Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P08235 | MCR_HUMAN | METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRS... | null | null | intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165] | chromatin [GO:0000785]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleoplasm [GO:0005654]; receptor complex [GO:0043235] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; sequence-specific double-stranded DNA bindin... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated. {ECO:0000269|PubMed:1655735}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane. | null | null | null | null | null | FUNCTION: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and b... | Homo sapiens (Human) |
P08236 | BGLR_HUMAN | MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFY... | 3.2.1.31 | null | carbohydrate metabolic process [GO:0005975]; chondroitin sulfate catabolic process [GO:0030207]; glucuronoside catabolic process [GO:0019391]; glycosaminoglycan catabolic process [GO:0006027]; heparan sulfate proteoglycan catabolic process [GO:0030200]; hyaluronan catabolic process [GO:0030214] | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; membrane [GO:0016020] | beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102] | PF00703;PF02836;PF02837; | 2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | PTM: N-linked glycosylated with 3 to 4 oligosaccharide chains. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000305|PubMed:3355537}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634; Evidence={ECO:0000305|... | null | null | null | null | FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates. | Homo sapiens (Human) |
P08237 | PFKAM_HUMAN | MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEA... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glucose homeostasis [GO:0042593]; glycogen catabolic process [GO:0005980]; glycolysis from storage polysaccharide through glucose-1-phosphate [GO:0093001]; glycolytic process... | 6-phosphofructokinase complex [GO:0005945]; apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; sperm principal piece [GO:0097228] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | Homo sapiens (Human) |
P08238 | HS90B_HUMAN | MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKH... | null | null | cellular response to heat [GO:0034605]; cellular response to interleukin-4 [GO:0071353]; chaperone-mediated protein complex assembly [GO:0051131]; negative regulation of apoptotic process [GO:0043066]; negative regulation of proteasomal protein catabolic process [GO:1901799]; negative regulation of proteasomal ubiquiti... | aryl hydrocarbon receptor complex [GO:0034751]; axonal growth cone [GO:0044295]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic growth cone [GO:0044294]; dynein axonemal particle [GO:0120293]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granu... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein binding [GO:0043008]; ATP-dependent protein folding chaperone [GO:0140662]; cadherin binding [GO:0045296]; disordered domain specific binding [GO:0097718]; DNA polymerase binding [GO:0070182]; double-stranded RNA binding [GO:0003725];... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). {ECO:0000269|PubMed:18042044}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: S-nitrosylated; negatively regulates the ATPase activity. {ECO:0000305|PubMed:19696785}.; PTM: Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide (P... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:24880080, ECO:0000269|PubMed:9482106}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:18239673}. Secreted {ECO:0000269|PubMed:20599762}. Cell membrane {ECO:0000269|PubMed:20599762}. Dynei... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for ATP {ECO:0000269|PubMed:18400751}; | 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 linked to its ATPase activity. This cycle probably induces conformational changes in the ... | Homo sapiens (Human) |
P08240 | SRPRA_HUMAN | MLDFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRLLREAEESSKIRAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKEGSDGPLATSKPVPAEKSGLPVGPENGVELSKEELIRRKREEFIQKHGRGMEKSNKSTKSDAPKEKGKKAPRVWELGGCANKEVLDYSTPTTNGTPEAALSEDINLIRGTGSGGQLQDLDCSSSDDEGAAQNSTKPSATKGTLGGM... | null | null | cotranslational protein targeting to membrane [GO:0006613]; intracellular protein transport [GO:0006886]; protein targeting to ER [GO:0045047]; SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition [GO:0006617] | endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; signal recognition particle receptor complex [GO:0005785] | ATP hydrolysis activity [GO:0016887]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]; signal recognition particle binding [GO:0005047] | PF04086;PF00448;PF02881; | 3.30.450.60;3.40.50.300;1.20.120.140; | GTP-binding SRP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32916}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32916}; Cytoplasmic side {ECO:0000250|UniProtKB:P32916}. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane doma... | null | null | null | null | null | FUNCTION: Component of the signal recognition particle (SRP) complex receptor (SR) (PubMed:16439358). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (PubMed:16675701, PubMed:34020957). Forms a guanosine 5'-triphosphate (... | Homo sapiens (Human) |
P08243 | ASNS_HUMAN | MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEG... | 6.3.5.4 | null | asparagine biosynthetic process [GO:0006529]; cellular response to glucose starvation [GO:0042149]; glutamine metabolic process [GO:0006541]; L-asparagine biosynthetic process [GO:0070981]; negative regulation of apoptotic process [GO:0043066]; positive regulation of mitotic cell cycle [GO:0045931] | cytosol [GO:0005829] | asparagine synthase (glutamine-hydrolyzing) activity [GO:0004066]; ATP binding [GO:0005524] | PF00733;PF13537; | 3.60.20.10;3.40.50.620; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC... | null | PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1. | null | null | null | Homo sapiens (Human) |
P08244 | PYRF_ECOLI | MTLTASSSSRAVTNSPVVVALDYHNRDDALAFVDKIDPRDCRLKVGKEMFTLFGPQFVRELQQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAREALVPFGKDAPLLIAVTVLTSMEASDLVDLGMTLSPADYAERLAALTQKCGLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSEAGDQRRIMTPEQALSAGVDYMVIGRPVTQSVDPAQTLKAINASLQRSA | 4.1.1.23 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; nucleobase-containing small molecule interconversion [GO:0015949] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; orotidine-5'-phosphate decarboxylase activity [GO:0004590] | PF00215; | 3.20.20.70; | OMP decarboxylase family, Type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. | null | null | FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Escherichia coli (strain K12) |
P08246 | ELNE_HUMAN | MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH | 3.4.21.37 | null | acute inflammatory response to antigenic stimulus [GO:0002438]; biosynthetic process of antibacterial peptides active against Gram-negative bacteria [GO:0002812]; defense response to bacterium [GO:0042742]; extracellular matrix disassembly [GO:0022617]; intracellular calcium ion homeostasis [GO:0006874]; leukocyte migr... | azurophil granule lumen [GO:0035578]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; phagocytic vesicle [GO:0045335]; secretory granul... | cytokine binding [GO:0019955]; endopeptidase activity [GO:0004175]; heparin binding [GO:0008201]; peptidase activity [GO:0008233]; protease binding [GO:0002020]; serine-type endopeptidase activity [GO:0004252]; transcription corepressor activity [GO:0003714] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:10947984}. Note=Localized in phagolysosomes following ingestion of E.coli by neutrophils. {ECO:0000269|PubMed:10947984}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.; EC=3.4.21.37; Evidence={ECO:0000269|PubMed:36899106}; | null | null | null | null | FUNCTION: Serine protease that modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed:15140022). Promotes cleavage of GSDMB, thereby inhibiting pyroptosis (PubMed:36899106). Capable of killing E.coli but not S.aureus in vitro; ... | Homo sapiens (Human) |
P08247 | SYPH_HUMAN | MLLLADMDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYSGELQLSVDCANKTESDLSIEVEFEYPFRLHQVYFDAPTCRGGTTKVFLVGDYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMLDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPVCRQTGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFLRAPPGAPEKQPAPGDAYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPAGSGGSGYGPQGDYGQQGYGPQGAPTSFSNQM | null | null | cellular response to organic substance [GO:0071310]; endocytosis [GO:0006897]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of opioid receptor signaling pathway [GO:2000474]; regulation of short-term neuronal synaptic plasticity [... | excitatory synapse [GO:0060076]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic vesicle [GO:0008021]; synaptic vesicle mem... | cholesterol binding [GO:0015485]; identical protein binding [GO:0042802]; SH2 domain binding [GO:0042169] | PF01284; | null | Synaptophysin/synaptobrevin family | PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:P07825}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:18662323}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000269|PubMed:18662323}. | null | null | null | null | null | FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
