO:0030018] | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF07479;PF01210; | 3.40.50.720; | NAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; | null | PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle. | null | null | null | Drosophila melanogaster (Fruit fly) |
P13707 | GPDA_MOUSE | MAGKKVCIVGSGNWGSAIAKIVGSNAGRLAHFDPRVTMWVFEEDIGGRKLTEIINTQHENVKYLPGHKLPPNVVAIPDVVQAATGADILVFVVPHQFIGKICDQLKGHLKANTIGISLIKGVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVAEEKFCETTIGCKDPAQGQLLKDLMQTPNFRITVVQEVDTVEICGALKNIVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGTVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKEMLNGQKLQGPQTARELHSILQHKGLVDKFP... | 1.1.1.8 | null | cellular response to cAMP [GO:0071320]; cellular response to tumor necrosis factor [GO:0071356]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerolipid metabolic pr... | cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]; mitochondrion [GO:0005739] | glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368]; glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF07479;PF01210; | 3.40.50.720; | NAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}. | CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000250|UniProtKB:P21695}; PhysiologicalDirection=left-to-right; Xref=R... | null | null | null | null | FUNCTION: Has glycerol-3-phosphate dehydrogenase activity. {ECO:0000250|UniProtKB:P21695}. | Mus musculus (Mouse) |
P13709 | FSH_DROME | MSSSEPPPRYEPPVEPVNGIVQPPVIPPAERPGRNTNQLQYLIKTVMKVIWKHHFSWPFQQPVDAKKLNLPDYHKIIKQPMDMGTIKKRLENNYYWSAKETIQDFNTMFNNCYVYNKPGEDVVVMAQTLEKVFLQKIESMPKEELELEPVTAKGGKKKQRAPATPKSSSGGAGASTGSGTSSAAVTSGPGSGSTKVSVAASSAQQSGLQGATGAGGGSSSTPGTQPGSGAGGAIAARPVSAMGGTVSSTAGGAPSIPPISTMPPHTVPGSTNTTTTAMAGGVGGPGAAGANPNAAALMASLLNAGQTGAYPGAPGQTAVN... | null | null | chromatin remodeling [GO:0006338]; dendrite morphogenesis [GO:0048813]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; protein phosphorylation [GO:... | chromatin [GO:0000785]; membrane [GO:0016020]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity [GO:0001216]; lysine-acetylated histone binding [GO:0070577]; P-TEFb complex binding [GO:0106140]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:00009... | PF17035;PF17105;PF00439; | 1.20.1270.220;1.20.920.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required maternally for proper expression of other homeotic genes involved in pattern formation, such as Ubx. {ECO:0000269|PubMed:2567251}. | Drosophila melanogaster (Fruit fly) |
P13712 | MSI1_YEAST | MNQCAKDITHEASSIPIDLQERYSHWKKNTKLLYDYLNTNSTKWPSLTCQFFPDLDTTSDEHRILLSSFTSSQKPEDETIYISKISTLGHIKWSSLNNFDMDEMEFKPENSTRFPSKHLVNDISIFFPNGECNRARYLPQNPDIIAGASSDGAIYIFDRTKHGSTRIRQSKISHPFETKLFGSHGVIQDVEAMDTSSADINEATSLAWNLQQEALLLSSHSNGQVQVWDIKQYSHENPIIDLPLVSINSDGTAVNDVTWMPTHDSLFAACTEGNAVSLLDLRTKKEKLQSNREKHDGGVNSCRFNYKNSLILASADSNGR... | null | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent chromatin assembly [GO:0006335]; regulation of DNA-templated transcription [GO:0006355] | CAF-1 complex [GO:0033186]; cytoplasm [GO:0005737]; nucleosome [GO:0000786]; nucleus [GO:0005634]; Rpd3L complex [GO:0033698]; Rpd3L-Expanded complex [GO:0070210] | histone binding [GO:0042393]; nucleosome binding [GO:0031491] | PF12265;PF08662;PF00400; | 2.130.10.10; | WD repeat RBAP46/RBAP48/MSI1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11238915}. Nucleus {ECO:0000269|PubMed:11238915}. | null | null | null | null | null | FUNCTION: Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor sub... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13716 | HEM2_HUMAN | MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYT... | 4.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11032836}; Note=Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit. {ECO:0000269|PubMed:11032836}; | cellular response to interleukin-4 [GO:0071353]; cellular response to lead ion [GO:0071284]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; negative regulation of proteasomal protein catabolic process ... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleus [GO:0005634]; secretory granule lumen [GO:0034774] | catalytic activity [GO:0003824]; identical protein binding [GO:0042802]; porphobilinogen synthase activity [GO:0004655]; proteasome core complex binding [GO:1904854]; zinc ion binding [GO:0008270] | PF00490; | 3.20.20.70; | ALAD family | null | null | CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000269|PubMed:11032836, ECO:0000269|PubMed:12897770, ECO:0000269|PubMed:19812033}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for 5-aminolevulinate at pH 7 {ECO:0000269|PubMed:11032836}; Vmax=43 umol/h/mg enzyme at pH 7 {ECO:0000269|PubMed:11032836}; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8-7.3. {ECO:0000269|PubMed:11032836}; | null | FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. {ECO:0000269|PubMed:11032836, ECO:0000269|PubMed:19812033}. | Homo sapiens (Human) |
P13717 | NUCA_SERMA | MRFNNKMLALAALLFAAQASADTLESIDNCAVGCPTGGSSNVSIVRHAYTLNNNSTTKFANWVAYHITKDTPASGKTRNWKTDPALNPADTLAPADYTGANAALKVDRGHQAPLASLAGVSDWESLNYLSNITPQKSDLNQGAWARLEDQERKLIDRADISSVYTVTGPLYERDMGKLPGTQKAHTIPSAYWKVIFINNSPAVNHYAAFLFDQNTPKGADFCQFRVTVDEIEKRTGLIIWAGLPDDVQASLKSKPGVLPELMGCKN | 3.1.30.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion.; | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA endonuclease activity [GO:0004521]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF01223; | 3.40.570.10; | DNA/RNA non-specific endonuclease family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.30.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10047}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of both DNA and RNA, double- or single-stranded, at the 3'position of the phosphodiester bond to produce 5'-phosphorylated mono-, di-, tri- and tetranucleotides. DNA is a slightly better substrate than RNA. | Serratia marcescens |
P13721 | SIAT1_RAT | MIHTNLKKKFSLFILVFLLFAVICVWKKGSDYEALTLQAKEFQMPKSQEKVAMGSASQVVFSNSKQDPKEDIPILSYHRVTAKVKPQPSFQVWDKDSTYSKLNPRLLKIWRNYLNMNKYKVSYKGPGPGVKFSVEALRCHLRDHVNVSMIEATDFPFNTTEWEGYLPKENFRTKVGPWQRCAVVSSAGSLKNSQLGREIDNHDAVLRFNGAPTDNFQQDVGSKTTIRLMNSQLVTTEKRFLKDSLYTEGILIVWDPSVYHADIPKWYQKPDYNFFETYKSYRRLNPSQPFYILKPQMPWELWDIIQEISADLIQPNPPSS... | 2.4.3.1 | null | N-acetylneuraminate metabolic process [GO:0006054]; negative regulation of chemotaxis [GO:0050922]; negative regulation of macrophage apoptotic process [GO:2000110]; positive regulation of mononuclear cell proliferation [GO:0032946]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:... | extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138] | beta-galactoside alpha-2,6-sialyltransferase activity [GO:0003835]; protein homodimerization activity [GO:0042803]; sialyltransferase activity [GO:0008373] | PF00777; | 3.90.1480.20; | Glycosyltransferase 29 family | PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000269|PubMed:3121604}.; PTM: N-glycosylated. {ECO:0000269|PubMed:3121604}. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:3121604}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:3121604}. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. {ECO:0000269|PubMed:112786... | CATALYTIC ACTIVITY: Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398; EC=2.4.3.1; Evidence={ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92 uM for donor CMP-Neu5Ac (at pH 6.5 and 37 degrees Celsius); KM=1.8 mM for acceptor beta-Gal1,4-GlcNAc (at pH 6.5 and 37 degrees Celsius); Note=kcat is 35.6 min(-1) for the donor CMP-Neu5Ac (at pH 6.5 and 37 degrees Celsius). kcat is 40.3 min(-1) for the acceptor... | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:3121604}. | null | null | FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates. {ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:24155237, ECO:0000269|PubMed:3121604}. | Rattus norvegicus (Rat) |
P13723 | HEXA1_DICDI | MIKKIILFFAVLIAIVIGQQPLNVVPYPQQVSIGTCVIPVAPGSILIESNIESATFSVSMDRYTNLFFPFSNESEPSSNESFLLSVTIYSDDETLQLGIDESYSLSIEQGSYQLKATNIYGAMRGLETFKQLIVYNELENSYSIVCVSISDSPRYPWRGFMVDSARHYIPKNMILHMIDSLGFSKFNTLHWHMVDAVAFPVESTTYPDLTKGAFSPSATFSHDDIQEVVAYAKTYGIRVIPEFDIPGHAAAWGIGYPELVATCPDYAANVNNIPLDISNPATFTFIQNLFTEIAPLFIDNYFHTGGDELVTGCWLEDPAI... | 3.2.1.52 | null | carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203] | lysosome [GO:0005764]; membrane [GO:0016020] | beta-N-acetylhexosaminidase activity [GO:0004563]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00728;PF14845; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | PTM: The N-terminus is blocked.; PTM: N-glycosylated. {ECO:0000269|PubMed:2972716}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2972716}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; | null | null | null | null | FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. This enzyme plays a role during the slug stage of development in the maintenance of pseudoplasmodia of normal size. {ECO:0000269|PubMed:2972716}. | Dictyostelium discoideum (Social amoeba) |
P13725 | ONCM_HUMAN | MGVLLTQRTLLSLVLALLFPSMASMAAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPGAFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDLEKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQRKLEGCRFLHGYHRFMHSVGRVFSKWGESPNRSRRHSPHQALRKGVRRTRPSRKGKRLMTRGQLPR | null | null | immune response [GO:0006955]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of hormone secretion [GO:0046888]; oncostatin-M-mediated signaling pathway [GO:0038165]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of cell division [GO:0051781]... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; oncostatin-M receptor binding [GO:0005147] | PF01291; | 1.20.1250.10; | LIF/OSM family | PTM: Propeptide processing is not important for receptor binding activity but may be important growth-inhibitory activity. {ECO:0000269|PubMed:2325640}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (... | Homo sapiens (Human) |
