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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P04739 | PILA_PSEAE | MKAQKGFTLIELMIVVAIIGILAAIAIPQYQNYVARSEGASALATINPLKTTVEESLSRGIAGSKIKIGTTASTATETYVGVEPDANKLGVIAVAIEDSGAGDITFTFQTGTSSPKNATKVITLNRTADGVWACKSTQDPMFTPKGCDN | null | null | cell adhesion involved in single-species biofilm formation [GO:0043709]; regulation of calcium-mediated signaling [GO:0050848]; single-species biofilm formation on inanimate substrate [GO:0044011]; type IV pilus-dependent motility [GO:0043107] | cell surface [GO:0009986]; cytosol [GO:0005829]; host cell endoplasmic reticulum membrane [GO:0044167]; pilus [GO:0009289]; plasma membrane [GO:0005886]; type IV pilus [GO:0044096] | null | PF07963;PF00114; | 3.30.700.10; | N-Me-Phe pilin family | PTM: Methylated by prepilin peptidase PilD at the amino group of the N-terminal phenylalanine once the leader sequence is cleaved. {ECO:0000269|PubMed:1429457}. | SUBCELLULAR LOCATION: Fimbrium. Cell inner membrane {ECO:0000269|PubMed:27162347}; Single-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23266901}. | null | null | null | null | null | FUNCTION: Major component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:26041805, PubMed:31431558, PubMed... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P04746 | AMYP_HUMAN | MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGH... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097, ECO:0000269|PubMed:8528071}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:117... | carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975]; polysaccharide digestion [GO:0044245] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:11914097}; | null | null | null | null | null | Homo sapiens (Human) |
P04751 | ACTC_XENLA | MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIQRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEIT... | 3.6.4.- | null | actin filament organization [GO:0007015]; actin-myosin filament sliding [GO:0033275]; heart contraction [GO:0060047]; mesenchyme migration [GO:0090131]; positive regulation of gene expression [GO:0010628] | actin filament [GO:0005884]; cell body [GO:0044297]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; sarcomere [GO:0030017] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; myosin binding [GO:0017022] | PF00022; | 3.30.420.40; | Actin family | PTM: [Actin, alpha cardiac muscle 1, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. {ECO:0000250|UniProtKB:P68033}.; PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MIC... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility. | Xenopus laevis (African clawed frog) |
P04756 | ACHA_MOUSE | MELSTVLLLLGLCSAGLVLGSEHETRLVAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPTTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHH... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell cellular homeostasis [GO:0046716]; neuromuscular junction development [GO:0007528]; neuromuscular synaptic transmission [GO:0007274]; neuron cellular homeostasis [GO:0070050... | acetylcholine-gated channel complex [GO:0005892]; cell surface [GO:0009986]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane pot... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P02709}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02709}; | null | null | null | null | FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250|UniProtKB:P02708}. | Mus musculus (Mouse) |
P04757 | ACHA3_RAT | MGVVLLPPPLSMLMLVLMLLPAASASEAEHRLFQYLFEDYNEIIRPVANVSHPVIIQFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWKPSDYQGVEFMRVPAEKIWKPDIVLYNNADGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHEIKYNCCEEIYQDITYSLYIRRLPLFYTINLIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVL... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; excitatory postsynaptic potential [GO:0060079]; heart development [GO:0007507]; locomotory behavior [GO:0007626]; membrane depolarization [GO:0051899]; nervous system development [GO:0007399]; presynaptic modulation of ... | acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; dopaminergic synapse [GO:0098691]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane r... | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; protein-containing complex binding [GO:0044877]; transmitter-gated monoatomic ion channel activity involved in regu... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-3/CHRNA3 sub-subfamily | PTM: Ubiquitinated; by STUB1/CHIP and thereafter degraded by the 26S proteosome complex. {ECO:0000269|PubMed:19474315, ECO:0000269|PubMed:26265139}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:19474315}; Multi-pass membrane protein. Endoplasmic reticulum {ECO:0000269|PubMed:19474315}. Golgi apparatus {ECO:0000269|PubMed:19474315}. Note=Interaction with UBXN2A/UBXD4 promotes translocation to the pl... | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Rattus norvegicus (Rat) |
P04758 | ACHB_BOVIN | MTPGALLLLLLGVLGAHLAPGARGSEAEGRLREKLFSGYDSTVRPAREVGDRVWVSIGLTLAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPEEHEGIDSLRISAESVWLPDVVLLNNNDGNFDVALDINVVVSSDGSMRWQPPGIYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLQTGLSPEGQERQEVYIHEGTFIENGQWEIIHKPSRLIQPSVDPRGGGEGRREEVTFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLSVPIIIKYLMFTMVLV... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell development [GO:0055001]; muscle contraction [GO:0006936]; nervous system process [GO:0050877]; neuromuscular synaptic transmis... | acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; channel activity [GO:0015267] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-1/CHRNB1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}. | Bos taurus (Bovine) |
P04759 | ACHD_BOVIN | MEGSVLTLVLLAALVVCGSWGLNEEERLIRHLFEEKAYNKELRPAAHKESVEISLALTLSNLISLKEVEETLTTNVWIEQGWTDSRLQWDAEDFGNISVLRLPADMVWLPEIVLENNNDGSFQISYSCNVLIYPSGSVYWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTTKEITLSLKQAEEDGRSYPVEWIIIDPEGFTENGEWEIVHRPARVNVDPSVPLDSPNRQDVTFYLIIRRKPLFYVINILVPCVLISFMINLVFYLPADCGEKTSMAISVLLAQSVFLLLISKRLPATSMAIPLIGKFLLFGMVLVT... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; musculoskeletal movement [GO:0050881]; skeletal muscle tissue growth [GO:0048630] | acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Delta/CHRND sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}. | Bos taurus (Bovine) |
P04760 | ACHG_MOUSE | MQGGQRPHLLLLLLAVCLGAQSRNQEERLLADLMRNYDPHLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPKDYEGLWILRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSSCSISVTYFPFDWQNCSLIFQSQTYSTSEINLQLSQEDGQAIEWIFIDPEAFTENGEWAIRHRPAKMLLDSVAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVATNVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLMVVTILIV... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; regulation of membrane potential [GO:0042391]; skeletal muscle contraction [GO:0003009] | acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; ligand-gated monoatomic ion channel activity [GO:0015276]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Mus musculus (Mouse) |
P04761 | ACM1_PIG | MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPAKQPPR... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; cognition [GO:0050890]; entrainment of circadian clock [GO:0009649]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor sign... | dendrite [GO:0030425]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Sus scrofa (Pig) |
P04762 | CATA_RAT | MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNR... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04040}; COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P04040}; | aerobic respiration [GO:0009060]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular oxidant detoxification [GO:0098869]; cellular response to growth factor stimulus [GO:0071363]; cholesterol metabolic process [GO:0008203]; hemoglobin metabolic process [GO:0020027]; hydrogen peroxide catabolic process ... | catalase complex [GO:0062151]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | aminoacylase activity [GO:0004046]; antioxidant activity [GO:0016209]; catalase activity [GO:0004096]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; oxidoreductase activity, acting on peroxide as acceptor [GO:00... | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:26961980}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and t... | Rattus norvegicus (Rat) |
P04764 | ENOA_RAT | MSILKIHAREIFDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDNDKTRFMGKGVSKAVEHINKTIAPALVSKKLNVVEQEKIDQLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKSAIAKAGYTDQVVIGMDVAASEFYRAGKYDLDFKSPDDASRYITPDQLADLYKSFIKDYPVVSIEDPFDQDDWDAWQKFTATAGIQVVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06733}; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. {ECO:0000250|UniProtKB:P06733}; | canonical glycolysis [GO:0061621]; cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; ERK1 and ERK2 cascade [GO:0070371]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; in utero embryonic development [GO:0001701]; negative regulation of cell growth [GO:0030308]; ... | cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear outer membrane [GO:0005640]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060... | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; enzyme binding [GO:0019899]; GTPase binding [GO:0051020]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein h... | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P06733}.; PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}. | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000269|PubMed:8594891}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000305|PubMed:8594891}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:8594891}. | null | null | FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its abilit... | Rattus norvegicus (Rat) |
P04768 | PR2C3_MOUSE | MLPSSIQPCSWILLLLLVNSSLLWKNVASFPMCAMRNGRCFMSFEDTFELAGSLSHNISIEVSELFNEFEKHYSNVSGLRDKSPMRCNTSFLPTPENKEQARLTHYAALLKSGAMILDAWESPLDDLVSELSTIKNVPDIIISKATDIKKKINAVRNGVNALMSTMLQNGDEEKKNPAWFLQSDNEDARIHSLYGMISCLDNDFKKVDIYLNVLKCYMLKIDNC | null | null | female pregnancy [GO:0007565]; hematopoietic stem cell proliferation [GO:0071425]; mammary gland development [GO:0030879]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; positive regulation of lactation [GO:1903489]; positive... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}. | null | null | null | null | null | FUNCTION: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May pla... | Mus musculus (Mouse) |
P04769 | PR7D1_MOUSE | MLPSLIQPCSSGTLLMLLMSNLFLWEKVSSAPINASEAVLSDLKDLFDNATVLSGEMSKLGVIMRKEFFMNSFSSETFNKIILDLHKSTENITKAFNSCHTVPINVPETVEDVRKTSFEEFLKMVLHMLLAWKEPLKHLVTELSALPECPYRILSKAEAIEAKNKDLLEYIIRIISKVNPAIKENEDYPTWSDLDSLKSADKETQFFALYMFSFCLRIDLETVDFLVNFLKCLLLYDDVCYSEF | null | null | blood vessel endothelial cell migration [GO:0043534]; female pregnancy [GO:0007565]; mammary gland development [GO:0030879]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; placenta blood vessel development [GO:0060674]; placenta development... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Mus musculus (Mouse) |