P08249 | MDHM_MOUSE | MLSALARPAGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMVCIIANPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAI... | 1.1.1.37 | null | aerobic respiration [GO:0009060]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209] | L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase (NADP+) activity [GO:0046554]; malate dehydrogenase activity [GO:0016615]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 1 family | PTM: Acetylation is enhanced after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri- and tetraacetylations. Glucose also increases acetylation (By similarity). Acetylation of Lys-239 and Lys-314 is observed in liver mitochondria from fasted mice but not from fed mice. {ECO:... | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P04636}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10004}; | null | null | null | null | null | Mus musculus (Mouse) |
P08250 | APOA1_CHICK | MRGVLVTLAVLFLTGTQARSFWQHDEPQTPLDRIRDMVDVYLETVKASGKDAIAQFESSAVGKQLDLKLADNLDTLSAAAAKLREDMAPYYKEVREMWLKDTEALRAELTKDLEEVKEKIRPFLDQFSAKWTEELEQYRQRLTPVAQELKELTKQKVELMQAKLTPVAEEARDRLRGHVEELRKNLAPYSDELRQKLSQKLEEIREKGIPQASEYQAKVMEQLSNLREKMTPLVQEFRERLTPYAENLKNRLISFLDELQKSVA | null | null | acylglycerol homeostasis [GO:0055090]; adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:00... | chylomicron [GO:0042627]; endocytic vesicle [GO:0030139]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [... | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). | Gallus gallus (Chicken) |
P08252 | CHI1_TOBAC | MRLCKFTALSSLLFSLLLLSASAEQCGSQAGGARCPSGLCCSKFGWCGNTNDYCGPGNCQSQCPGGPTPTPPTPPGGGDLGSIISSSMFDQMLKHRNDNACQGKGFYSYNAFINAARSFPGFGTSGDTTARKREIAAFFAQTSHETTGGWATAPDGPYAWGYCWLREQGSPGDYCTPSGQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDPVISFKSALWFWMTPQSPKPSCHDVIIGRWQPSAGDRAANRLPGFGVITNIINGGLECGRGTDSRVQDRIGFYRRYCSILGVSPGDNLDCGNQRSF... | 3.2.1.14 | null | cell wall macromolecule catabolic process [GO:0016998]; chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; polysaccharide catabolic process [GO:0000272] | vacuole [GO:0005773] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00187;PF00182; | 1.10.530.10;3.30.20.10;3.30.60.10; | Glycosyl hydrolase 19 family, Chitinase class I subfamily | PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein. | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:1946457}. Note=Vacuolar and protoplast. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; | null | null | null | null | FUNCTION: Defense against chitin-containing fungal pathogens. | Nicotiana tabacum (Common tobacco) |
P08253 | MMP2_HUMAN | MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTT... | 3.4.24.24 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12147339, ECO:0000269|PubMed:21813640, ECO:0000269|PubMed:8549817}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:21813640, ECO:0000269|PubMed:8549817}; COFACTOR: Name=Zn(2+)... | angiogenesis [GO:0001525]; blood vessel maturation [GO:0001955]; bone trabecula formation [GO:0060346]; cellular response to amino acid stimulus [GO:0071230]; cellular response to estradiol stimulus [GO:0071392]; cellular response to fluid shear stress [GO:0071498]; cellular response to interleukin-1 [GO:0071347]; cell... | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcomere [GO:0030017] | endopeptidase activity [GO:0004175]; fibronectin binding [GO:0001968]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270] | PF00040;PF00045;PF00413; | 3.40.390.10;2.10.10.10;2.110.10.10; | Peptidase M10A family | PTM: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro. {ECO:0000269|PubMed:17435175}.; PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be ... | SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2834383}. Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocyte... | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; EC=3.4.24.24; Evidence={ECO:0000305|PubMed:11179305, ECO:0000305|PubMed:11431697, ECO:0000305|PubMed:12147339, ECO:0000305|PubMed:2834383}; | null | null | null | null | FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big ... | Homo sapiens (Human) |
P08254 | MMP3_HUMAN | MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLR... | 3.4.24.17 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 4 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | cellular response to amino acid stimulus [GO:0071230]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nitric oxide [GO:0071732]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix di... | cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: Directly cleaved by HTRA2 to produce active form. {ECO:0000269|PubMed:22265821}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Nucleus {ECO:0000269|PubMed:35940311}. Cytoplasm {ECO:0000269|PubMed:35940311}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic residues.; EC=3.4.24.17; Evidence={ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:21330369}; | null | null | null | null | FUNCTION: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 ... | Homo sapiens (Human) |
P08255 | OPS4_DROME | MEPLCNASEPPLRPEARSSGNGDLQFLGWNVPPDQIQYIPEHWLTQLEPPASMHYMLGVFYIFLFCASTVGNGMVIWIFSTSKSLRTPSNMFVLNLAVFDLIMCLKAPIFIYNSFHRGFALGNTWCQIFASIGSYSGIGAGMTNAAIGYDRYNVITKPMNRNMTFTKAVIMNIIIWLYCTPWVVLPLTQFWDRFVPEGYLTSCSFDYLSDNFDTRLFVGTIFFFSFVCPTLMILYYYSQIVGHVFSHEKALREQAKKMNVESLRSNVDKSKETAEIRIAKAAITICFLFFVSWTPYGVMSLIGAFGDKSLLTPGATMIPA... | null | null | 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) |
P08258 | HBA_MANSP | VLSPADKKNVKAAWDKVGGHAGEYGAEALERMFLSFPTTKTYFPHFNLSHGSDQVKGHGKKVADALTLAVGHVDDMPQALSKLSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Mandrillus sphinx (Mandrill) (Papio sphinx) |
P08261 | HBB_CHRRI | VHWSAEEKQLITGLWGKVNVADCGAEALARLLIVYPWTQRFFASFGNLSSPTAINGNPMVRAHGKKVLTSFGEAVKNLDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIIVLAAHFAKDFTPDSQAAWQKLVRVVAHALARKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Chroicocephalus ridibundus (Black-headed gull) (Larus ridibundus) |
P08263 | GSTA1_HUMAN | MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF | 1.11.1.-; 2.5.1.18; 5.3.3.- | null | epithelial cell differentiation [GO:0030855]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; linoleic acid metabolic process [GO:0043651]; prostaglandin metabolic process [GO:0006693]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | fatty acid binding [GO:0005504]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; steroid delta-isomerase activity [GO:0004769] | 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:0000269|PubMed:20606271}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for prostaglandin A2 (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:9084911}; KM=160 uM for glutathione (at pH 8.0) {ECO:0000269|PubMed:11152686}; KM=58 uM for androst-5-ene-3,17-dione (at pH 8.0) {ECO:0000269|PubMed:11152686}; Vmax=121 nmol/min/mg e... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the isomerization of androst-5-ene-3,17-dione. {ECO:0000269|PubMed:11152686}; | null | FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (Probable). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubM... | Homo sapiens (Human) |
P08289 | PPBT_RAT | MILPFLVLAIGTCLTNSFVPEKEKDPSYWRQQAQETLKNALKLQKLNTNVAKNIIMFLGDGMGVSTVTAARILKGQLHHNTGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERTRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIKDIDVIMGGGRKYMYPKNRTDVEYELDEKARGTRLDGLDLISIWKSFKPRHKHSHYVWNRTELLALDPSRVDYLLGLFEPGDMQYELNRNNLTDPSLSEMVEVALRIL... | 3.1.3.1; 3.9.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05187}; Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P05187}; Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187}; COFACTOR: Name=Ca(2+); Xref=C... | bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cellular homeostasis [GO:0019725]; cellular response to organic cyclic compound [GO:0071407]; cementum mineralization [GO:0071529]; dephosphorylation [GO:0016311]; developmental process involved in reproduction [GO:0003006]; endochondral ossificati... | extracellular matrix [GO:0031012]; extracellular membrane-bounded organelle [GO:0065010]; extracellular space [GO:0005615]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | ADP phosphatase activity [GO:0043262]; alkaline phosphatase activity [GO:0004035]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; inorganic diphosphate phosphatase activity [GO:0004427]; phosphoamidase activity [GO:0050187]; phosphoethanolamine phosphatase activity [GO:0052732]; pyridoxal phosp... | PF00245; | 3.40.720.10; | Alkaline phosphatase family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05186}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P05186}. Extracellular vesicle membrane {ECO:0000269|PubMed:32710882}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P09242}. Mitochondrion membrane {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-anc... | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000305|PubMed:2895632}; PhysiologicalDirection=left-to-right; Xref=Rhea:RH... | null | null | null | null | FUNCTION: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis. Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi... | Rattus norvegicus (Rat) |