P13726 | TF_HUMAN | METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS | null | null | activation of blood coagulation via clotting cascade [GO:0002543]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of plasma proteins involved in acute inflammatory response [GO:0002541]; blood coagulation [GO:0007596]; cytokine-mediated signaling pathway [GO:00... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]; serine-type peptidase complex [GO:1905286] | cytokine receptor activity [GO:0004896]; phospholipid binding [GO:0005543]; protease binding [GO:0002020] | PF09294;PF01108; | 2.60.40.10; | Tissue factor family | null | SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000269|PubMed:12652293}; Single-pass type I membrane protein {ECO:0000269|PubMed:12652293}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:12652293}. | null | null | null | null | null | FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. {ECO:0000269|... | Homo sapiens (Human) |
P13727 | PRG2_HUMAN | MKLPLLLALLFGAVSALHLRSETSTFETPLGAKTLPEDEETPEQEMEETPCRELEEEEEWGSGSEDASKKDGAVESISVPDMVDKNLTCPEEEDTVKVVGIPGCQTCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYRIQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFAYWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY | null | null | defense response to bacterium [GO:0042742]; defense response to nematode [GO:0002215]; immune response [GO:0006955]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of macrophage cytokine production [GO:0010936]; positive regulation of interleukin-4 production [GO:0032753] | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; transport vesicle [GO:0030133] | carbohydrate binding [GO:0030246]; extracellular matrix structural constituent conferring compression resistance [GO:0030021]; heparin binding [GO:0008201] | PF00059; | 3.10.100.10; | null | PTM: Nitrated. {ECO:0000269|PubMed:18694936}. | SUBCELLULAR LOCATION: [Bone marrow proteoglycan]: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=The proform is secreted.; SUBCELLULAR LOCATION: [Eosinophil granule major basic protein]: Cytoplasmic vesicle, secretory vesicle. Note=The proform is secreted. The mat... | null | null | null | null | null | FUNCTION: Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA. {ECO:0000269|PubMed:10913121}. | Homo sapiens (Human) |
P13738 | NHAA_ECOLI | MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNMLLWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPALLYLAFNYADPITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLSMASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLKEKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLQGVTLDGLTSILPLGIIAGLLIGKPLGISLFCWLALRLKLAHLP... | null | null | regulation of intracellular pH [GO:0051453]; response to alkaline pH [GO:0010446]; response to salt stress [GO:0009651] | plasma membrane [GO:0005886] | cardiolipin binding [GO:1901612]; sodium:proton antiporter activity [GO:0015385] | PF06965; | 1.20.1530.10; | NhaA Na(+)/H(+) (TC 2.A.33) antiporter family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:15988517, ECO:0000269|PubMed:1645730, ECO:0000269|PubMed:19396973, ECO:0000269|PubMed:25422503}; Multi-pass membrane protein {ECO:0000269|PubMed:15988517, ECO:0000269|PubMed:19396973, ECO:0000269|PubMed:25422503}. | CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:23836890, ECO:0000269|PubMed:8383669}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29252; Evidence={ECO:0000269|PubMed:23836890, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.98 mM for Na(+) {ECO:0000269|PubMed:8019504}; KM=0.2 mM for Na(+) {ECO:0000269|PubMed:22915592}; KM=0.91 mM for Li(+) {ECO:0000269|PubMed:8019504}; KM=0.02 mM for Li(+) {ECO:0000269|PubMed:22915592}; | null | null | null | FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons (PubMed:1645730, PubMed:23836890, PubMed:2839489, PubMed:7737413, PubMed:8019504, PubMed:8383669). Plays an important role in the regulation of intracellular pH, cellular Na(+) content and cell volume (PubMed:33129932). Catalyzes the ... | Escherichia coli (strain K12) |
P13745 | GSTA1_MOUSE | MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLEVLLYVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPPMDAKQIQEARKAFKIQ | 1.11.1.-; 2.5.1.18; 5.3.3.- | null | glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; prostaglandin metabolic process [GO:0006693]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | dinitrosyl-iron complex binding [GO:0035731]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; peroxidase activity [GO:0004601]; protein homodimerization activity [GO:0042803]; steroid delta-isomerase activity [GO:0004769] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | null | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:9606968, ECO:0000305|PubMed:11027134}; PhysiologicalDirecti... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 uM for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; Vmax=5200 nmol/min/mg enzyme for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; | null | null | null | FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (PubMed:9606968). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2)... | Mus musculus (Mouse) |
P13747 | HLAE_HUMAN | MVDGTLLLLLSEALALTQTWAGSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPIVGIIAGLVLLGSVVS... | null | null | adaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen pro... | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; lumenal side of endoplasmic reticulum membrane [GO:00985... | beta-2-microglobulin binding [GO:0030881]; MHC class I protein binding [GO:0042288]; natural killer cell lectin-like receptor binding [GO:0046703]; peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]; T cell receptor binding [GO:0042608] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | PTM: N-glycosylated. {ECO:0000269|PubMed:17179229}.; PTM: The soluble form (sHLA-E) can be partly produced by proteolytic cleavage at the cell surface (shedding) by a matrix metalloproteinase. Alternative splicing is also suggested as a mechanism for generation of sHLA-E, although it remains to be proved. {ECO:0000269|... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17179229, ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:9427624}; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000269|PubMed:17179229}.; SUBCELLULAR LOCATION: [Soluble HLA class I histocompatibility antigen, alpha chain E]: Secreted {ECO:0... | null | null | null | null | null | FUNCTION: Non-classical major histocompatibility class Ib molecule involved in immune self-nonself discrimination. In complex with B2M/beta-2-microglobulin binds nonamer self-peptides derived from the signal sequence of classical MHC class Ia molecules (VL9 peptides - VMAPRT[V/L][L/V/I/F]L) (PubMed:18083576, PubMed:183... | Homo sapiens (Human) |
P13748 | 1A03_PANTR | MAVMPPRTLLLLLSGALALTQTWAGSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNMKASAQTDRVDLGTLRGYYNQSEDGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAAAMAAQITKRKWEAAHAAEQLRAYLEGRCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAVITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLLGA... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P13749 | 1A04_PANTR | MAVMAPRTLVLLLSGALALTQTWAGSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDEETRSVKASAQTDRVDLGTLRGYYNQSEDGSHTIQLMFGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITQRKWEAAHAAEQLRAYLEGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDREATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLLGA... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P13750 | 1B01_PANTR | APRTVLLLLSAALALTETWAGSHSMRYFYTSVSRPGRGEPRFITVGYVDDTQFVRFDSDAASPRMEPRAPWIEQEGPEYWDRETRNMKASAQTDRENLRIALRYYNQSEAGSHTWQTMYGCDMGPDGRLLRGYGQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQRRAYLEGTCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPEGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTIPIVGIVAGLAVLVVTVAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P13751 | 1B02_PANTR | MQVTAPRTVLLLLSAALALTETWAGSHSMKYFYTAVSRPGRGEPRFISVGYVDDTQFVWFDSDAASPREEPRAPWIEQEGPEYWDRETQISKTNAQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDMGPDGRLLRGYEQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARWAEQLRAYLEGTCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTIPIVGIVAGLAVLAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P13752 | HA1A_BOVIN | MGPRALLLLLSGVLILTETRAGSHSLRYFSTAVSRPGLGEPRYLEVGYVDDTQFVQFDSDAPNPRMEPRARWVEQEGPEYWDRNTRNAKGNAQSFRVNLNTLRGYYNQSEAGSHTLQWMSGCDVGPDGALRRGFMQYGYDGRDYLALNEDLRSWTAGETEAQITKRKWEAAGYAEVQRNYLEGECVEWLRRYLENGKDTLLRADPPKAHVTHHPISGREVTLRCWALGFYPEEISLTWQHDGEDQTQDMELVETRPSGDGTFQKWAALVVPSGDEQRYTCRVQHEGLQEPLTLRWEPPQPSFLTMGIIVGLVLLVVTGAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Bos taurus (Bovine) |
P13753 | HA1B_BOVIN | MRVMRVMRPRTLLLLLSGVLVLTETLAGSHSLRYFYTGVSRPGLGEPRFIAVGYVDDTQFVRFDSDAPNPREEPRVPWMEQEGPEYWDRNTRIYKDTAQIFRVDLNTLRGYYNQSETGSHNIQAMYGCDVGPDGRLLRGFWQFGYDGRDYIALNEELRSWTAADTAAQITKRKWEAAGAAETWRNYLEGECVEWLRRYLENGKDTLLRADPPKAHVTHHSISDREVTLRCWALGFYPEEISLTWQREGEDQTQDMELVETRPSGDGTFQKWAALVVPSGEEQRYTCRVQHEGLQEPLTLRWEPPQTSFLIMGIIVGLVLL... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Bos taurus (Bovine) |
