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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P10111 | PPIA_RAT | MVNPTVFFDITADGEPLGRVCFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMSIVEAMERFGSRNGKTSKKITISDCGQL | 5.2.1.8 | null | activation of protein kinase B activity [GO:0032148]; apoptotic process [GO:0006915]; cell adhesion molecule production [GO:0060352]; cellular response to oxidative stress [GO:0034599]; endothelial cell activation [GO:0042118]; leukocyte chemotaxis [GO:0030595]; lipid droplet organization [GO:0034389]; negative regulat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cyclosporin A binding [GO:0016018]; heparan sulfate binding [GO:1904399]; integrin binding [GO:0005178]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family, PPIase A subfamily | PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization (By similarity). PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity). Acetylation at Lys-125 favors the ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}. Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus {ECO:0000250|UniProtKB:P62937}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, ... | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000250|UniProtKB:P62937}; | null | null | null | null | FUNCTION: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity). ... | Rattus norvegicus (Rat) |
P10114 | RAP2A_HUMAN | MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ | 3.6.5.2 | null | actin cytoskeleton organization [GO:0030036]; cellular response to xenobiotic stimulus [GO:0071466]; establishment of protein localization [GO:0045184]; microvillus assembly [GO:0030033]; negative regulation of cell migration [GO:0030336]; positive regulation of protein autophosphorylation [GO:0031954]; positive regula... | cytosol [GO:0005829]; midbody [GO:0030496]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO:0097060] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and diubiquitination by NEDD4. Multiple lysine residues are probably modified. Ubiquitination requires TNIK, prevents interaction with effectors and inactivates RAP2A. {ECO:0000269|PubMed:20159449}.; PTM: Palmitoylated. Palmitoylation is required for association... | SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Midbody. Note=May also localize to the Golgi (PubMed:7962206) and the gelatinase-containing granules of neutrophils (PubMed:8391995). Colocalizes with RASGEF1B to midbody at telophase (PubMed:23894443). {ECO:0000269|PubMed:23894443, ECO:... | 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:1900290}; | null | null | null | null | FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arb... | Homo sapiens (Human) |
P10121 | FTSY_ECOLI | MAKEKKRGFFSWLGFGQKEQTPEKETEVQNEQPVVEEIVQAQEPVKASEQAVEEQPQAHTEAEAETFAADVVEVTEQVAESEKAQPEAEVVAQPEPVVEETPEPVAIEREELPLPEDVNAEAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEELETALAAEAAEEAVMVVPPAEEEQPVEEIAQEQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLARQFEQQ... | 3.6.5.4 | null | protein targeting [GO:0006605]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; stringent response [GO:0015968] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP hydrolysis activity [GO:0016887]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein homodimerization activity [GO:0042803]; signal recognition particle binding [GO:0005047] | PF00448;PF02881; | 3.40.50.300;1.20.120.140; | GTP-binding SRP family, FtsY subfamily | PTM: Proteolytically cleaved. The cleavage may regulate function and subcellular location of FtsY. Full-length FtsY is found primarily associated with the membrane, while cleaved protein is predominantly present in the cytoplasm. {ECO:0000269|PubMed:18281057}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11353766, ECO:0000269|PubMed:17726013, ECO:0000269|PubMed:18281057, ECO:0000269|PubMed:19414018, ECO:0000269|PubMed:21543314, ECO:0000269|PubMed:8194520, ECO:0000269|PubMed:9177162}; Peripheral membrane protein {ECO:0000269|PubMed:11353766, ECO:0000269|PubMe... | 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=3.6.5.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00920, ECO:0000269|PubMed:11735405, ECO:0000269|PubMed:17682051}; | null | null | null | null | FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... | Escherichia coli (strain K12) |
P10124 | SRGN_HUMAN | MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFML | null | null | apoptotic process [GO:0006915]; biomineral tissue development [GO:0031214]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; maintenance of granzyme B location in T cell secretory granule [GO:0033382]; maintenance of protease location in mast cell secretory granule [GO:0033373]; mast cell secreto... | cytolytic granule [GO:0044194]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; mast cell granule [GO:0042629]; platelet alpha granule lumen [GO:0031093]; secretory granule [GO:0030141] | null | PF04360; | null | Serglycin family | PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:11154222}. Cytolytic granule {ECO:0000269|PubMed:11154222}. Secreted, extracellular space {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:16870619}. Golgi apparatus {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}. Note=Found in mast cell granules... | null | null | null | null | null | FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in a... | Homo sapiens (Human) |
P10126 | EF1A1_MOUSE | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV... | 3.6.5.- | null | cellular response to epidermal growth factor stimulus [GO:0071364]; regulation of D-erythro-sphingosine kinase activity [GO:1900022]; translation [GO:0006412]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; heterocyclic compound binding [GO:1901363]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; translation elongation factor activity [GO:0003746] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily | PTM: ISGylated. {ECO:0000250|UniProtKB:P68104}.; PTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytopla... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68104}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6810... | null | null | null | null | FUNCTION: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing ... | Mus musculus (Mouse) |
P10127 | ADH4_YEAST | MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQEDPEET... | 1.1.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:3282541}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:3282541}; Note=Zinc. May bind iron when zinc levels are limiting. {ECO:0000269|PubMed:3282541}; | amino acid catabolic process to alcohol via Ehrlich pathway [GO:0000947]; fermentation [GO:0006113] | mitochondrion [GO:0005739] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; metal ion binding [GO:0046872] | PF00465; | 3.40.50.1970;1.20.1090.10; | Iron-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:3282541}; CATALYTIC ACTIVITY: Reaction=ethanol + NAD(+) = acetaldehyde + H(+)... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 mM for NAD {ECO:0000269|PubMed:3282541}; KM=122 uM for NADH {ECO:0000269|PubMed:3282541}; KM=2.83 mM for acetaldehyde {ECO:0000269|PubMed:3282541}; KM=16.7 mM for ethanol {ECO:0000269|PubMed:3282541}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3. {ECO:0000269|PubMed:3282541}; | null | FUNCTION: Alcohol dehydrogenase specific for ethanol. Acts mainyl as a mitochondrial formaldehyde dehydrogenase and has no effect on ethanol production (PubMed:2193925). Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols an... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10144 | GRAB_HUMAN | MQPILLLLAFLLLPRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY | 3.4.21.79 | null | apoptotic process [GO:0006915]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; killing of cells of another organism [GO:0031640]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of translation [GO:0017148]; protein maturation [GO:0051604]; proteolysis involved in pro... | cytolytic granule [GO:0044194]; cytolytic granule lumen [GO:1904856]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; immunological synapse [GO:0001772]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634] | serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:8258716}. Cytolytic granule {ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:24088571, ECO:0000269|PubMed:8258716}. Note=Delivered into the target cell by perforin (PubMed:20038786). {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:8258716}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79; Evidence={ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:8258716, ECO:0000269|PubMed:9852092}; | null | null | null | null | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:1985927, PubMed:3262682, PubMed:3263427). It cleaves after Asp (PubMed:1985927, PubMed:8258716). Once deliv... | Homo sapiens (Human) |
P10145 | IL8_HUMAN | MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS | null | null | angiogenesis [GO:0001525]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; calcium-mediated signaling [GO:0019722]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; heparin binding [GO:0008201]; interleukin-8 receptor binding [GO:0005153] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | PTM: Several N-terminal processed forms are produced by proteolytic cleavage after secretion from at least peripheral blood monocytes, leukcocytes and endothelial cells. In general, IL-8(1-77) is referred to as interleukin-8. IL-8(6-77) is the most promiment form. {ECO:0000269|PubMed:11023497, ECO:0000269|PubMed:119787... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection (PubMed:18692776, PubMed:7636208). Also plays an important role in neutrophil activation (PubMed:2145175, PubMed:9623510). Released in response to an ... | Homo sapiens (Human) |
P10146 | CCL1_MOUSE | MKPTAMALMCLLLAAVWIQDVDSKSMLTVSNSCCLNTLKKELPLKFIQCYRKMGSSCPDPPAVVFRLNKGRESCASTNKTWVQNHLKKVNPC | null | null | cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-17 [GO:0097398]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]... | extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009]; cytokine activity [GO:0005125] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | null | null | null | null | null | null | FUNCTION: Cytokine that is chemotactic for neutrophils. | Mus musculus (Mouse) |
P10147 | CCL3_HUMAN | MQVSTAALAVLLCTMALCNQFSASLAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQKYVSDLELSA | null | null | astrocyte cell migration [GO:0043615]; calcium ion transport [GO:0006816]; calcium-mediated signaling [GO:0019722]; cell activation [GO:0001775]; cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II inter... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR1 chemokine receptor binding [GO:0031726]; CCR5 chemokine receptor binding [GO:0031730]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; phospholipase activator activity [GO:0016... | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: N-terminal processed form LD78-alpha(4-69) is produced by proteolytic cleavage after secretion from HTLV1-transformed T-cells. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). {ECO:0000269|PubMe... | Homo sapiens (Human) |
P10148 | CCL2_MOUSE | MQVPVMLLGLLFTVAGWSIHVLAQPDAVNAPLTCCYSFTSKMIPMSRLESYKRITSSRCPKEAVVFVTKLKREVCADPKKEWVQTYIKNLDRNQMRSEPTTLFKTASALRSSAPLNVKLTRKSEANASTTFSTTTSSTSVGVTSVTVN | null | null | angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; astrocyte cell migration [GO:0043615]; cellular response to ATP [GO:0071318]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to estradiol stimulus [GO:0071392]; cellular response to fatty acid [GO:0071398]; cellular response... | axon terminus [GO:0043679]; C-fiber [GO:0044299]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471] | CCR chemokine receptor binding [GO:0048020]; CCR2 chemokine receptor binding [GO:0031727]; chemokine activity [GO:0008009]; cytokine activity [GO:0005125]; G protein-coupled receptor binding [GO:0001664]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: Processing at the N-terminus can regulate receptor and target cell selectivity (By similarity). Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant (By similarity). {ECO:0000250|UniProtKB:P13500}.; PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P13500}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13500}. | null | null | null | null | null | FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinoph... | Mus musculus (Mouse) |