P08290 | ASGR2_RAT | MEKDFQDIQQLDSEENDHQLIGDEEQGSHVQNLRTENPRWGGQPPSRPFPQRLCSKFRLSLLALAFNILLLVVICVVSSQSMQLQKEFWTLKETLSNFSTTTLMEFKALDSHGGSRNDNLTSWETILEKKQKDIKADHSTLLFHLKHFPLDLRTLTCQLAFFLSNGTECCPVNWVEFGGSCYWFSRDGLTWAEADQYCQMENAHLLVINSREEQEFVVKHRGAFHIWIGLTDKDGSWKWVDGTEYRSNFKNWAFTQPDNWQGHEEGGSEDCAEILSDGLWNDNFCQQVNRWACERKRDITY | null | null | bone mineralization [GO:0030282]; endocytosis [GO:0006897]; glycoprotein metabolic process [GO:0009100]; lipid homeostasis [GO:0055088]; regulation of protein stability [GO:0031647] | endoplasmic reticulum quality control compartment [GO:0044322]; external side of plasma membrane [GO:0009897]; perinuclear region of cytoplasm [GO:0048471] | fucose binding [GO:0042806]; mannose binding [GO:0005537]; signaling receptor activity [GO:0038023] | PF00059;PF03954; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transp... | Rattus norvegicus (Rat) |
P08291 | POLG_CXB1J | MGAQVSTQKTGAHETGLNASGNSIIHYTNINYYKDAASNSANRQDFTQDPGKFTEPVKDIMIKSMPALNSPSAEECGYSDRVRSITLGNSTITTQECANVVVGYGVWPEYLKDNEATGEDQPTQPDVATCRFYTLESVQWMKNSAGWWWKLPDALSQMGLFGQNMQYHYLGRTGYTIHVQCNASKFHQGCLLVVCVPEAEMGCSNLNNTPKFAELSGGDNARMFTDTEVGTSNDKKVQTAVWNAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYINSVPMDNMYRHNNLTLMIIPFVPLNYSEGSSPYVPITVTIAPMC... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Coxsackievirus B1 (strain Japan) |
P08292 | POLG_CXB4J | MGAQVSTQKTGAHETSLSASGNSIIHYTNINYYKDAASNSANRQDFTQDPSKFTEPVKDVMIKSLPALNSPTVEECGYSDRVRSITLGNSTITTQECANVVVGYGVWPDYLSDEEATAEDQPTQPDVATCRFYTLNSVKWEMQSAGWWWKFPDALSEMGLFGQNMQYHYLGRSGYTIHVQCNASKFHQGCLLVVCVPEAEMGCTNAENAPAYGDLCGGETAKSFEQNAATGKTAVQTAVCNAGMGVGVGNLTIYPHQWINLRTNNSATIVMPYINSVPMDNMFRHNNFTLMIIPFAPLDYVTGASSYIPITVTVAPMSAE... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Coxsackievirus B4 (strain JVB / Benschoten / New York/51) |
P08294 | SODE_HUMAN | MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | blood vessel diameter maintenance [GO:0097746]; removal of superoxide radicals [GO:0019430]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666] | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | copper ion binding [GO:0005507]; heparin binding [GO:0008201]; molecular adaptor activity [GO:0060090]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O09164}. Note=99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. | Homo sapiens (Human) |
P08306 | COX2_PARDE | MMAIATKRRGVAAVMSLGVATMTAVPALAQDVLGDLPVIGKPVNGGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANPVPARFTHNTPIEVIWTLVPVLILVAIGAFSLPILFRSQEMPNDPDLVIKAIGHQWYWSYEYPNDGVAFDALMLEKEALADAGYSEDEYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAADASDYLPASPVKLASAE | 7.1.1.9 | COFACTOR: Name=binuclear copper center (CuA); Xref=ChEBI:CHEBI:47357; Note=Binds a binuclear copper A center per subunit.; | ATP synthesis coupled electron transport [GO:0042773] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | copper ion binding [GO:0005507]; cytochrome-c oxidase activity [GO:0004129] | PF00116;PF02790; | 1.10.287.90;2.60.40.420; | Cytochrome c oxidase subunit 2 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; | null | null | null | null | FUNCTION: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Paracoccus denitrificans |
P08308 | OTCC_PSEAE | MAFNMHNRNLLSLMHHSTRELRYLLDLSRDLKRAKYTGTEQQHLKRKNIALIFEKTSTRTRCAFEVAAYDQGANVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQEIVEELAKFAGVPVFNGLTDEYHPTQMLADVLTMREHSDKPLHDISYAYLGDARNNMGNSLLLIGAKLGMDVRIAAPKALWPHDEFVAQCKKFAEESGAKLTLTEDPKEAVKGVDFVHTDVWVSMGEPVEAWGERIKELLPYQVNMEIMKATGNPRAKFMHCLPAFHNSETKVGKQIAEQYPNLANGIEVTEDVFESPYNIAFEQAEN... | 2.1.3.3 | null | arginine biosynthetic process via ornithine [GO:0042450]; arginine catabolic process to ornithine [GO:0019547]; arginine deiminase pathway [GO:0019546]; citrulline biosynthetic process [GO:0019240] | cytoplasm [GO:0005737] | amino acid binding [GO:0016597]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, OTCase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01109}; | null | PATHWAY: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2. {ECO:0000305|PubMed:113384, ECO:0000305|PubMed:4962140, ECO:0000305|PubMed:6438064}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|PubMed:4962140}; | null | FUNCTION: Involved in the catabolism of arginine. Catalyzes the phosphorolysis of citrulline, the reverse reaction of the biosynthetic one, yielding ornithine and carbamoyl phosphate which serve to generate ATP from ADP (PubMed:2118516, PubMed:4962140). This catabolic OTCase does not carry out the biosynthetic reaction... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P08310 | CATB_PSEPU | MTSVLIERIEAIIVHDLPTIRPPHKLAMHTMQTQTLVLIRVRCSDGVEGIGEATTIGGLAYGYESPEGIKANIDAHLAPALVGLPADNINAAMLKLDKLAKGNTFAKSGIESALLDAQGKRLGLPVSELLGGRVRDSLEVAWTLASGDTARDIAEAQHMLEIRRHRVFKLKIGANPLAQDLKHVVAIKRELGDSASVRVDVNQYWDESQAIRACQVLGDNGIDLIEQPISRINRSGQVRLNQRSPAPIMADESIESVEDAFSLAADGAASIFALKIAKNGGPRAVLRTAQIAEAAGIALYGGTMLEGSIGTLASAHAFLT... | 5.5.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; | amino acid catabolic process [GO:0009063]; beta-ketoadipate pathway [GO:0042952] | null | chloromuconate cycloisomerase activity [GO:0018850]; manganese ion binding [GO:0030145]; muconate cycloisomerase activity [GO:0018849] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-muconolactone = cis,cis-muconate + H(+); Xref=Rhea:RHEA:30031, ChEBI:CHEBI:15378, ChEBI:CHEBI:32379, ChEBI:CHEBI:58736; EC=5.5.1.1; Evidence={ECO:0000269|PubMed:5330966}; | null | PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3. | null | null | FUNCTION: Catalyzes a syn cycloisomerization. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P08311 | CATG_HUMAN | MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL | 3.4.21.20 | null | angiotensin maturation [GO:0002003]; antibacterial humoral response [GO:0019731]; biofilm matrix disassembly [GO:0098786]; cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050... | azurophil granule lumen [GO:0035578]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded orga... | caspase binding [GO:0089720]; heparin binding [GO:0008201]; peptidase activity [GO:0008233]; receptor ligand activity [GO:0048018]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family | PTM: Two C-terminal truncation variants have been identified, one which ends at Arg-243 and one which ends at Ser-244. {ECO:0000269|PubMed:26274980}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:8194606}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic granule {ECO:0000269|PubMed:7499346}. Secreted {ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:3390156}. Cytopl... | CATALYTIC ACTIVITY: Reaction=Specificity similar to chymotrypsin C.; EC=3.4.21.20; Evidence={ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:29652924, ECO:0000269|PubMed:7744748, ECO:0000269|PubMed:7842483, ECO:0000269|PubMed:8194606}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.15 mM for Z-Lys-SBzl {ECO:0000269|PubMed:8194606}; KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl {ECO:0000269|PubMed:8194606}; | null | null | null | FUNCTION: Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:29652924, PubMed:8194606). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of sub... | Homo sapiens (Human) |
P08312 | SYFA_ECOLI | MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELESAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKAQQPPIRIIAPGRVYRNDYDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQIRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDL... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; | phenylalanyl-tRNA aminoacylation [GO:0006432] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF02912;PF01409; | null | Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Escherichia coli (strain K12) |
P08317 | IL8_CHICK | MNGKLGAVLALLLVSAALSQGRTLVKMGNELRCQCISTHSKFIHPKSIQDVKLTPSGPHCKNVEIIATLKDGREVCLDPTAPWVQLIVKALMAKAQLNSDAPL | null | null | angiogenesis [GO:0001525]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; hemopoiesis [GO:0030097]; inflammatory response [GO:0006954]; leukocyte activation involved in inflamm... | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be an autocrine factor that promotes the growth of fibroblasts and is involved in the neoplastic transformation of fibroblasts by v-Src. Chemotactic for peripheral blood mononuclear cells as well as for heterophils. | Gallus gallus (Chicken) |
P08318 | PP150_HCMVA | MSLQFIGLQRRDVVALVNFLRHLTQKPDVDLEAHPKILKKCGEKRLHRRTVLFNELMLWLGYYRELRFHNPDLSSVLEEFEVRCVAVARRGYTYPFGDRGKARDHLAVLDRTEFDTDVRHDAEIVERALVSAVILAKMSVRETLVTAIGQTEPIAFVHLKDTEVQRIEENLEGVRRNMFCVKPLDLNLDRHANTALVNAVNKLVYTGRLIMNVRRSWEELERKCLARIQERCKLLVKELRMCLSFDSNYCRNILKHAVENGDSADTLLELLIEDFDIYVDSFPQSAHTFLGARSPSLEFDDDANLLSLGGGSAFSSVPKK... | null | null | null | host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell viral assembly compartment [GO:0072517]; viral tegument [GO:0019033] | structural molecule activity [GO:0005198] | PF06070; | null | Herpesviridae large structural phosphoprotein family | PTM: Phosphorylated by host CCNA2. {ECO:0000269|PubMed:24101496}. | SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:9049366}. Host cytoplasm {ECO:0000269|PubMed:21411515, ECO:0000269|PubMed:9049366}. Host nucleus {ECO:0000269|PubMed:9049366}. Note=Found initially localized in the host nucleus, associated either with the nuclear membrane or with viral assembly regions, and lat... | null | null | null | null | null | FUNCTION: Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expressi... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P08319 | ADH4_HUMAN | MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGVAAGSKGLTIFPEELIIGRTI... | 1.1.1.105 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | alcohol catabolic process [GO:0046164]; alcohol metabolic process [GO:0006066]; cellular aldehyde metabolic process [GO:0006081]; ethanol oxidation [GO:0006069]; fatty acid omega-oxidation [GO:0010430]; formaldehyde catabolic process [GO:0046294]; quinone metabolic process [GO:1901661]; retinoid metabolic process [GO:0... | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; all-trans retinal binding [GO:0005503]; benzaldehyde dehydrogenase [NAD(P)+] activity [GO:0019115]; NAD binding [GO:0051287]; NAD-retinol dehydrogenase a... | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-II subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:17279314}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 uM for all-trans-retinol {ECO:0000269|PubMed:17279314}; KM=0.29 uM for all-trans-retinal {ECO:0000269|PubMed:17279314}; KM=0.054 uM for 9-cis-retinol {ECO:0000269|PubMed:17279314}; KM=0.21 uM for 9-cis-retinal {ECO:0000269|PubMed:17279314}; KM=9.5 uM for 20-HE... | null | null | null | FUNCTION: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate... | Homo sapiens (Human) |