P13762 | DRB4_HUMAN | MVCLKLPGGSCMAALTVTLTVLSSPLALAGDTQPRFLEQAKCECHFLNGTERVWNLIRYIYNQEEYARYNSDLGEYQAVTELGRPDAEYWNSQKDLLERRRAEVDTYCRYNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSMMSPLTVQWSARSESAQSKMLSGVGGFVLGLLFLGTGLFIYFRNQKGHSGLQPTGLLS | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870] | clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; MHC class... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II. When associated with ubiquitination of the alpha subunit of HLA-DR: HLA-DRA 'Lys-244', the down-regulation of MHC class II may be highly effective. {ECO:0000269|PubMed:18305173, ECO:000026... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I... | null | null | null | null | null | FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mos... | Homo sapiens (Human) |
P13765 | DOB_HUMAN | MGSGWVPWVVALLVNLTRLDSSMTQGTDSPEDFVIQAKADCYFTNGTEKVQFVVRFIFNLEEYVRFDSDVGMFVALTKLGQPDAEQWNSRLDLLERSRQAVDGVCRHNYRLGAPFTVGRKVQPEVTVYPERTPLLHQHNLLHCSVTGFYPGDIKIKWFLNGQEERAGVMSTGPIRNGDWTFQTVVMLEMTPELGHVYTCLVDHSSLLSPVSVEWRAQSEYSWRKMLSGIAAFLLGLIFLLVGIVIQLRAQKGYVRTQMSGNEVSRAVLLPQSC | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; negative regulation of antigen processing and presentation of peptide antigen via MHC class II [GO:0002587]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; pos... | late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613] | MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization is necessary to exit the ER. | null | null | null | null | null | FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM. | Homo sapiens (Human) |
P13773 | CAR1_DICDI | MGLLDGNPANETSLVLLLFADFSSMLGCMAVLIGFWRLKLLRNHVTKVIACFCATSFCKDFPSTILTLTNTAVNGGFPCYLYAIVITYGSFACWLWTLCLAISIYMLIVKREPEPERFEKYYYLLCWGLPLISTIVMLAKNTVQFVGNWCWIGVSFTGYRFGLFYGPFLFIWAISAVLVGLTSRYTYVVIHNGVSDNKEKHLTYQFKLINYIIVFLVCWVFAVVNRIVNGLNMFPPALNILHTYLSVSHGFWASVTFIYNNPLMWRYFGAKILTVFTFFGYFTDVQKKLEKNKNNNNPSPYSSSRGTSGKTMGGHPTGDD... | null | null | adaptation of signaling pathway [GO:0023058]; adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway [GO:0140582]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; aggregation involved in sorocarp development [GO:0031152]; cGMP-mediated signaling [GO:001993... | cell leading edge [GO:0031252]; cell surface [GO:0009986]; cytosol [GO:0005829]; early endosome [GO:0005769]; plasma membrane [GO:0005886] | adenylate cyclase regulator activity [GO:0010854]; cAMP binding [GO:0030552]; cAMP receptor activity [GO:0001646]; G protein-coupled chemoattractant receptor activity [GO:0001637]; G protein-coupled receptor activity [GO:0004930]; GTPase regulator activity [GO:0030695]; pathogen-derived receptor ligand activity [GO:014... | PF05462; | 1.20.1070.10; | G-protein coupled receptor 5 family | PTM: C-terminal Ser or Thr residues may be phosphorylated. {ECO:0000269|PubMed:7721769, ECO:0000269|PubMed:8120068, ECO:0000269|PubMed:9880518}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7876207, ECO:0000269|PubMed:9334341}; Multi-pass membrane protein {ECO:0000269|PubMed:7876207, ECO:0000269|PubMed:9334341}. | null | null | null | null | null | FUNCTION: Receptor for cAMP. Coordinates the aggregation of individual cells into a multicellular organism and regulates the expression of a large number of developmentally regulated genes. The activity of this receptor is mediated by G proteins. {ECO:0000269|PubMed:11319871, ECO:0000269|PubMed:11559759, ECO:0000269|Pu... | Dictyostelium discoideum (Social amoeba) |
P13796 | PLSL_HUMAN | MARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGRISFDEFIKIFHGLKSTDVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTNDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCNKIGNFSTDIKDSKAYYHLLEQVAPKGDEEGVPAVVI... | null | null | actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; actin filament network formation [GO:0051639]; animal organ regeneration [GO:0031100]; cell migration [GO:0016477]; cortical actin cytoskeleton organization [GO:0030866]; extracellular matrix disassembly [GO:0022617]; positive regulati... | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; actin filament bundle [GO:0032432]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; glial cell projection [G... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; GTPase binding [GO:0051020]; integrin binding [GO:0005178] | PF00307;PF13499; | 1.10.418.10;1.10.238.10; | null | PTM: Phosphorylated on a serine residue in response to costimulation through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes association with the actin cytoskeleton and targeting to peripheral cell projections. {ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16636079}. Cell junction {ECO:0000269|PubMed:17294403}. Cell projection {ECO:0000269|PubMed:16636079}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q61233, ECO:0000269|PubMed:16636079}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q61233... | null | null | null | null | null | FUNCTION: Actin-binding protein (PubMed:16636079, PubMed:17294403, PubMed:28493397). Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). Modulates the cell surface expression of IL2RA/CD25 and CD69 (PubMed:17294403). {ECO:0000269|PubMed:16636079, ECO... | Homo sapiens (Human) |
P13797 | PLST_HUMAN | MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPR... | null | null | actin filament bundle assembly [GO:0051017]; actin filament network formation [GO:0051639]; bone development [GO:0060348] | actin filament [GO:0005884]; actin filament bundle [GO:0032432]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509] | PF00307;PF13499; | 1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Actin-bundling protein. | Homo sapiens (Human) |
P13798 | ACPH_HUMAN | MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYP... | 3.4.19.1 | null | amyloid-beta metabolic process [GO:0050435]; proteolysis [GO:0006508]; translational termination [GO:0006415] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nuclear membrane [GO:0031965] | identical protein binding [GO:0042802]; omega peptidase activity [GO:0008242]; RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252] | PF19283;PF00326; | 3.40.50.1820;2.120.10.30; | Peptidase S9C family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10719179}. | CATALYTIC ACTIVITY: Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.; EC=3.4.19.1; Evidence={ECO:0000269|PubMed:10719179, ECO:0000269|PubMed:1740429, ECO:0000269|PubMed:2006156}; | null | null | null | null | FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus (PubMed:10719179, PubMed:1740429, PubMed:2006156). It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Also, involved ... | Homo sapiens (Human) |
P13799 | DEGS_BACSU | MNKTKMDSKVLDSILMKMLKTVDGSKDEVFQIGEQSRQQYEQLVEELKQIKQQVYEVIELGDKLEVQTRHARNRLSEVSRNFHRFSEEEIRNAYEKAHKLQVELTMIQQREKQLRERRDDLERRLLGLQEIIERSESLVSQITVVLNYLNQDLREVGLLLADAQAKQDFGLRIIEAQEEERKRVSREIHDGPAQMLANVMMRSELIERIFRDRGAEDGFQEIKNLRQNVRNALYEVRRIIYDLRPMALDDLGLIPTLRKYLYTTEEYNGKVKIHFQCIGETEDQRLAPQFEVALFRLAQEAVSNALKHSESEEITVKVEI... | 2.7.13.3; 3.1.3.- | null | null | cytoplasm [GO:0005737]; membrane [GO:0016020] | ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein dimerization activity [GO:0046983] | PF05384;PF02518;PF07730; | 1.20.5.1930;3.30.565.10; | null | PTM: Autophosphorylated. Phosphorylated in vitro at Ser-76 by the serine/threonine-protein kinase YbdM, which stimulates the phosphate transfer to DegU. {ECO:0000269|PubMed:17218307, ECO:0000269|PubMed:21304896}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation and biofilm ... | Bacillus subtilis (strain 168) |
P13800 | DEGU_BACSU | MTKVNIVIIDDHQLFREGVKRILDFEPTFEVVAEGDDGDEAARIVEHYHPDVVIMDINMPNVNGVEATKQLVELYPESKVIILSIHDDENYVTHALKTGARGYLLKEMDADTLIEAVKVVAEGGSYLHPKVTHNLVNEFRRLATSGVSAHPQHEVYPEIRRPLHILTRRECEVLQMLADGKSNRGIGESLFISEKTVKNHVSNILQKMNVNDRTQAVVVAIKNGWVEMR | null | null | phosphorelay signal transduction system [GO:0000160]; positive regulation of DNA-templated transcription [GO:0045893] | cytoplasm [GO:0005737] | DNA binding [GO:0003677] | PF00196;PF00072; | 3.40.50.2300; | null | PTM: Phosphorylated and dephosphorylated by DegS. {ECO:0000269|PubMed:1901568, ECO:0000269|PubMed:2123196}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation, biofilm for... | Bacillus subtilis (strain 168) |
P13801 | SP2G_BACSU | MKIYLDVIWLLNFCFDALLLLLTAFILKRHVKKRRLVGGAFIGSSIVLLMFTPFSPIVEHPAGKLAFSVVIVVVTFGFKRFRFFFQNLFSFYFATFLMGGGIIGAHSLLQSNSIVQNGVMITNQTGFGDPISWLFIVGGFPALWFFSKRRIEDIETKNIQYEERVSVQADLGSQTLHVRGLIDSGNQLYDPLTKTPVMIIYIDKLEPIFGTAETMIIRNTDPLEAIEQLDDSFRFLDKMRLIPYRGVGQQNQFLLCVKPDHVTIMTKEEMISADKCLIGISTTKLSADGEFDAIIHPKMLSGKAVKHVS | 3.4.23.- | null | asexual sporulation [GO:0030436]; proteolysis [GO:0006508]; sporulation resulting in formation of a cellular spore [GO:0030435] | plasma membrane [GO:0005886] | aspartic-type endopeptidase activity [GO:0004190]; peptidase activity [GO:0008233]; protein self-association [GO:0043621] | PF03419; | null | Peptidase U4 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1744037, ECO:0000269|PubMed:18378688, ECO:0000269|PubMed:9663680}; Multi-pass membrane protein {ECO:0000269|PubMed:1744037, ECO:0000269|PubMed:18378688, ECO:0000269|PubMed:9663680}. Note=Localized to the sporulation septum. | null | null | null | null | null | FUNCTION: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR. {ECO:0000269|... | Bacillus subtilis (strain 168) |