P04773 | GLNA_CRIGR | MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSESSNSDMYLSPVAMFRDPFRKEPNKLVFCEVFKYNQKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSDGFPGPQGLYYCGVGADKAYRRDIMEAHYRACLYAGVKITGTYAEVKHAQWEFQIGPCEGIRMGDHLWVARFILHRVCKDFGVIATFDSKPIPGNWNGAGCHTNFSTKTMREENGLKHIKEAIEKLSKRHRYHIRAYDPKGGLDNARRLTGFHKTSNINDFSAGVADRS... | 2.3.1.225; 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P09606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15104}; | angiogenesis [GO:0001525]; glutamine biosynthetic process [GO:0006542]; protein palmitoylation [GO:0018345]; regulation of endothelial cell migration [GO:0010594]; regulation of sprouting angiogenesis [GO:1903670] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872]; protein-cysteine S-palmitoyltransferase activity [GO:0019706] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000250|UniProtKB:P15104}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P15104}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000250|UniProtKB:P15104}; Lipid-anchor {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol, with a fraction associated wit... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P15104}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of th... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P04774 | SCN1A_RAT | MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVQWPPTNASLEEHSIEKNVTTDYNGTLVNETVFEFDWKSYIQD... | null | null | adult walking behavior [GO:0007628]; cardiac muscle cell action potential involved in contraction [GO:0086002]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; determination of adult lifespan [GO:0008340]; establishment of localization in cell [GO:0051649]; membrane depolarization ... | axon [GO:0030424]; axon initial segment [GO:0043194]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; sodium channel complex [GO:0034706]; T-tubule [GO:0030315]; voltage-gated sodium ch... | sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.1/SCN1A subfamily | PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35498}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P35498}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Pl... | Rattus norvegicus (Rat) |
P04775 | SCN2A_RAT | MARSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRNPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTVNMFNWDEYI... | null | null | axon development [GO:0061564]; cellular response to hypoxia [GO:0071456]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; intrinsic apoptotic signaling pathway in response to osmotic stress [GO:0008... | axon [GO:0030424]; axon initial segment [GO:0043194]; glutamatergic synapse [GO:0098978]; intercalated disc [GO:0014704]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; T-tubule [GO:0030315]; voltage-gated sodiu... | calmodulin binding [GO:0005516]; leucine zipper domain binding [GO:0043522]; sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.2/SCN2A subfamily | PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis.; PTM: Phosphorylation at Ser-1506 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000269|PubMed:1322892, ECO:0000269|PubMed:1658937, ECO:0000269|PubMed:20131913}.; PTM... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827969, ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:28029095, ECO:0000269|PubMed:9893979}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:24297919, ECO:0000269|PubMed:28029095}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Im... | Rattus norvegicus (Rat) |
P04776 | GLYG1_SOYBN | MAKLVFSLCFLLFSGCCFAFSSREQPQQNECQIQKLNALKPDNRIESEGGLIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSKSRRNGIDETICTMR... | null | null | null | endoplasmic reticulum [GO:0005783]; protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269|PubMed:29037738}.; PTM: The precursor is post-translationally processed to form a covalently linked A1a-Bx subunit complex. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:29348620}. Protein storage vacuole {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles. {ECO:0000269|PubMed:29348620}. | null | null | null | null | null | FUNCTION: Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating... | Glycine max (Soybean) (Glycine hispida) |
P04778 | CB1C_ARATH | MAASTMALSSPAFAGKAVKLSPAASEVLGSGRVTMRKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK | null | COFACTOR: Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin. {ECO:0000250}; | photosynthesis, light harvesting in photosystem I [GO:0009768]; response to light stimulus [GO:0009416] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; nucleus [GO:0005634]; photosystem I [GO:0009522]; photosystem II [GO:0009523]; plastoglobule [GO:0010287]; thylakoid [GO:0009579] | chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904] | PF00504; | 1.10.3460.10; | Light-harvesting chlorophyll a/b-binding (LHC) protein family | PTM: Photoregulated by reversible phosphorylation of its threonine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. | Arabidopsis thaliana (Mouse-ear cress) |
P04785 | PDIA1_RAT | MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDAGSDSAKQFLLAAEAVDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLI... | 5.3.4.1 | null | cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; insulin processing [GO:0030070]; positive regulation of cell adhesion [GO:0045785]; positive regulation of substrate adhesion-dependent cell spreading [GO:1... | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; lamellipodium [GO:0030027... | actin binding [GO:0003779]; enzyme binding [GO:0019899]; integrin binding [GO:0005178]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; protein-disulfide reducta... | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Phosphorylation of Ser-359 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone. It also promotes interaction with ERN1. {ECO:0000250|UniProtKB:P07237}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000250|UniProtKB:P09103}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to b... | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P07237}; | null | null | null | null | FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to for... | Rattus norvegicus (Rat) |
P04786 | TOP1_YEAST | MTIADASKVNHELSSDDDDDVPLSQTLKKRKVASMNSASLQDEAEPYDSDEAISKISKKKTKKIKTEPVQSSSLPSPPAKKSATSKPKKIKKEDGDVKVKTTKKEEQENEKKKREEEEEEDKKAKEEEEEYKWWEKENEDDTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLTSQEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSK... | 5.6.2.1 | null | chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA topological change [GO:0006265]; mitotic chromosome condensation [GO:0007076]; nuclear migration [GO:0007097]; rDNA heterochromatin formation [GO:00... | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298] | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917] | PF14370;PF01028;PF02919; | 1.10.132.10;2.170.11.10;1.10.10.41; | Type IB topoisomerase family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04789 | TPIS_TRYBB | MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ | 5.3.1.1 | null | gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; glycosome [GO:0020015] | triose-phosphate isomerase activity [GO:0004807] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | SUBCELLULAR LOCATION: Glycosome. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. | null | null | null | Trypanosoma brucei brucei |
P04792 | HSPB1_HUMAN | MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK | null | null | anterograde axonal protein transport [GO:0099641]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; chaperone-mediated protein folding [GO:0061077]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of oxidative stres... | axon cytoplasm [GO:1904115]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; spindle [GO:0005819]; Z disc [G... | identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein kinase C inhibitor activity [GO:0008426]; RNA binding [GO:0003723]; RNA polymerase II-specific DNA-binding t... | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | PTM: Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effe... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777697, ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during ... | null | null | null | null | null | FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous ... | Homo sapiens (Human) |
P04797 | G3P_RAT | MVKVGVNGFGRIGRLVTRAAFSCDKVDIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQAAEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSN... | 1.2.1.12; 2.6.99.- | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cAMP-mediated signaling [GO:0019933]; canonical glycolysis [GO:0061621]; cellular response to type II interferon [GO:0071346]; female pregnancy [GO:0007565]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; microtubule c... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; glutamatergic synapse [GO:0098978]; lipid droplet [GO:0005811]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density, intracellular component [GO:0099092]; ribonucleoprotein complex [GO:19... | aspartic-type endopeptidase inhibitor activity [GO:0019828]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:00... | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus (PubMed:1281150, PubMed:15951807, PubMed:20972425, PubMed:8626764). The effect of S-nitrosylation on enzymatic activity is unclear: according to some authors, it inhibits enzymatic activity and increases endogenous... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15312048}. Nucleus {ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794, ECO:0000269|PubMed:20972425}. Note=Translocates to the nucleus follo... | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PR... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:15951807, PubMed:17934141, PubMed:20972425). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of th... | Rattus norvegicus (Rat) |
P04798 | CP1A1_HUMAN | MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPHLALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQSMSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAGPGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPILRYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANVQLSDEKIINIVLDLFGAGFD... | 1.14.14.1; 4.2.1.152 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23508959}; | 9-cis-retinoic acid biosynthetic process [GO:0042904]; amine metabolic process [GO:0009308]; camera-type eye development [GO:0043010]; cellular response to copper ion [GO:0071280]; cellular response to organic cyclic compound [GO:0071407]; coumarin metabolic process [GO:0009804]; dibenzo-p-dioxin catabolic process [GO:... | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; flavonoid... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Microsome membrane {ECO:0000250|UniProtKB:P00185}; Per... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for all-trans retinol {ECO:0000269|PubMed:10681376}; KM=9.5 uM for 17beta-estradiol (2-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=11.8 uM for 17beta-estradiol (4-hydroxylation) {ECO:0000269|PubMed:15805301}; KM=79 uM for 17beta-estradiol (6alpha-hydroxyl... | PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847, ECO:0000269|PubMed:15805301}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:18577768, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972... | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Mechanist... | Homo sapiens (Human) |