P08337 | MUTT_ECOLI | MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANEPVIAKLKRL | 3.6.1.55 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12939141, ECO:0000269|PubMed:1851162, ECO:0000269|PubMed:19864691, ECO:0000269|PubMed:9063868}; | dGDP catabolic process [GO:0046067]; dGTP catabolic process [GO:0006203]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; nucleotide-excision repair [GO:0006289] | null | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030... | PF00293; | 3.90.79.10; | Nudix hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+); Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55; Evidence={ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400, ECO:0000269|PubMed:23481913, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.058 uM for 8-oxo-dGDP {ECO:0000269|PubMed:15850400}; KM=0.081 uM for 8-oxo-dGTP {ECO:0000269|PubMed:15850400}; KM=0.48 uM for 8-oxo-dGTP {ECO:0000269|PubMed:1309939}; KM=0.045 uM for 8-oxo-GDP {ECO:0000269|PubMed:15850400}; KM=0.26 uM for 8-oxo-GTP {ECO:0000269|P... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:1851162}; | null | FUNCTION: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA (PubMed:1309939, PubMed:15850400, PubMed:9311918). It pr... | Escherichia coli (strain K12) |
P08353 | ICP34_HHV1F | MARRRRHRGPRRPRPPGPTGAVPTAQSQVTSTPNSEPAVRSAPAAAPPPPPASGPPPSCSLLLRQWLHVPESASDDDDDDDWPDSPPPEPAPEARPTAAAPRPRSPPPGAGPGGGANPSHPPSRPFRLPPRLALRLRVTAEHLARLRLRRAGGEGAPEPPATPATPATPATPATPATPATPATPATPATPARVRFSPHVRVRHLVVWASAARLARRGSWARERADRARFRRRVAEAEAVIGPCLGPEARARALARGAGPANSV | null | null | response to endoplasmic reticulum stress [GO:0034976]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defe... | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; protein phosphatase type 1 complex [GO:0000164]; virion component [GO:0044423] | protein serine/threonine phosphatase inhibitor activity [GO:0004865] | null | null | PPP1R15 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:12186925}. Host nucleus {ECO:0000269|PubMed:12186925}. Host nucleus, host nucleolus {ECO:0000269|PubMed:12186925}. Virion. Note=At early times in infection, colocalizes with PCNA and replication proteins in the host cell nucleus, before accumulating in the host c... | null | null | null | null | null | FUNCTION: Inhibits the establishment of the immune response and of the integrated stress response (ISR) in the infected cell (PubMed:15705855, PubMed:21622569). Plays essential roles in viral nuclear egress to mediate capsid transit across the nuclear membrane (By similarity). Facilitates nuclear egress cooperatively w... | Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1) |
P08359 | ENV_FLVGL | MESPTHPKPSKDKTLSWNLAFLVGILFTIDIGMANPSPHQIYNVTWVITNVQTNTQANATSMLGTLTDAYPTLHVDLCDLVGDTWEPIVLNPTNVKHGARYSSSKYGCKTTDRKKQQQTYPFYVCPGHAPSLGPKGTHCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSSQDNSCEGKCNPLVLQFTQKGRQASWDGPKMWGLRLYRTGYDPIALFTVSRQVSTITPPQAMGPNLVLPDQKPPSRQSQTGSKVATQRPQTNESAPRSVAPTTMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRP... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; 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] | null | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Feline leukemia virus (strain A/Glasgow-1) |
P08360 | ENV_MLVCB | MEGPAFSKSPKDKTIERAFLGVLGILFVTGGLASRDNPHQVYNITWEVTNGEQDTVWAVTGNHPLWTWWPDLTPDLCMLALHGPTHWGLDNHPPYSSPPGPPCCSGDAGAVSGCARDCDEPLTSYSPRCNTAWNRLKLARVTHAPKEGFYICPGSHRPRWARSCGGLDAYYCASWGCETTGRAAWNPTSSWDYITVSNNLTSSQATKACKNNGWCNPLVIRFTGPGKRATSWTTGHFWGLRLYISGHDPGLTFGIRLKVTDLGPRVPIGPNPVLSDQRPPSRPVPARPPPPSASPSTPTIPPQQGTGDRLLNLVQGAYLT... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; 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] | metal ion binding [GO:0046872] | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Cas-Br-E murine leukemia virus |
P08361 | POL_MLVCB | MGQTVTTPLSLTLDHWKDVERTAHNQSVDVKKRRWVTFCSVEWPTFNVGWPQDGTFNRDIITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPLPPSAPSLLPEPPLSTSPRSSLYPALTPSLGAKPKPQVLPDSGGPLIDLLTEDPPPYRDPGPPPSDRDRDDGEAAPAGEAPDPSPMASRLRGRRELPVADSTTSQAFPLRSGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLLTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGEDGRPTQLPNEINDAFPLERPDWDYN... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; virion a... | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yie... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Cas-Br-E murine leukemia virus |
P08364 | POLS_IBDVA | MTNLSDQTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTMQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITNLSVGGELVFQTSVQGLVLNATIYLVGFDGTTVTTRAVAAGNGLTAGTDNLMPFNLVIPTSEITQPVTSIKLEIVTSKSGGQ... | 3.4.21.- | null | proteolysis [GO:0006508] | host cell cytoplasm [GO:0030430]; T=13 icosahedral viral capsid [GO:0039621] | metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198] | PF01766;PF01767;PF01768; | 2.60.120.20;6.10.250.1030;1.10.8.880;1.10.150.620;2.60.120.660; | null | PTM: Specific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, givin... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Stru... | null | null | null | null | null | FUNCTION: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity). {EC... | Avian infectious bursal disease virus (strain Australian 002-73) (IBDV) (Gumboro disease virus) |
P08373 | MURB_ECOLI | MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNV... | 1.3.1.98 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; UDP-N-acetylmuramate dehydrogenase activity [GO:0008762] | PF01565;PF02873; | 3.30.465.10;3.90.78.10;3.30.43.10; | MurB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Cell wall formation. | Escherichia coli (strain K12) |
P08392 | ICP4_HHV11 | MASENKQRPGSPGPTDGPPPTPSPDRDERGALGWGAETEEGGDDPDHDPDHPHDLDDARRDGRAPAAGTDAGEDAGDAVSPRQLALLASMVEEAVRTIPTPDPAASPPRTPAFRADDDDGDEYDDAADAAGDRAPARGREREAPLRGAYPDPTDRLSPRPPAQPPRRRRHGRWRPSASSTSSDSGSSSSSSASSSSSSSDEDEDDDGNDAADHAREARAVGRGPSSAAPAAPGRTPPPPGPPPLSEAAPKPRAAARTPAASAGRIERRRARAAVAGRDATGRFTAGQPRRVELDADATSGAFYARYRDGYVSGEPWPGAG... | null | null | DNA-templated viral transcription [GO:0039695]; positive regulation of DNA-templated transcription [GO:0045893]; response to type I interferon [GO:0034340] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | DNA binding [GO:0003677] | PF03585;PF03584; | null | Herpesviridae ICP4 family | PTM: ADP-ribosylated.; PTM: The long stretch of Ser is a major site of phosphorylation. Only the phosphorylated forms are capable of interacting with beta or gamma genes. {ECO:0000269|PubMed:1846804}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:17959681}. Host cytoplasm {ECO:0000269|PubMed:17959681}. Virion tegument {ECO:0000269|PubMed:17959681}. Note=Localizes to the cytoplasm when phosphorylated. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays an essential role in the regulation of viral gene expression by both activating and repressing host RNA polymerase II-mediated transcription. Binds with high affinity to the sequence 5'-ATCGTC-3'. Activates transcription by recruiting a form of the host TFIID to promoters and stabilizing the pre-initiat... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P08393 | ICP0_HHV11 | MEPRPGASTRRPEGRPQREPAPDVWVFPCDRDLPDSSDSEAETEVGGRGDADHHDDDSASEADSTDTELFETGLLGPQGVDGGAVSGGSPPREEDPGSCGGAPPREDGGSDEGDVCAVCTDEIAPHLRCDTFPCMHRFCIPCMKTWMQLRNTCPLCNAKLVYLIVGVTPSGSFSTIPIVNDPQTRMEAEEAVRAGTAVDFIWTGNQRFAPRYLTLGGHTVRALSPTHPEPTTDEDDDDLDDADYVPPAPRRTPRAPPRRGAAAPPVTGGASHAAPQPAAARTAPPSAPIGPHGSSNTNTTTNSSGGGGSRQSRAAAPRGA... | 2.3.2.27 | null | positive regulation of protein catabolic process [GO:0045732]; protein polyubiquitination [GO:0000209]; release from viral latency [GO:0019046]; response to type I interferon [GO:0034340]; suppression by virus of host type I interferon production [GO:0039501]; symbiont-mediated disruption of host cell PML body [GO:0075... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00097; | 3.30.40.10; | Simplexviruses ICp0 family | PTM: Phosphorylated at Thr-67, leading to promote interaction with host RNF8 (PubMed:22405594). Phosphorylated by host CHEK2; leading to increased SUMO-targeted ubiquitin ligase activity of ICP0 (PubMed:32001251). {ECO:0000269|PubMed:22405594, ECO:0000269|PubMed:32001251}.; PTM: Auto-ubiquitinated. Deubiquitinated by h... | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:20454685}. Host nucleus {ECO:0000269|PubMed:20454685}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: SUMO-targeted ubiquitin ligase that plays an essential role in nuclear antiviral defense evasion triggered by dsDNA viruses (PubMed:32001251). Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML, S... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P08394 | RECB_ECOLI | MSDVAETLDPLRLPLQGERLIEASAGTGKTFTIAALYLRLLLGLGGSAAFPRPLTVEELLVVTFTEAATAELRGRIRSNIHELRIACLRETTDNPLYERLLEEIDDKAQAAQWLLLAERQMDEAAVFTIHGFCQRMLNLNAFESGMLFEQQLIEDESLLRYQACADFWRRHCYPLPREIAQVVFETWKGPQALLRDINRYLQGEAPVIKAPPPDDETLASRHAQIVARIDTVKQQWRDAVGELDALIESSGIDRRKFNRSNQAKWIDKISAWAEEETNSYQLPESLEKFSQRFLEDRTKAGGETPRHPLFEAIDQLLAEP... | 3.1.11.5; 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01485, ECO:0000269|PubMed:15538360, ECO:0000269|PubMed:16388588, ECO:0000269|PubMed:18668125}; Note=Binds 1 Mg(2+) ion per subunit. Magnesium is required for both helicase and nuclease activity; its relative concentration alters helicase... | clearance of foreign intracellular DNA [GO:0044355]; DNA recombination [GO:0006310]; double-strand break repair via homologous recombination [GO:0000724]; recombinational repair [GO:0000725]; response to radiation [GO:0009314] | cytosol [GO:0005829]; exodeoxyribonuclease V complex [GO:0009338] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; DNA helicase activity [GO:0003678]; DNA translocase activity [GO:0015616]; exodeoxyribonuclease ... | PF12705;PF00580;PF13361; | 3.90.320.10;3.40.50.300;1.10.3170.10; | Helicase family, UvrD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01485, ECO:0000269|PubMed:4552016}; CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of d... | 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) |