P13804 | ETFA_HUMAN | MFRAAAPGQLRRAASLLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLF... | null | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0000269|PubMed:9334218}; Note=Binds 1 FAD per dimer. {ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055}; | amino acid catabolic process [GO:0009063]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; respiratory electron transport chain [GO:0022904] | electron transfer flavoprotein complex [GO:0045251]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491] | PF01012;PF00766; | 3.40.50.620;3.40.50.1220; | ETF alpha-subunit/FixB family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. | null | null | null | null | null | FUNCTION: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:10356313, PubMed:15159392, PubMed:15975918, PubMed:27499296, PubMed:9334218). It transfers the electrons to the mai... | Homo sapiens (Human) |
P13805 | TNNT1_HUMAN | MSDTEEQEYEEEQPEEEAAEEEEEAPEEPEPVAEPEEERPKPSRPVVPPLIPPKIPEGERVDFDDIHRKRMEKDLLELQTLIDVHFEQRKKEEEELVALKERIERRRSERAEQQRFRTEKERERQAKLAEEKMRKEEEEAKKRAEDDAKKKKVLSNMGAHFGGYLVKAEQKRGKRQTGREMKVRILSERKKPLDIDYMGEEQLRARSAWLPPSQPSCPAREKAQELSDWIHQLESEKFDLMAKLKQQKYEINVLYNRISHAQKFRKGAGKGRVGGRWK | null | null | negative regulation of muscle contraction [GO:0045932]; sarcomere organization [GO:0045214]; skeletal muscle contraction [GO:0003009]; slow-twitch skeletal muscle fiber contraction [GO:0031444]; transition between fast and slow fiber [GO:0014883] | cytosol [GO:0005829]; troponin complex [GO:0005861] | tropomyosin binding [GO:0005523]; troponin T binding [GO:0031014] | PF00992; | 1.20.5.350; | Troponin T family | null | null | null | null | null | null | null | FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. | Homo sapiens (Human) |
P13806 | CA2D1_RABIT | MAAGRPLAWTLTLWQAWLILIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVHQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIDDANFRRQVSYQHAAVHIPTDIYEGSTIVLNELNWTSALDDVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVL... | null | null | calcium ion import across plasma membrane [GO:0098703] | L-type voltage-gated calcium channel complex [GO:1990454]; T-tubule [GO:0030315] | calcium channel regulator activity [GO:0005246]; metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245] | PF08473;PF00092;PF08399; | 3.30.450.20;3.40.50.410; | Calcium channel subunit alpha-2/delta family | PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked. {ECO:0000269|PubMed:2168391}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P54289}. | null | null | null | null | null | FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel (By similarity). Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250|UniProtKB:P54289}. | Oryctolagus cuniculus (Rabbit) |
P13807 | GYS1_HUMAN | MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNL... | 2.4.1.11 | null | glycogen biosynthetic process [GO:0005978]; heart development [GO:0007507] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; inclusion body [GO:0016234]; membrane [GO:0016020] | glucose binding [GO:0005536]; glycogen (starch) synthase activity [GO:0004373]; glycogen synthase activity, transferring glucose-1-phosphate [GO:0061547] | PF05693; | 3.40.50.2000; | Glycosyltransferase 3 family | PTM: Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641... | null | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11; Evidence={ECO:0000269|PubMed:35835870}; ... | null | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:35835870}. | null | null | FUNCTION: Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to ... | Homo sapiens (Human) |
P13808 | B3A2_MOUSE | MSSAPRRPASGADSLHTPEPESLSPGTPGFPEQEEDELRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEEEASEAEGFRAPPQQPSPATTPSAVQFFLQEDEGAERKPERTSPSPPTQTPHQEAAPRASKGAQTGTLVEEMVAVASATAGGDDGGAAGRPLTKAQPGHRSYNLQERRRIGSMTGVEQALLPRVPTDESEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQAAREGREPGPTPRARPRAPHKPHEVF... | null | null | amelogenesis [GO:0097186]; bicarbonate transport [GO:0015701]; chloride transport [GO:0006821]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000565]; osteoclast differentiation [GO:0030316]; positive regula... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886] | chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; transmembrane transporter activity [GO:0022857] | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P04920}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:12958022, ECO:0000269|PubMed:18971331, ECO:0000269|PubMed:23341620, ECO:0000269|PubMed:2371270}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12958022, ECO:0000269|PubMed:23341620, ECO:0000269|PubMed:2371270, ECO:0000269|PubMed:24515893}; | null | null | null | null | FUNCTION: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:12958022, PubMed:18971331, PubMed:23341620, PubMed:2371270, PubMed:24515893). Plays an important role in osteoclast differentiation and function (PubMed:18971331, Pub... | Mus musculus (Mouse) |
P13833 | MLR_DICDI | MASTKRRLNREESSVVLGEEQVAELKEAFELFDKDRTGFIKKDALKTTCKQFGVFVMEDQLDAMFAEADTTKSGAIGFPEFMSMMSRRMKQTSNEQILMNAFKTFDPEGNGYILTKDLSKALTTLGDKLTEAELQELLSISENEQKQVKYDLFVNTLFSKK | null | null | actomyosin structure organization [GO:0031032]; locomotion [GO:0040011]; mitotic cytokinesis [GO:0000281]; myosin filament assembly [GO:0031034]; myosin II filament organization [GO:0031038]; post-embryonic development [GO:0009791]; response to differentiation-inducing factor 1 [GO:1903013]; sorocarp development [GO:00... | actomyosin [GO:0042641]; cytoplasm [GO:0005737]; myosin II complex [GO:0016460] | calcium ion binding [GO:0005509]; cytoskeletal motor activator activity [GO:0140660]; myosin heavy chain binding [GO:0032036] | PF13499; | 1.10.238.10; | null | null | null | null | null | null | null | null | null | Dictyostelium discoideum (Social amoeba) |
P13834 | GYS1_RABIT | MPLSRTLSVSSLPGLEDWEDEFDLENSVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEPPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQNEEKPHVVAHFHEWLAGIGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNL... | 2.4.1.11 | null | glycogen biosynthetic process [GO:0005978] | skeletal muscle myofibril [GO:0098723] | glycogen (starch) synthase activity [GO:0004373]; protein kinase binding [GO:0019901] | PF05693; | 3.40.50.2000; | Glycosyltransferase 3 family | PTM: Phosphorylation at Ser-8 is required for modification of Ser-11 by casein kinase I. {ECO:0000269|PubMed:2842154, ECO:0000269|PubMed:6772446}.; PTM: Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates... | null | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11; Evidence={ECO:0000269|PubMed:14593110, E... | null | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:14593110, ECO:0000269|PubMed:16275910}. | null | null | FUNCTION: Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to ... | Oryctolagus cuniculus (Rabbit) |
P13838 | LEUK_RAT | WAQVVSQENLPNTMTMLPFTPNSESPSTSEALSTYSSIATVPVTEDPKESISPWGQTTAPASSIPLGTPELSSFFFTSAGASGNTPVPELTTSQEVSTEASLVLFPKSSGVASDPPVTITNPATSSAVASTSLETFKGTSAPPVTVTSSTMTSGPFVATTVSSETSGPPVTMATGSLGPSKETHGLSATIATSSGESSSVAGGTPVFSTKISTTSTPNPITTVPPRPGSSGMLLVSMLIALTVVLVLVALLLLWRQRQKRRTGALTLSRGGKRNGTVDAWAGPARVPDEEATTASGSGGNKSSGAPETDGSGQRPTLTTF... | null | null | apoptotic signaling pathway [GO:0097190]; cell surface receptor signaling pathway [GO:0007166]; chronic inflammatory response [GO:0002544]; defense response to bacterium [GO:0042742]; leukocyte tethering or rolling [GO:0050901]; monocyte activation [GO:0042117]; negative regulation of cell adhesion [GO:0007162]; negati... | basement membrane [GO:0005604]; cell surface [GO:0009986]; cleavage furrow [GO:0032154]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; PML body [GO:0016605]; uropod [GO:0001931] | heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; protein domain specific binding [GO:0019904]; transmembrane signaling receptor activity [GO:0004888] | null | null | null | PTM: Has a high content of sialic acid and O-linked carbohydrate structures.; PTM: Phosphorylation at Ser-330 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to lymph nodes. {ECO:0000250|UniProtKB:P15702}... | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Cell projection, uropodium {ECO:0000250|UniProtKB:P15702}. Note=Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN). ... | null | null | null | null | null | FUNCTION: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively reg... | Rattus norvegicus (Rat) |
P13843 | FUS_HRSV1 | MELLIHRSSAIFLTLAVNALYLTSSQNITEEFYQSTCSAVSRGYFSALRTGWYTSVITIELSNIKETKCNGTDTKVKLIKQELDKYKNAVTELQLLMQNTPAANNRARREAPQYMNYTINTTKNLNVSISKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYINNRLLPIVNQQSCRISNIETVIEFQQMNSRLLEITREFSVNAGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYVVQLPIYGVIDTPCWKLHTSP... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of syncytium formation by virus [GO:0060141]; symbiont entry into host cell [GO:0046718] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00523; | 1.10.287.2480;6.10.250.1160;6.20.370.50; | Paramyxoviruses fusion glycoprotein family | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavag... | SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 c... | Human respiratory syncytial virus B (strain 18537) |