P10152 | ANG1_BOVIN | MVMVLSPLLLVFILGLGLTPVAPAQDDYRYIHFLTQHYDAKPKGRNDEYCFNMMKNRRLTRPCKDRNTFIHGNKNDIKAICEDRNGQPYRGDLRISKSEFQITICKHKGGSSRPPCRYGATEDSRVIVVGCENGLPVHFDESFITPRH | 3.1.27.- | null | actin filament polymerization [GO:0030041]; activation of phospholipase A2 activity [GO:0032431]; activation of phospholipase C activity [GO:0007202]; angiogenesis [GO:0001525]; antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell differ... | angiogenin-PRI complex [GO:0032311]; basement membrane [GO:0005604]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleus [GO:0005634] | actin binding [GO:0003779]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; heparin binding [GO:0008201]; RNA nuclease activity [GO:0004540]; signaling receptor binding [GO:0005102] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000269|PubMed:2775757, ECO:0000269|PubMed:3064806, ECO:0000269|PubMed:3197838}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Rapidly endocytosed by target cells and translocated to the nucleus wh... | null | null | null | null | null | FUNCTION: Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragment... | Bos taurus (Bovine) |
P10153 | RNAS2_HUMAN | MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII | 4.6.1.18 | null | chemotaxis [GO:0006935]; defense response to virus [GO:0051607]; innate immune response in mucosa [GO:0002227]; RNA catabolic process [GO:0006401] | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | PTM: A particular signal processing and glycosylation pattern may differentiate the UpI2 RNase, found specifically in pregnant women urine, from other nonsecretory RNases. {ECO:0000269|PubMed:7947762, ECO:0000269|PubMed:9450956}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000250|UniProtKB:P47784}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleoti... | null | null | null | null | FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities. {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:3458170}. | Homo sapiens (Human) |
P10155 | RO60_HUMAN | MEESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIH... | null | null | cellular response to interferon-alpha [GO:0035457]; cilium assembly [GO:0060271]; immune system development [GO:0002520]; regulation of gene expression [GO:0010468]; response to UV [GO:0009411]; smoothened signaling pathway [GO:0007224]; transcription by RNA polymerase III [GO:0006383] | cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:1990904] | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; U2 snRNA binding [GO:0030620] | PF05731; | 3.40.50.410; | Ro 60 kDa family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}. | null | null | null | null | null | FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (PubMed:18056422, PubMed:26382853). Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:263828... | Homo sapiens (Human) |
P10158 | FOSL1_RAT | MYRDFGEPGPSSGAGSAYGRPAQPQQAQTQTVQQQKFHLVPSINAVSGSQELQWMVQPHFLGPSGYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEEDKKDTGGTSSTSGAGSPPGPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCSSAHRKSSSSSGDPSSDPLGSPTLLAL | null | null | cellular response to extracellular stimulus [GO:0031668]; cytokine-mediated signaling pathway [GO:0019221]; female pregnancy [GO:0007565]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; learning [GO:0007612]; negative regulation of cell population prolifer... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynaptic membrane [GO:0042734]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}. | null | null | null | null | null | null | Rattus norvegicus (Rat) |
P10160 | IF5A1_RABIT | MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDSGEEILITVLSAMTEEAAVAIKAMAK | null | null | positive regulation of translation [GO:0045727]; positive regulation of translational elongation [GO:0045901]; positive regulation of translational termination [GO:0045905]; translational elongation [GO:0006414] | endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634] | ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF01287;PF21485; | 2.30.30.30;2.40.50.140; | EIF-5A family | PTM: Acetylated by PCAF/KAT2B, regulating its subcellular localization (By similarity). Deacetylated by SIRT2 (By similarity). {ECO:0000250|UniProtKB:P63241}.; PTM: Lys-50 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63241}. Nucleus {ECO:0000250|UniProtKB:P63241}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P63241}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63241}; Cytoplasmic side {ECO:0000250|UniProtKB:P63241}. Note=Hypusine modification promotes the nucl... | null | null | null | null | null | FUNCTION: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient t... | Oryctolagus cuniculus (Rabbit) |
P10163 | PRB4_HUMAN | MLLILLSVALLALSSAESSSEDVSQEESLFLISGKPEGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPAGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ | null | null | null | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF15240; | null | null | PTM: N-glycosylated. {ECO:0000269|PubMed:20879038}.; PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P(3) position is mostly lysine. The endoprotease may be of microbial origin. Pyroglutamate formation found on at least Gln-46, Gln-48, Gln-67, Gln-88; Gln-90; Gln-193; Gln-288 Gln-214 and Gl... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Homo sapiens (Human) |
P10168 | IL7_MOUSE | MFHVSFRYIFGIPPLILVLLPVTSSECHIKDKEGKAYESVLMISIDELDKMTGTDSNCPNNEPNFFRKHVCDDTKEAAFLNRAARKLKQFLKMNISEEFNVHLLTVSQGTQTLVNCTSKEEKNVKEQKKNDACFLKRLLREIKTCWNKILKGSI | null | null | B cell proliferation [GO:0042100]; bone resorption [GO:0045453]; cytokine-mediated signaling pathway [GO:0019221]; extrinsic apoptotic signaling pathway [GO:0097191]; homeostasis of number of cells within a tissue [GO:0048873]; immune response [GO:0006955]; negative regulation of extrinsic apoptotic signaling pathway [... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-7 receptor binding [GO:0005139] | PF01415; | 1.20.1250.50; | IL-7/IL-9 family | PTM: Three disulfide bonds are present. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13232}. | null | null | null | null | null | FUNCTION: Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis (PubMed:28811625, PubMed:7699333). Mechanistically, exerts its biological effects thr... | Mus musculus (Mouse) |
P10173 | FUMH_PIG | MDRALRLLARSRCLSRVPASAPGPGPGSSPSGVSRLLLRPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPIPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHEALLPGLQKLHDALDAKSREFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAITRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAH... | 4.2.1.2 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; fumarate metabolic process [GO:0006106]; malate metabolic process [GO:0006108]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; regulation of arginine metabolic process [GO:0000821]; tricarboxylic acid cycle [GO:000... | chromosome [GO:0005694]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; tricarboxylic acid cycle enzyme complex [GO:0045239] | fumarate hydratase activity [GO:0004333] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Fumarase subfamily | PTM: [Isoform Cytoplasmic]: Phosphorylation at Thr-238 by PRKDC in response to DNA damage promotes translocation to the nucleus and recruitment to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P07954}. | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P07954}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07954}. Nucleus {ECO:0000250|UniProtKB:P07954}. Chromosome {ECO:0000250|UniProtKB:P07954}. Note=Translocates to the nucleus in response to... | CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:21498518}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462; Evidence={ECO:0000269|PubMed:21498518}; CATALY... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000269|PubMed:21498518}. | null | null | FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:21498518). Experiments in different species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). {ECO:0000269|PubMed:21498518, ECO:0000305}.; F... | Sus scrofa (Pig) |
P10174 | COX7_YEAST | MANKVIQLQKIFQSSTKPLWWRHPRSALYLYPFYAIFAVAVVTPLLYIPNAIRGIKAKKA | null | null | cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; proton transmembrane transport [GO:1902600] | mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | oxidoreductase activity [GO:0016491] | PF02238; | null | Cytochrome c oxidase VIIa family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10175 | COX8B_BOVIN | MLRLAPTVRLLQAPLRGWAVPKAHITAKPAKTPTSPKEQAIGLSVTFLSFLLPAGWVLYHLDNYKKSSAA | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | null | PF02285; | 4.10.81.10; | Cytochrome c oxidase VIII family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305|PubMed:27605664}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Bos taurus (Bovine) |
P10176 | COX8A_HUMAN | MSVLTPLLLRGLTGSARRLPVPRAKIHSLPPEGKLGIMELAVGLTSCFVTFLLPAGWILSHLETYRRPE | null | null | cellular respiration [GO:0045333]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | cytochrome-c oxidase activity [GO:0004129] | PF02285; | 4.10.81.10; | Cytochrome c oxidase VIII family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P10175}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P10180 | CUT_DROME | MQPTLPQAAGTADMDLTAVQSINDWFFKKEQIYLLAQFWQQRATLAEKEVNTLKEQLSTGNPDSNLNSENSDTAAAAATAAAVAAVVAGATATNDIEDEQQQQLQQTASGGILESDSDKLLNSSIVAAAITLQQQNGSNLLANTNTPSPSPPLLSAEQQQQLQSSLQQSGGVGGACLNPKLFFNHAQQMMMMEAAAAAAAAALQQQQQQQSPLHSPANEVAIPTEQPAATVATGAAAAAAAAATPIATGNVKSGSTTSNANHTNSNNSHQDEEELDDEEEDEEEDEDEDDEEENASMQSNADDMELDAQQETRTEPSATT... | null | null | antennal development [GO:0007469]; antennal joint development [GO:0048098]; central nervous system development [GO:0007417]; compound eye morphogenesis [GO:0001745]; dendrite arborization [GO:0140059]; dendrite guidance [GO:0070983]; dendrite morphogenesis [GO:0048813]; female gonad development [GO:0008585]; formation ... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription cis-regulatory region binding [GO:0000976] | PF02376;PF00046; | 1.10.10.60;1.10.260.40; | CUT homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Regulator of cell fate decisions in multiple lineages. Specifically, functions as a determination factor that specifies sensory organ identity in precursor cells. Probably also involved in cell type specification of Malpighian tubules. In absence of cut gene external sensory organs are transformed into chordo... | Drosophila melanogaster (Fruit fly) |
P10181 | ROUGH_DROME | MQRHKVEIGSPDGSPGIKRSDSLDPIANTTILSVPQRPSSPRQFFERLYGHLETRSSENGEIDVGTHAHKPPPCDTPYHSDGGSVSSPDISISDERTSLAAYPAYDFYGHAKDYPQHPSQQHQQHHHHHHHPPQLVHQKLSYVSPPPAIAAGGAANPVLPHAFPAGFPSDPHFSAGFSAFLARRRRKEGRQRRQRTTFSTEQTLRLEVEFHRNEYISRSRRFELAETLRLTETQIKIWFQNRRAKDKRIEKAQIDQHYRNFVVANGFMSSIMGQAATTMPPGGVTGGVAVGVGLNYYAAAATPAALPKDNTQDANFIDID... | null | null | establishment of ommatidial planar polarity [GO:0042067]; positive regulation of transcription by RNA polymerase II [GO:0045944]; R2/R5 cell differentiation [GO:0048054]; R2/R5 cell fate commitment [GO:0007463]; regulation of transcription by RNA polymerase II [GO:0006357]; response to stimulus [GO:0050896]; visual per... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:1974228}. Note=Restricted to nuclei in the developing retina. | null | null | null | null | null | FUNCTION: Required to establish the unique cell identity of photoreceptors R2 and R5 and consequently for ommatidial assembly in the developing eye imaginal disk. Repression of expression in R8 photoreceptor by senseless (sens) is an essential mechanism of R8 cell fate determination. {ECO:0000269|PubMed:11709152, ECO:0... | Drosophila melanogaster (Fruit fly) |
P10184 | IOV7_CHICK | MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQFVQVALALCCFADIAFGIEVNCSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGICLYNREHGANVEKEYDGECRPKHVTIDCSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGICAYNAEHHTNISKLHDGECKLEIGSVDCSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGICAHNAEQRTHVSKKHDGKCRQEIPEIDCDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGICAHNAQHGTEVK... | null | null | negative regulation of viral genome replication [GO:0045071]; response to corticosterone [GO:0051412] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | ion channel inhibitor activity [GO:0008200]; peptidase inhibitor activity [GO:0030414]; potassium channel inhibitor activity [GO:0019870]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00050; | 3.30.60.30; | null | PTM: Glycosylated. {ECO:0000269|PubMed:3025257}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22010862}. | null | null | null | null | null | FUNCTION: Serine protease inhibitor involved in antimicrobial egg defense preventing contamination of table eggs (non-fertilized eggs) and protecting the chick embryo (fertilized eggs) (Probable). Inhibits trypsin, chymotrypsin, elastase, subtilisin and a proteinase of fungus Aspergillus oryzae (PubMed:13944692, PubMed... | Gallus gallus (Chicken) |