P08395 | SPPA_ECOLI | MRTLWRFIAGFFKWTWRLLNFVREMVLNLFFIFLVLVGVGIWMQVSGGDSKETASRGALLLDISGVIVDKPDSSQRFSKLSRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVMDLKNFAGGDQPSMQYIGKALKEFRDSGKPVYAVGENYSQGQYYLASFANKIWLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYLNTVAANRQIPAEQVFPGAQGLLEGLTKTGGDTAKYALENKLVDALASSAEIEKALTKEFGWSKTDKNYRAISYYDYALKT... | 3.4.21.- | null | signal peptide processing [GO:0006465] | membrane [GO:0016020]; plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175]; serine-type peptidase activity [GO:0008236] | PF01343; | 6.20.330.10; | Peptidase S49 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:3522590}; Single-pass membrane protein {ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:3522590}. | null | null | null | null | null | FUNCTION: Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane. {ECO:0000269|PubMed:18164727, ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:21810987, ECO:0000269|PubMed:3522590}. | Escherichia coli (strain K12) |
P08397 | HEM3_HUMAN | MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITA... | 2.5.1.61 | COFACTOR: Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; Note=Binds 1 dipyrromethane group covalently. {ECO:0000269|PubMed:18936296}; | heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; protoporphyrinogen IX biosynthetic process [GO:0006782] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | hydroxymethylbilane synthase activity [GO:0004418] | PF01379;PF03900; | 3.40.190.10;3.30.160.40; | HMBS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+); Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61; Evidence={ECO:0000269|PubMed:18004775, ECO:0000269|PubMed:18936296, ECO:0000269|PubMed:19138865, ECO:0000269|PubMed:238156... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for porphobilinogen {ECO:0000269|PubMed:23815679}; KM=15.3 uM for porphobilinogen (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:18936296}; KM=48.4 uM for porphobilinogen {ECO:0000269|PubMed:18004775}; Vmax=1261 nmol/h/mg enzyme (at 37 degrees Celsius... | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. {ECO:0000269|PubMed:19138865}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:18004775}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Displays high thermal stability. The half-denaturation temperature (Tm) is about 74 degrees Celsius. {ECO:0000269|PubMed:23815679}; | FUNCTION: As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen (PubMed:18004775, PubMed:18936296, PubMed:19138865, PubMed:23815679). Catalysis begins with the assembly of the dipyrromethane c... | Homo sapiens (Human) |
P08405 | TY1A_YEASX | MESQQLSQHSPNSHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | null | null | null | cytoplasm [GO:0005737] | RNA binding [GO:0003723] | PF01021; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (Baker's yeast) |
P08411 | POLN_SFV | MAAKVHVDIEADSPFIKSLQKAFPSFEVESLQVTPNDHANARAFSHLATKLIEQETDKDTLILDIGSAPSRRMMSTHKYHCVCPMRSAEDPERLVCYAKKLAAASGKVLDREIAGKITDLQTVMATPDAESPTFCLHTDVTCRTAAEVAVYQDVYAVHAPTSLYHQAMKGVRTAYWIGFDTTPFMFDALAGAYPTYATNWADEQVLQARNIGLCAASLTEGRLGKLSILRKKQLKPCDTVMFSVGSTLYTESRKLLRSWHLPSVFHLKGKQSFTCRCDTIVSCEGYVVKKITMCPGLYGKTVGYAVTYHAEGFLVCKTTD... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; poly(A) RNA polymerase activity [GO:1990817]; polynucleotide 5... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:11257180, PubMed:12917405, PubMed:29695431). The processing of the polyprotein is temporally regulated (PubMed:12917405, PubMed:29695431). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease act... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.99 mM for nsP2 RNA triphosphatase activity (at pH 8.0) {ECO:0000269|PubMed:10748213}; KM=90 mM for nsP2 NTPase activity (at pH 7.5) {ECO:0000269|PubMed:10748213}; | null | null | null | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similar... | Semliki forest virus (SFV) |
P08413 | KCC2B_RAT | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQT... | 2.7.11.17 | null | activation of meiosis involved in egg activation [GO:0060466]; apoptotic signaling pathway [GO:0097190]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cell projection morphogenesis [GO:0048858]; cellular response to homocysteine [GO:1905375]; G1/S transition of mitotic cell cycle [GO:0000082]; ... | calcium- and calmodulin-dependent protein kinase complex [GO:0005954]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; sarcoplasmic reticulum memb... | ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; identical protein binding [GO:0042802]; phospholipase binding [GO:0043274]; protein homodimerization activity [GO:0042803]; prote... | PF08332;PF00069; | 3.10.450.50;6.10.140.620;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state. {ECO:0000269|PubMed:17272343}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Synapse {ECO:0000269|PubMed:22579289}. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with the cortical actin cyt... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:11972023}; CATALYTI... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle (PubMed:12873385, PubMed:1... | Rattus norvegicus (Rat) |
P08414 | KCC4_MOUSE | MLKVTVPSCPSSPCSSVTASTENLVPDYWIDGSNRDPLGDFFEVESELGRGATSIVYRCKQKGTQKPYALKVLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDARDAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVEHQVLMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGIITYILLCGFEPFYDERGDQFMFRRILNCEYYFISPWWDEVSLNAKDLVKKLIVLDPKKRLTTFQALQHPWVTGKAANFVHMDTAQKKLQEFNARR... | 2.7.11.17 | null | adaptive immune response [GO:0002250]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; long-term memory [GO:0007616]; myeloid dendritic cell differentiation [GO:0043011]; neuron-neuron synaptic transmission [GO:0007270]; nucleocytoplasmic transport [GO:0006913]; phosphorylation [GO:0... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynapse [GO:0098794] | ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-196. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-11 and Ser-12 (By similarity). {ECO:0000250}.; PTM: Glycosylation at Ser-185 modulates the phosphorylation of CaMK4 at Thr-196 and negatively regulates its activity toward CREB1 in basal conditions... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10932193}. Nucleus {ECO:0000269|PubMed:10932193}. Note=Localized in hippocampal neuron nuclei (By similarity). In spermatids, associated with chromatin and nuclear matrix. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory... | Mus musculus (Mouse) |
P08417 | FUMH_YEAST | MLRFTNCSCKTFVKSSYKLNIRRMNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQVHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDI... | 4.2.1.2 | null | DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; fumarate metabolic process [GO:0006106]; malate metabolic process [GO:0006108]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; tricarboxylic acid cycle enzyme complex [GO:0045239] | fumarate hydratase activity [GO:0004333] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Fumarase subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:3040736}. Cytoplasm {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:3040736}. Nucleus {ECO:0000269|PubMed:20231... | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:3040736}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461; Evidence={ECO:... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000269|PubMed:20231875}. | null | null | FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:11585823, PubMed:1587456, PubMed:20231875, PubMed:3040736). In mitochondrion, catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08419 | CEL2A_PIG | MIRALLLSTLVAGALSCGLPANLPQLPRVVGGEDARPNSWPWQVSLQYDSSGQWRHTCGGTLVDQSWVLTAAHCISSSRTYRVVLGRHSLSTNEPGSLAVKVSKLVVHQDWNSNQLSNGNDIALLKLASPVSLTDKIQLGCLPAAGTILPNNYVCYVTGWGRLQTNGASPDILQQGQLLVVDYATCSKPGWWGSTVKTNMICAGGDGIISSCNGDSGGPLNCQGANGQWQVHGIVSFGSSLGCNYYHKPSVFTRVSNYIDWINSVIANN | 3.4.21.71 | null | insulin catabolic process [GO:1901143]; proteolysis [GO:0006508]; regulation of insulin secretion [GO:0050796]; regulation of platelet aggregation [GO:0090330]; response to insulin [GO:0032868] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08217}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.; EC=3.4.21.71; Evidence={ECO:0000250|UniProtKB:P08217}; | null | null | null | null | FUNCTION: Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity. {ECO:0000250|UniProtKB:P08217}. | Sus scrofa (Pig) |