P13847 | HBSAG_HHBV | MGHTQAKSTTDRRVEGGELLLQHLAGRMIPPEFSGPITTAGKFPTIQHVMDHIDSVEELRTLQAGGHWPEGTARRLGLDQPRPTPPPITWTEEEDKKAKEFFKQYQENRPKPAETAPPPITELHAAEPPQWKISPEDPLLKAKALIPVKEPEVPILKVPKLTNKKKMGATFGGILAGLIGLLVGFFLLTKILEILRKLDWWWISLSSPKEKMLCAFQNTGAQTSPHYVGSCPWGCPGFLWTYLRLFIIFLLLLLVAAGLLFLTENKSTIFEKLQWESVSALSSSIYSLLPSEPKSLVALTFGLFLIWTTSSSVTQVLVTL... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Avihepadnavirus major surface antigen family | PTM: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles.; PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg). | SUBCELLULAR LOCATION: Virion membrane. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Heron hepatitis B virus (HHBV) |
P13852 | PRIO_RAT | MANLGYWLLALFVTTCTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQSGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWSQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMLHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLIVG | null | null | calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; cellular response to xenobiotic stimulus [GO:0071466]; learning or memory [GO:0007611]; negative regulation of activated T cell proliferation [GO:0046... | cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]... | amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; ATP-dependent protein binding [GO:0043008]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; ... | PF00377;PF11587; | 1.10.790.10; | Prion family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- an... | null | null | null | null | null | FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble ... | Rattus norvegicus (Rat) |
P13856 | RSR1_YEAST | MRDYKLVVLGAGGVGKSCLTVQFVQGVYLDTYDPTIEDSYRKTIEIDNKVFDLEILDTAGIAQFTAMRELYIKSGMGFLLVYSVTDRQSLEELMELREQVLRIKDSDRVPMVLIGNKADLINERVISVEEGIEVSSKWGRVPFYETSALLRSNVDEVFVDLVRQIIRNEMESVAVKDARNQSQQFSKIESPSTRLPSSAKQDTKQSNNKQSSKGLYNKSSQGQAKVKQSTPVNEKHKPSHAVPKSGSSNRTGISATSQQKKKKKNASTCTIL | 3.6.5.2 | null | axial cellular bud site selection [GO:0007120]; bipolar cellular bud site selection [GO:0007121]; cellular response to cAMP [GO:0071320]; cytogamy [GO:0000755]; establishment of protein localization [GO:0045184]; maintenance of protein location in cell [GO:0032507]; negative regulation of synaptic vesicle exocytosis [G... | cell division site [GO:0032153]; cell periphery [GO:0071944]; cellular bud neck [GO:0005935]; endoplasmic reticulum [GO:0005783]; incipient cellular bud site [GO:0000131]; plasma membrane [GO:0005886]; site of polarized growth [GO:0030427]; vacuolar membrane [GO:0005774] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:1910037}; | null | null | null | null | FUNCTION: Ras-related protein which binds GDP/GTP and possesses intrinsic GTPase activity (PubMed:1910037). Involved in development of cell polarity during the cell division cycle, and essential for bud emergence (PubMed:2690082). {ECO:0000269|PubMed:1910037, ECO:0000269|PubMed:2690082}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13861 | KAP2_HUMAN | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSRTKSNKDG... | null | null | intracellular signal transduction [GO:0035556]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480] | cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleotide-activated protein kinase complex [GO:0031588]; plasma membrane [GO:0005... | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by the activated catalytic chain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. | Homo sapiens (Human) |
P13863 | CDK1_CHICK | MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELHHPNIVCLQDVLMQDARLYLIFEFLSMDLKKYLDTIPSGQYLDRSRVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGVIKLADFGLARAFGIPVRVYTHEVVTLWYRSPEVLLGSALYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNDVWPDVESLQDYKNTFPKWKPGSLGTHVQNLDEDGLDLLSKMLIYDPAKRISGKMALNHPYFDDLDKSTLPANLIKKF | 2.7.11.22; 2.7.11.23 | null | cell division [GO:0051301]; cellular response to heat [GO:0034605]; double-strand break repair via homologous recombination [GO:0000724]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; phosphorylation [GO:0016310]; regulation of circadian rhythm [GO:0042752] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts negative regulator of entry into mitosis (G2 to M transition). {ECO:0000250|UniProtKB:P06493}.; PTM: (Microbial infection) Phosphorylated at Tyr-15 by Rous sarcoma virus v-oncogene Src, possibly causing mitotic slippage. {ECO:... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06493}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06493}. | 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; Evidence={ECO:0000269|PubMed:2188731}; CATALYTIC... | null | null | null | null | FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition via association with multiple interphase cyclins (PubMed:2188731). During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complex... | Gallus gallus (Chicken) |
P13864 | DNMT1_MOUSE | MPARTAPARVPALASPAGSLPDHVRRRLKDLERDGLTEKECVREKLNLLHEFLQTEIKSQLCDLETKLHKEELSEEGYLAKVKSLLNKDLSLENGTHTLTQKANGCPANGSRPTWRAEMADSNRSPRSRPKPRGPRRSKSDSDTLSVETSPSSVATRRTTRQTTITAHFTKGPTKRKPKEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSLRRHTRELSLRRKSKEDPDREARPETHLDEDEDGKKDKRSSRPRSQPRDPAAKRRPKEAEPEQVAPETPEDRDEDEREEK... | 2.1.1.37 | null | cellular response to amino acid stimulus [GO:0071230]; cellular response to bisphenol A [GO:1903926]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chromosomal DNA methylation maintenance following DNA replication [GO:0141119]; DNA methylation-dependent heterochromatin formation [GO:000634... | cytoplasm [GO:0005737]; female germ cell nucleus [GO:0001674]; germ cell nucleus [GO:0043073]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; protein-containing complex [GO:0032991]; replication fork [GO:0005657] | chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates [GO:0051718]; DNA binding [GO:0003677]; DNA-methyltransferase activity [GO:0009008]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; ln... | PF01426;PF06464;PF00145;PF12047;PF02008; | 1.10.10.2230;2.30.30.490;3.90.120.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | PTM: Sumoylated; sumoylation increases activity. {ECO:0000250|UniProtKB:P26358}.; PTM: Phosphorylation at Ser-146 by CK1 reduces DNA-binding activity. {ECO:0000269|PubMed:17965600, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:9211941}.; PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290321}. Cytoplasm {ECO:0000269|PubMed:11290321}. Note=It is nucleoplasmic through most of the cell cycle and associates with replication foci during S-phase. In germ cells, spermatogonia, preleptotene and leptotene spermatocytes all express high levels of nuclear pro... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.... | null | null | null | null | FUNCTION: Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylatio... | Mus musculus (Mouse) |
P13866 | SC5A1_HUMAN | MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYL... | null | null | alpha-glucoside transport [GO:0000017]; fucose transmembrane transport [GO:0015756]; galactose transmembrane transport [GO:0015757]; glucose import across plasma membrane [GO:0098708]; glucose transmembrane transport [GO:1904659]; intestinal D-glucose absorption [GO:0001951]; intestinal hexose absorption [GO:0106001]; ... | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; intracellular organelle [GO:0043229]; intracellular vesicle [GO:0097708]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | alpha-glucoside transmembrane transporter activity [GO:0015151]; D-glucose transmembrane transporter activity [GO:0055056]; fucose transmembrane transporter activity [GO:0015150]; galactose transmembrane transporter activity [GO:0005354]; galactose:sodium symporter activity [GO:0015371]; glucose transmembrane transport... | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | PTM: N-glycosylation is not necessary for the cotransporter function. {ECO:0000269|PubMed:8567640}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:26945065}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) + 2 Na(+)(out) = D-glucose(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70495, ChEBI:CHEBI:4167, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:35077764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70496; Evidence={ECO:0000305|PubMed:20980548, ECO:0000305|PubMed:34880492, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.74 mM for D-glucose {ECO:0000269|PubMed:35077764}; KM=3.12 mM for D-galactose {ECO:0000269|PubMed:35077764}; | null | null | null | FUNCTION: Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:34880492, PubMe... | Homo sapiens (Human) |
P13886 | POLN_ONNVG | MDSVYVDIDADSAFLKALQQAYPMFEVEPKQVTPNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVTDKNISGKINDLQAVMAVPNMETSTFCLHTDATCKQRGDVAIYQDVYAVHAPTSLYHQAIKGVRVAYWIGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLSEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRKLLQSWHLPSVFHLKGKLSFTCRCDTIVSCEGYVVKRVTMSPGIYGKTSGYAVTHHAGGFLMCKTTDT... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123 and nsP4, which associate to form... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similar... | O'nyong-nyong virus (strain Gulu) (ONNV) |
P13887 | POLN_RRVN | MKVTVDVEADSPFLKALQKAFPAFEVESQQVTPNDHANARAFSHLATKLIEQEVPANITILDVGSAPARRLMSDHSYHCICPMKSAEDPERLANYARKLAKTAGEVLDKNVSGKITDLQDVMATPDLESPTFCLHTDETCRTRAEVAVYQDVXXHAPTSLYHQAMKGVRTVYWIGFDTTPFMFEVVAGAYPTYSTNWADEQVLQARNIGLCATSLSEGHRGKISIMRKKRLRPSDRXMFSVGXTLYIESRRLLKSWHLPSVFHLKGKNSFTCRCDTIVSCEGYVVKKITMSPGTYGKTVGYAVTHHAEGFLMCKVTDTVR... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to for... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similar... | Ross river virus (strain NB5092) (RRV) |