P10185 | GL_HHV11 | MGILGWVGLIAVGVLCVRGGLPSTEYVIRSRVAREVGDILKVPCVPLPSDDLDWRYETPSAINYALIDGIFLRYHCPGLDTVLWDRHAQKAYWVNPFLFVAGFLEDLSYPAFPANTQETETRLALYKEIRQALDSRKQAASHTPVKAGCVNFDYSRTRRCVGRQDLGPTNGTSGRTPVLPPDDEAGLQPKPLTTPPPIIATSDPTPRRDAATKSRRRRPHSRRL | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718] | host cell Golgi apparatus [GO:0044177]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF12524;PF05259; | 3.30.390.170; | Herpesviridae glycoprotein L (gL) family, Alphaherpesvirinae gL subfamily | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:18596102}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04034}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04034}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:25746217}; Peripheral membran... | null | null | null | null | null | FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10210 | SCAF_HHV11 | MAADAPGDRMEEPLPDRAVPIYVAGFLALYDSGDSGELALDPDTVRAALPPDNPLPINVDHRAGCEVGRVLAVVDDPRGPFFVGLIACVQLERVLETAASAAIFERRGPPLSREERLLYLITNYLPSVSLATKRLGGEAHPDRTLFAHVALCAIGRRLGTIVTYDTGLDAAIAPFRHLSPASREGARRLAAEAELALSGRTWAPGVEALTHTLLSTAVNNMMLRDRWSLVAERRRQAGIAGHTYLQASEKFKMWGAEPVSAPARGYKNGAPESTDIPPGSIAAAPQGDRCPIVRQRGVALSPVLPPMNPVPTSGTPAPAP... | 3.4.21.97 | null | nuclear capsid assembly [GO:0039708]; proteolysis [GO:0006508]; viral release from host cell [GO:0019076] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252] | PF00716; | 3.20.16.10; | Herpesviridae capsid scaffolding protein family | PTM: Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release and tail site. {ECO:0000255|HAMAP-Rule:MF_04008}. | SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}. | CATALYTIC ACTIVITY: Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008}; | null | null | null | null | FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and s... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10211 | GB_HHV11 | MRQGAPARGRRWFVVWALLGLTLGVLVASAAPSSPGTPGVAAATQAANGGPATPAPPAPGAPPTGDPKPKKNRKPKPPKPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTSYAADRFK... | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF17416;PF17417;PF00606; | 1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280; | Herpesviridae glycoprotein B family | PTM: The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface (By similarity). {ECO:0000250}.; PTM: ubiquitinated. {ECO:0000269|PubMed:17686835}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:17686835}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane... | null | null | null | null | null | FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its hos... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10220 | LTP_HHV11 | MGGGNNTNPGGPVHKQAGSLASRAHMIAGTPPHSTMERGGDRDIVVTGARNQFAPDLEPGGSVSCMRSSLSFLSLIFDVGPRDVLSAEAIEGCLVEGGEWTRATAGPGPPRMCSIVELPNFLEYPGARGGLRCVFSRVYGEVGFFGEPAAGLLETQCPAHTFFAGPWALRPLSYTLLTIGPLGMGLFRDGDTAYLFDPHGLPEGTPAFIAKVRAGDMYPYLTYYTRDRPDVRWAGAMVFFVPSGPEPAAPADLTAAALHLYGASETYLQDEAFSERRVAITHPLRGEIAGLGEPCVGVGPREGVGGPGPHPPTAAQSPPP... | 3.4.19.12; 3.4.22.- | null | nuclear capsid assembly [GO:0039708]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway [GO:0039537]; viral DNA genome replication [GO:0039693] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | cysteine-type deubiquitinase activity [GO:0004843]; deNEDDylase activity [GO:0019784]; deubiquitinase activity [GO:0101005] | PF04843;PF03586; | 3.90.70.120; | Herpesviridae large tegument protein family | PTM: Proteolytically processed, possibly into several polypeptides. Enzymatic activity is only detectable following cleavage of the UL36 protein, which occurs late during viral replication. {ECO:0000269|PubMed:18216103}. | SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:18596102}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:17715218, ECO:0000269|PubMed:18385239, ECO:0000269|PubMed:23186167}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:17715218, ECO:0... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:161093... | null | null | null | null | FUNCTION: Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequ... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10221 | ITP_HHV11 | MADRGLPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSRE... | 3.5.1.-; 3.5.1.44 | null | microtubule-dependent intracellular transport of viral material towards cell periphery [GO:0039701]; symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway [GO:0039537]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition o... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | identical protein binding [GO:0042802]; protein-glutamine glutaminase activity [GO:0050568] | PF03970; | null | Herpesviridae inner tegument protein family | null | SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04043, ECO:0000269|PubMed:7856080}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04043, ECO:0000269|PubMed:20505007, ECO:0000269|PubMed:7856080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04043, ECO:0000269|PubMed:17223150, ECO:0000269|PubMed:7856080}. Host Go... | CATALYTIC ACTIVITY: Reaction=H2O + L-asparaginyl-[protein] = L-aspartyl-[protein] + NH4(+); Xref=Rhea:RHEA:57416, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:12804, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29961, ChEBI:CHEBI:50347; Evidence={ECO:0000269|PubMed:27866900, ECO:0000269|PubMed:30092200}; CATALYTIC ACTIVITY... | null | null | null | null | FUNCTION: Plays an essential role in cytoplasmic secondary envelopment during viral egress. Interacts with the capsid via the large tegument protein/LTP and participates in its transport to the host trans-Golgi network (TGN) where secondary envelopment occurs. Modulates tegumentation and capsid accumulation at the vira... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10226 | PAP_HHV11 | MTDSPGGVAPASPVEDASDASLGQPEEGAPCQVVLQGAELNGILQAFAPLRTSLLDSLLVMGDRGILIHNTIFGEQVFLPLEHSQFSRYRWRGPTAAFLSLVDQKRSLLSVFRANQYPDLRRVELAITGQAPFRTLVQRIWTTTSDGEAVELASETLMKRELTSFVVLVPQGTPDVQLRLTRPQLTKVLNATGADSATPTTFELGVNGKFSVFTTSTCVTFAAREEGVSSSTSTQVQILSNALTKAGQAAANAKTVYGENTHRTFSVVVDDCSMRAVLRRLQVGGGTLKFFLTTPVPSLCVTATGPNAVSAVFLLKPQKI... | null | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication [GO:0006260] | DNA polymerase complex [GO:0042575]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; DNA polymerase processivity factor activity [GO:0030337] | PF02282; | 3.70.10.10; | Herpesviridae DNA polymerase processivity factor family | null | SUBCELLULAR LOCATION: Host nucleus. | null | null | null | null | null | FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein UL9 loading onto DNA thus increasing its ability to ass... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10238 | ICP27_HHV11 | MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGQRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGP... | null | null | regulation of DNA-templated transcription [GO:0006355]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated suppression of host mRNA processing [GO:0039524] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF05459;PF16852; | null | HHV-1 ICP27 protein family | PTM: Methylated within the RGG box possibly by host PRMT1. When hypomethylated, ICP27 is exported to the cytoplasm earlier and more rapidly. {ECO:0000269|PubMed:19321610}.; PTM: Phosphorylated. {ECO:0000269|PubMed:10074178}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:9501050}. Host nucleus {ECO:0000269|PubMed:26062451, ECO:0000269|PubMed:9501050}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:9501050}. | null | null | null | null | null | FUNCTION: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of un... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P10242 | MYB_HUMAN | MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNH... | null | null | cellular response to hydrogen peroxide [GO:0070301]; cellular response to retinoic acid [GO:0071300]; erythrocyte differentiation [GO:0030218]; mitotic cell cycle [GO:0000278]; myeloid cell development [GO:0061515]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hematopoietic pr... | cytosol [GO:0005829]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF09316;PF07988;PF00249; | 1.10.10.60; | null | PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000305}.; PTM: SUMOylated by TRAF7; leading to MYB transcriptional activity inhibition. {ECO:0000250|UniProtKB:P06876}.; PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal degradation. {ECO:0000250}.;... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19646965}. | null | null | null | null | null | FUNCTION: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. | Homo sapiens (Human) |
P10243 | MYBA_HUMAN | MAKRSRSEDEDDDLQYADHDYEVPQQKGLKKLWNRVKWTRDEDDKLKKLVEQHGTDDWTLIASHLQNRSDFQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSLIAKHLKGRIGKQCRERWHNHLNPEVKKSSWTEEEDRIIYEAHKRLGNRWAEIAKLLPGRTDNSIKNHWNSTMRRKVEQEGYLQDGIKSERSSSKLQHKPCAAMDHMQTQNQFYIPVQIPGYQYVSPEGNCIEHVQPTSAFIQQPFIDEDPDKEKKIKELEMLLMSAENEVRRKRIPSQPGSFSSWSGSFLMDDNMSNTLNSLDEHTSE... | null | null | cell differentiation [GO:0030154]; male meiosis I [GO:0007141]; mitotic cell cycle [GO:0000278]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of piRNA transcription [GO:0140543]; positive regulation of transcription by RNA polymerase II [GO:0045944]; siRNA-mediated retrotransposo... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF09316;PF07988;PF13921;PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51960}. | null | null | null | null | null | FUNCTION: Transcription factor that specifically recognizes the sequence 5'-YAAC[GT]G-3' (PubMed:7987850, PubMed:8058310). Acts as a master regulator of male meiosis by promoting expression of piRNAs: activates expression of both piRNA precursor RNAs and expression of protein-coding genes involved in piRNA metabolism (... | Homo sapiens (Human) |
P10244 | MYBB_HUMAN | MSRRTRCEDLDELHYQDTDSDVPEQRDSKCKVKWTHEEDEQLRALVRQFGQQDWKFLASHFPNRTDQQCQYRWLRVLNPDLVKGPWTKEEDQKVIELVKKYGTKQWTLIAKHLKGRLGKQCRERWHNHLNPEVKKSCWTEEEDRIICEAHKVLGNRWAEIAKMLPGRTDNAVKNHWNSTIKRKVDTGGFLSESKDCKPPVYLLLELEDKDGLQSAQPTEGQGSLLTNWPSVPPTIKEEENSEEELAAATTSKEQEPIGTDLDAVRTPEPLEEFPKREDQEGSPPETSLPYKWVVEAANLLIPAVGSSLSEALDLIESDPD... | null | null | cellular response to leukemia inhibitory factor [GO:1990830]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly [GO:0090307]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytosol [GO:0005829]; Myb complex [GO:0031523]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF09316;PF13921;PF00249; | 1.10.10.60; | null | PTM: Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-520 is probably involved in transcriptional activity. {ECO:0000269|PubMed:10095772, ECO:0000269|PubMed:9840932}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene. {ECO:0000269|PubMed:10770937}. | Homo sapiens (Human) |
P10247 | HG2A_RAT | MDDQRDLISNHEQLPILGQRARAPESNCNRGVLYTSVSVLVALLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKSAKPVSPMRMATPLLMRPLSMDNMLQAPVKNVTKYGNMTQDHVMHLLTKSGPVNYPQLKGSFPENLKHLKNSMNGLDWKVFESWMKQWLLFEMSKNSLEEKQPTQTPPKVLTKCQEEVSHIPDVHPGAFRPKCDENGNYMPLQCHGSTGYCWCVFPNGTEVPHTKSRGRHNCSEPLDMEDPSSGLGVTKQDMGQMFL | null | null | antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; chaperone cofactor-dependent protein refolding [GO:0051085]; defense response [GO:0006952]; immunoglobulin mediated immune response [GO:0016064]; intracellular protein transp... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; macrophage migration inhib... | amyloid-beta binding [GO:0001540]; CD4 receptor binding [GO:0042609]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; macrophage migration inhibitory factor binding [GO:0035718]; MHC class II protein binding [GO:0042289]; MHC class II protein binding, via antigen binding groove [GO:0042658]; MHC... | PF09307;PF08831;PF00086; | 1.10.870.10;4.10.800.10; | null | null | SUBCELLULAR LOCATION: [Isoform Long]: Late endosome {ECO:0000250|UniProtKB:P04441}. Lysosome {ECO:0000250|UniProtKB:P04441}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04233}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P04233}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04... | null | null | null | null | null | FUNCTION: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Enhance also the st... | Rattus norvegicus (Rat) |
P10252 | CD48_RAT | MYFKKRRWFLILESLLLSLVTGFQDQSVPNVNAITGSNVTLTILKHPLASYQRLTWLHTTNQKILEYFPNGKKTVFESVFKDRVDLDKTNGALRIYNVSKEDRGDYYMRMLHETEDQWKITMEVYDLVSKPAIKIEKTKNLTDSCHLRLSCKVEDQGVDYTWYEDSGPFPQRNPGYVLEITITPHNKSTFYTCQVSNPVSSENDTLYFIPPCTLARSSGVHWIAAWLVVTLSIIPSILLA | null | null | mast cell activation [GO:0045576]; natural killer cell activation involved in immune response [GO:0002323]; signal transduction [GO:0007165]; T cell activation [GO:0042110] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; protein-containing complex [GO:0032991] | MHC class I protein binding [GO:0042288] | PF13895;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3181129}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:3181129}. Secreted {ECO:0000250|UniProtKB:P09326}. | null | null | null | null | null | FUNCTION: Glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that interacts via its N-terminal immunoglobulin domain with cell surface receptors including 2B4/CD244 or CD2 to regulate immune cell function and activation. Participates in T-cell signaling transduction by associating with CD2 and effici... | Rattus norvegicus (Rat) |