P04799 | CP1A2_RAT | MAFSQYISLAPELLLATAIFCLVFWVLRGTRTQVPKGLKSPPGPWGLPFIGHMLTLGKNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLITNGKSMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSVSSCYLEEHVSKEANHLISKFQKLMAEVGHFEPVNQVVESVANVIGAMCFGKNFPRKSEEMLNLVKSSKDFVENVTSGNAVDFFPVLRYLPNPALKRFKNFNDNFVLFLQKTVQEHYQDFNKNSIQDITGALFKHSENYKDNGGLIPQEKIVNIVNDIFGAGFETV... | 1.14.14.1; 4.2.1.152 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | alkaloid metabolic process [GO:0009820]; arachidonic acid metabolic process [GO:0019369]; cellular aromatic compound metabolic process [GO:0006725]; cellular respiration [GO:0045333]; cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cholesterol metabolic process [GO:0008203];... | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:002003... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05177}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P05177}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NA... | Rattus norvegicus (Rat) |
P04800 | CP3A1_RAT | MDLLSALTLETWVLLAVVLVLLYGFGTRTHGLFKKQGIPGPKPLPFFGTVLNYYMGLWKFDVECHKKYGKIWGLFDGQMPLFAITDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIEFFKKFVYRMKETRLDSVQKHRVDFLQLMMNAHNDSKDKESHTALSDMEITAQSIIFIFAGYEPTSSTLSFVLH... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | oxidative demethylation [GO:0070989]; response to cadmium ion [GO:0046686]; response to dexamethasone [GO:0071548]; response to glucocorticoid [GO:0051384]; response to metal ion [GO:0010038]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; steroid metabolic process [GO:0008202]; xenobi... | endoplasmic reticulum membrane [GO:0005789] | aromatase activity [GO:0070330]; demethylase activity [GO:0032451]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; testosterone 6-beta-hydroxylase activity [GO:0050649] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P04802 | SYDC_YEAST | MSQDENIVKAVEESAEPAQVILGEDGKPLSKKALKKLQKEQEKQRKKEERALQLEAEREAREKKAAAEDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEI... | 6.1.1.12 | null | aspartyl-tRNA aminoacylation [GO:0006422] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | aspartate-tRNA ligase activity [GO:0004815]; ATP binding [GO:0005524]; RNA binding [GO:0003723] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12; | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04805 | SYE_ECOLI | MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVA... | 6.1.1.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204}; | glutamyl-tRNA aminoacylation [GO:0006424] | cytosol [GO:0005829] | ATP binding [GO:0005524]; glutamate-tRNA ligase activity [GO:0004818]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270] | PF19269;PF00749; | 1.10.10.350;3.40.50.620; | Class-I aminoacyl-tRNA synthetase family, Glutamate--tRNA ligase type 1 subfamily | PTM: Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu). {ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24343429}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.32 uM for tRNA(Glu) {ECO:0000269|PubMed:14764088}; KM=0.105 mM for Glu {ECO:0000269|PubMed:14764088}; | null | null | null | FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000269|PubMed:14764088, ECO:0000269|PubMed:6280993, ECO:0000269|PubMed:6986385, ECO:0000269|PubMed:7797500, ECO:0000269|Pu... | Escherichia coli (strain K12) |
P04806 | HXKA_YEAST | MVHLGPKKPQARKGSMADVPKELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHDMRTTKHQEELWSFIADSLKDFMVEQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLIASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLADDIPSNSPMAINCEYGSFDNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLE... | 2.7.1.1 | null | carbohydrate phosphorylation [GO:0046835]; fructose import across plasma membrane [GO:1990539]; fructose metabolic process [GO:0006000]; glucose 6-phosphate metabolic process [GO:0051156]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeost... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; mannokinase activity [GO:0019158] | PF00349;PF03727; | 1.10.287.1250;3.30.420.40;3.40.367.20; | Hexokinase family | null | null | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidenc... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:332086}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:332086}. | null | null | FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:332086). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:332086). {ECO:0... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04807 | HXKB_YEAST | MVHLGPKKPQARKGSMADVPKELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDAMRTTQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSAPMAINCEYGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMD... | 2.7.1.1 | null | carbohydrate phosphorylation [GO:0046835]; fructose import across plasma membrane [GO:1990539]; fructose metabolic process [GO:0006000]; glucose 6-phosphate metabolic process [GO:0051156]; glucose import [GO:0046323]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeost... | cytosol [GO:0005829]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; mannokinase activity [GO:0019158] | PF00349;PF03727; | 1.10.287.1250;3.30.420.40;3.40.367.20; | Hexokinase family | null | null | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000305|PubMed:332086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidenc... | null | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:332086}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:332086}. | null | null | FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:332086). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:332086). {ECO:0... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04810 | HSP83_DROSI | MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQL... | null | null | cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; pole plasm mRNA localization [GO:0019094]; positive r... | centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... | Drosophila simulans (Fruit fly) |
P04811 | HSP83_DROVI | MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLFIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEDDEKKEGDEKKEMDTDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLE... | null | null | cellular response to heat [GO:0034605]; centrosome cycle [GO:0007098]; cold acclimation [GO:0009631]; membrane bending [GO:0097753]; multivesicular body fusion to apical plasma membrane [GO:0098866]; negative regulation of cell population proliferation [GO:0008285]; pole plasm mRNA localization [GO:0019094]; positive r... | centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; polytene chromosome interband [GO:0005705]; protein folding chaperone complex [GO:0101031] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; insulin receptor binding [GO:0005158]; TPR domain binding [GO:0030911]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... | Drosophila virilis (Fruit fly) |
P04817 | CAN1_YEAST | MTNSKEDADIEEKHMYNEPVTTLFHDVEASQTHHRRGSIPLKDEKSKELYPLRSFPTRVNGEDTFSMEDGIGDEDEGEVQNAEVKRELKQRHIGMIALGGTIGTGLFIGLSTPLTNAGPVGALISYLFMGSLAYSVTQSLGEMATFIPVTSSFTVFSQRFLSPAFGAANGYMYWFSWAITFALELSVVGQVIQFWTYKVPLAAWISIFWVIITIMNLFPVKYYGEFEFWVASIKVLAIIGFLIYCFCMVCGAGVTGPVGFRYWRNPGAWGPGIISKDKNEGRFLGWVSSLINAAFTFQGTELVGITAGEAANPRKSVPRA... | null | null | amino acid transmembrane transport [GO:0003333]; basic amino acid transport [GO:0015802]; L-arginine transmembrane transport [GO:1903826]; transmembrane transport [GO:0055085] | eisosome [GO:0032126]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | amino acid transmembrane transporter activity [GO:0015171]; basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459] | PF00324; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, YAT (TC 2.A.3.10) family | PTM: Phosphorylated probably at multiple sites (PubMed:9544242). {ECO:0000269|PubMed:9544242}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12100990, ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946, ECO:0000269|PubMed:21880895, ECO:0000269|PubMed:37005249}; Multi-pass membrane protein {ECO:0000269|PubMed:21880895}. Endosome membrane {ECO:0000269|PubMed:21880895}; Multi-pass membrane protein {... | null | null | null | null | null | FUNCTION: High-affinity permease for arginine. {ECO:0000269|PubMed:10654085, ECO:0000269|PubMed:11746604, ECO:0000269|PubMed:8436127, ECO:0000269|PubMed:9231419}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04818 | TYSY_HUMAN | MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV | 2.1.1.45 | null | cartilage development [GO:0051216]; circadian rhythm [GO:0007623]; developmental growth [GO:0048589]; DNA biosynthetic process [GO:0071897]; dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; intestinal epithelial cell maturation [GO:0060574]; liver regeneration [GO:0097421]; methylation [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | dihydrofolate reductase activity [GO:0004146]; folic acid binding [GO:0005542]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; sequence-specific mRNA binding [GO:1990825]; thymidylate synthase activity [GO:0004799] | PF00303; | 3.30.572.10; | Thymidylate synthase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21876188}. Cytoplasm {ECO:0000269|PubMed:21876188}. Mitochondrion {ECO:0000269|PubMed:21876188}. Mitochondrion matrix {ECO:0000269|PubMed:21876188}. Mitochondrion inner membrane {ECO:0000269|PubMed:21876188}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000269|PubMed:11278511}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12105;... | null | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000305|PubMed:11278511}. | null | null | FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:000026... | Homo sapiens (Human) |