P13888 | POLN_RRVT | APSYRVRRTDISGHAEEAVVNAANAKGTVGDGVCRAVARKWPDSFKGAATPVGTAKLVQANGMNVIHAVGPNFSTVTEAEGDRELAAAYRAVAGIINASNIKSVAIPLLSTGVFSGGKDRVMQSLNHLFTAMDTTDADVVIYCRDKAWEKKIQEAIDRRTAVELVSEDISLESDLIRVHPDSCLVGRKGYSITDGKLHSYLEGTRFHQTAVDMAEISTLWPKLQDANEQICLYALGESMDSIRTKCPVEDADSSTPPKTVPCLCRYAMTAERVARLRMNNTKAIIVCSSFPLPKYRIEGVQKVKCDRVLIFDQTVPSLVS... | 2.7.7.19; 2.7.7.48; 3.1.3.84 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF01661;PF20852;PF00978; | 3.40.220.10;3.40.50.150; | null | PTM: Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form ... | SUBCELLULAR LOCATION: [Polyprotein P123']: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=4-O-(ADP... | null | null | null | null | FUNCTION: Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarit... | Ross river virus (strain T48) (RRV) |
P13889 | POLN_RUBVT | MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRPCTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE... | 2.7.7.48; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01237}; Note=Zn(2+) is necessary for the protease activity. The protease can also function efficiently with Cd(2+) and Co(2+). {ECO:0000255|PROSITE-ProRule:PRU01237}; | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694] | host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; mRNA methyltransferase activity [GO:0008174]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-depend... | PF01661;PF05407;PF00978;PF12601;PF01443; | 3.40.220.10;3.40.50.300; | null | PTM: [Non-structural polyprotein p200]: Specific enzymatic cleavage by its own cysteine protease yield mature proteins p150 and p90. {ECO:0000250|UniProtKB:Q86500}. | SUBCELLULAR LOCATION: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}.; SUBCELLULAR LOCATIO... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:Q86500, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}.; FUNCTION: [Protease/methyltrans... | Rubella virus (strain Therien) (RUBV) |
P13890 | POLS_RRVN | MNYIPTQTFYGRRWRPRPAFRPWQVPMQPTPTMVTPMLQAPDLQAQQMQQLISAVSALTTKQNVKAPKGQRKQKQQKPKEKKEKQKKKPTXKKKQQQKPKPQAKKKKPGRRERMCMKIENDCIFEVKLDGKVTGYACLVGDKVMKPAHVKGTIDNPDLAKLTYKKSSKYDLECAQIPVHMKSDASKYTHEKPEGHYNWHHGAVQYSXGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWTKDMVTRVTPEGTEEWSAALMMCILANTSFPCSSPPCYPCCYEKQPEQTLRMLEDNVNRPGYYELL... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity). The remaining polyprotein is then targeted to the host endoplasmic reticulum, wh... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Ross river virus (strain NB5092) (RRV) |
P13892 | VP2_BFPYV | MGAIISAIAGLFELGALGGLAVDAAVNTAEIEAFIGELVLQDFSVAEIFDAIETSGIPLANTAVPVAELQQTAATSGLIGQALSAPSLIAASVKAFAGDPVAAGNNMALQVWRDQMDILFPGAEWFSNAVHNINPLAWAQSLYEQVGQSIWNYMTGNIGQAVIHQIEERTTALIVYQSRGIYDILARALETARWTLTTAAVDTYQTLKSYYGELPAVSGRVEAFRRYHEVAQGRSFFEDSDIQDVLEGKKAQKRIEGPQEMTGQTIEQQTPPGGAMQRHANDWLLPLILGLYGDLTPEWRYQLKERLNVPKRKRKLPTTS... | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; structural molecule activity [GO:0005198] | PF00761; | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | Budgerigar fledgling disease virus (BFPyV) (Aves polyomavirus 1) |
P13896 | POLN_WEEV | MERIHVDLDADSPYVKSLQRTFPQFEIEARQVTDNDHANARAFSHVATKLIESEVDRDQVILDIGSAPVRHAHSNHRYHCICPMISAEDPDRLQRYAERLKKSDITDKNIASKAADLLEVMSTPDAETPSLCMHTDATCRYFGSVAVYQDVYAVHAPTSIYHQALKGVRTIYWIGFDTTPFMYKNMAGSYPTYNTNWADERVLEARNIGLGNSDLQESRLGKLSILRKKRLQPTNKIIFSVGSTIYTEDRSLLRSWHLPNVFHLKGKSNFTGRCGTIVSCEGYVIKKITISPGLYGKVENLASTMHREGFLSCKVTDTLR... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to for... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes the minus-strand RNAs (antige... | Western equine encephalitis virus (WEEV) |
P13897 | POLS_WEEV | MFPYPQLNFPPVYPTNPMAYRDPNPPRCRWRPFRPPLAAQIEDLRRSIANLTFKQRSPNPPPGPPPKKKKSAPKPKPTQPKKKKQQAKKTKRKPKPGKRQRMCMKLESDKTFPIMLNGQVNGYACVVGGRLMKPLHVEGKIDNEQLAAVKLKKASMYDLEYGDVPQNMKSDTLQYTSDKPPGFYNWHHGAVQYENGRFTVPRGVGGKGDSGRPILDNRGRVVAIVLGGANEGTRTALSVVTWNQKGVTIKDTPEGSEPWSLVTALCVLSNVTFPCDKPPVCYSLAPERTLDVLEENVDNPNYDTLLENVLKCPSRRPKRS... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host ... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal ... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:P09592}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:P09592}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:Q8JUX5}; Si... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Western equine encephalitis virus (WEEV) |
P13899 | POLG_TMEVD | MACKHGYPDVCPICTAVDVTPGFEYLLLADGEWFPTDLLCVDLDDDVFWPSNSSNQSETMEWTDLPLVRDIVMEPQGNASSSDKSNSQSSGNEGVIINNFYSNQYQNSIDLSASGGNAGDAPQNNGQLSNILGGAANAFATMAPLLLDQNTEEMENLSDRVASDKAGNSATNTQSTVGRLCGYGEAHHGEHPASCADTATDKVLAAERYYTIDLASWTTTQEAFSHIRIPLPHVLAGEDGGVFGATLRRHYLCKTGWRVQVQCNASQFHAGSLLVFMAPEFYTGKGTKTGDMEPTDPFTMDTTWRAPQGAPTGYRYDSRT... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cyto... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail t... | Theiler's murine encephalomyelitis virus (strain DA) (TMEV) |
P13900 | POLG_SVDVU | MGAQVSTQKTGAHETSLSAAGNSVIHYTNINYYKDAASNSANRQDFTQDPGKFTEPVKDIMVKSMPALNSPSAEECGYSDRVRSITLGNSTITTQECANVVVGYGVWPTYLKDEEATAEDQPTQPDVATCRFYTLESVMWQQSSPGWWWKFPDALSNMGLFGQNMQYHYLGRAGYTIHVQCNASKFHQGCLLVVCVPEAEMGCATLANKPDPKSLSKGEIANMFESQNSTGETAVQANVINAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYINSVPMDNMFRHNNFTLMVIPFAPLSYSTGATTYVPITVTVAPMCAE... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Swine vesicular disease virus (strain UKG/27/72) (SVDV) |
P13901 | POLG_HAVMB | MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQ... | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome re... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:000025... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a d... | Human hepatitis A virus genotype IB (isolate MBB) (HHAV) (Human hepatitis A virus (isolate Human/Northern Africa/MBB/1978)) |
P13922 | DRTS_PLAFK | MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFRAVTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTNWESIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQIISVSDVYTSNNTTLDFIIYKKTNNKMLNEQNCIKGEEKNNDMPLKNDDKDTCHMKKLTEFYKNVDKYKINYENDDDDEEEDDFVYFNFNKEKEEKNKNSIHPNDFQIYNSLKY... | 1.5.1.3; 2.1.1.45 | null | dTMP biosynthetic process [GO:0006231]; methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate biosynthetic process [GO:0046654] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | dihydrofolate reductase activity [GO:0004146]; thymidylate synthase activity [GO:0004799] | PF00186;PF00303; | 6.10.250.2210;3.40.430.10;3.30.572.10; | Dihydrofolate reductase family; Thymidylate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8... | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. | null | null | FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. | Plasmodium falciparum (isolate K1 / Thailand) |
P13928 | ANXA8_HUMAN | MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALL... | null | null | blood coagulation [GO:0007596]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; negative regulation of phospholipase A2 activity [GO:1900138]; negative regulation of serine-type endopeptidase activity [GO:1900004] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidyls... | PF00191; | 1.10.220.10; | Annexin family | null | null | null | null | null | null | null | FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | Homo sapiens (Human) |
P13929 | ENOB_HUMAN | MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGKGVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVNIQIVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000250|UniProtKB:P15429}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000250|UniProtKB:P15429}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P15429}. | null | null | FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration. {ECO:0000250|UniProtKB:P15429}. | Homo sapiens (Human) |
P13941 | CO3A1_RAT | MMSFVQCGTWFLLTLLHPSLILAQQSNVDELGCNYLGQSYESRDVWKPEPCQICVCDSGSVLCDDIMCDDEPLDCPNPEIPFGECCAICPQPSTPAPVIPDGNRPQGPKGDPGPPGIPGRNGDPGLPGQPGLPGPPGSPGICESCPTGGQNYSPQFDSYDVKSGVGGMGGYPGPAGPPGPPGPPGSSGHPGSPGSPGYQGPPGEPGQAGPAGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGDNGAPGPMGPRGAPGERGRPGLPGAAGARG... | null | null | aorta development [GO:0035904]; aorta smooth muscle tissue morphogenesis [GO:0060414]; basement membrane organization [GO:0071711]; blood vessel development [GO:0001568]; cartilage development [GO:0051216]; cell-matrix adhesion [GO:0007160]; cellular response to amino acid stimulus [GO:0071230]; cerebral cortex develop... | collagen trimer [GO:0005581]; collagen type III trimer [GO:0005586]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]; SMAD binding [GO:0046332] | PF01410;PF01391;PF00093; | 2.60.120.1000;2.10.70.10; | Fibrillar collagen family | PTM: O-glycosylated. {ECO:0000250}.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly G... | Rattus norvegicus (Rat) |
P13942 | COBA2_HUMAN | MERCSRCHRLLLLLPLVLGLSAAPGWAGAPPVDVLRALRFPSLPDGVRRAKGICPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQV... | null | null | cartilage development [GO:0051216]; collagen fibril organization [GO:0030199]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; soft palate development [GO:0060023] | collagen trimer [GO:0005581]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674] | PF01410;PF01391;PF02210; | 2.60.120.1000;2.60.120.200; | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: A disulfide-bonded peptide called proline/arginine-rich protein or PARP is released from the N-terminus during extracellular processing and is subsequently retained in the cartilage matrix f... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. | Homo sapiens (Human) |