P10253 | LYAG_HUMAN | MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDV... | 3.2.1.20 | null | aorta development [GO:0035904]; cardiac muscle contraction [GO:0060048]; diaphragm contraction [GO:0002086]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; glycophagy [GO:0061723]; heart morphogenesis [GO:0003007]; locomotory behavior [GO:0007626]; lysosome organization [GO:0007040]; m... | autolysosome lumen [GO:0120282]; azurophil granule membrane [GO:0035577]; extracellular exosome [GO:0070062]; ficolin-1-rich granule membrane [GO:0101003]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; ... | alpha-1,4-glucosidase activity [GO:0004558]; alpha-glucosidase activity [GO:0090599]; carbohydrate binding [GO:0030246]; maltose alpha-glucosidase activity [GO:0032450] | PF13802;PF01055;PF21365;PF00088; | 3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10; | Glycosyl hydrolase 31 family | PTM: The different forms of acid glucosidase are obtained by proteolytic processing. {ECO:0000269|PubMed:3049072}.; PTM: Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor. | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000269|PubMed:17897319}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; Evidence={ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:1856189, ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:7717400}; | null | null | null | null | FUNCTION: Essential for the degradation of glycogen in lysosomes (PubMed:14695532, PubMed:18429042, PubMed:1856189, PubMed:7717400). Has highest activity on alpha-1,4-linked glycosidic linkages, but can also hydrolyze alpha-1,6-linked glucans (PubMed:29061980). {ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:18429042,... | Homo sapiens (Human) |
P10255 | CYPH_NEUCR | MFGPRHFSVLKTTGSLVSSTFSSSLKPTATFSCARAFSQTSSIMSKVFFDLEWEGPVLGPNNKPTSEIKAQSGRINFTLYDDVVPKTARNFKELCTGQNGFGYKGSSFHRIIPEFMLQGGDFTRGNGTGGKSIYGEKFADENFAKKHVRPGLLSMANAGPNTNGSQFFVTTVPTSWLDGRHVVFGEVADDESMKVVKALEATGSSSGAIRYSKKPTIVDCGAL | 5.2.1.8 | null | protein folding [GO:0006457] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family | null | SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P10258 | GAG_MMTVB | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSTSSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKIKKVVQRKENSEGKRKEKDSKAFLATDWNDDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVVKKKPQALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQ... | null | null | viral budding via host ESCRT complex [GO:0039702] | viral nucleocapsid [GO:0019013] | DNA binding [GO:0003677]; nucleotide binding [GO:0000166]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02337;PF00607;PF19317;PF00098;PF14787; | 1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:1331110}.; PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral ... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000269|PubMed:205999}. | null | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Binds strongly to viral nucleic acids and promotes their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid prote... | Mouse mammary tumor virus (strain BR6) (MMTV) |
P10262 | GAG_FLV | MGQTITTPLSLTLDHWSEVRARAHNQGVEVRKKKWITLCEAEWVMMNVGWPREGTFSLDNISQVEKKIFAPGPYGHPDQVPYITTWRSLATDPPSWVRPFLPPPKPPTPLPQPLSPQPSAPLTSSLYPVLPKSDPPKPPVLPPDPSSPLIDLLTEEPPPYPGGHGPPPSGPRTPTASPIASRLRERRENPAEESQALPLREGPNNRPQYWPFSASDLYNWKSHNPPFSQDPVALTNLIESILVTHQPTWDDCQQLLQALLTGEERQRVLLEARKQVPGEDGRPTQLPNVIDETFPLTRPNWDFATPAGREHLRLYRQLLL... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03332}.; PTM: RNA-binding phosphoprotein p12 is phosphoryl... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Feline leukemia virus |
P10265 | VPK10_HUMAN | WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSMEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMTKMGYIPGKGLGKNEDGIKVPVEAKINQEREGIGYPF | 3.4.23.50 | null | proteolysis [GO:0006508] | null | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676] | PF01585;PF00077; | 2.40.70.10; | Peptidase A2 family, HERV class-II K(HML-2) subfamily | PTM: Autoproteolytically processed at the N-terminus. Expected C-terminal autoprocessing not detected. The sequence shown is that of the processed Pro protein. | null | CATALYTIC ACTIVITY: Reaction=Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ- cleavage site.; EC=3.4.23.50; Evidence={ECO:0000269|PubMed:11278433, ECO:0000269|PubMed:9860826}; | null | null | null | null | FUNCTION: Retroviral proteases have roles in processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. This endogenous protein has retained most of the characteristics of retroviral proteases... | Homo sapiens (Human) |
P10269 | ENV_BAEVM | MGFTTKIIFLYNLVLVYAGFDDPRKAIELVQKRYGRPCDCSGGQVSEPPSDRVSQVTCSGKTAYLMPDQRWKCKSIPKDTSPSGPLQECPCNSYQSSVHSSCYTSYQQCRSGNKTYYTATLLKTQTGGTSDVQVLGSTNKLIQSPCNGIKGQSICWSTTAPIHVSDGGGPLDTTRIKSVQRKLEEIHKALYPELQYHPLAIPKVRDNLMVDAQTLNILNATYNLLLMSNTSLVDDCWLCLKLGPPTPLAIPNFLLSYVTRSSDNISCLIIPPLLVQPMQFSNSSCLFSPSYNSTEEIDLGHVAFSNCTSITNVTGPICAV... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; syncytium formation by plasma membrane fusion [GO:0000768]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by cont... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Baboon endogenous virus (strain M7) |
P10271 | PRO_MMTVB | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSTSSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKIKKVVQRKENSEGKRKEKDSKAFLATDWNDDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVVKKKPQALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQ... | 3.4.23.-; 3.6.1.23 | null | proteolysis [GO:0006508]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00692;PF02337;PF00607;PF19317;PF00077;PF00098;PF14787; | 1.10.1200.30;2.70.40.10;2.40.70.10;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Protease]: Released by autocatalytic processing. {ECO:0000269|PubMed:1331110}.; PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|U... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000269|PubMed:205999}. | CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000250|UniProtKB:P11283}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6 for protease. {ECO:0000269|PubMed:1331110}; | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein.... | Mouse mammary tumor virus (strain BR6) (MMTV) |
P10272 | POL_BAEVM | MGQTLTTPLSLTLTHFSDVRARAHNLSVGVRKGRWQTFCSSEWPTLHVGWPRDGTFDLSVILQVKTKVMDPGPHGHPDQVAYIITWEDLVRNPPPWVKPFLHTPSTSKSTLLALEVPKNRTLDPPKPVLPDESQQDLLFQDPLPHPPHNPLLEPPPYNSPSPPVLSPVSPTTPSAPTPSSLVSSSTPPSSPAPPELTPRTPPQTPRLRLRRAEGQDGPSTWQSSLFPLRTVNRTIQYWPFSASDLYNWKTHNPSFSQDPQALTSLIESILLTHQPTWDDCQQLLQVLLTTEERQRVLLEARKNVPGPGGLPTQLPNEIDE... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]; virion assembly [GO:0019068] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF09337; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03355}.; PTM: [RNA-binding phosphoprotein p12]: Phosph... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Baboon endogenous virus (strain M7) |
P10273 | POL_FLV | MGQTITTPLSLTLDHWSEVRARAHNQGVEVRKKKWITLCEAEWVMMNVGWPREGTFSLDNISQVEKKIFAPGPYGHPDQVPYITTWRSLATDPPSWVRPFLPPPKPPTPLPQPLSPQPSAPLTSSLYPVLPKSDPPKPPVLPPDPSSPLIDLLTEEPPPYPGGHGPPPSGPRTPTASPIASRLRERRENPAEESQALPLREGPNNRPQYWPFSASDLYNWKSHNPPFSQDPVALTNLIESILVTHQPTWDDCQQLLQALLTGEERQRVLLEARKQVPGEDGRPTQLPNVIDETFPLTRPNWDFATPAGREHLRLYRQLLL... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]; virion assembly [GO:0019068] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03355}.; PTM: [RNA-binding phosphoprotein p12]: Phosph... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Feline leukemia virus |
P10274 | PRO_HTL1A | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPARICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 3.4.23.- | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000269|PubMed:10037763, ECO:0000269|PubMed:12438640, ... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P10275 | ANDR_HUMAN | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGL... | null | null | activation of prostate induction by androgen receptor signaling pathway [GO:0060520]; androgen receptor signaling pathway [GO:0030521]; animal organ formation [GO:0048645]; cell-cell signaling [GO:0007267]; cellular response to estrogen stimulus [GO:0071391]; cellular response to steroid hormone stimulus [GO:0071383]; ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | androgen binding [GO:0005497]; ATPase binding [GO:0051117]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA pol... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated. Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity. {ECO:0000269|PubMed:11121022, ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20501646}.; PTM: Phosphorylated in prostate... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:15634333, ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107, ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:25091737}. Cytoplasm {ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107}. Note=Detected a... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues (PubMed:19022849). Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that rec... | Homo sapiens (Human) |
P10276 | RARA_HUMAN | MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTTLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLE... | null | null | apoptotic cell clearance [GO:0043277]; cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; cellular response to estrogen stimulus [GO:0071391]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to retinoic acid [GO:0071300]; chondroblast d... | actin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; RNA p... | alpha-actinin binding [GO:0051393]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; enzyme binding [G... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | PTM: Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular l... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19850744, ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:19850744, ECO:0000269|PubMed:28167758}. Note=Nuclear localization depends on ligand binding, phosphorylation and sumoylation (PubMed:19850744). Translocation to the nucleus in the absence of ligand is... | null | null | null | null | null | FUNCTION: Receptor for retinoic acid (PubMed:16417524, PubMed:19850744, PubMed:20215566). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes (PubMed:28167758). The RXR... | Homo sapiens (Human) |
P10279 | PRIO_BOVIN | MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG | 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]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; protein destabili... | cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | amyloid-beta binding [GO:0001540]; copper ion binding [GO:0005507]; cuprous ion binding [GO:1903136]; G-quadruplex RNA binding [GO:0002151]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; molecular condensate scaffold activity [GO:0140693]; protein-containing complex binding [GO:0044877]; typ... | 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 ... | Bos taurus (Bovine) |
P10284 | HXB4_MOUSE | MAMSSFLINSNYVDPKFPPCEEYSQSDYLPSDHSPGYYAGGQRRESGFQPEAAFGRRAPCTVQRYAACRDPGPPPPPPPPPPPPPPGLSPRAPVQPTAGALLPEPGQRSEAVSSSPPPPPCAQNPLHPSPSHSACKEPVVYPWMRKVHVSTVNPNYAGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRVEIAHALCLSERQIKIWFQNRRMKWKKDHKLPNTKIRSGGTAGAAGGPPGRPNGGPPAL | null | null | anterior/posterior pattern specification [GO:0009952]; bone marrow development [GO:0048539]; definitive hemopoiesis [GO:0060216]; embryonic skeletal system morphogenesis [GO:0048704]; hematopoietic stem cell differentiation [GO:0060218]; hematopoietic stem cell proliferation [GO:0071425]; hemopoiesis [GO:0030097]; morp... | centrosome [GO:0005813]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P10287 | CADH3_MOUSE | MELLSGPHAFLLLLLQVCWLRSVVSEPYRAGFIGEAGVTLEVEGTDLEPSQVLGKVALAGQGMHHADNGDIIMLTRGTVQGGKDAMHSPPTRILRRRKREWVMPPIFVPENGKGPFPQRLNQLKSNKDRGTKIFYSITGPGADSPPEGVFTIEKESGWLLLHMPLDREKIVKYELYGHAVSENGASVEEPMNISIIVTDQNDNKPKFTQDTFRGSVLEGVMPGTSVMQVTATDEDDAVNTYNGVVAYSIHSQEPKEPHDLMFTIHKSTGTISVISSGLDREKVPEYRLTVQATDMDGEGSTTTAEAVVQILDANDNAPEF... | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; hair cycle process... | adherens junction [GO:0005912]; catenin complex [GO:0016342]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. | Mus musculus (Mouse) |