P04819 | DNLI1_YEAST | MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVL... | 6.5.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | base-excision repair [GO:0006284]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA ligation [GO:0006266]; DNA recombination [GO:0006310]; lagging strand elongation [GO:0006273]; maintenance of DNA trinucleotide repeats [GO:0035753]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:... | mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872] | PF04679;PF01068;PF04675; | 3.30.1490.70;1.10.3260.10;3.30.470.30;2.40.50.140; | ATP-dependent DNA ligase family | null | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; | null | null | null | null | FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. The mitochondrial form is required for mitochondrial DNA maintenance but is non-essential while the nuclear form is essential for cell viability. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04821 | CDC25_YEAST | MSDTNTSIPNTSSAREAGNASQTPSISSSSNTSTTTNTESSSASLSSSPSTSELTSIRPIGIVVAAYDFNYPIKKDSSSQLLSVQQGETIYILNKNSSGWWDGLVIDDSNGKVNRGWFPQNFGRPLRDSHLRKHSHPMKKYSSSKSSRRSSLNSLGNSAYLHVPRNPSKSRRGSSTLSASLSNAHNAETSSGHNNTVSMNNSPFSAPNDASHITPQSSNFNSNASLSQDMTKSADGSSEMNTNAIMNNNETNLQTSGEKAGPPLVAEETIKILPLEEIEMIINGIRSNIASTWSPIPLITKTSDYKLVYYNKDLDIYCSE... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; Ras protein signal transduction [GO:0007265]; regulation of cell cycle [GO:0051726]; traversing start control point of mitotic cell cycle [GO:0007089] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF00617;PF00618;PF00018; | 1.10.840.10;2.30.30.40;1.20.870.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered. {ECO:0000269|PubMed:2017169}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04822 | IL1A_RABIT | MAKVPDLFEDLKNCFSENEEYSSAIDHLSLNQKSFYDASYEPLHEDCMNKVVSLSTSETSVSPNLTFQENVVAVTASGKILKKRRLSLNQPITDVDLETNVSDPEEGIIKPRSVPYTFQRNMRYKYLRIIKQEFTLNDALNQSLVRDTSDQYLRAAPLQNLGDAVKFDMGVYMTSEDSILPVTLRISQTPLFVSAQNEDEPVLLKEMPETPRIITDSESDILFFWETQGNKNYFKSAANPQLFIATKPEHLVHMARGLPSMTDFQIS | null | null | cellular response to heat [GO:0034605]; cellular response to lipopolysaccharide [GO:0071222]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; cytokine-mediated signaling pathway [GO:0019221]; ectopic germ cell programmed cell death [GO:0035234]; extrinsic apoptotic signaling ... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | copper ion binding [GO:0005507]; cytokine activity [GO:0005125]; interleukin-1 receptor binding [GO:0005149] | PF00340;PF02394; | 2.80.10.50; | IL-1 family | PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000250|UniProtKB:P01583}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000250|UniProtKB:P01583}.; PTM: Phosphorylat... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that use... | null | null | null | null | null | FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 r... | Oryctolagus cuniculus (Rabbit) |
P04823 | IL3_RAT | MVLASSTTSILCMLLPLLMLFHQGLQISDRGSDAHHLLRTLDCRTIALEILVKLPVSGLNNSDDKANLRNSTLRRVNLDEFLKSQEEFDSQDTTDIKSKLQKLKCCIPAAASDSVLPGVYNKDLDDFKKKLRFYVIHLKDLQPVSVSRPPQPTSSSDNFRPMTVEC | null | null | B cell apoptotic process [GO:0001783]; B cell proliferation [GO:0042100]; cell population proliferation [GO:0008283]; cytokine-mediated signaling pathway [GO:0019221]; embryonic hemopoiesis [GO:0035162]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; hematopoietic progenitor cell differentiati... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-3 receptor binding [GO:0005135] | PF02059; | 1.20.1250.10; | IL-3 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Stimulates also mature basophils, eosinophils, and monocytes to become functionally activate... | Rattus norvegicus (Rat) |
P04824 | MEL1_YEASX | MFAFYFLTACISLKGVFGVSPSYNGLGLTPQMGWDNWNTFACDVSEQLLLDTADRISDLGLKDMGYKYIILDDCWSSGRDSDGFLVADEQKFPNGMGHVADHLHNNSFLFGMYSSAGEYTCAGYPGSLGREEEDAQFFANNRVDYLKYDNCYNKGQFGTPEISYHRYKAMSDALNKTGRPIFYSLCNWGQDLTFYWGSGIANSWRMSGDVTAEFTRPDSRCPCDGDEYDCKYAGFHCSIMNILNKAAPMGQNAGVGGWNDLDNLEVGVGNLTDDEEKAHFSMWAMVKSPLIIGANVNNLKASSYSIYSQASVIAINQDSN... | 3.2.1.22 | null | glycoside catabolic process [GO:0016139]; oligosaccharide metabolic process [GO:0009311] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | alpha-galactosidase activity [GO:0004557] | PF16499;PF17801; | 3.20.20.70;2.60.40.1180; | Glycosyl hydrolase 27 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20592022}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; | null | null | null | null | null | Saccharomyces cerevisiae (Baker's yeast) |
P04825 | AMPN_ECOLI | MTQQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIVAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNWTGNRVTCRDWFQLSLKE... | 3.4.11.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; | proteolysis [GO:0006508] | plasma membrane [GO:0005886] | aminopeptidase activity [GO:0004177]; identical protein binding [GO:0042802]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF11940;PF17432;PF01433;PF17900; | 2.60.40.1840;3.30.2010.30;1.10.390.10;1.25.50.10;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; E... | null | null | null | null | FUNCTION: Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}. | Escherichia coli (strain K12) |
P04839 | CY24B_HUMAN | MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKME... | 1.-.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; | cellular response to cadmium ion [GO:0071276]; cellular response to ethanol [GO:0071361]; cellular response to L-glutamine [GO:1904845]; defense response [GO:0006952]; hydrogen peroxide biosynthetic process [GO:0050665]; hypoxia-inducible factor-1alpha signaling pathway [GO:0097411]; inflammatory response [GO:0006954];... | dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; monoatomic ion channel complex [GO:0034702]; NADPH oxidase complex [GO:0043020]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; perinuclear endoplasmic reticulum [GO:0097038]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [... | flavin adenine dinucleotide binding [GO:0050660]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; superoxide-generating NAD(P)H oxidase activity [GO:0016175] | PF08022;PF01794;PF08030; | 3.40.50.80;2.40.30.10; | null | PTM: Glycosylated. {ECO:0000269|PubMed:19159218}.; PTM: Phosphorylated on Ser and Thr residues. {ECO:0000269|PubMed:19028840}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000250|UniProtKB:Q61093}. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:28351984}. | null | null | null | null | null | FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel ... | Homo sapiens (Human) |
P04840 | VDAC1_YEAST | MSPPVYSDISRNINDLLNKDFYHATPAAFDVQTTTANGIKFSLKAKQPVKDGPLSTNVEAKLNDKQTGLGLTQGWSNTNNLQTKLEFANLTPGLKNELITSLTPGVAKSAVLNTTFTQPFFTARGAFDLCLKSPTFVGDLTMAHEGIVGGAEFGYDISAGSISRYAMALSYFAKDYSLGATLNNEQITTVDFFQNVNAFLQVGAKATMNCKLPNSNVNIEFATRYLPDASSQVKAKVSDSGIVTLAYKQLLRPGVTLGVGSSFDALKLSEPVHKLGWSLSFDA | null | null | apoptotic process [GO:0006915]; cell redox homeostasis [GO:0045454]; DNA transport [GO:0051027]; mitochondrion organization [GO:0007005]; monoatomic ion transport [GO:0006811]; positive regulation of protein import into nucleus [GO:0042307] | cytoplasm [GO:0005737]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; pore complex [GO:0046930] | porin activity [GO:0015288]; ubiquinone binding [GO:0048039]; voltage-gated monoatomic anion channel activity [GO:0008308] | PF01459; | 2.40.160.10; | Eukaryotic mitochondrial porin family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane. | null | null | null | null | null | FUNCTION: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selec... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04842 | ALOX1_KOMPG | MAIPEEFDILVLGGGSSGSCIAGRLANLDHSLKVGLIEAGENNLNNPWVYLPGIYPRNMKLDSKTASFYTSNPSPHLNGRRAIVPCANVLGGGSSINFMMYTRGSASDYDDFQAEGWKTKDLLPLMKKTETYQRACNNPDIHGFEGPIKVSFGNYTYPVCQDFLRASESQGIPYVDDLEDLVTAHGAEHWLKWINRDTGRRSDSAHAFVHSTMRNHDNLYLICNTKVDKIIVEDGRAAAVRTVPSKPLNPKKPSHKIYRARKQIVLSCGTISSPLVLQRSGFGDPIKLRAAGVKPLVNLPGVGRNFQDHYCFFSPYRIKP... | 1.1.3.13 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | methane catabolic process [GO:0046188]; methanol metabolic process [GO:0015945] | peroxisomal matrix [GO:0005782] | alcohol oxidase activity [GO:0047639]; flavin adenine dinucleotide binding [GO:0050660] | PF05199;PF00732; | 3.50.50.60;3.30.560.10; | GMC oxidoreductase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:9396748}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + O2 = an aldehyde + H2O2; Xref=Rhea:RHEA:19829, ChEBI:CHEBI:15379, ChEBI:CHEBI:15734, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478; EC=1.1.3.13; | null | PATHWAY: Energy metabolism; methane degradation. | null | null | FUNCTION: Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. {ECO:0000269|PubMed:9396748}. | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) |
P04843 | RPN1_HUMAN | MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRF... | null | null | protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; melanosome [GO:0042470]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791] | RNA binding [GO:0003723] | PF04597; | null | OST1 family | PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, promoting reticulophagy of endoplasmic reticulum sheets. {ECO:0000269|PubMed:32160526}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000305}. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:31831667}. | null | null | FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... | Homo sapiens (Human) |
P04844 | RPN2_HUMAN | MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVL... | null | null | protein modification process [GO:0036211]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear body [GO:0016604]; oligosaccharyltransferase complex [GO:0008250] | null | PF05817; | null | SWP1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:31831667}. | null | null | FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... | Homo sapiens (Human) |
P04850 | HN_PIV5 | MVAEDAPVRATCRVLFRTTTLIFLCTLLALSISILYESLITQKQIMSQAGSTGSNSGLGSITDLLNNILSVANQIIYNSAVALPLQLDTLESTLLTAIKSLQTSDKLEQNCSWSAALINDNRYINGINQFYFSIAEGRNLTLGPLLNMPSFIPTATTPEGCTRIPSFSLTKTHWCYTHNVILNGCQDHVSSNQFVSMGIIEPTSAGFPFFRTLKTLYLSDGVNRKSCSISTVPGGCMMYCFVSTQPERDDYFSAAPPEQRIIIMYYNDTIVERIINPPGVLDVWATLNPGTGSGVYYLGWVLFPIYGGVIKGTSLWNNQA... | 3.2.1.18 | null | symbiont entry into host cell [GO:0046718]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; host cell surface receptor binding [GO:0046789]; identical protein binding [GO:0042802] | PF00423; | 1.20.5.110;2.120.10.10; | Paramyxoviruses hemagglutinin-neuraminidase family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). {ECO:0000250}.; FUNCTION: Neuraminidase activity ensures the ef... | Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5) |
P04853 | HN_SENDZ | MDGDRGKRDSYWSTSPSGSTTKPASGWERSSKADTWLLILSFTQWALSIATVIICIIISARQGYSMKEYSMTVEALNMSSREVKESLTSLIRQEVIARAVNIQSSVQTGIPVLLNKNSRDVIQMIDKSCSRQELTQHCESTIAVHHADGIAPLEPHSFWRCPVGEPYLSSDPEISLLPGPSLLSGSTTISGCVRLPSLSIGEAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMFPDLNPVVSHTYDINDNRKSCSVVATGTRGYQLCSMPTVDERTDYSSDGIEDLVLDVLDLKGRTKSHRYRNSEVDLDHPFSAL... | 3.2.1.18 | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; host cell surface receptor binding [GO:0046789] | PF00423; | 2.120.10.10; | Paramyxoviruses hemagglutinin-neuraminidase family | PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. {ECO:0000269|PubMed:10876159, ECO:0000269|PubMed:6263875}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Folded in the endoplasmic reticulum. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.; FUNCTION: Neuraminidase activity ensures the efficient spread of the virus by ... | Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) |
P04855 | FUS_SENDZ | MTAYIQRSQCISTSLLVVLTTLVSCQIPRDRLSNIGVIVDEGKSLKIAGSHESRYIVLSLVPGVDFENGCGTAQVIQYKSLLNRLLIPLRDALDLQEALITVTNDTTQNAGAPQSRFFGAVIGTIALGVATSAQITAGIALAEAREAKRDIALIKESMTKTHKSIELLQNAVGEQILALKTLQDFVNDEIKPAISELGCETAALRLGIKLTQHYSELLTAFGSNFGTIGEKSLTLQALSSLYSANITEIMTTIKTGQSNIYDVIYTEQIKGTVIDVDLERYMVTLSVKIPILSEVPGVLIHKASSISYNIDGEEWYVTVP... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00523; | 1.10.287.2480;2.60.40.1690;2.40.490.10; | Paramyxoviruses fusion glycoprotein family | PTM: In natural infection, inactive F0 is matured into F1 and F2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing occu... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Folded in the endoplasmic reticulum by the human CANX and HSPA5 chaperones. | null | null | null | null | null | FUNCTION: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, p... | Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) |