P13943 | MMP1_RABIT | MPGLPLLLLLLWGVGSHGFPAASETQEQDVEMVQKYLENYYNLKDDWRKIPKQRGNGLAVEKLKQMQEFFGLKVTGKPDAETLKMMKQPRCGVPDVAQFVLTPGNPRWEQTHLTYRIENYTPDLSRADVDNAIEKAFQLWSNVTPLTFTKVSKGQADIMISFVRGDHRDNSPFDGPEGQLAHAFQPGLGIGGDVHFDEDDRWTKDFRNYNLYRVAAHELGHSLGLSHSTDIGALMYPNYMFSGDVQLAQDDIDGIQAIYGPSQNPSQPVGPQTPKVCDSKLTFDAITTIRGEIMFFKDRFYMRANPYYSEVELNFISVFW... | 3.4.24.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000250|UniProtKB:P03956}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; | null | null | null | null | FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. | Oryctolagus cuniculus (Rabbit) |
P13944 | COCA1_CHICK | MRTALCSAVAALCAAALLSSIEAEVNPPSDLNFTIIDEHNVQMSWKRPPDAIVGYRITVVPTNDGPTKEFTLSPSTTQTVLSDLIPEIEYVVSIASYDEVEESLPVFGQLTIQTGGPGIPEEKKVEAQIQKCSISAMTDLVFLVDGSWSVGRNNFRYILDFMVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYFRRSDLLDAIKRIPYKGGNTMTGEAIDYLVKNTFTESAGARKGFPKVAIVITDGKAQDEVEIPARELRNIGVEVFSLGIKAADAKELKLIASQPSLKHVFNVANFDGIVDIQNEIILQVCSGVD... | null | null | cell adhesion [GO:0007155]; endodermal cell differentiation [GO:0035987] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576] | null | PF01391;PF00041;PF00092; | 2.60.120.200;2.60.40.10;3.40.50.410; | Fibril-associated collagens with interrupted helices (FACIT) family | PTM: The triple-helical tail is stabilized by disulfide bonds at each end.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: O-glycosylated; glycosaminoglycan of chondroitin-sulfate type. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. | Gallus gallus (Chicken) |
P13945 | ADRB3_HUMAN | MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGP... | null | null | activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; brown fat cell differentiation [GO:0050873]; carbohydrate metabolic process [GO:0005975]; diet i... | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | beta-3 adrenergic receptor binding [GO:0031699]; beta-adrenergic receptor activity [GO:0004939]; beta3-adrenergic receptor activity [GO:0015052]; epinephrine binding [GO:0051379]; norepinephrine binding [GO:0051380]; protein homodimerization activity [GO:0042803] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB3 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis. | Homo sapiens (Human) |
P13956 | ERM_BACIU | MNEKNIKHSQNFITSKHNIDKIMTNIRLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEIDHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYKIFGNIPYNISTDIIRKIVFDSIADEIYLIVEYGFAKRLLNTKRSLALFLMAEVDISILSMVPREYFHPKPKVNSSLIRLNRKKSRISHKDKQKYNYFVMKWVNKEYKKIFTKNQFNNSLKHAGIDDLNNISFEQFLSLFNSYKLFNK | 2.1.1.184 | null | response to antibiotic [GO:0046677] | cytosol [GO:0005829] | 23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity [GO:0052910]; RNA binding [GO:0003723]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179] | PF00398; | 1.10.8.100;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, rRNA adenine N(6)-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(6)-dimethyladenosine(2085) in 23S rRNA + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42784, Rhea:RHEA-COMP:10237, Rhea:RHEA-COMP:10238, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEB... | null | null | null | null | FUNCTION: This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics. {ECO:0000269|PubMed:12907737, ECO:0000269|PubMed:12946350}. | Bacillus subtilis |
P13984 | T2FB_HUMAN | MAERGELDLTGAKQNTGVWLVKVPKYLSQQWAKASGRGEVGKLRIAKTQGRTEVSFTLNEDLANIHDIGGKPASVSAPREHPFVLQSVGGQTLTVFTESSSDKLSLEGIVVQRAECRPAASENYMRLKRLQIEESSKPVRLSQQLDKVVTTNYKPVANHQYNIEYERKKKEDGKRARADKQHVLDMLFSAFEKHQYYNLKDLVDITKQPVVYLKEILKEIGVQNVKGIHKNTWELKPEYRHYQGEEKSD | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367] | microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor TFIIF complex [GO:0005674] | DNA binding [GO:0003677]; RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF02270;PF17683; | 1.10.10.10; | TFIIF beta subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454543}. | null | null | null | null | null | FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. {ECO:0000269|PubMed:2477704}. | Homo sapiens (Human) |
P13987 | CD59_HUMAN | MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP | null | null | blood coagulation [GO:0007596]; cell surface receptor signaling pathway [GO:0007166]; negative regulation of activation of membrane attack complex [GO:0001971]; regulation of complement activation [GO:0030449]; regulation of complement-dependent cytotoxicity [GO:1903659] | cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; fo... | complement binding [GO:0001848] | PF00021; | 2.10.60.10; | null | PTM: N- and O-glycosylated. The N-glycosylation mainly consists of a family of biantennary complex-type structures with and without lactosamine extensions and outer arm fucose residues. Also significant amounts of triantennary complexes (22%). Variable sialylation also present in the Asn-43 oligosaccharide. The predomi... | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Note=Soluble form found in a number of tissues. | null | null | null | null | null | FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. In... | Homo sapiens (Human) |
P13988 | TNSA_ECOLX | MAKANSSFSEVQIARRIKEGRGQGHGKDYIPWLTVQEVPSSGRSHRIYSHKTGRVHHLLSDLELAVFLSLEWESSVLDIREQFPLLPSDTRQIAIDSGIKHPVIRGVDQVMSTDFLVDCKDGPFEQFAIQVKPAAALQDERTLEKLELERRYWQQKQIPWFIFTDKEINPVVKENIEWLYSVKTEEVSAELLAQLSPLAHILQEKGDENIINVCKQVDIAYDLELGKTLSEIRALTANGFIKFNIYKSFRANKCADLCISQVVNMEELRYVAN | 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10911996, ECO:0000269|PubMed:15257292}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:8947057}; Note=The active site binds 2 Mg(2+) ions (PubMed:10911996, PubMed:15257292). According to PubMed:10704304, no transposition occu... | DNA transposition [GO:0006313] | chromosome [GO:0005694] | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; transposase activity [GO:0004803] | PF08721;PF08722; | 3.40.1350.10;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Required for Tn7 transposition. Forms the transposase, together with TnsB (PubMed:8947057). TnsA executes the 5'-DNA strand breakage reaction (PubMed:10704304). TnsABC and TnsD promote high-frequency insertion of Tn7 into a specific target site known as ATT-Tn7 whereas TnsABC and TnsD promote low-frequency in... | Escherichia coli |
P13994 | YJU2B_HUMAN | MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMADNEQVLTTEHEKKQKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRRRFREKKKAIQEEEERDQALQAKASLTIPLVPETEDDRKLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSAPGSASSSKVSGVLKKLAQSRRTALATSPITVGDLGIVRRRSRDVPESPQHAADTPKSGEPR... | null | null | mRNA splicing, via spliceosome [GO:0000398]; response to virus [GO:0009615]; RNA splicing [GO:0008380] | post-mRNA release spliceosomal complex [GO:0071014]; U2-type spliceosomal complex [GO:0005684] | null | PF04502; | null | CWC16 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW85}. | null | null | null | null | null | FUNCTION: May be involved in mRNA splicing. {ECO:0000250|UniProtKB:Q9BW85}. | Homo sapiens (Human) |
P13995 | MTDC_HUMAN | MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAML... | 1.5.1.15; 3.5.4.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8218174}; | folic acid metabolic process [GO:0046655]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653] | extracellular space [GO:0005615]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | magnesium ion binding [GO:0000287]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]; phosphate ion binding [GO:0042301] | PF00763;PF02882; | 3.40.50.10860;3.40.50.720; | Tetrahydrofolate dehydrogenase/cyclohydrolase family | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.15; Evidence={ECO:0000269|PubMed:16100107, ECO:0000269|PubMed:8218174}; CATALYTIC ACT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=202 uM for NAD {ECO:0000269|PubMed:16100107}; KM=352 uM for NADP {ECO:0000269|PubMed:16100107}; Vmax=22.5 umol/min/mg enzyme with NAD as substrate {ECO:0000269|PubMed:16100107}; Vmax=2.92 umol/min/mg enzyme with NADP as substrate {ECO:0000269|PubMed:16100107}; | null | null | null | FUNCTION: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency. {ECO:0000269|PubMed:16100107}. | Homo sapiens (Human) |
P14003 | HAIR_DROME | MVTGVTAANMTNVLGTAVVPAQLKETPLKSDRRSNKPIMEKRRRARINNCLNELKTLILDATKKDPARHSKLEKADILEKTVKHLQELQRQQAAMQQAADPKIVNKFKAGFADCVNEVSRFPGIEPAQRRRLLQHLSNCINGVKTELHQQQRQQQQQSIHAQMLPSPPSSPEQDSQQGAAAPYLFGIQQTASGYFLPNGMQVIPTKLPNGSIALVLPQSLPQQQQQQLLQHQQQQQQLAVAAAAAAAAAAQQQPMLVSMPQRTASTGSASSHSSAGYESAPGSSSSCSYAPPSPANSSYEPMDIKPSVIQRVPMEQQPLS... | null | null | anterior/posterior pattern specification [GO:0009952]; cell morphogenesis [GO:0000902]; membrane organization [GO:0061024]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; open tracheal syst... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-sp... | PF07527;PF00010; | 6.10.250.980;4.10.280.10; | null | PTM: Ubiquitinated by Topors. {ECO:0000269|PubMed:14871887}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Pair-rule protein that regulates embryonic segmentation and adult bristle patterning. Transcriptional repressor of genes that require a bHLH protein for their transcription (e.g. ftz). {ECO:0000269|PubMed:8649374}. | Drosophila melanogaster (Fruit fly) |