P08422 | HBA3_XENTR | MTLTDSEKAAVVALWSKIAPQASAIGAEALERLFLSYPQTKTYFSHFDVSHGSADLQNHGGKVVNALGEAAKHLNDLDAALSTLSDLHAYNLRVDPGNFKLLSHTIQVTLAVHFQKEFDAATQAAWDKFLSEVATVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is a larval (tadpole) alpha-globin. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
P08423 | HBB2_XENTR | MVHWTAEEKATIASVWGKVDIEQDGHDALSRLLVVYPWTQRYFSSFGNLSNVSAVSGNVKVKAHGNKVLSAVGSAIQHLDDVKSHLKGLSKSHAEDLHVDPENFKRLADVLVIVLAAKLGSAFTPQVQAVWEKLNATLVAALSHGYF | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: This is a larval (tadpole) beta-globin. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
P08424 | RENI_RAT | MGGRRMPLWALLLLWTSCSFSLPTDTASFGRILLKKMPSVREILEERGVDMTRISAEWGEFIKKSSFTNVTSPVVLTNYLDTQYYGEIGIGTPSQTFKVIFDTGSANLWVPSTKCGPLYTACEIHNLYDSSESSSYMENGTEFTIHYGSGKVKGFLSQDVVTVGGIIVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVDGVIPVFDHILSQRVLKEEVFSVYYSRESHLLGGEVVLGGSDPQHYQGNFHYVSISKAGSWQITMKGVSVGPATLLCEEGCMAVVDTGTSYISGPTSSLQLIMQALGVKEKRANNYVVN... | 3.4.23.15 | null | amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; cell maturation [GO:0048469]; cellular response to xenobiotic stimulus [GO:0071466]; drinking behavior [GO:0042756]; hormone-mediated signaling pathway [GO:0009755]; juxtaglomerular apparatus development [GO:0072051]; kidney development [... | apical part of cell [GO:0045177]; extracellular space [GO:0005615]; membrane [GO:0016020] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; insulin-like growth factor receptor binding [GO:0005159]; peptidase activity [GO:0008233]; signaling receptor binding [GO:0005102] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00797}. Membrane {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}. | CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; Evidence={ECO:0000250|UniProtKB:P00797}; | null | null | null | null | FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. {ECO:0000250|UniProtKB:P00797}. | Rattus norvegicus (Rat) |
P08425 | SYFM_YEAST | MFLNRMMKTRTGLYRLYSTLKVPHVEINGIKYKTDPQTTNVTDSIIKLTDRSLHLKESHPVGILRDLIEKKLNSVDNTFKIFNNFKPVVTTMENFDSLGFPKDHPGRSKSDTYYINETHLLRTHTSAHELECFQKIRNDSDNIKSGFLISADVYRRDEIDKTHYPVFHQMEGATIWKRTKADVGVKEPMYIEKIREDIRQVENLLNKENVKITVDDDTIPLKENNPKQEYMSDLEVDLCSQHLKRSIELIVSEVFNKKISSMIKNKANNTPKELKVRWINAYFPWTAPSWEIEVWWQGEWLELCGCGLIRQDVLLRAGYK... | 6.1.1.20 | null | mitochondrial phenylalanyl-tRNA aminoacylation [GO:0070156]; phenylalanyl-tRNA aminoacylation [GO:0006432] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF03147;PF01409; | 3.30.70.380; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | FUNCTION: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08427 | SFTPA_RAT | MSLCSLAFTLFLTVVAGIKCNVTDVCAGSPGIPGAPGNHGLPGRDGRDGVKGDPGPPGPMGPPGGMPGLPGRDGLPGAPGAPGERGDKGEPGERGLPGFPAYLDEELQTELYEIKHQILQTMGVLSLQGSMLSVGDKVFSTNGQSVNFDTIKEMCTRAGGNIAVPRTPEENEAIASIAKKYNNYVYLGMIEDQTPGDFHYLDGASVNYTNWYPGEPRGQGKEKCVEMYTDGTWNDRGCLQYRLAVCEF | null | null | cellular response to mechanical stimulus [GO:0071260]; cellular response to nitric oxide [GO:0071732]; circadian rhythm [GO:0007623]; opsonization [GO:0008228]; positive regulation of phagocytosis [GO:0050766]; respiratory gaseous exchange by respiratory system [GO:0007585]; response to epidermal growth factor [GO:0070... | collagen trimer [GO:0005581]; extracellular space [GO:0005615]; multivesicular body [GO:0005771] | carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF00059; | 3.10.100.10; | SFTPA family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWL2}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8IWL2}. Secreted, extracellular space, surface film {ECO:0000250|UniProtKB:Q8IWL2}. | null | null | null | null | null | FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages. {ECO:0000250|UniProtKB:P35... | Rattus norvegicus (Rat) |
P08430 | UD16_RAT | MACLLPAARLPAGFLFLVLWGSVLGDKLLVVPQDGSHWLSMKEIVEHLSERGHDIVVLVPEVNLLLGESKYYRRKSFPVPYNLEELRTRYRSFGNNHFAASSPLMAPLREYRNNMIVIDMCFFSCQSLLKDSATLSFLRENQFDALFTDPAMPCGVILAEYLKLPSIYLFRGFPCSLEHIGQSPSPVSYVPRFYTKFSDHMTFPQRLANFIANILENYLYHCLYSKYEILASDLLKRDVSLPALHQNSLWLLRYDFVFEYPRPVMPNMIFIGGTNCKKKGNLSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAE... | 2.4.1.17 | null | 4-chlorobiphenyl metabolic process [GO:0018880]; cellular glucuronidation [GO:0052695]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hormone stimulus [GO:0032870]; liver development [GO:0001889]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; protein-containing complex [GO:0032991] | enzyme binding [GO:0019899]; glucuronosyltransferase activity [GO:0015020]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; | null | null | null | null | FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. | Rattus norvegicus (Rat) |
P08432 | DCOR_YEAST | MSSTQVGNALSSSTTTLVDLSNSTVTQKKQYYKDGETLHNLLLELKNNQDLELLPHEQAHPKIFQALKARIGRINNETCDPGEENSFFICDLGEVKRLFNNWVKELPRIKPFYAVKCNPDTKVLSLLAELGVNFDCASKVEIDRVLSMNISPDRIVYANPCKVASFIRYAASKNVMKSTFDNVEELHKIKKFHPESQLLLRIATDDSTAQCRLSTKYGCEMENVDVLLKAIKELGLNLAGVSFHVGSGASDFTSLYKAVRDARTVFDKAANEYGLPPLKILDVGGGFQFESFKESTAVLRLALEEFFPVGCGVDIIAEPG... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6795198}; | pantothenate biosynthetic process [GO:0015940]; putrescine biosynthetic process [GO:0009446]; putrescine biosynthetic process from ornithine [GO:0033387] | cytoplasm [GO:0005737] | ornithine decarboxylase activity [GO:0004586] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000269|PubMed:6795198}; | null | PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000305|PubMed:6754461}. | null | null | FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08434 | NSP4_ROTBN | MEKLTDLNYTSSVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIHDKLMIRAVDEIDMTKEINQKNVRTLEEWENGKNPYEPKEVTAAM | null | null | induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259] | extracellular region [GO:0005576]; host caveola [GO:0044155]; host cell rough endoplasmic reticulum membrane [GO:0044169]; membrane [GO:0016020] | metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; toxin activity [GO:0090729] | PF01452; | 1.20.5.430; | Rotavirus NSP4 family | PTM: Mannosylated.; PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc. {ECO:0000255|HAMAP-Rule:MF_04091}. | SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:2548854}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associate... | Rotavirus A (strain RVA/Cow/United States/NCDV-Lincoln/1969/G6P6[1]) (RV-A) (Rotavirus A (strain Nebraska calf diarrhea virus)) |
P08458 | SPS1_YEAST | MESKEISIRSRTPPSKLYSIQSCIGRGNFGDVYKAVDRVTQEIVAIKVVNLEHSDEDIELLAQEIFFLAELKSPLITNYIATMLEDVSMWIVMEYCGGGSCSDLLKRSYVNGLPEEKVSFIIHEVTLGLKYLHEQRKIHRDIKAANILLNEEGMVKLGDFGVSGHIRSTLKRDTFVGTPYWMAPEVVCCEVDGYNEKADIWSLGITTYELLKGLPPLSKYDPMKVMTNLPKRKPPKLQGPFSDAAKDFVAGCLVKTPADRPSAYNLLSFEFVKNITITNLKSDVDLIKQKKVQERYTKVPKYPLQNRLYKNSNTVRGKEF... | 2.7.11.1 | null | ascospore formation [GO:0030437]; ascospore wall assembly [GO:0030476]; meiotic spindle disassembly [GO:0051229]; negative regulation of protein localization to nucleolus [GO:1904750]; phosphorylation [GO:0016310]; positive regulation of ascospore-type prospore membrane formation [GO:1903024] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; prospore membrane [GO:0005628] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase required for spore wall development. {ECO:0000269|PubMed:7958886}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08460 | NID1_RAT | EFHPGTFPPSFGSVAPFLADLDTTDGLGNVYYREDLSPFIIQMAAEYVQRGFPEVSFQPTSVVVVTWESMAPYGGPSGSLVEEGKRNTFQAVLASSNSSSYAIFLYPDDGLQFFTTFSKKDENQVPAVVGFSKGLEGFLWKSNGAYNIFANDRESIENLAKSSNAGHQGVWVFEIGSPATAKGVVPADVNLDVDDDGADYEDEDYDLQTSHLGLEDVATQPFPSHSPRRGYPDPHNVPRTLAPSYEATERPHGIPTERTKSFQLPVERFPQKHPQVIDVDEVEETGVVFSYNTGSQQTCANNRHQCSVHAECRDYATGFC... | null | null | cell-matrix adhesion [GO:0007160]; extracellular matrix organization [GO:0030198]; glomerular basement membrane development [GO:0032836]; positive regulation of cell-substrate adhesion [GO:0010811] | basement membrane [GO:0005604]; cell periphery [GO:0071944]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; laminin binding [GO:0043236]; laminin-1 binding [GO:0043237]; proteoglycan binding [GO:0043394] | PF06119; | null | null | PTM: N- and O-glycosylated. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. | Rattus norvegicus (Rat) |
P08461 | ODP2_RAT | MWRVCARRVQSAVPRAGFRARWATLKGPRTGPAAVRCGSGIPSYGVRSLCGWSYGSATVPRNRILQQLLGSPSRRSYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEAFKNYTLDSATAATQAAPAPAAAPAAAPAAPSASAPGSSYPVHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKQEDIAAFADYRPTEVTSLKPQAPPPVPPPVAAVP... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250|UniProtKB:P10515}; Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250|UniProtKB:P10515}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glucose metabolic process [GO:0006006]; tricarboxylic acid cycle [GO:0006099] | mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; pyruvate dehydrogenase complex [GO:0045254] | acetyltransferase activity [GO:0016407]; dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | PTM: Delipoylated at Lys-123 and Lys-249 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000250|UniProtKB:P10515}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:3571977}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:000... | null | null | null | null | FUNCTION: As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety. The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) c... | Rattus norvegicus (Rat) |