P04859 | PHOSP_SENDH | MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLESDSTKKGIGE... | null | null | DNA-templated transcription [GO:0006351]; negative stranded viral RNA replication [GO:0039689] | host cell cytoplasm [GO:0030430]; protein-containing complex [GO:0032991] | disordered domain specific binding [GO:0097718]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF01806; | 1.10.287.340;1.10.8.10;1.10.287.320; | Respirovirus P protein family | PTM: Phosphorylated by PKC/PRKCZ, and other unknown kinases. Phosphorylation is necessary for viral transcription and replication. The N-terminus contains the majority of phosphorylated sites. Ser-249 is the major site of phosphorylation, but is not necessary for most functions. {ECO:0000269|PubMed:10544094, ECO:000026... | SUBCELLULAR LOCATION: Host cytoplasm. | null | null | null | null | null | FUNCTION: Essential cofactor of the RNA polymerase L that plays a central role in the transcription and replication by forming the polymerase complex with RNA polymerase L and recruiting L to the genomic N-RNA template for RNA synthesis. Plays also a central role in the encapsidation of nascent RNA chains by forming th... | Sendai virus (strain Harris) (SeV) |
P04862 | C_SENDZ | MASATLTAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSMLSCRVNQLTSEGTEAGSTTPSTLPKDQALLIEPKVRAKEKSQHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWAMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQVIMEEAWSLAAHIVQE | null | null | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated pert... | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | null | PF01692; | null | Respirovirus protein C family | PTM: Y1 and Y2 proteins are produced not only by alternative initiation, but also by proteolytic cleavage of C'. Only alternative initiation is detected in vitro, whereas in vivo cleavage seems to be predominant. {ECO:0000250|UniProtKB:P04861}. | SUBCELLULAR LOCATION: [Isoform C' protein]: Host cytoplasm {ECO:0000269|PubMed:2171459, ECO:0000269|PubMed:3026113}. Note=Protein C' seems to localize around the Golgi. {ECO:0000269|PubMed:3026113}.; SUBCELLULAR LOCATION: [Isoform C protein]: Host cytoplasm {ECO:0000269|PubMed:2171459, ECO:0000269|PubMed:3026113}. Viri... | null | null | null | null | null | FUNCTION: The different isoforms prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN-alpha/beta pathway requires binding to STAT1 i... | Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) |
P04867 | TGB1_BSMV | MDMTKTVEEKKTNGTDSVKGVFENSTIPKVPTGQEMGGDGSSTSKLKETLKVADQTPLSVDNGAKSKLDSSDRQVPGVADQTPLSVDNGAKSKLDSSDRQVPGPELKPNVKKSKKKRIQKPAQPSGPNDLKGGTKGSSQVGENVSENYTGISKEAAKQKQKTPKSVKMQSNLADKFKANDTRRSELINKFQQFVHETCLKSDFEYTGRQYFRARSNFFEMIKLASLYDKHLKECMARACTLERERLKRKLLLVRALKPAVDFLTGIISGVPGSGKSTIVRTLLKGEFPAVCALANPALMNDYSGIEGVYGLDDLLLSAVP... | 3.6.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12069530}; | transport of virus in host, cell to cell [GO:0046740] | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; host cell plasmodesma [GO:0044219]; host cytoskeleton [GO:0044163] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; RNA binding [GO:0003723] | PF01443; | 3.40.50.300; | Virgaviridae/benyvirus TGB1 movement protein family | null | SUBCELLULAR LOCATION: Host cell junction, host plasmodesma {ECO:0000269|PubMed:19570874}. Host nucleus {ECO:0000269|PubMed:28872759}. Host cytoplasm {ECO:0000269|PubMed:28872759}. Host nucleus, host nucleolus {ECO:0000269|PubMed:28872759}. Host cytoplasm, host cytoskeleton {ECO:0000250|UniProtKB:Q9IV54}. Note=TGB1 nucl... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:8995680}; | null | null | null | null | FUNCTION: Participates in the transport of viral genome to neighboring plant cells directly through plasmodesmata, without any budding (PubMed:18353960). Multifunctional movement protein with RNA-binding, ATPase and helicase activities (PubMed:12069530, PubMed:8995680). Engages in homologous interactions leading to the... | Barley stripe mosaic virus (BSMV) |
P04884 | GLYCO_VSIVO | MKCLLYLAFLFIGVNCKFTIVFPHNQKGNWKNVPSNYHYCPSSSDLNWHNDLIGTALQVKMPKSHKAIQADGWMCHASKWVTTCDFRWYGPKYITHSIRSFTPSVEQCKESIEQTKQGTWLNPGFPPQSCGYATVTDAEAAIVQVTPHHVLVDEYTGEWVDSQFINGKCSNDICPTVHNSTTWHSDYKVKGLCDSNLISTDITFFSEDGELSSLGKEGTGFRSNYFAYETGDKACKMQYCKHWGVRLPSGVWFEMADKDLFAAARFPECPEGSSISAPSQTSVDVSLIQDVERILDYSLCQETWSKIRAGLPISPVDLSY... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | host cell membrane [GO:0033644]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00974; | 2.30.29.130;2.30.30.640; | Vesiculovirus glycoprotein family | PTM: Glycosylated by host. Palmitoylated by host on Cys-489 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. Host membrane; Single-pass type I membrane protein. Note=The cytoplasmic domain sorts the protein to neurons dentrites instead of axons. When expressed in ex vivo polarized cells like epithelial cells, it sorts the protein to the basolateral si... | null | null | null | null | null | FUNCTION: Attaches the virus to host cellular receptor, inducing clathrin-dependent endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane. In neurons, neo-synthesized glycoproteins are sorted to the ... | Vesicular stomatitis Indiana virus (strain Orsay) (VSIV) |
P04896 | GNAS2_BOVIN | MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTT... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; sensory perception of chemical stimulus [GO:0007606] | cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834] | adenylate cyclase activator activity [GO:0010856]; beta-2 adrenergic receptor binding [GO:0031698]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; D1 dopamine receptor binding [GO:0031748]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(s) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63094}; Lipid-anchor {ECO:0000250|UniProtKB:P63094}. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:11087399, PubMed:15591060, Pub... | Bos taurus (Bovine) |
P04897 | GNAI2_RAT | MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEI... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; G protein-coupled acetylcholine receptor signal... | cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; neuronal dense core vesicle [GO:0098992]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/o... | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. | Rattus norvegicus (Rat) |
P04899 | GNAI2_HUMAN | MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPSRADDARQLFALSCTAEEQGVLPDDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITHSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEI... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; G protein-coupled acetylcholine receptor signal... | cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; midbody [GO:0030496]; neuronal dense core vesicle [GO:009899... | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | PTM: (Microbial infection) Deamidated at Gln-205 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes in the centrosomes of interphase and mitotic ce... | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. ... | Homo sapiens (Human) |
P04903 | GSTA2_RAT | MSGKPVLHYFNARGRMECIRWLLAAAGVEFEEKLIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILDLTEMIIQLVICPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLELLLYVEEFDASLLTSFPLLKAFKSRISSLPNVKKFLQPGSQRKPAMDAKQIEEARKVFKF | 2.5.1.18 | null | epithelial cell differentiation [GO:0030855]; glutathione metabolic process [GO:0006749]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | dinitrosyl-iron complex binding [GO:0035731]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | 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:P10648}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. {ECO:0000250|UniProtKB:P10648}. | Rattus norvegicus (Rat) |
P04904 | GSTA3_RAT | MPGKPVLHYFDGRGRMEPIRWLLAAAGVEFEEQFLKTRDDLARLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIATKYNLYGKDMKERALIDMYAEGVADLDEIVLHYPYIPPGEKEASLAKIKDKARNRYFPAFEKVLKSHGQDYLVGNRLSRADVYLVQVLYHVEELDPSALANFPLLKALRTRVSNLPTVKKFLQPGSQRKPLEDEKCVESAVKIFS | 2.5.1.18 | null | glutathione metabolic process [GO:0006749]; lipid metabolic process [GO:0006629]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | 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:Q16772}; 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. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregne... | Rattus norvegicus (Rat) |
P04905 | GSTM1_RAT | MPMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK | 2.5.1.18 | null | cellular detoxification of nitrogen compound [GO:0070458]; cellular response to xenobiotic stimulus [GO:0071466]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; nitrobenzene metabolic process [GO:0018916]; prostaglandin ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | enzyme binding [GO:0019899]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; nickel cation binding [GO:0016151]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; steroid binding [GO:0005496] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:8110735, ECO:0000269|PubMed:8664265}; PhysiologicalDirectio... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process (PubMed:8110735, PubMed:8664265). Participates in the formation of novel hepoxilin regioisomers (By similarity). {ECO:0000250|UniP... | Rattus norvegicus (Rat) |
P04906 | GSTP1_RAT | MPPYTIVYFPVRGRCEATRMLLADQGQSWKEEVVTIDVWLQGSLKSTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKDQKEAALVDMVNDGVEDLRCKYGTLIYTNYENGKDDYVKALPGHLKPFETLLSQNQGGKAFIVGNQISFADYNLLDLLLVHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPDHLNRPINGNGKQ | 2.5.1.18 | null | animal organ regeneration [GO:0031100]; cellular response to cell-matrix adhesion [GO:0071460]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; TRAF2-GSTP1 complex [GO:0097057] | dinitrosyl-iron complex binding [GO:0035731]; fatty acid binding [GO:0005504]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; JUN kinase binding [GO:0008432]; kinase regulator activity [GO:0019207]; organic cyclic compound binding [GO:0097159]; protein kinase binding [GO:00... | PF14497;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Pi family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}. | 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. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Negatively regulates CDK5 a... | Rattus norvegicus (Rat) |
P04908 | H2A1B_HUMAN | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; negative regulation of cell population proliferation [GO:0008285]; protein localization to CENP-A containing chromatin [GO:0061644] | CENP-A containing nucleosome [GO:0043505]; extracellular exosome [GO:0070062]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000269|PubMed:15823041}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involv... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Homo sapiens (Human) |