P10288 | CADH2_CHICK | MCRIAGTPPRILPPLALMLLAALQQAPIKATCEDMLCKMGFPEDVHSAVVSRSVHGGQPLLNVRFQSCDENRKIYFGSSEPEDFRVGEDGVVYAERSFQLSAEPTEFVVSARDKETQEEWQMKVKLTPEPAFTGASEKDQKKIEDIIFPWQQYKDSSHLKRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKSLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIASFHLRAHAVDVNGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNAQNGMLRYRILSQAPSS... | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; brain morphogenesis [GO:0048854]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cartilage condensation [GO:0001502]; cell adhesion [GO:0007155]; cell agg... | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; cell body [GO:0044297]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cortical actin cyt... | alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; extracellular matrix binding [GO:0050840]; gamma-catenin binding [GO:0045295]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein phosphatase binding ... | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1638632, ECO:0000269|PubMed:2831236}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P15116}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {... | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion (PubMed:2831236). Cadherins may thus contribute to the sorting of heterogeneous cell types, and thereby play an important role during embryonic development (By similarity). Required for proper neurite branching, and ... | Gallus gallus (Chicken) |
P10290 | MYBC_MAIZE | MGRRACCAKEGVKRGAWTSKEDDALAAYVKAHGEGKWREVPQKAGLRRCGKSCRLRWLNYLRPNIRRGNISYDEEDLIIRLHRLLGNRWSLIAGRLPGRTDNEIKNYWNSTLGRRAGAGAGAGGSWVVVAPDTGSHATPAATSGACETGQNSAAHRADPDSAGTTTTSAAAVWAPKAVRCTGGLFFFHRDTTPAHAGETATPMAGGGGGGGGEAGSSDDCSSAASVSLRVGSHDEPCFSGDGDGDWMDDVRALASFLESDEDWLRCQTAGQLA | null | null | cell differentiation [GO:0030154]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Controls the expression of genes involved in anthocyanin biosynthesis. Regulates the expression of at least 3 structural genes: chalcone synthase, dihydroflavonol reductase and flavonol O(3) glucosyltransferase. C1 acts as a trans-acting factor. | Zea mays (Maize) |
P10297 | RIP1_PHYAM | MKSMLVVTISIWLILAPTSTWAVNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTYNQNAMFPQLIMSTYYNYMVNLGDLFEGF | 3.2.2.22 | null | defense response to virus [GO:0051607]; negative regulation of translation [GO:0017148] | null | rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729] | PF00161; | 3.40.420.10;4.10.470.10; | Ribosome-inactivating protein family, Type 1 RIP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22; Evidence={ECO:0000269|PubMed:10403789, ECO:0000269|PubMed:10595542, ECO:0000269|PubMed:2930487}; | null | null | null | null | FUNCTION: Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein synthesis (PubMed:10403789, PubMed:10595542, PubMed:2248976, PubMed:2930487, PubMed:6091760). Releases both adenine and guanine from Escherichia coli rRNA in vitro. Activity on guanine is... | Phytolacca americana (American pokeweed) (Phytolacca decandra) |
P10299 | GSTP1_CAEEL | MTLKLTYFDIHGLAEPIRLLLADKQVAYEDHRVTYEQWADIKPKMIFGQVPCLLSGDEEIVQSGAIIRHLARLNGLNGSNETETTFIDMFYEGLRDLHTKYTTMIYRNYEDGKAPYIKDVLPGELARLEKLFHTYKNGEHYVIGDKESYADYVLFEELDIHLILTPNALDGVPALKKFHERFAERPNIKAYLNKRAAINPPVNGNGKQ | 2.5.1.18 | null | cellular detoxification [GO:1990748]; defense response to Gram-negative bacterium [GO:0050829]; glutathione metabolic process [GO:0006749]; innate immune response [GO:0045087]; negative regulation of cellular response to manganese ion [GO:1905803]; positive regulation of cellular response to manganese ion [GO:1905804] | cytosol [GO:0005829] | glutathione transferase activity [GO:0004364] | PF14497;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Pi 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:0000250|UniProtKB:P09211}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (By similarity). Prevents dopaminergic CEP neuron degeneration in response to Mn(2+) (PubMed:23721876). {ECO:0000250|UniProtKB:P09211, ECO:0000269|PubMed:23721876}. | Caenorhabditis elegans |
P10300 | CD8B_MOUSE | MQPWLWLVFSMKLAALWSSSALIQTPSSLLVQTNHTAKMSCEVKSISKLTSIYWLRERQDPKDKYFEFLASWSSSKGVLYGESVDKKRNIILESSDSRRPFLSIMNVKPEDSDFYFCATVGSPKMVFGTGTKLTVVDVLPTTAPTKKTTLKMKKKKQCPFPHPETQKGLTCSLTTLSLLVVCILLLLAFLGVAVYFYCVRRRARIHFMKQFHK | null | null | adaptive immune response [GO:0002250]; T cell activation [GO:0042110]; T cell receptor signaling pathway [GO:0050852] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | coreceptor activity [GO:0015026]; MHC class I protein binding [GO:0042288] | PF07686; | 2.60.40.10; | null | PTM: Palmitoylated at the cytoplasmic tail and thereby targets the heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers. {ECO:0000250|UniProtKB:P10966}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10966}; Single-pass type I membrane protein. Note=Requires the partner CD8A for efficient cell surface expression. The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation. {ECO:0000250|UniProtKB:P10966}. | null | null | null | null | null | FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are de... | Mus musculus (Mouse) |
P10301 | RRAS_HUMAN | MSSGAASGTGRGRPRGGGPGPGDPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICSVDGIPARLDILDTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPVVLVGNKADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVDEAFEQLVRAVRKYQEQELPPSPPSAPRKKGGGCPCVLL | 3.6.5.- | null | face morphogenesis [GO:0060325]; leukocyte differentiation [GO:0002521]; negative regulation of Schwann cell migration [GO:1900148]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matrix adhesion via fibronectin [... | extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: S-palmitoylated by ZDHHC19, leading to increased association with membranes and with rafts/caveolae as well as enhanced cell viability. {ECO:0000269|PubMed:20074548}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P62070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6207... | null | null | null | null | FUNCTION: Regulates the organization of the actin cytoskeleton (PubMed:16537651, PubMed:18270267). With OSPBL3, modulates integrin beta-1 (ITGB1) activity (PubMed:18270267). {ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:18270267}. | Homo sapiens (Human) |
P10310 | TERL_BPT3 | MSTQSNRNALVVAQLKGDFVAFLFVLWKALNLPVPTKCQIDMAKVLANGDNKKFILQAFRGIGKSFITCAFVVWTLWRDPQLKILIVSASKERADLNSIFIKNIIDLLPFLDELKPSPGQRDSVISFDVGPAKPDHSPSVKSVGITGQLTGSRADIIIADDVEIPSNSATQGAREKLWTLVQEFRALLKPLPTSRVIYLGTPQTEMTLYKELEDNRGYTTIIWPALYPRSREEDLYYGERLAPMLREEFNDGFEMLQGQPTDPVRFDMEDLRERELEYGKAGFTLQFMLNPNLSDAEKYPLRLRDAIVCGLDFEKAPMHY... | 3.1.21.-; 3.6.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04147, ECO:0000269|PubMed:3617498, ECO:0000269|PubMed:3754362, ECO:0000305|PubMed:8289246}; | chromosome organization [GO:0051276]; viral DNA genome packaging [GO:0019073] | viral terminase, large subunit [GO:0098009] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | null | 3.40.50.300; | Teseptimavirus large terminase family | null | null | null | null | null | null | null | FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome at a unique and precise dsDNA sequence to initiate and to end a packaging reaction (PubMed:3617498, PubMed:3754362). The terminase lies a... | Enterobacteria phage T3 (Bacteriophage T3) |
P10321 | HLAC_HUMAN | MRVMAPRALLLLLSGGLALTETWACSHSMRYFDTAVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPRGEPRAPWVEQEGPEYWDRETQKYKRQAQADRVSLRNLRGYYNQSEDGSHTLQRMSGCDLGPDGRLLRGYDQSAYDGKDYIALNEDLRSWTAADTAAQITQRKLEAARAAEQLRAYLEGTCVEWLRRYLENGKETLQRAEPPKTHVTHHPLSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHMQHEGLQEPLTLSWEPSSQPTIPIMGIVAGLAVLVV... | null | null | adaptive immune response [GO:0002250]; 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]; innate immune response [GO... | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]; TAP binding [GO:0046977] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | null | PTM: N-linked glycosylation at Asn-110 is required for efficient interaction with CANX and CALR chaperones and appropriate HLA-C-B2M folded conformers prior to peptide loading. {ECO:0000269|PubMed:18420581, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18420581, ECO:0000269|PubMed:20972337, ECO:0000269|PubMed:28649982}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:18420581}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Antigen-presenting major histocompatibility complex class I (MHCI) molecule with an important role in reproduction and antiviral immunity (PubMed:11172028, PubMed:20104487, PubMed:20439706, PubMed:20972337, PubMed:24091323, PubMed:28649982, PubMed:29312307). In complex with B2M/beta 2 microglobulin displays a... | Homo sapiens (Human) |
P10323 | ACRO_HUMAN | MVEMLPTAILLVLAVSVVAKDNATCDGPCGLRFRQNPQGGVRIVGGKAAQHGAWPWMVSLQIFTYNSHRYHTCGGSLLNSRWVLTAAHCFVGKNNVHDWRLVFGAKEITYGNNKPVKAPLQERYVEKIIIHEKYNSATEGNDIALVEITPPISCGRFIGPGCLPHFKAGLPRGSQSCWVAGWGYIEEKAPRPSSILMEARVDLIDLDLCNSTQWYNGRVQPTNVCAGYPVGKIDTCQGDSGGPLMCKDSKESAYVVVGITSWGVGCARAKRPGIYTATWPYLNWIASKIGSNALRMIQSATPPPPTTRPPPIRPPFSHPI... | 3.4.21.10 | null | acrosome matrix dispersal [GO:0002077]; acrosome reaction [GO:0007340]; activation of adenylate cyclase activity [GO:0007190]; binding of sperm to zona pellucida [GO:0007339]; penetration of zona pellucida [GO:0007341]; response to steroid hormone [GO:0048545]; single fertilization [GO:0007338] | acrosomal matrix [GO:0043159]; extracellular region [GO:0005576]; Golgi-associated vesicle [GO:0005798]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | amidase activity [GO:0004040]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; fucose binding [GO:0042806]; mannose binding [GO:0005537]; protease binding [GO:0002020]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; zinc ion binding [GO:0008270] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10; | null | null | null | null | FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. {ECO:0000269|PubMed:37004249}. | Homo sapiens (Human) |
P10333 | MS2A_DROME | MNQILLCSPILLLLFTVASCDSEQQLDSAMHLKSDSTKSASLKNVAPKNDETQAKIAKDDVALKDAKKGDYIMDIDISDLPLDDYPINRSKSLKSSSIDLNNIPFNKGLDDFPAKEKNQGSNQSALKALQQRLLTEQNNSLLLRNHSIYLMKEIEARKTDIIKVRQLNLDLELELNTVNRRLLELNGQLQNTRKSTKPCKKRSSKDSAPPAANQFQEANVRNTYRNKYLTLLKELSQKINNEIAKVATDVPTETNPSQGNLPTL | null | null | mating [GO:0007618]; positive regulation of octopamine signaling pathway [GO:2000130]; positive regulation of ovulation [GO:0060279]; sexual reproduction [GO:0019953]; sperm competition [GO:0046692] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | identical protein binding [GO:0042802] | PF03082; | null | null | PTM: Glycosylation. {ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:7556947}.; PTM: Undergoes several cleavages as it is secreted and is further processed in the recipient female (PubMed:10612039, PubMed:2257979, PubMed:24514904, PubMed:3142802, PubMed:7556947). The precursor molecule is proteolytically cleaved by the ... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3142802}. Cytoplasm {ECO:0000269|PubMed:2257979}. Note=In 1 day old virgin males, secreted into the cytoplasm of accessory gland cells (PubMed:2257979). In 5 day old males it localizes to cytoplasmic vesicles of the secondary cells (PubMed:2257979). {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Male seminal protein which enhances ovulation in female Drosophila by stimulating the release of oocytes by the ovary following mating (PubMed:10662669, PubMed:15640356, PubMed:24101486, PubMed:7479736). Acts by increasing octopamine (OA) neuronal signaling in the female genital tract leading to the postmatin... | Drosophila melanogaster (Fruit fly) |
P10342 | ISOA_PSEAY | MKCPKILAALLGCAVLAGVPAMPAHAAINSMSLGASYDAQQANITFRVYSSQATRIVLYLYSAGYGVQESATYTLSPAGSGVWAVTVPVSSIKAAGITGAVYYGYRAWGPNWPYASNWGKGSQAGFVSDVDANGDRFNPNKLLLDPYAQEVSQDPLNPSNQNGNVFASGASYRTTDSGIYAPKGVVLVPSTQSTGTKPTRAQKDDVIYEVHVRGFTEQDTSIPAQYRGTYYGAGLKASYLASLGVTAVEFLPVQETQNDANDVVPNSDANQNYWGYMTENYFSPDRRYAYNKAAGGPTAEFQAMVQAFHNAGIKVYMDVV... | 3.2.1.68 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9719642}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:9719642}; | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576] | isoamylase activity [GO:0019156]; metal ion binding [GO:0046872] | PF00128;PF02922;PF21331; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2248978}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; Evidence={ECO:0000269|PubMed:2248978}; | null | null | null | null | null | Pseudomonas amyloderamosa |
P10351 | XDH_DROME | MSNSVLVFFVNGKKVTEVSPDPECTLLTFLREKLRLCGTKLGCAEGGCGACTVMVSRLDRRANKIRHLAVNACLTPVCSMHGCAVTTVEGIGSTKTRLHPVQERLAKAHGSQCGFCTPGIVMSMYALLRNAEQPSMRDLEVAFQGNLCRCTGYRPILEGYKTFTKEFACGMGEKCCKVSGKGCGTDAETDDKLFERSEFQPLDPSQEPIFPPELQLSDAFDSQSLIFSSDRVTWYRPTNLEELLQLKAKHPAAKLVVGNTEVGVEVKFKHFLYPHLINPTQVKELLEIKENQDGIYFGAAVSLMEIDALLRQRIEQLPES... | 1.17.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P2298... | arginine metabolic process [GO:0006525]; compound eye pigmentation [GO:0048072]; determination of adult lifespan [GO:0008340]; glycerophospholipid metabolic process [GO:0006650]; purine nucleobase metabolic process [GO:0006144]; pyrimidine nucleobase metabolic process [GO:0006206]; tryptophan metabolic process [GO:0006... | peroxisome [GO:0005777] | 2 iron, 2 sulfur cluster binding [GO:0051537]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdopterin cofactor binding [GO:0043546]; xanthine dehydrogenase activity [GO:0004854] | PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate; Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.17.1.4; CATALYTIC ACTIVITY: Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine; Xref=Rhea:RH... | null | null | null | null | FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity). {ECO:0000250, ECO:0000269|PubMed:3036645}. | Drosophila melanogaster (Fruit fly) |