P08463 | CKS1_SCHPO | MSKSGVPRLLTASERERLEPFIDQIHYSPRYADDEYEYRHVMLPKAMLKAIPTDYFNPETGTLRILQEEEWRGLGITQSLGWEMYEVHVPEPHILLFKREKDYQMKFSQQRGG | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; regulation of mitotic cell cycle [GO:0007346]; signaling [GO:0023052] | cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytosol [GO:0005829]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; histone binding [GO:0042393]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270] | PF01111; | 3.30.170.10; | CKS family | null | null | null | null | null | null | null | FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinase (cdc2) and is essential for its biological function. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P08466 | NUC1_YEAST | MCSRILLSGLVGLGAGTGLTYLLLNKHSPTQIIETPYPPTQKPNSNIQSHSFNVDPSGFFKYGFPGPIHDLQNREEFISCYNRQTQNPYWVLEHITPESLAARNADRKNSFFKEDEVIPEKFRGKLRDYFRSGYDRGHQAPAADAKFSQQAMDDTFYLSNMCPQVGEGFNRDYWAHLEYFCRGLTKKYKSVRIVTGPLYLPKKDPIDNKFRVNYEVIGNPPSIAVPTHFFKLIVAEAPTANPAREDIAVAAFVLPNEPISNETKLTDFEVPIDALERSTGLELLQKVPPSKKKALCKEVNCQIVVRDFSNAAIKQSKDVK... | 3.1.30.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; defense response to virus [GO:0051607]; DNA catabolic process [GO:0006308]; DNA recombination [GO:0006310]; RNA catabolic process [GO:0006401] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA endonuclease activity [GO:0004520]; DNA exonuclease activity [GO:0004529]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA endonuclease activity [GO:0004521]; RNA nuclease activity [GO:0004540]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF01223; | 3.40.570.10; | DNA/RNA non-specific endonuclease family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane. | null | null | null | null | null | FUNCTION: This enzyme has both RNase and DNase activity. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08473 | NEP_HUMAN | MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKP... | 3.4.24.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566}; | amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; amyloid-beta metabolic process [GO:0050435]; bradykinin catabolic process [GO:0010815]; cellular response to cytokine stimulus [GO:0071345]; cellular response to UV-A [GO:0071492]; cellular response to UV-B [GO:00714... | axon [GO:0030424]; brush border [GO:0005903]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection ter... | cardiolipin binding [GO:1901612]; endopeptidase activity [GO:0004175]; exopeptidase activity [GO:0008238]; metalloendopeptidase activity [GO:0004222]; oligopeptidase activity [GO:0070012]; peptide binding [GO:0042277]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; zinc ion bin... | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000269|PubMed:19756956}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566, ECO:... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20876573}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:27588448, ECO:0000269|PubMed:6208535, ECO:0000269|PubMed:6349683, ECO:0000269|PubMed:8168535}; CATALYTIC ACTIVITY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55.1 uM for angiotensin-1 {ECO:0000269|PubMed:15283675}; KM=179 uM for angiotensin-2 {ECO:0000269|PubMed:15283675}; KM=111.4 uM for angiotensin 1-9 {ECO:0000269|PubMed:15283675}; | null | null | null | FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991... | Homo sapiens (Human) |
P08476 | INHBA_HUMAN | MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNI... | null | null | activin receptor signaling pathway [GO:0032924]; autophagy [GO:0006914]; cardiac fibroblast cell development [GO:0060936]; cell differentiation [GO:0030154]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; cellular response to angiotensin [GO:1904385]; cellular response to choles... | activin A complex [GO:0043509]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; peptide hormone binding [GO:0017046]; protein-containing complex binding [GO:0044877]; type II activin receptor binding [GO:0070699] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Homo sapiens (Human) |
P08478 | AMDA_XENLA | MASLSSSFLVLFLLFQNSCYCFRSPLSVFKRYEESTRSLSNDCLGTTRPVMSPGSSDYTLDIRMPGVTPTESDTYLCKSYRLPVDDEAYVVDFRPHANMDTAHHMLLFGCNIPSSTDDYWDCSAGTCMDKSSIMYAWAKNAPPTKLPEGVGFRVGGKSGSRYFVLQVHYGNVKAFQDKHKDCTGVTVRVTPEKQPQIAGIYLSMSVDTVIPPGEEAVNSDIACLYNRPTIHPFAYRVHTHQLGQVVSGFRVRHGKWSLIGRQSPQLPQAFYPVEHPVEISPGDIIATRCLFTGKGRTSATYIGGTSNDEMCNLYIMYYMD... | 1.14.17.3; 4.3.2.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Zn(2+) is required for the lyase reaction. {ECO:0000250}; COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; Note=Binds 2 copper ions per subunit for the monooxygenase reaction. {ECO:0000250}; | peptide metabolic process [GO:0006518] | extracellular region [GO:0005576]; transport vesicle membrane [GO:0030658] | copper ion binding [GO:0005507]; peptidylamidoglycolate lyase activity [GO:0004598]; peptidylglycine monooxygenase activity [GO:0004504] | PF03712;PF01082;PF01436; | 2.60.120.230;2.60.120.310;2.120.10.30; | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Secretory granules. | CATALYTIC ACTIVITY: Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:C... | null | null | null | null | FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptid... | Xenopus laevis (African clawed frog) |
P08482 | ACM1_RAT | MNTSVPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPESPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDSEAQAPTKQPPK... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; cognition [GO:0050890]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide s... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; syn... | 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. | Rattus norvegicus (Rat) |
P08483 | ACM3_RAT | MTLHSNSTTSPLFPNISSSWVHSPSEAGLPLGTVTQLGSYNISQETGNFSSNDTSSDPLGGHTIWQVVFIAFLTGFLALVTIIGNILVIVAFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLSIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAEAENFVHPTGSSRSCSSYELQQQGVKRSSRRKYGRCHFWFTTKSWK... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; calcium-mediated signaling [GO:0019722]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G pr... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; pre... | acetylcholine binding [GO:0042166]; G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled acetylcholine receptor binding [GO:0031789]; G protein-coupled serotonin receptor activity [GO:0004993]; quaternary ammonium group binding [GO:0050997] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM3 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1527051}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P20309}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:000... | 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. {ECO:0000269|PubMed:1527051, ECO:0000269|PubMed... | Rattus norvegicus (Rat) |
P08485 | ACM4_RAT | MXNFTPVNGSSANQSVRLVTAAHNHLETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLGCADLIIGAFSMNLYTLYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKPSIKKPPPGGASREELRNGKLEEAPPPALPPPPRPVPDKDTSNESSSGSATQNTKERPPTELSTAEATTP... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; chemical synaptic transmission, postsynaptic [GO:0099565]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling path... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM4 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 inhibition of adenylate cyclase. | Rattus norvegicus (Rat) |
P08487 | PLCG1_BOVIN | MAGAASPCANGCGPSAPSDAEVVHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIRGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRTSDITYGQFAQLYRSLMYSAQKTMDLPFLEASALRAGERPELCRVSLPEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSIWNSQLDEVCPD... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P10686}; | cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; epidermal growth factor receptor signaling pathway [GO:0007173]; in utero embryonic development [GO:0001701]; phosphatidylinositol metabolic process [GO:0046488]; phosphatid... | COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase C activity [GO:0050429]; guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol phospholipase C activity [GO:0004435] | PF00168;PF00169;PF00388;PF00387;PF00017;PF00018; | 2.60.40.150;3.20.20.190;2.30.29.30;3.30.505.10;2.30.30.40; | null | PTM: Ubiquitinated by CBLB in activated T-cells. {ECO:0000250|UniProtKB:Q62077}.; PTM: Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phos... | SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250|UniProtKB:P19174}. Cell projection, ruffle {ECO:0000250|UniProtKB:P19174}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000250|UniProtKB:P19174}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, P... | Bos taurus (Bovine) |
P08491 | POLS_RRVT | MNYIPTQTFYGRRWRPRPAFRPWQVSMQPTPTMVTPMLQAPDLQAQQMQQLISAVSALTTKQNVKAPKGQRQKKQQKPKEKKENQKKKPTQKKKQQQKPKPQAKKKKPGRRERMCMKIENDCIFEVKLDGKVTGYACLVGDKVMKPAHVKGTIDNPDLAKLTYKKSSKYDLECAQIPVHMKSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWTKDMVTRVTPEGTEEWSAALMMCILANTSFPCSSPPCYPCCYEKQPEQTLRMLEDNVNRPGYYELL... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity). The remaining polyprotein is then targeted to the host endoplasmic reticulum, wh... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Ross river virus (strain T48) (RRV) |
P08493 | MGP_HUMAN | MKSLILLAILAALAVVTLCYESHESMESYELNPFINRRNANTFISPQQRWRAKVQERIRERSKPVHELNREACDDYRLCERYAMVYGYNAAYNRYFRKRRGTK | null | null | cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; ossification [GO:0001503]; regulation of bone mineralization [GO:0030500] | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Requires vitamin K-dependent gamma-carboxylation for its function. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. | Homo sapiens (Human) |