P04909 | H2A1_SCHPO | MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKTSGRTGKPSQEL | null | null | double-strand break repair [GO:0006302]; heterochromatin organization [GO:0070828]; homologous chromosome segregation [GO:0045143]; mitotic chromosome condensation [GO:0007076]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 DNA damage checkpoint signaling [GO:0007095] | chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553] | chromatin-protein adaptor activity [GO:0140463]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark t... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04910 | H2A2_SCHPO | MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL | null | null | double-strand break repair [GO:0006302]; heterochromatin organization [GO:0070828]; homologous chromosome segregation [GO:0045143]; mitotic chromosome condensation [GO:0007076]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 DNA damage checkpoint signaling [GO:0007095] | chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553] | chromatin-protein adaptor activity [GO:0140463]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark t... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04911 | H2A1_YEAST | MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKATKASQEL | null | null | chromatin organization [GO:0006325]; DNA repair [GO:0006281]; heterochromatin organization [GO:0070828]; negative regulation of transcription by RNA polymerase II [GO:0000122] | nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298] | DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark t... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04912 | H2A2_YEAST | MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL | null | null | chromatin organization [GO:0006325]; DNA repair [GO:0006281]; heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298] | DNA binding [GO:0003677]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark t... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04913 | H2B1_SCHPO | MSAAEKKPASKAPAGKAPRDTMKSADKKRGKNRKETYSSYIYKVLKQVHPDTGISNQAMRILNSFVNDIFERIATEASKLAAYNKKSTISSREIQTAVRLILPGELAKHAVTEGTKSVTKYSSSAQ | null | null | chromatin remodeling [GO:0006338]; double-strand break repair via homologous recombination [GO:0000724] | nucleosome [GO:0000786]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | chromatin-protein adaptor activity [GO:0140463]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitinated by the rhp6/ubc2-bre1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damag... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P04916 | RET4_RAT | MEWVWALVLLAALGGGSAERDCRVSSFRVKENFDKARFSGLWYAIAKKDPEGLFLQDNIIAEFSVDEKGHMSATAKGRVRLLSNWEVCADMVGTFTDTEDPAKFKMKYWGVASFLQRGNDDHWIIDTDYDTFALQYSCRLQNLDGTCADSYSFVFSRDPNGLTPETRRLVRQRQEELCLERQYRWIEHNGYCQSRPSRNSL | null | null | cardiac muscle tissue development [GO:0048738]; detection of light stimulus involved in visual perception [GO:0050908]; embryonic organ morphogenesis [GO:0048562]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; embryonic skeletal system development [GO:0048706]; eye development [GO:0001654]; female gen... | extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | protein-containing complex binding [GO:0044877]; retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4708098}. | null | null | null | null | null | FUNCTION: Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues (PubMed:4708098). Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane (By similarity). {ECO:0000250|UniProtKB:P... | Rattus norvegicus (Rat) |
P04917 | SRGN_RAT | MRQVPVGTRLVLALAFVLVWGSSVQGYPARRARYQWVRCKPDGIFANCIEEKGPRFDLIAEESNVGPPMTDPVLMRGFPNDFFPISDDYSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSLADMEWEYQPTDENNIVYFNYGPFDRMLTEQNQEQPGDFII | 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 space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; mast cell granule [GO:0042629]; postsynaptic specialization, intracellular component [GO:0099091]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granule [GO:0030141]; zymogen g... | collagen binding [GO:0005518] | PF04360; | null | Serglycin family | PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250|UniProtKB:P10124}. Cytolytic granule {ECO:0000250|UniProtKB:P10124}. Secreted, extracellular space {ECO:0000250|UniProtKB:P10124}. Golgi apparatus {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T-lymphocyte... | 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... | Rattus norvegicus (Rat) |
P04919 | B3AT_MOUSE | MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREEL... | null | null | bicarbonate transport [GO:0015701]; blood coagulation [GO:0007596]; chloride transport [GO:0006821]; erythrocyte development [GO:0048821]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; negative regulation of urine volume [GO:0035811]; pH elevation [GO:0045852]; plasma membrane pho... | ankyrin-1 complex [GO:0170014]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cortical cytoskeleton [GO:0030863]; cytoplasmic side of plasma membrane [GO:0009898]; intercalated disc [GO:0014704]; membrane [GO:0016020]; plasma membrane [GO:0005886]; Z disc [GO:0030018] | actin binding [GO:0003779]; ankyrin binding [GO:0030506]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; hemoglobin binding [GO:0030492]; protein homodimerization a... | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2713407}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the erythrocyte cell membrane and on the basolateral membra... | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P02730}; | null | null | null | null | FUNCTION: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the i... | Mus musculus (Mouse) |
P04920 | B3A2_HUMAN | MSSAPRRPAKGADSFCTPEPESLGPGTPGFPEQEEDELHRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEDEASEAEGARALTQPSPVSTPSSVQFFLQEDDSADRKAERTSPSSPAPLPHQEATPRASKGAQAGTQVEEAEAEAVAVASGTAGGDDGGASGRPLPKAQPGHRSYNLQERRRIGSMTGAEQALLPRVPTDEIEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQSGREGREPGPTPRARPRAPHKP... | null | null | amelogenesis [GO:0097186]; bicarbonate transport [GO:0015701]; digestive tract development [GO:0048565]; monoatomic anion transport [GO:0006820]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000565]; osteoc... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886] | chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; monoatomic anion transmembrane transporter activity [GO:0008509]; solute:inorganic anion antiporter activity [GO:0005452]; transmembrane transporter activity [GO:0022857] | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: [Isoform A]: Apical cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15184086}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform B1]: Apical cell membrane {ECO:0000269|PubMed:15184086}; M... | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:34668226}; CATALYTIC ACTIVITY: [Isoform A]: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbona... | null | null | null | null | FUNCTION: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent acti... | Homo sapiens (Human) |
P04921 | GLPC_HUMAN | MWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDGRMETSTPTIMDIVVIAGVIAAVAIVLVSLLFVMLRYMYRHKGTYHTNEAKGTEFAESADAALQGDPALQDAGDSSRKEYFI | null | null | null | cortical cytoskeleton [GO:0030863]; membrane [GO:0016020]; plasma membrane [GO:0005886] | null | null | null | Glycophorin-C family | PTM: O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7106126}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Note=Linked to the membrane via band 4.1. | null | null | null | null | null | FUNCTION: This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells. | Homo sapiens (Human) |
P04924 | TNFA_RABIT | MSTESMIRDVELAEGPLPKKAGGPQGSKRCLCLSLFSFLLVAGATTLFCLLHFRVIGPQEEEQSPNNLHLVNPVAQMVTLRSASRALSDKPLAHVVANPQVEGQLQWLSQRANALLANGMKLTDNQLVVPADGLYLIYSQVLFSGQGCRSYVLLTHTVSRFAVSYPNKVNLLSAIKSPCHRETPEEAEPMAWYEPIYLGGVFQLEKGDRLSTEVNQPEYLDLAESGQVYFGIIAL | null | null | antiviral innate immune response [GO:0140374]; cellular response to amino acid stimulus [GO:0071230]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nicotine [GO:0071316]; cellular response to type II interferon [GO:0071346]; chronic inflammatory response to antigenic stimulus [GO:0002439]; ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; phagocytic cup [GO:0001891]; recycling endosome [GO:0055037] | cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secre... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:00... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain c... | Oryctolagus cuniculus (Rabbit) |
P04925 | PRIO_MOUSE | MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG | null | null | activation of protein kinase activity [GO:0032147]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; cellular response to xenobiotic stimulus [GO:0071466]; intracellular copper ion homeostasis [GO:00... | cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; side o... | amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; ATP-dependent protein binding [GO:0043008]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; ... | PF00377;PF11587; | 1.10.790.10; | Prion family | PTM: N-glycosylated. {ECO:0000269|PubMed:16492732, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19568430}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:9837873}; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000269|PubMed:11756421}. 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- and pe... | 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 ... | Mus musculus (Mouse) |
P04932 | MSP1_PLAFK | MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFHKEKMILNEEEITTKGASAQSGTSGTSGTSGPSGPSGTSPSSRSNTLPRSNTSSGASPPADASDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLDKINEIKNPP... | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; vacuolar membrane [GO:0005774] | null | PF12946;PF07462; | 2.10.25.10; | null | PTM: The p190 precursor is cleaved by SUB1 prior to merozoite egress into 4 subunits p83, p30, p38, and p42 which remain non-covalently associated. SUB1-mediated proteolytic cleavage occurs in an orderly manner; the first cleavage occurs at the p83/p30 site, followed by cleavage at the p30/p38 site, the last cleavage o... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04933}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P04933}.; SUBCELLULAR LOCATION: [p19 subunit]: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q8I0U8}... | null | null | null | null | null | FUNCTION: During the asexual blood stage, involved in merozoite egress from host erythrocytes possibly via its interaction with the host cytoskeleton protein spectrin resulting in the destabilization of the host cytoskeleton and thus leading to erythrocyte cell membrane rupture (By similarity). Involved in the binding ... | Plasmodium falciparum (isolate K1 / Thailand) |