P14020 | DPM1_YEAST | MSIEYSVIVPAYHEKLNIKPLTTRLFAGMSPEMAKKTELIFVDDNSQDGSVEEVDALAHQGYNVRIIVRTNERGLSSAVLKGFYEAKGQYLVCMDADLQHPPETVPKLFESLHDHAFTLGTRYAPGVGIDKDWPMYRRVISSTARMMARPLTIASDPMSGFFGLQKKYLENCNPRDINSQGFKIALELLAKLPLPRDPRVAIGEVPFTFGVRTEGESKLSGKVIIQYLQQLKELYVFKFGANNLILFITFWSILFFYVCYQLYHLVF | 2.4.1.83 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3}; | dolichol metabolic process [GO:0019348]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GPI anchor biosynthetic process [GO:0006506]; protein O-linked mannosylation [GO:0035269] | cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175] | dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; metal ion binding [GO:0046872] | PF00535; | null | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15657391}; Cytoplasmic side {ECO:0000269|PubMed:15657391}. | CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000269|PubMed:15548536, ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for GDP-mannose {ECO:0000269|PubMed:15548536}; Vmax=25.1 nmol/min/mg enzyme for GDP-mannose {ECO:0000269|PubMed:15548536}; Note=For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP-mannose, in... | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:3053713}. | null | null | FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins. {ECO:0000269|PubMed:3053713, ECO:0000269|PubMed:350... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14056 | ARAF_RAT | MEPPRGPPASGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRRQFYHSIQDLSGGSRQQEVPSNLSVNELLTPQGPSPFTQQRDQEHFSFPAPANPPLQRIRSTSTPNVHMVSTTAPMDSSLMQFTAQSFSTDAAGRGGDGAPRGSPSPASVSSGRKSPHSKLPAEQRERKSLADEKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFG... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; Ras protein signal transduction [GO:0007265]; regulation of proteasomal ubiquitin-dependent... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF07714;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade (By similarity). Phosphorylates PFKFB2 (By similarity). {ECO:0000250|UniProtKB:P10398}. | Rattus norvegicus (Rat) |
P14060 | 3BHS1_HUMAN | MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIV... | 1.1.1.145; 1.1.1.210; 1.1.1.270; 5.3.3.1 | null | androgen biosynthetic process [GO:0006702]; C21-steroid hormone metabolic process [GO:0008207]; estrogen biosynthetic process [GO:0006703]; hippocampus development [GO:0021766]; response to corticosterone [GO:0051412]; steroid biosynthetic process [GO:0006694] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; nucleolus [GO:0005730]; smooth end... | 3-beta-hydroxy-delta5-steroid dehydrogenase activity [GO:0003854]; 3-keto sterol reductase activity [GO:0000253]; 5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; cholesterol dehydrogenase activity [GO:0102294]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as accepto... | PF01073; | 3.40.50.720; | 3-beta-HSD family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722, ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.145; Evidence={ECO:0000269|PubMed:1401999}; CATALYTIC ACTIVITY: Reaction=NAD(+) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 uM for dehydroepiandrosterone (in the presence of NAD(+)) {ECO:0000269|PubMed:1401999}; KM=0.33 uM for pregnenolone (in the presence of NAD(+)) {ECO:0000269|PubMed:1401999}; KM=2.1 uM for dihydrotestosterone (in the presence of NADH) {ECO:0000269|PubMed:140199... | PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:1401999}.; PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:1401999}. | null | null | FUNCTION: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydrox... | Homo sapiens (Human) |
P14061 | DHB1_HUMAN | MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPEL... | 1.1.1.51; 1.1.1.62 | null | adipose tissue development [GO:0060612]; bone development [GO:0060348]; cellular response to metal ion [GO:0071248]; estrogen biosynthetic process [GO:0006703]; estrogen metabolic process [GO:0008210]; gene expression [GO:0010467]; lysosome organization [GO:0007040]; skeletal muscle tissue development [GO:0007519]; ste... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 17-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0072582]; catalytic activity [GO:0003824]; dihydrotestosterone 17-beta-dehydrogenase activity [GO:0035410]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; estradiol binding [GO:1903924]; NADP binding [GO:0050661]; NADP+ binding [GO:0070401]; pro... | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:8994190}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.11 uM for 17beta-estradiol {ECO:0000269|PubMed:8994190}; KM=0.9 uM for estrone {ECO:0000269|PubMed:8994190}; | PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000269|PubMed:8994190}. | null | null | FUNCTION: Favors the reduction of estrogens and androgens. Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2) (PubMed:8994190). Also has 20-alpha-HSD activity. Uses preferentially NADH. {ECO:0000269|PubMed:8994190}. | Homo sapiens (Human) |
P14064 | HAP4_YEAST | MTAKTFLLQASASRPRSNHFKNEHNNIPLAPVPIAPNTNHHNNSSLEFENDGSKKKKKSSLVVRTSKHWVLPPRPRPGRRSSSHNTLPANNTNNILNVGPNSRNSSNNNNNNNIISNRKQASKEKRKIPRHIQTIDEKLINDSNYLAFLKFDDLENEKFHSSASSISSPSYSSPSFSSYRNRKKSEFMDDESCTDVETIAAHNSLLTKNHHIDSSSNVHAPPTKKSKLNDFDLLSLSSTSSSATPVPQLTKDLNMNLNFHKIPHKASFPDSPADFSPADSVSLIRNHSLPTNLQVKDKIEDLNEIKFFNDFEKLEFFNKY... | null | null | carbon catabolite activation of transcription from RNA polymerase II promoter [GO:0000436]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of cellular respiration [GO:0043457]; regulation of DNA-templated transcription [GO:0006355] | CCAAT-binding factor complex [GO:0016602]; mitochondrial respirasome [GO:0005746] | DNA binding [GO:0003677]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713] | PF10297; | null | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP4 encodes a regulatory subuni... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14065 | GCY1_YEAST | MPATLHDSTKILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEVALDQSLKRLGLDYVDLYLMHWPARLDPAYIKNEDILSVPTKKDGSRAVDITNWNFIKTWELMQELPKTGKTKAVGVSNFSINNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNISKEKGEKRVVHPNWSPFEVFK | 1.1.1.156 | null | arabinose catabolic process [GO:0019568]; cellular response to oxidative stress [GO:0034599]; D-xylose catabolic process [GO:0042843]; glycerol to glycerone phosphate metabolic process [GO:0061610] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; glycerol 2-dehydrogenase (NADP+) activity [GO:0047953]; glycerol dehydrogenase [NAD(P)+] activity [GO:1990042]; mRNA binding [GO:0003729]; oxidoreductase activity [GO:0016491] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH; Xref=Rhea:RHEA:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.156; Evidence={ECO:0000269|PubMed:10818358, ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678, ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.3 mM for D,L-glyceraldehyde {ECO:0000269|PubMed:10818358, ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678, ECO:0000269|PubMed:23770562}; KM=0.007 mM for NADPH {ECO:0000269|PubMed:10818358, ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678, ECO:00... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:10818358, ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678, ECO:0000269|PubMed:23770562}; | null | FUNCTION: Glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. Has mRNA binding activity. {ECO:0000269|PubMed:11113971, ECO:0000269|PubMed:15127164, ECO:0000269|PubMed:17140678, ECO:0000269|PubMed:22979944, ECO:0000269|PubMed:23770562, ECO:0000269|PubMed:23896974}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14068 | XPO1_SCHPO | MEGILAFDRELDVALLDRVVQTFYQGVGAEQQQAQQVLTQFQAHPDAWSQAYSILEKSEYPQTKYIALSVLDKLITTRWKMLPKEQRLGIRNYIVAVMIKNSSDETVLQQQKTFLNKLDLTLVQILKQEWPHNWPNFIPEIVQASKTNLSLCENNMIVLRLLSEEIFDYSAEQMTQLKTKNLKNQMCGEFAEIFQLCSQILERAQKPSLIKATLGTLLRFLNWIPLGYIFETNIVELITNRFLNVPDFRNVTIECLTEIASLTSQPQYNDKFVTMFNLVMTSVNSMLPLQTDFREAYEESSTNEQDFIQNLALFLCAFFS... | null | null | protein export from nucleus [GO:0006611]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from nucleus [GO:0000056] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nucleus [GO:0005634] | GTP binding [GO:0005525]; nuclear export signal receptor activity [GO:0005049]; small GTPase binding [GO:0031267] | PF08767;PF18777;PF18784;PF18787;PF03810;PF08389; | 1.25.10.10; | Exportin family | null | SUBCELLULAR LOCATION: Nucleus. Note=Localized in the nucleus and at its periphery. | null | null | null | null | null | FUNCTION: Receptor for the leucine-rich nuclear export signal (NES). {ECO:0000269|PubMed:19502236}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P14069 | S10A6_MOUSE | MACPLDQAIGLLVAIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMDDLDRNKDQEVNFQEYVAFLGALALIYNEALK | null | null | null | collagen-containing extracellular matrix [GO:0062023]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; monoatomic ion transmembrane transporter activity [GO:0015075]; protein homodimerization activity [GO:0042803]; S100 protein binding [GO:0044548]; tropomyosin binding [GO:0005523]; zinc ion binding [GO:0008270] | PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Bind... | Mus musculus (Mouse) |
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