P10354 | CMGA_RAT | MRSSAALALLLCAGQVFALPVNSPMTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERVLSILRHQNLLKELQDLALQGAKERAQQQQQQQQQQQQQQQQQQQQHSSFEDELSEVFENQSPAAKHGDAASEAPSKDTVEKREDSDKGQQDAFEGTTEGPRPQAFPEPKQESSMMGNSQSPGEDTANNTQSPTSLPSQEHGIPQTTEGSERGPSAQQQARKAKQEEKEEEEEEKEEEEEEKEEKAIAREKAGPKEVPTAASSSHFYSGYKKIQKDDDGQSESQAVNGKTGASEAVPSEGKGELEHSQQEEDGEE... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation [GO:0086030]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; mast cell activation [GO:0045576]; mast c... | chromaffin granule [GO:0042583]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; perinuclear region of cytoplasm [GO:0048471]; secretory granule [GO:0030141]; transport vesicle [GO:0030133] | null | PF01271; | null | Chromogranin/secretogranin protein family | PTM: O-glycosylated; contains chondroitin sulfate (CS). CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro. {ECO:0000250|UniProtKB:P10645}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:3896848}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000269|PubMed:29166604}. Secreted. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that... | null | null | null | null | null | FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: Catestatin inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. Can induce mast cell migration, degranulation and producti... | Rattus norvegicus (Rat) |
P10358 | POLR_TYMV | MAFQLALDALAPTTHRDPSLHPILESTVDSIRSSIQTYPWSIPKELLPLLNSYGIPTSGLGTSHHPHAAHKTIETFLLCTHWSFQATTPSSVMFMKPSKFNKLAQVNSNFRELKNYRLHPNDSTRYPFTSPDLPVFPTIFMHDALMYYHPSQIMDLFLRKPNLERLYASLVVPPEAHLSDQSFYPKLYTYTTTRHTLHYVPEGHEAGSYNQPSDAHSWLRINSIRLGNHHLSVTILESWGPVHSLLIQRGTPPPDPSLQAPPTLMTSDLFRSYQEPRLDVVSFRIPDAIELPQATFLQQPLRDRLVPRAVYNALFTYTRA... | 2.1.1.-; 2.7.7.48; 3.4.19.12; 3.4.22.-; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; RNA processing [GO:0006396]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; viral RNA genome replication [GO:0039694] | null | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF05381;PF00978;PF19227;PF01443;PF01660; | 3.90.70.100;3.40.50.300; | Tymovirus NS35 RNA replicase polyprotein family | null | SUBCELLULAR LOCATION: [Methyltransferase/Protease/Ubiquitinyl hydrolase]: Host chloroplast envelope.; SUBCELLULAR LOCATION: [Putative helicase]: Host chloroplast envelope.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host chloroplast envelope {ECO:0000269|PubMed:11222099}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:22117220, ECO:0000269|PubMed:23345508};... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70.2 uM for Ub-AMC {ECO:0000269|PubMed:23345508}; | null | null | null | FUNCTION: Acts as a cysteine protease, methyltransferase and deubiquitinase (Probable) (PubMed:22117220, PubMed:23966860, PubMed:29117247, PubMed:32732284). The cysteine protease activity cleaves the polyprotein giving rise to mature proteins (PubMed:23966860). The methyltransferase domain is probably involved in viral... | Turnip yellow mosaic virus |
P10360 | P53_CHICK | MAEEMEPLLEPTEVFMDLWSMLPYSMQQLPLPEDHSNWQELSPLEPSDPPPPPPPPPLPLAAAAPPPLNPPTPPRAAPSPVVPSTEDYGGDFDFRVGFVEAGTAKSVTCTYSPVLNKVYCRLAKPCPVQVRVGVAPPPGSSLRAVAVYKKSEHVAEVVRRCPHHERCGGGTDGLAPAQHLIRVEGNPQARYHDDETTKRHSVVVPYEPPEVGSDCTTVLYNFMCNSSCMGGMNRRPILTILTLEGPGGQLLGRRCFEVRVCACPGRDRKIEEENFRKRGGAGGVAKRAMSPPTEAPEPPKKRVLNPDNEIFYLQVRGRRR... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; DNA damage response [GO:0006974]; positive regulation of apoptotic process [GO:0043065]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein tetramerization [GO:0051262]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00870;PF07710; | 2.60.40.720;4.10.170.10; | P53 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of t... | Gallus gallus (Chicken) |
P10361 | P53_RAT | MEDSQSDMSIELPLSQETFSCLWKLLPPDDILPTTATGSPNSMEDLFLPQDVAELLEGPEEALQVSAPAAQEPGTEAPAPVAPASATPWPLSSSVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSISLNKLFCQLAKTCPVQLWVTSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNPYAEYLDDRQTFRHSVVVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEEHCPELPPGSAKRALPTSTSSSPQQKKKP... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; autophagy [GO:0006914]; B cell lineage commitment [GO:0002326]; bone marrow development [GO:0048539]; cardiac muscle cell apoptotic process [GO:0010659]; cardiac septum morphogenesis [GO:0060411]; cell population proliferation [GO:0008283]; cellu... | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; germ cell nucleus [GO:0043073]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:000... | 14-3-3 protein binding [GO:0071889]; ATP-dependent DNA/DNA annealing activity [GO:0036310]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; copper ion binding [GO:0005507]; core promoter sequence-specific DNA binding [GO:0001046]; disordered domain specific binding [GO:... | PF00870;PF08563;PF07710; | 2.60.40.720;6.10.50.20;4.10.170.10; | P53 family | PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which p... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, cen... | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of t... | Rattus norvegicus (Rat) |
P10362 | SCG2_RAT | MTESKAYRFGAVLLLIHLIFLVPGTEAASFQRNQLLQKEPDLRLENVQKFPSPEMIRALEYIEKLRQQAHREESSPDYNPYQGISVPLQLKENGEESHLAESSRDVLSEDEWMRIILEALRQAENEPPSALKENKPYALNLEKNFPVDTPDDYETQQWPERKLKHMRFPLMYEENSRENPFKRTNEIVEEQYTPQSLATLESVFQELGKLTGPSNQKRERVDEEQKLYTDDEDDVYKTNNIAYEDVVGGEDWSPMEEKIETQTQEEVRDSKENTEKNEQINEEMKRSGHLGLPDEGNRKESKDQLSEDASKVITYLRRLV... | null | null | angiogenesis [GO:0001525]; eosinophil chemotaxis [GO:0048245]; induction of positive chemotaxis [GO:0050930]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway [G... | dense core granule [GO:0031045]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; secretory granule [GO:0030141] | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125] | PF01271; | null | Chromogranin/secretogranin protein family | null | SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. | null | null | null | null | null | FUNCTION: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules. {ECO:0000250|UniProtKB:P13521}. | Rattus norvegicus (Rat) |
P10363 | PRI1_YEAST | MTNSVKTNGPSSSDMEYYYKSLYPFKHIFNWLNHSPKPSRDMINREFAMAFRSGAYKRYNSFNSVQDFKAQIEKANPDRFEIGAIYNKPPRERDTLLKSELKALEKELVFDIDMDDYDAFRTCCSGAQVCSKCWKFISLAMKITNTALREDFGYKDFIWVFSGRRGAHCWVSDKRARALTDVQRRNVLDYVNVIRDRNTDKRLALKRPYHPHLARSLEQLKPFFVSIMLEEQNPWEDDQHAIQTLLPALYDKQLIDSLKKYWLDNPRRSSKEKWNDIDQIATSLFKGPKQDSHIIKLRECKEDLVLMTLYPKLDVEVTKQ... | 2.7.7.- | null | DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269] | alpha DNA polymerase:primase complex [GO:0005658]; nuclear replication fork [GO:0043596] | ATP binding [GO:0005524]; DNA primase activity [GO:0003896]; metal ion binding [GO:0046872] | PF01896; | 3.90.920.10; | Eukaryotic-type primase small subunit family | null | null | null | null | null | null | null | FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active cente... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10370 | HISX_SALTY | MSFNTLIDWNSCSPEQQRALLTRPAISASDSITRTVSDILDNVKTRGDDALREYSAKFDKTEVTALRVTPEEIAAAGARLSDELKQAMTAAVKNIETFHSAQTLPPVDVETQPGVRCQQVTRPVSSVGLYIPGGSAPLFSTVLMLATPARIAGCQKVVLCSPPPIADEILYAAQLCGVQEIFNVGGAQAIAALAFGSESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGATPDFVASDLLSQAEHGPDSQVILLTPDADIARKVAEAVERQLAELPRADTARQALSASRLIVTKDLAQCVAIS... | 1.1.1.23 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:2665648}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:2665648}; Note=Binds 1 zinc ion per subunit. At high pH manganese can replace zinc. {ECO:0000269|PubMed:2665648}; | histidine biosynthetic process [GO:0000105] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | histidinol dehydrogenase activity [GO:0004399]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270] | PF00815; | 1.20.5.1300;3.40.50.1980; | Histidinol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; | null | PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. | null | null | FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P10378 | ENTE_ECOLI | MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDSIAVIDGERQLSYRELNQAADNLACSLRRQGIKPGETALVQLGNVAELYITFFALLKLGVAPVLALFSHQRSELNAYASQIEPALLIADRQHALFSGDDFLNTFVTEHSSIRVVQLLNDSGEHNLQDAINHPAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSVEICQFTQQTRYLCAIPAAHNYAMSSPGSLGVFLAGGTVVLAADPSATLCFPLIEKHQVNVTALVPPAVSLWLQALIEGESRAQLASLKLLQVGGARLSATLAARI... | 6.2.1.71; 6.3.2.14 | null | enterobactin biosynthetic process [GO:0009239] | cytosol [GO:0005829]; membrane [GO:0016020] | (2,3-dihydroxybenzoyl)adenylate synthase activity [GO:0008668]; 2,3-dihydroxybenzoate-serine ligase activity [GO:0047527]; acyltransferase activity [GO:0016746]; ATP binding [GO:0005524] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family, EntE subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10692387}. | CATALYTIC ACTIVITY: Reaction=3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6 diphosphate + enterobactin + 4 H(+); Xref=Rhea:RHEA:30571, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805, ChEBI:CHEBI:456215; EC=6.3.2.14; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 uM for holo-EntB (at pH 8.8 and 37 degrees Celsius) {ECO:0000269|PubMed:9214294}; KM=0.5 uM for holo-EntB {ECO:0000269|PubMed:16567620}; KM=2.5 uM for DHB (at pH 7.8 and 25 degrees Celsius) {ECO:0000269|PubMed:20359185}; KM=2.7 uM for DHB {ECO:0000269|PubMed:25... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000305|PubMed:9485415}. | null | null | FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) a... | Escherichia coli (strain K12) |
P10383 | OTU_DROME | MDMQVQRPITSGSRQAPDPYDQYLESRGLYRKHTARDASSLFRVIAEQMYDTQMLHYEIRLECVRFMTLKRRIFEKEIPGDFDSYMQDMSKPKTYGTMTELRAMSCLYRRNVILYEPYNMGTSVVFNRRYAENFRVFFNNENHFDSVYDVEYIERAAICQSIAFKLLYQKLFKLPDVSFAVEIMLHPHTFNWDRFNVEFDDKGYMVRIHCTDGRVFKLDLPGDTNCILENYKLCNFHSTNGNQSINARKGGRLEIKNQEERKASGSSGHEPNDLLPMCPNRLESCVRQLLDDGISPFPYKVAKSMDPYMYRNIEFDCWND... | null | null | female germ-line sex determination [GO:0019099]; germ cell development [GO:0007281]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; oogenesis [GO:0048477]; positive regulation of DNA endoreduplication [GO:0032877]; positive regulation of stem cell differentiation [GO:2000738]; ... | cytosol [GO:0005829] | cysteine-type deubiquitinase activity [GO:0004843]; deubiquitinase activity [GO:0101005]; mRNA binding [GO:0003729]; serine-type peptidase activity [GO:0008236] | PF02338; | 3.90.70.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1737618}. | null | null | null | null | null | FUNCTION: Essential for female fertility; germ cell division and differentiation. {ECO:0000269|PubMed:1737618}. | Drosophila melanogaster (Fruit fly) |
P10398 | ARAF_HUMAN | MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGS... | 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}; | MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; protein modification process [GO:0036211]; Ras protein signal transduction [GO:0007265]; regulation of proteasomal ubiquitin-dependent prot... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; 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. Phosphorylates PFKFB2 (PubMed:36402789). {ECO:0000269|PubMed:22609986, ECO:0000269|PubMed:36402789}.; FUNCTION: [Isoform 2]: Serves as a positive regulator of myogenic differen... | Homo sapiens (Human) |
P10404 | ENV1_MOUSE | MEGPAFSKPLKDKINPWGPLIVLGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRRNTPQNQGPCYDSSAVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRQVLNIGPRVPIGPNPVITDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAGPPYYEG... | null | null | null | plasma membrane [GO:0005886] | metal ion binding [GO:0046872] | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be ... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Mus musculus (Mouse) |