P04933 | MSP1_PLAFW | MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSKGSVASGGSGGSVASGGSVASGGSVASGGSVASGGSGNSRRTNPSDNSSDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLD... | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; vacuolar membrane [GO:0005774] | null | PF12946;PF07462; | 2.10.25.10; | null | PTM: The p190 precursor is cleaved by SUB1 prior to merozoite egress into 4 subunits p83, p30, p38, and p42 which remain non-covalently associated (PubMed:12404375, PubMed:14766224, PubMed:20735778, PubMed:2995820). SUB1-mediated proteolytic cleavage occurs in an orderly manner; the first cleavage occurs at the p83/p30... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20735778}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:2995820}.; SUBCELLULAR LOCATION: [p19 subunit]: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q8I0U8}; L... | null | null | null | null | null | FUNCTION: During the asexual blood stage, involved in merozoite egress from host erythrocytes possibly via its interaction with the host cytoskeleton protein spectrin resulting in the destabilization of the host cytoskeleton and thus leading to erythrocyte cell membrane rupture (By similarity). Involved in the binding ... | Plasmodium falciparum (isolate Wellcome) |
P04936 | POLG_HRV2 | MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDVLEKGIPTLQSPTVEACGYSDRIIQITRGDSTITSQDVANAIVAYGVWPHYLSSKDASAIDKPSQPDTSSNRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQGTLIVALIPEHQIASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTLLGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPLETSSAINTIPITISISPMCA... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.40.10.120;2.60.120.20;3.30.70.270;3.40.50.300;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Human rhinovirus 2 (HRV-2) |
P04937 | FINC_RAT | MLRGPGPGRLLLLAVLCLGTSVRCTETGKSKRQAQQIVQPPSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHVLQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGM... | null | null | acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; cellular response to amyloid-beta [GO:1904646]; cellular response to angiotensin [GO:1904385]... | apical plasma membrane [GO:0016324]; basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; fibrinogen complex [GO:0... | extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; mercury ion binding [GO:0045340]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]; proteoglycan binding [GO:0043394]; signaling receptor... | PF00039;PF00040;PF00041; | 2.10.70.10;2.10.10.10;2.60.40.10; | null | PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11276}. Secreted {ECO:0000250|UniProtKB:P11276}. | null | null | null | null | null | FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrilloge... | Rattus norvegicus (Rat) |
P04938 | MUP11_MOUSE | MKMLLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE | null | null | aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; cellular response to testosterone stimulus [GO:0071394]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negat... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q5FW60}. | null | null | null | null | null | FUNCTION: Major urinary proteins (Mups) bind pheromones, and thus stabilize them to allow slow release into the air from urine marks. May protect pheromones from oxidation. May also act as pheromones themselves. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suc... | Mus musculus (Mouse) |
P04939 | MUP3_MOUSE | MKLLLPLLLLLCLELTLVCIHAEESSSMERNFNVEQISGYWFSIAEASYEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE | null | null | aerobic respiration [GO:0009060]; cellular response to lipid [GO:0071396]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; heat generation [GO:0031649]; locomotor rhythm [GO:0045475]; mitochondrion organization [GO:0007005]; negative regulation of DNA-templated transcription [GO:0045892... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | insulin receptor activity [GO:0005009]; odorant binding [GO:0005549]; pheromone binding [GO:0005550]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | PTM: Glycosylated. {ECO:0000269|PubMed:16944957}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. | Mus musculus (Mouse) |
P04950 | OPS3_DROME | MESGNVSSSLFGNVSTALRPEARLSAETRLLGWNVPPEELRHIPEHWLTYPEPPESMNYLLGTLYIFFTLMSMLGNGLVIWVFSAAKSLRTPSNILVINLAFCDFMMMVKTPIFIYNSFHQGYALGHLGCQIFGIIGSYTGIAAGATNAFIAYDRFNVITRPMEGKMTHGKAIAMIIFIYMYATPWVVACYTETWGRFVPEGYLTSCTFDYLTDNFDTRLFVACIFFFSFVCPTTMITYYYSQIVGHVFSHEKALRDQAKKMNVESLRSNVDKNKETAEIRIAKAAITICFLFFCSWTPYGVMSLIGAFGDKTLLTPGAT... | null | null | absorption of UV light [GO:0016039]; cellular response to light stimulus [GO:0071482]; detection of UV [GO:0009589]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; phototransduction, UV [GO:0007604]; visual perception [GO:0007601] | membrane [GO:0016020] | G protein-coupled photoreceptor activity [GO:0008020] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Drosophila melanogaster (Fruit fly) |
P04958 | TETX_CLOTE | MPITINNFRYSDPVNNDTIIMMEPPYCKGLDIYYKAFKITDRIWIVPERYEFGTKPEDFNPPSSLIEGASEYYDPNYLRTDSDKDRFLQTMVKLFNRIKNNVAGEALLDKIINAIPYLGNSYSLLDKFDTNSNSVSFNLLEQDPSGATTKSAMLTNLIIFGPGPVLNKNEVRGIVLRVDNKNYFPCRDGFGSIMQMAFCPEYVPTFDNVIENITSLTIGKSKYFQDPALLLMHELIHVLHGLYGMQVSSHEIIPSKQEIYMQHTYPISAEELFTFGGQDANLISIDIKNDLYEKTLNDYKAIANKLSQVTSCNDPNIDID... | 3.4.24.68 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | modulation by symbiont of host neurotransmitter secretion [GO:0044079]; proteolysis [GO:0006508] | clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.; EC=3.4.24.68; | null | null | null | null | FUNCTION: Tetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endop... | Clostridium tetani (strain Massachusetts / E88) |
P04961 | PCNA_RAT | MFEARLIQGSILKKVLEALKDLINEACWDISSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVSIEMNEPVQLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS | null | null | base-excision repair, gap-filling [GO:0006287]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; epithelial cell differentiation [GO:0030855]; estrous cycle [GO:0044849]; heart development [GO:0007507]; leading strand elong... | centrosome [GO:0005813]; chromatin [GO:0000785]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nuclear lamina [GO:0005652]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]; PCNA complex [GO:0043626]; PCNA-p21 complex [GO:0070... | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; dinucleotide insertion or deletion binding [GO:0032139]; DNA polymerase binding [GO:0070182]; DNA polymerase processivity factor activity [GO:0030337]; enzyme binding [GO:0019899]; histone acetyltransferase binding [GO:0035035]; identical protein binding... | PF02747;PF00705; | 3.70.10.10; | PCNA family | PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity). {ECO:0000250|UniProtKB:P12004}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to U... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12004}. Note=Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. Colocalizes with CREBBP, EP30... | null | null | null | null | null | FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimi... | Rattus norvegicus (Rat) |
P04963 | PRXC_LEPFU | MFSKVLPFVGAVAALPHSVRQEPGSGIGYPYDNNTLPYVAPGPTDSRAPCPALNALANHGYIPHDGRAISRETLQNAFLNHMGIANSVIELALTNAFVVCEYVTGSDCGDSLVNLTLLAEPHAFEHDHSFSRKDYKQGVANSNDFIDNRNFDAETFQTSLDVVAGKTHFDYADMNEIRLQRESLSNELDFPGWFTESKPIQNVESGFIFALVSDFNLPDNDENPLVRIDWWKYWFTNESFPYHLGWHPPSPAREIEFVTSASSAVLAASVTSTPSSLPSGAIGPGAEAVPLSFASTMTPFLLATNAPYYAQDPTLGPNDK... | 1.11.1.10 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mn(2+) ion per subunit.; | null | null | chloride peroxidase activity [GO:0016691]; metal ion binding [GO:0046872] | PF01328; | 1.10.489.10; | Chloroperoxidase family | PTM: N- and O-glycosylated. | null | CATALYTIC ACTIVITY: Reaction=RH + Cl(-) + H2O2 = RCl + 2 H2O.; EC=1.11.1.10; | null | null | null | null | FUNCTION: Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases. | Leptoxyphium fumago (Caldariomyces fumago) |
P04964 | DAPDH_CORGL | MTNIRVAIVGYGNLGRSVEKLIAKQPDMDLVGIFSRRATLDTKTPVFDVADVDKHADDVDVLFLCMGSATDIPEQAPKFAQFACTVDTYDNHRDIPRHRQVMNEAATAAGNVALVSTGWDPGMFSINRVYAAAVLAEHQQHTFWGPGLSQGHSDALRRIPGVQKAVQYTLPSEDALEKARRGEAGDLTGKQTHKRQCFVVADAADHERIENDIRTMPDYFVGYEVEVNFIDEATFDSEHTGMPHGGHVITTGDTGGFNHTVEYILKLDRNPDFTASSQIAFGRAAHRMKQQGQSGAFTVLEVAPYLLSPENLDDLIARDV | 1.4.1.16 | null | diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process via diaminopimelate [GO:0009089] | null | diaminopimelate dehydrogenase activity [GO:0047850] | PF16654; | 3.40.50.720; | Diaminopimelate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:13561, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:57791, ChEBI:CHEBI:58349, ChEBI:CHEBI:58556; EC=1.4.1.16; Evidence={ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for meso-2,6-diaminoheptanedioate {ECO:0000269|Ref.4}; KM=0.12 mM for NADP(+) {ECO:0000269|Ref.4}; KM=0.13 mM for NADPH {ECO:0000269|Ref.4}; KM=0.28 mM for L-2-amino-6-oxoheptanedioate {ECO:0000269|Ref.4}; KM=36 mM for ammonia {ECO:0000269|Ref.4}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 9.8 for the oxidative deamination of meso-diaminopimelate and 7.9 for the reductive amination of L-2-amino-6-oxopimelate. {ECO:0000269|Ref.4}; | null | FUNCTION: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since... | Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) |
P04968 | ILVA_ECOLI | MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVN... | 4.3.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:5321308}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; threonine catabolic process [GO:0006567]; threonine metabolic process [GO:0006566] | null | amino acid binding [GO:0016597]; L-serine ammonia-lyase activity [GO:0003941]; pyridoxal phosphate binding [GO:0030170]; threonine deaminase activity [GO:0004794] | PF00291;PF00585; | 3.40.50.1100; | Serine/threonine dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1. | null | null | FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and sh... | Escherichia coli (strain K12) |
P04971 | VSPF_BOTAT | MVLIRVIANLLILQVSYAQKSSELVIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIHLGKHAGSVANYDEVVRYPKEKFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP | 3.4.21.74 | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; | null | null | null | null | FUNCTION: Thrombin-like snake venom serine protease. Cleaves Arg-Gly bonds in fibrinogen alpha chains (FGA). {ECO:0000269|PubMed:1011993}. | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
P04972 | CNRG_BOVIN | MNLEPPKAEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII | 3.1.4.35 | null | positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment membrane [GO:0042622] | 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; ion binding [GO:0043167]; molecular adaptor activity [GO:0060090]; zinc ion binding [GO:0008270] | PF04868; | 4.10.1120.10; | Rod/cone cGMP-PDE gamma subunit family | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; | null | null | null | null | FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. | Bos taurus (Bovine) |
P04975 | CLCB_BOVIN | MADDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDEGFGAPAGSQGGLAQPGPASGASEDMGATVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQRKRLQELDAASKVMEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADIIGYVASEEAFVKESKEETPGTEWEKVAQLCDFNPKSSKQCKDVSRLRSVLMSLKQTPLSR | null | null | clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886] | clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin vesicle coat [GO:0030125]; plasma membrane [GO:0005886]; postsynaptic endocytic zone cytoplasmic component [GO:0099631]; synaptic vesicle membrane [GO:0030672] | clathrin heavy chain binding [GO:0032050]; structural molecule activity [GO:0005198] | PF01086; | null | Clathrin light chain family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles. | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. | Bos taurus (Bovine) |
P04977 | TOX1_BORPE | MRCTRAIRQTARTGWLTWLAILAVTAPVTSPAWADDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF | 2.4.2.- | null | null | extracellular region [GO:0005576] | NAD+ ADP-ribosyltransferase activity [GO:0003950]; nucleotidyltransferase activity [GO:0016779]; toxin activity [GO:0090729] | PF02917; | 3.90.210.10; | Bacterial exotoxin subunit A family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11854200}. Note=The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secre... | null | null | null | null | null | FUNCTION: S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catal... | Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) |
P04982 | RBSD_ECOLI | MKKGTVLNSDISSVISRLGHTDTLVVCDAGLPIPKSTTRIDMALTQGVPSFMQVLGVVTNEMQVEAAIIAEEIKHHNPQLHETLLTHLEQLQKHQGNTIEIRYTTHEQFKQQTAESQAVIRSGECSPYANIILCAGVTF | 5.4.99.62 | null | D-ribose catabolic process [GO:0019303] | cytosol [GO:0005829] | D-ribose pyranase activity [GO:0062193]; identical protein binding [GO:0042802]; intramolecular lyase activity [GO:0016872]; intramolecular transferase activity [GO:0016866]; monosaccharide binding [GO:0048029] | PF05025; | 3.40.1650.10; | RbsD / FucU family, RbsD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=beta-D-ribopyranose = beta-D-ribofuranose; Xref=Rhea:RHEA:25432, ChEBI:CHEBI:27476, ChEBI:CHEBI:47002; EC=5.4.99.62; Evidence={ECO:0000269|PubMed:15060078}; CATALYTIC ACTIVITY: Reaction=beta-D-allofuranose = beta-D-allopyranose; Xref=Rhea:RHEA:25609, ChEBI:CHEBI:40656, ChEBI:CHEBI:50256; EC... | null | PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2. | null | null | FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. {ECO:0000269|PubMed:15060078}. | Escherichia coli (strain K12) |
P04983 | RBSA_ECOLI | MEALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGTLLWLGKETTFTGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKTMYAEADKLLAKLNLRFKSDKLVGDLSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVASLTEDSLIEMMVGRKLEDQYPHLDKAPGDIRLKVDNLCGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS... | 7.5.2.7 | null | D-ribose transmembrane transport [GO:0015752] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020] | ABC-type D-ribose transporter activity [GO:0015611]; ABC-type monosaccharide transporter activity [GO:0015407]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; D-ribose transmembrane transporter activity [GO:0015591] | PF00005; | 3.40.50.300; | ABC transporter superfamily, Ribose importer (TC 3.A.1.2.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:8762140}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for ATP {ECO:0000269|PubMed:8762140}; | null | null | null | FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:8762140}. | Escherichia coli (strain K12) |
P04985 | ELN_BOVIN | MRSLTAAARRPEVLLLLLCILQPSQPGGVPGAVPGGVPGGVFFPGAGLGGLGVGGLGPGVKPAKPGVGGLVGPGLGAEGSALPGAFPGGFFGAGGGAAGAAAAYKAAAKAGAAGLGVGGIGGVGGLGVSTGAVVPQLGAGVGAGVKPGKVPGVGLPGVYPGGVLPGAGARFPGIGVLPGVPTGAGVKPKAQVGAGAFAGIPGVGPFGGQQPGLPLGYPIKAPKLPAGYGLPYKTGKLPYGFGPGGVAGSAGKAGYPTGTGVGPQAAAAAAKAAAKLGAGGAGVLPGVGVGGPGIPGAPGAIPGIGGIAGVGAPDAAAAAA... | null | null | null | collagen-containing extracellular matrix [GO:0062023]; elastic fiber [GO:0071953]; extracellular region [GO:0005576] | extracellular matrix structural constituent [GO:0005201] | null | null | Elastin family | PTM: Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tet... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of elastic fibers. {ECO:0000250|UniProtKB:P15502}. | null | null | null | null | null | FUNCTION: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity). {ECO:0000250... | Bos taurus (Bovine) |
P04992 | RBL_PETHY | MSPQTETKASVGFKAGVKEYKLTYYTPEYQAKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGHRYRIERVIGERDQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLKATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRM... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250}. | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Petunia hybrida (Petunia) |
P04993 | RECD_ECOLI | MKLQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENNEASHPLLATCVSEIGELQNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLFPVSDEINWQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYANAG... | 5.6.2.3 | null | DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; double-strand break repair via homologous recombination [GO:0000724]; recombinational repair [GO:0000725] | exodeoxyribonuclease V complex [GO:0009338] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exodeoxyribonuclease V activity [GO:0008854]; helicase activity [GO:0004386]; isomerase activity [GO:0016853]; single-stranded DNA helicase activity [GO:0017116] | PF13245;PF21185;PF13538; | 3.40.50.300;1.10.10.1020; | RecD family | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous stran... | null | null | null | null | FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence fro... | Escherichia coli (strain K12) |
P04994 | EX7L_ECOLI | MLPSQSPAIFTVSRLNQTVRLLLEHEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKKPLPSPAHCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGDDAPGQIVRAIELANQRNECDVLIVGRGGGSLEDLWSFNDERVARAIFTSRIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQVQSTRQRLEMAMDYYLANRTRRFTQIHHRLQQQHPQLRLARQQTMLE... | 3.1.11.6 | COFACTOR: Note=Does not require a metal cofactor. {ECO:0000269|PubMed:4602029}; | DNA catabolic process [GO:0006308]; mismatch repair [GO:0006298] | cytoplasm [GO:0005737]; exodeoxyribonuclease VII complex [GO:0009318] | DNA binding [GO:0003677]; exodeoxyribonuclease VII activity [GO:0008855] | PF02601;PF13742; | null | XseA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:6284744}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00378, ECO:0000269|PubMed:22718974, ECO:0000269|PubMed:4602029, ECO:0000269|PubMed:4602030}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 to 7.9. {ECO:0000269|PubMed:4602029}; | null | FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. It can also excise thymine dimers i... | Escherichia coli (strain K12) |
P04995 | EX1_ECOLI | MMNDGKQQSTFLFHDYETFGTHPALDRPAQFAAIRTDSEFNVIGEPEVFYCKPADDYLPQPGAVLITGITPQEARAKGENEAAFAARIHSLFTVPKTCILGYNNVRFDDEVTRNIFYRNFYDPYAWSWQHDNSRWDLLDVMRACYALRPEGINWPENDDGLPSFRLEHLTKANGIEHSNAHDAMADVYATIAMAKLVKTRQPRLFDYLFTHRNKHKLMALIDVPQMKPLVHVSGMFGAWRGNTSWVAPLAWHPENRNAVIMVDLAGDISPLLELDSDTLRERLYTAKTDLGDNAAVPVKLVHINKCPVLAQANTLRPEDA... | 3.1.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:18591666}; | DNA catabolic process [GO:0006308]; DNA repair [GO:0006281] | null | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; magnesium ion binding [GO:0000287]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310]; single-stranded DNA binding [GO:0003697] | PF08411;PF00929; | 1.10.287.1240;3.30.1520.20;1.20.1280.70;3.30.420.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}; | null | null | null | null | FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027). {... | Escherichia coli (strain K12) |
P05000 | IFNW1_HUMAN | MALLFPLLAALVMTSYSPVGSLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMSVLHEMLQQIFSLFHTERSSAAWNMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISSPALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS | null | null | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved ... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; type I interferon receptor binding [GO:0005132] | PF00143; | 1.20.1250.10; | Alpha/beta interferon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Homo sapiens (Human) |
P05013 | IFNA6_HUMAN | MALPFALLMALVVLSCKSSCSLDCDLPQTHSLGHRRTMMLLAQMRRISLFSCLKDRHDFRFPQEEFDGNQFQKAEAISVLHEVIQQTFNLFSTKDSSVAWDERLLDKLYTELYQQLNDLEACVMQEVWVGGTPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSSSRNLQERLRRKE | null | null | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved ... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132] | PF00143; | 1.20.1250.10; | Alpha/beta interferon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. | Homo sapiens (Human) |
P05014 | IFNA4_HUMAN | MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRHDFGFPEEEFDGHQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD | null | null | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; humoral immune response [GO:0006959]; natural killer cell activation involved ... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; type I interferon receptor binding [GO:0005132] | PF00143; | 1.20.1250.10; | Alpha/beta interferon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. | Homo sapiens (Human) |
P05017 | IGF1_MOUSE | MGKISSLPTQLFKICLCDFLKIKIHIMSSSHLFYLALCLLTFTSSTTAGPETLCGAELVDALQFVCGPRGFYFNKPTGYGSSIRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPTKAARSIRAQRHTDMPKTQKEVHLKNTSRGSAGNKTYRM | null | null | androgen receptor signaling pathway [GO:0030521]; blood vessel remodeling [GO:0001974]; branching morphogenesis of an epithelial tube [GO:0048754]; cell activation [GO:0001775]; cell development [GO:0048468]; cell population proliferation [GO:0008283]; cellular response to glucose stimulus [GO:0071333]; cellular respon... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; insulin-like growth factor ternary complex [GO:0042567]; interstitial matrix [GO:0005614]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0... | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; protein serine/threonine kinase activator activity [GO:0043539]; receptor ligand activity [GO:0048018]; steroid binding [GO:0005496]; transmembrane recepto... | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496647}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bon... | Mus musculus (Mouse) |
P05019 | IGF1_HUMAN | MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK | null | null | activation of protein kinase B activity [GO:0032148]; bone mineralization involved in bone maturation [GO:0035630]; cell activation [GO:0001775]; cell population proliferation [GO:0008283]; cellular response to amyloid-beta [GO:1904646]; epithelial to mesenchymal transition [GO:0001837]; glycolate metabolic process [GO... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; insulin-like growth factor binding protein complex [GO:0016942]; insulin-like growth factor ternary complex [GO:0042567]; platelet alpha granule lumen [GO:0031093] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bon... | Homo sapiens (Human) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.