P10408 | SECA_ECOLI | MLIKLLTKVFGSRNDRTLRRMRKVVNIINAMEPEMEKLSDEELKGKTAEFRARLEKGEVLENLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNERCIAEMRTGEGKTLTATLPAYLNALTGKGVHVVTVNDYLAQRDAENNRPLFEFLGLTVGINLPGMPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYKRVNKIIPHLIRQEKEDSETFQGEGHFSVDEKSRQVNLTERGLVLIEELLVKEGIMDEGESLYSPANIMLMHHVTAALRAHALF... | 7.4.2.8 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:10213615}; Note=Binds 1 zinc ion per subunit. Zinc is required for binding of the SecB chaperone to the extreme C-terminus of SecA. {ECO:0000269|PubMed:10213615}; | chaperone-mediated protein folding [GO:0061077]; intracellular protein transmembrane transport [GO:0065002]; protein import [GO:0017038]; protein secretion [GO:0009306]; protein targeting [GO:0006605]; protein targeting to membrane [GO:0006612]; protein transport [GO:0015031]; protein transport by the Sec complex [GO:0... | cell envelope Sec protein transport complex [GO:0031522]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; preprotein binding [GO:0070678]; protein-exporting ATPase activity [GO:0008564]; ribonucleoprotein complex binding [GO:0043021]; ribosome binding [GO:0043022]; zinc ion binding [GO:0008270] | PF21090;PF02810;PF07517;PF01043;PF07516; | 1.10.3060.10;3.40.50.300;3.90.1440.10; | SecA family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:1825804, ECO:0000269|PubMed:2542029, ECO:0000305|PubMed:2153463}; | null | null | null | null | FUNCTION: Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving... | Escherichia coli (strain K12) |
P10412 | H14_HUMAN | MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK | null | null | chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334] | heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1. {ECO:0000269|PubMed:15469825}.; PTM: Ci... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Homo sapiens (Human) |
P10415 | BCL2_HUMAN | MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK | null | null | actin filament organization [GO:0007015]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; axonogenesis [GO:0007409]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; B cell lineage commitment [GO:0002326]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:00... | BAD-BCL-2 complex [GO:0097138]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nuclear membrane [GO:0031965]; nucleus ... | BH3 domain binding [GO:0051434]; channel activity [GO:0015267]; channel inhibitor activity [GO:0016248]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]... | PF00452;PF02180; | 1.10.437.10; | Bcl-2 family | PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:11368354). Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle (PubMed:11368354). In the absence of growth factors, BCL2 appears... | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21358617, ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed:1508712, PubMed:8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed:11368354). Appears to function in a feedback loop system with caspases (PubMed... | Homo sapiens (Human) |
P10417 | BCL2_MOUSE | MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDADAAPLGAAPTPGIFSFQPESNPMPAVHRDMAARTSPLRPLVATAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK | null | null | actin filament organization [GO:0007015]; animal organ morphogenesis [GO:0009887]; apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; axonogenesis [GO:0007409]; B cell apoptotic process [GO:0001783]; B cell differentiation [GO:0030183]; B cell homeostasis [GO:0... | BAD-BCL-2 complex [GO:0097138]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:00057... | BH domain binding [GO:0051400]; BH3 domain binding [GO:0051434]; channel activity [GO:0015267]; channel inhibitor activity [GO:0016248]; DNA-binding transcription factor binding [GO:0140297]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803];... | PF00452;PF02180; | 1.10.437.10; | Bcl-2 family | PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:9115213). Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle (PubMed:9115213). In the absence of growth factors, BCL2 appears t... | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:000... | null | null | null | null | null | FUNCTION: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the releas... | Mus musculus (Mouse) |
P10443 | DPO3A_ECOLI | MSEPRFVHLRVHSDYSMIDGLAKTAPLVKKAAALGMPALAITDFTNLCGLVKFYGAGHGAGIKPIVGADFNVQCDLLGDELTHLTVLAANNTGYQNLTLLISKAYQRGYGAAGPIIDRDWLIELNEGLILLSGGRMGDVGRSLLRGNSALVDECVAFYEEHFPDRYFLELIRTGRPDEESYLHAAVELAEARGLPVVATNDVRFIDSSDFDAHEIRVAIHDGFTLDDPKRPRNYSPQQYMRSEEEMCELFADIPEALANTVEIAKRCNVTVRLGEYFLPQFPTGDMSTEDYLVKRAKEGLEERLAFLFPDEEERLKRRPE... | 2.7.7.7 | null | DNA-templated DNA replication [GO:0006261]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA polymerase III complex [GO:0009360]; DNA polymerase III, core complex [GO:0044776]; replisome [GO:0030894] | DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887] | PF07733;PF17657;PF20914;PF14579;PF02811;PF01336; | 1.10.150.870;1.10.10.1600;3.20.20.140;2.40.50.140; | DNA polymerase type-C family, DnaE subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:2932432}; | null | null | null | null | FUNCTION: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria (PubMed:2932432). This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit (PubMed:2932432). It is tethered to replicating DNA by the... | Escherichia coli (strain K12) |
P10451 | OSTP_HUMAN | MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN | null | null | androgen catabolic process [GO:0006710]; biomineral tissue development [GO:0031214]; cell adhesion [GO:0007155]; cellular response to testosterone stimulus [GO:0071394]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; negative regulation of collateral sprouting of intact axon in response to injury [GO:0... | cell projection [GO:0042995]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178]; ion binding [GO:0043167]; small molecule binding [GO:0036094] | PF00865; | null | Osteopontin family | PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers, increasing its collagen binding properties. {ECO:0000250|UniProtKB:P31096}.; PTM: Extensively phosphorylated by FAM20C in the extracellular med... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. | null | null | null | null | null | FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin... | Homo sapiens (Human) |
P10477 | CELE_ACET2 | MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTI... | 3.1.1.-; 3.1.1.72; 3.2.1.4 | null | cellulose catabolic process [GO:0030245]; glucomannan catabolic process [GO:2000884]; xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | acetylxylan esterase activity [GO:0046555]; cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF17996;PF00150;PF00404;PF00657; | 1.10.1330.10;2.60.120.260;3.20.20.80;3.40.50.1110; | Glycosyl hydrolase 5 (cellulase A) family; Carbohydrate esterase 2 (CE2) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}; CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=165 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:19338387}; KM=2.7 mM for acetylated birchwood xylan {ECO:0000269|PubMed:19338387}; KM=0.019 mM for acetylated glucomannan {ECO:0000269|PubMed:19338387}; Note=kcat is 7032 min(-1) for the deacetylation of 4-nitrop... | PATHWAY: Glycan metabolism; cellulose degradation. {ECO:0000269|PubMed:3066698}.; PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19338387}. | null | null | FUNCTION: Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:1991028, PubMed:3066698). Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preferenc... | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
P10486 | T1R1_ECOLX | MTHQTHTIAESNNFIVLDKYIKAEPTGDSYQSESDLERELIQDLRNQGYEFISVKSQSAMLANVREQLQNLNGVVFNDSEWRRFTEQYLDNPSDGILDKTRKIHIDYICDFIFDDERLENIYLIDKKNLMRNKVQIIQQFEQAGSHANRYDVTILVNGLPLVQIELKKRGVAIREAFNQIHRYSKESFNSENSLFKYLQLFVISNGTDTRYFANTTKRDKNSFDFTMNWAKSDNTLIKDLKDFTATCFQKHTLLNVLVNYSVFDSSQTLLVMRPYQIAATERILWKIKSSFTAKNWSKPESGGYIWHTTGSGKTLTSFKA... | 3.1.21.3 | null | DNA restriction-modification system [GO:0009307] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; type I site-specific deoxyribonuclease activity [GO:0009035] | PF12008;PF04313;PF18766; | 1.10.10.2110;1.20.58.2040;3.90.1570.50;3.40.50.300; | HsdR family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000269|PubMed:32483229}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=88 uM for ATP {ECO:0000269|PubMed:15300241}; | null | null | null | FUNCTION: The restriction (R) subunit of a type I restriction enzyme that recognizes 5'-GAAN(6)RTCG-3' (for EcoR124I) and 5'-GAAN(7)RTCG-3' (for EcoR124II) and cleaves a random distance away (PubMed:2784505). Subunit R is required for both nuclease and ATPase activities, but not for modification (Probable) (PubMed:1265... | Escherichia coli |
P10493 | NID1_MOUSE | MLDASGCSWAMWTWALLQLLLLVGPGGCLNRQELFPFGPGQGDLELEAGDDVVSPSLELIGELSFYDRTDITSVYVTTNGIIAMSEPPATEYHPGTFPPSFGSVAPFLADLDTTDGLGNVYYREDLSPFIIQMAAEYVQRGFPEVSFQPTSVVVVTWESVAPYGGPSSSPAEEGKRNTFQAVLASSNSSSYAIFLYPEDGLQFFTTFSKKDESQVPAVVGFSKGLVGFLWKSNGAYNIFANDRESIENLAKSSNAGHQGVWVFEIGSPATAKGVVSADVNLDLDDDGADYEDEDYDLVTSHLGLEDVATPSPSHSPRRGY... | null | null | canonical Wnt signaling pathway [GO:0060070]; cell-matrix adhesion [GO:0007160]; extracellular matrix organization [GO:0030198]; glomerular basement membrane development [GO:0032836]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of i... | basement membrane [GO:0005604]; cell periphery [GO:0071944]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; protein complex involved in cell-matrix adhesion [GO:0098637] | calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; laminin-1 binding [GO:0043237]; proteoglycan binding [GO:0043394]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF12662;PF12947;PF07645;PF14670;PF07474;PF00058;PF06119;PF00086; | 2.40.155.10;2.10.25.10;4.10.800.10;2.120.10.30; | null | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:8326911}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. | Mus musculus (Mouse) |
P10499 | KCNA1_RAT | MTVMSGENADEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTIHRIDNTTVIYTSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLK... | null | null | axon development [GO:0061564]; brain development [GO:0007420]; cell communication by electrical coupling [GO:0010644]; cellular response to magnesium ion [GO:0071286]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; detection of mechanical stimulus involved in sensory perception of p... | anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; calyx of Held [GO:0044305]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; endopl... | delayed rectifier potassium channel activity [GO:0005251]; disordered domain specific binding [GO:0097718]; voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1905030]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane p... | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.1/KCNA1 sub-subfamily | PTM: Palmitoylated on Cys-243; which may be required for membrane targeting. {ECO:0000250|UniProtKB:Q09470}.; PTM: N-glycosylated. {ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:8038169}.; PTM: Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (By simil... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12114518, ECO:0000269|PubMed:12681381, ECO:0000269|PubMed:17855588, ECO:0000269|PubMed:22206926, ECO:0000269|PubMed:2348860, ECO:0000269|PubMed:23725331, ECO:0000269|PubMed:2539643, ECO:0000269|PubMed:8038169}; Multi-pass membrane protein {ECO:0000305}. Membrane {... | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:22206926, ECO:0000269|PubMed:2348860, ECO:0000269|PubMed:23725331, ECO:0000269|PubMed:2539643, ECO:0000269|PubMed:8038169}; | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:12... | Rattus norvegicus (Rat) |
P10503 | PUTA_SALTY | MGTTTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLENSDTLPELPALFVGAANESEEPVAPQDEPHQPFLEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRNQKSASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGI... | 1.2.1.88; 1.5.5.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | cellular response to proline [GO:0071235]; negative regulation of DNA-templated transcription [GO:0045892]; proline biosynthetic process [GO:0006561]; proline catabolic process [GO:0006562]; proline catabolic process to glutamate [GO:0010133]; response to proline [GO:0010238] | cytoplasmic side of membrane [GO:0098562]; cytoplasmic side of plasma membrane [GO:0009898] | 1-pyrroline-5-carboxylate dehydrogenase activity [GO:0003842]; core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription repressor activity [GO:0001217]; ligand-activated transcription factor activity [GO:0098531]; proline binding [GO:1901973]; proline dehydrogenase activity [GO:0004657]; sequ... | PF00171;PF01619;PF14850;PF18327;PF21775; | 3.20.20.220;1.10.1220.10;1.20.5.550;1.20.5.460; | Proline dehydrogenase family; Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039, ChEBI:CHEBI:132124; EC=1.5.5.2; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glut... | null | PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.; PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. | null | null | FUNCTION: Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P10505 | APC3_SCHPO | MTDRLKCLIWYCIDNQNYDNSIFYSERLHAIEDSNESLYLLAYSHFLNLDYNIVYDLLDRVISHVPCTYLFARTSLILGRYKQGISAVEACRSNWRSIQPNINDSISSRGHPDASCMLDVLGTMYKKAGFLKKATDCFVEAVSINPYNFSAFQNLTAIGVPLDANNVFVIPPYLTAMKGFEKSQTNATASVPEPSFLKKSKESSSSSNKFSVSESIANSYSNSSISAFTKWFDRVDASELPGSEKERHQSLKLQSQSQTSKNLLAFNDAQKADSNNRDTSLKSHFVEPRTQALRPGARLTYKLREARSSKRGESTPQSFR... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle switching, mitotic to meiotic cell cycle [GO:0051728]; cell division [GO:0051301]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic sister chromatid segregation [GO:0000070]; mitotic sister chromatid separation [GO:... | anaphase-promoting complex [GO:0005680]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677] | PF12895;PF00515;PF14559;PF13181; | 1.25.40.10; | APC3/CDC27 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P10506 | BYR1_SCHPO | MFKRRRNPKGLVLNPNASVKSSDNDHKEELINNQKSFESNVEAFMEQCAHMNRRPAWISDLDNSSLEVVRHLGEGNGGAVSLVKHRNIFMARKTVYVGSDSKLQKQILRELGVLHHCRSPYIVGFYGAFQYKNNISLCMEYMDCGSLDAILREGGPIPLDILGKIINSMVKGLIYLYNVLHIIHRDLKPSNVVVNSRGEIKLCDFGVSGELVNSVAQTFVGTSTYMSPERIRGGKYTVKSDIWSLGISIIELATQELPWSFSNIDDSIGILDLLHCIVQEEPPRLPSSFPEDLRLFVDACLHKDPTLRASPQQLCAMPYF... | 2.7.12.2 | null | conjugation with cellular fusion [GO:0000747]; MAPK cascade [GO:0000165]; pheromone response MAPK cascade [GO:0071507]; phosphorylation [GO:0016310]; regulation of ascospore formation [GO:0034307]; sporulation resulting in formation of a cellular spore [GO:0030435] | cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11683500}. Note=Localizes to the cell tips and septum forming regions. | 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=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in conjugation and sporulation. It is thought that it is phosphorylated by the byr2 protein kinase and that it can phosphorylate the spk1 kinase. When bound to bob1, is involved in the regulation of sexual differentiation. {ECO:0000269|PubMed:11683500, ECO:0000269|PubM... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P10507 | MPPB_YEAST | MFSRTASKFRNTRRLLSTISSQIPGTRTSKLPNGLTIATEYIPNTSSATVGIFVDAGSRAENVKNNGTAHFLEHLAFKGTQNRSQQGIELEIENIGSHLNAYTSRENTVYYAKSLQEDIPKAVDILSDILTKSVLDNSAIERERDVIIRESEEVDKMYDEVVFDHLHEITYKDQPLGRTILGPIKNIKSITRTDLKDYITKNYKGDRMVLAGAGAVDHEKLVQYAQKYFGHVPKSESPVPLGSPRGPLPVFCRGERFIKENTLPTTHIAIALEGVSWSAPDYFVALATQAIVGNWDRAIGTGTNSPSPLAVAASQNGSLA... | 3.4.24.64 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9654444}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9654444}; | protein processing involved in protein targeting to mitochondrion [GO:0006627] | mitochondrial matrix [GO:0005759]; mitochondrial processing peptidase complex [GO:0017087]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:3044780}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000269|PubMed:2007593, ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444}; | null | null | null | null | FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity). {ECO:0000250|UniProtKB:Q03346,... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10515 | ODP2_HUMAN | MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPP... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000305|PubMed:25525879}; Note=Binds 2 lipoyl cofactors covalently. {ECO:0000269|PubMed:25525879}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glucose metabolic process [GO:0006006]; tricarboxylic acid cycle [GO:0006099] | intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; pyruvate dehydrogenase complex [GO:0045254] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; identical protein binding [GO:0042802] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | PTM: Delipoylated at Lys-132 and Lys-259 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000269|PubMed:25525879}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P08461}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:000... | null | null | null | null | FUNCTION: As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (Probable). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic a... | Homo sapiens (Human) |
P10517 | APOE_MACFA | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEGQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPIDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
P10518 | HEM2_MOUSE | MHHQSVLHSGYFHPLLRSWQTAASTVSASNLIYPIFVTDVPDDVQPIASLPGVARYGVNQLEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPSLLVACDVCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKAALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVARDIQEGADMLMVKPGLPYLDMVREVKDKHPELPLAVYQVSGEFAMLWHGAQAGAFDLRTAVLETMTAFRRAGADIIITYFA... | 4.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; 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:0000250}; | 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 space [GO:0005615] | 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; | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. | null | 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 (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P10522 | MYP0_BOVIN | MAPGAPSSSPSPILAALLFSSLVLSPVQAIVVYTDKEVHGAVGSQVTLYCSFWSSEWVSDDLSFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPHRKDGSIVIHNLDYGDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGVLGVVLLALLLFYLIRYCWLRRQAALQRRLSAMEKGKLHKTAKDASKRGRQTPVLYAMLDHSRSTKAASEKKTKGLGESRKDKK | null | null | cell aggregation [GO:0098743]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; myelination [GO:0042552] | plasma membrane [GO:0005886] | null | PF10570;PF07686; | 2.60.40.10; | Myelin P0 protein family | PTM: N-glycosylated; contains sulfate-substituted glycan. {ECO:0000269|PubMed:2435734}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25189}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25189}. | null | null | null | null | null | FUNCTION: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction. {ECO:0000250|UniProtKB:P25189}. | Bos taurus (Bovine) |
P10523 | ARRS_HUMAN | MAASGKTSKSEPNHVIFKKISRDKSVTIYLGNRDYIDHVSQVQPVDGVVLVDPDLVKGKKVYVTLTCAFRYGQEDIDVIGLTFRRDLYFSRVQVYPPVGAASTPTKLQESLLKKLGSNTYPFLLTFPDYLPCSVMLQPAPQDSGKSCGVDFEVKAFATDSTDAEEDKIPKKSSVRLLIRKVQHAPLEMGPQPRAEAAWQFFMSDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVKPVAMEEAQEKVPPNSTLTKTLTLLPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGI... | null | null | cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor internalization [GO:0002031]; rhodopsin mediated signaling pathway [GO:0016056] | cytosol [GO:0005829]; membrane [GO:0016020]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | G protein-coupled receptor binding [GO:0001664]; opsin binding [GO:0002046]; phosphoprotein binding [GO:0051219]; protein phosphatase inhibitor activity [GO:0004864] | PF02752;PF00339; | 2.60.40.640;2.60.40.840; | Arrestin family | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:3720866}. Membrane {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina. Evenly distributed throughout rod p... | null | null | null | null | null | FUNCTION: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (By similarity). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (PubMed:9565049). {ECO:0000250|UniProtKB:P08168, ECO:... | Homo sapiens (Human) |
P10536 | RAB1B_RAT | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC | 3.6.5.2 | null | autophagosome assembly [GO:0000045]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; positive regulation of glycoprotein metabolic process [GO:1903020]; regulation of autophagosome assembly [GO:2000785] | endomembrane system [GO:0012505]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; perinuclear region of cytoplasm [GO:0048471]; phagophore assembly site membrane [GO:0034045]; synapse [GO:0045202] | G protein activity [GO:0003925]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1). {ECO:0000250|UniProtKB:Q9H0U4}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}. Membrane {ECO:0000269|PubMed:1918138}; Lipid-anchor {ECO:0000269|PubMed:1918138}; Cytoplasmic side {ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cyt... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P62820}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... | Rattus norvegicus (Rat) |
P10538 | AMYB_SOYBN | MATSDSNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVWWGIIELKGPKQYDWRAYRSLFQLVQECGLTLQAIMSFHQCGGNVGDIVNIPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYSDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIGEFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYVTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKVENHAAELTAGYYNL... | 3.2.1.2 | null | polysaccharide catabolic process [GO:0000272] | null | amylopectin maltohydrolase activity [GO:0102229]; beta-amylase activity [GO:0016161] | PF01373; | 3.20.20.80; | Glycosyl hydrolase 14 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2; Evidence={ECO:0000269|PubMed:15178253}; | null | null | null | null | null | Glycine max (Soybean) (Glycine hispida) |
P10547 | LSTP_STASI | MKKTKNNYYTRPLAIGLSTFALASIVYGGIQNETHASEKSNMDVSKKVAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKALVQNRTALRAATHEHSAQWLNNYKKGYGYGPYPLGINGGMHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIEND... | 3.4.24.75 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | cell wall organization [GO:0071555]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF20481;PF01551;PF08460; | 2.70.70.10;2.30.30.40; | Peptidase M23B family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.; EC=3.4.24.75; | null | null | null | null | FUNCTION: Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. | Staphylococcus simulans |
P10548 | LSTP_STAST | MKKTKNNYYTTPLAIGLSTFALASIVYGGIQNETHASEKSNMDVSKKVAEVETSKPPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKAPVENTAEVETSKALVQNRTALRAATHEHSAQWLNNYKKGYGYGPYPLGINGGIHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKY... | 3.4.24.75 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | cell wall organization [GO:0071555]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF20481;PF01551;PF08460; | 2.70.70.10;2.30.30.40; | Peptidase M23B family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.; EC=3.4.24.75; | null | null | null | null | FUNCTION: Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. | Staphylococcus staphylolyticus |
P10552 | FMRF_DROME | MGIALMFLLALYQMQSAIHSEIIDTPNYAGNSLQDADSEVSPSQDNDLVDALLGNDQTERAELEFRHPISVIGIDYSKNAVVLHFQKHGRKPRYKYDPELEAKRRSVQDNFMHFGKRQAEQLPPEGSYAGSDELEGMAKRAAMDRYGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRTPAEDFMRFGRTPAEDFMRFGRSDNFMRFGRSPHEELRSPKQDFMRFGRPDNFMRFGRSAPQDFVRSGKMDSNFIRFGKSLKPAAPESKPVKSNQGNPGERSPVDKAMTELFKKQEL... | null | null | adult locomotory behavior [GO:0008344]; behavioral defense response [GO:0002209]; larval locomotory behavior [GO:0008345]; negative regulation of heart contraction [GO:0045822]; negative regulation of heart rate [GO:0010459]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cytosolic calcium ion conc... | extracellular space [GO:0005615] | neuropeptide receptor binding [GO:0071855]; receptor ligand activity [GO:0048018] | PF01581; | null | FARP (FMRFamide related peptide) family | PTM: This precursor includes 13 peptides that have FMRF or related sequences at their C-termini, and other putative neuropeptides. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs. | Drosophila melanogaster (Fruit fly) |
P10567 | MYSP_CAEEL | MSLYRSPSAALLKSPSQAAFGAPFGSMSVADLGSLTRLEDKIRLLQEDLESERELRNRVERERADLSVQVIALTDRLEDAEGTTDSQIESNRKREGELSKLRKLLEESQLESEDAMNVLRKKHQDSCLDYQDQIEQLQKKNAKIDRERQRVQHEVIELTATIDQLQKDKHTAEKAAERFEAQANELANKVEDLNKHVNDLAQQRQRLQAENNDLLKEVHDQKVQLDNLQHVKYTLAQQLEEARRRLEDAERERSQLQSQLHQVQLELDSVRTALDEESIARSDAEHKLNLANTEITQWKSKFDAEVALHHEEVEDLRKKM... | null | null | locomotion [GO:0040011]; mitotic actomyosin contractile ring contraction [GO:1902404]; muscle contraction [GO:0006936]; positive regulation of ovulation [GO:0060279]; positive regulation of sarcomere organization [GO:0060298]; regulation of cytoskeleton organization [GO:0051493]; sarcomere organization [GO:0045214]; sk... | A band [GO:0031672]; mitotic actomyosin contractile ring [GO:0110085]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; cytoskeletal protein binding [GO:0008092]; microfilament motor activity [GO:0000146]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124] | PF01576; | 1.20.5.340;1.20.5.370;1.20.5.1160; | Paramyosin family | PTM: Phosphorylated on serine residues in the N-terminal non-helical region. {ECO:0000269|PubMed:2754733}. | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:27009202}. Note=Localizes in punctate patterns along the myosin heavy chain myo-3 filaments in myoepithelial sheath cells. {ECO:0000269|PubMed:17326220}. | null | null | null | null | null | FUNCTION: Structural component of the muscle thick filaments which is involved in assembly and organization of sarcomere myofilaments (PubMed:27009202, PubMed:2754728). Involved in ovulation (PubMed:17326220). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall ... | Caenorhabditis elegans |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.