P08494 | MGP_RAT | MKSLLPLAILAALAVAALCYESHESMESYEVSPFTTRRNANTFISPQQRWHAKAQERVRELNKPAQEINREACDDYKLCERYALIYGYNAAYNRYFRQRRGAK | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cartilage development [GO:0051216]; cell differentiation [GO:0030154]; lung development [GO:0030324]; ossification [GO:0001503]; protein-containing complex assembly [GO:0065003]; regulation of bone mineralization [GO:0030500]; response to calcium ion [GO:00515... | collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306] | null | null | Osteocalcin/matrix Gla protein family | PTM: Requires vitamin K-dependent gamma-carboxylation for its function. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. | Rattus norvegicus (Rat) |
P08495 | AK2_BACSU | MGLIVQKFGGTSVGSVEKIQNAANRAIAEKQKGHQVVVVVSAMGKSTDELVSLAKAISDQPSKREMDMLLATGEQVTISLLSMALQEKGYDAVSYTGWQAGIRTEAIHGNARITDIDTSVLADQLEKGKIVIVAGFQGMTEDCEITTLGRGGSDTTAVALAAALKADKCDIYTDVPGVFTTDPRYVKSARKLEGISYDEMLELANLGAGVLHPRAVEFAKNYQVPLEVRSSTETEAGTLIEEESSMEQNLIVRGIAFEDQITRVTIYGLTSGLTTLSTIFTTLAKRNINVDIIIQTQAEDKTGISFSVKTEDADQTVAVL... | 2.7.2.4 | null | diaminopimelate biosynthetic process [GO:0019877]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524] | PF00696;PF01842;PF13840; | 3.40.1160.10;3.30.2130.10; | Aspartokinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:15033471}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.5 mM for ATP {ECO:0000269|PubMed:15033471}; KM=10 mM for aspartate {ECO:0000269|PubMed:15033471}; Note=kcat is 952 min(-1).; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threon... | null | null | FUNCTION: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. {ECO:0000269|PubMed:15033471}. | Bacillus subtilis (strain 168) |
P08503 | ACADM_RAT | MAAALRRGYKVLRSVSHFECRAQHTKPSLKQEPGLGFSFELTEQQKEFQTIARKFAREEIIPVAPDYDKSGEYPFPLIKRAWELGLINTHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAGIKTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVS... | 1.3.8.7 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:3968063}; | cardiac muscle cell differentiation [GO:0055007]; carnitine biosynthetic process [GO:0045329]; carnitine metabolic process [GO:0009437]; carnitine metabolic process, CoA-linked [GO:0019254]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; glycogen biosyntheti... | axon [GO:0030424]; cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | acyl-CoA dehydrogenase activity [GO:0003995]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | PTM: Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3. {ECO:0000250|UniProtKB:P11310}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:3813556, ECO:0000269|PubMed:3968063}. | CATALYTIC ACTIVITY: Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:5830... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=135 uM for butanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=39.6 uM for pentanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=9.4 uM for hexanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=4 uM for octanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=5.4 uM for decanoyl-CoA {ECO:0000269|... | PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000305|PubMed:3968063}. | null | null | FUNCTION: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:3968063). The first step of fatty aci... | Rattus norvegicus (Rat) |
P08505 | IL6_MOUSE | MKFLSARDFHPVAFLGLMLVTTTAFPTSQVRRGDFTEDTTPNRPVYTTSQVGGLITHVLWEIVEMRKELCNGNSDCMNNDDALAENNLKLPEIQRNDGCYQTGYNQEICLLKISSGLLEYHSYLEYMKNNLKDNKKDKARVLQRDTETLIHIFNQEVKDLHKIVLPTPISNALLTDKLESQKEWLRTKTIQFILKSLEEFLKVTLRSTRQT | null | null | acute-phase response [GO:0006953]; branching involved in salivary gland morphogenesis [GO:0060445]; cell redox homeostasis [GO:0045454]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-17 [GO:0097398]; cellular respon... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; interleukin-6 receptor complex [GO:0005896] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-6 receptor binding [GO:0005138]; signaling receptor binding [GO:0005102] | PF00489; | 1.20.1250.10; | IL-6 superfamily | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P05231}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27893700}. | null | null | null | null | null | FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism (Probable). Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (PubMed:8910279). The interaction with the membrane-bound IL6R an... | Mus musculus (Mouse) |
P08506 | DACC_ECOLI | MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV... | 3.4.16.4 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to xenobiotic stimulus [GO:0009410] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | carboxypeptidase activity [GO:0004180]; penicillin binding [GO:0008658]; protein homodimerization activity [GO:0042803]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF07943;PF00768; | 2.60.410.10;3.40.710.10; | Peptidase S11 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:3330754}; Peripheral membrane protein {ECO:0000269|PubMed:3330754}; Periplasmic side {ECO:0000269|PubMed:3330754}. Note=N-terminus lies in the periplasmic space, targeted there by the C-terminal amphiphilic helix (PMID:3330754). | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | Escherichia coli (strain K12) |
P08508 | FCGR3_MOUSE | MFQNAHSGSQWLLPPLTILLLFAFADRQSAALPKAVVKLDPPWIQVLKEDMVTLMCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQRVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYKSNFSIPKANHSHSGDYYCKGSLGSTQHQSKPVTITVQDPATTSSISLVWYHTAFSLVMCLLFAVDTGLYFYVRRNLQTPREYWRKSLSIRKHQAPQDK | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; cell surface receptor signaling pathway [GO:0007166]; mast cell activation [GO:0045576]; neutrophil chemotaxis [GO:0030593]; phagocytosis, engulfment [GO:0006911]; phagoc... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897] | IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]; immunoglobulin receptor binding [GO:0034987] | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17558411}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor which binds to IgG1, IgG2a and IgG2b (PubMed:17558411). Mediates neutrophil activation by IgG complexes redundantly with Fcgr4 (PubMed:18097064). {ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064}. | Mus musculus (Mouse) |
P08509 | NIA2_TOBAC | MAASVENRQFSHLEAGLSRSFKPRSDSPVRGCNFPSPNSTNFQKKPNSTIYLDYSSSEDDDDDDEKNEYLQMIKKGNSELEPSVHDTRDEGTADNWIERNFSMIRLTGKHPFNSEPPLNRLMHHGFITPVPLHYVRNHGPVPKGTWDDWTVEVTGLVKRPMKFTMDQLVNEFPCRELPVTLVCAGNRRKEQNMVKQTIGFNWGAAAVSTTIWRGVPLRALLKRCGVFSKNKGALNVCFEGADVLPGGGGSKYGTSIKKEFAMDPARDIIVAYMQNGEKLAPDHGFPVRMIIPGFIGGRMVKWIKRIIVTTQESDSYYHFK... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 heme group per subunit. {ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250}; Note=... | nitrate assimilation [GO:0042128]; nitric oxide biosynthetic process [GO:0006809]; sulfur compound metabolic process [GO:0006790] | mitochondrion [GO:0005739] | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase (NADPH) activity [GO:0050464]; sulfite oxidase activity [GO:0008482] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; | null | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | Nicotiana tabacum (Common tobacco) |
P08510 | KCNAS_DROME | MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAI... | null | null | action potential [GO:0001508]; axon extension [GO:0048675]; behavioral response to ether [GO:0048150]; cellular response to dopamine [GO:1903351]; courtship behavior [GO:0007619]; detection of visible light [GO:0009584]; larval locomotory behavior [GO:0008345]; learning or memory [GO:0007611]; mating behavior, sex disc... | membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; voltage-gated monoatomic cation channel activity [GO:0022843]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Shaker sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2448636}; Multi-pass membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21813698}; Multi-pass membrane protein {ECO:0000305}. Cell projection, neuron projection {ECO:0000269|PubMed:20010822}. Perikaryon {ECO:0000269|PubMed:20010822}. Note=Localizes ... | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which pot... | Drosophila melanogaster (Fruit fly) |
P08514 | ITA2B_HUMAN | MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYF... | null | null | angiogenesis [GO:0001525]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; positive regulation of leukocyte migration [GO:0002687] | blood microparticle [GO:0072562]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092] | extracellular matrix binding [GO:0050840]; fibrinogen binding [GO:0070051]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090] | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/be... | Homo sapiens (Human) |
P08516 | CP4AA_RAT | MSVSALSSTRFTGSISGFLQVASVLGLLLLLVKAVQFYLQRQWLLKAFQQFPSPPFHWFFGHKQFQGDKELQQIMTCVENFPSAFPRWFWGSKAYLIVYDPDYMKVILGRSDPKANGVYRLLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWEQLAGQDSSIEIFQHISLMTLDTVMKCAFSHNGSVQVDGNYKSYIQAIGNLNDLFHSRVRNIFHQNDTIYNFSSNGHLFNRACQLAHDHTDGVIKLRKDQLQNAGELEKVKKKRRLDFLDILLLARMENGDSLSDKDLRAEVDTFMFE... | 1.14.14.80 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:11139583, ECO:0000269|PubMed:11821421}; | arachidonic acid metabolic process [GO:0019369]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651]; lipid hydroxylation [GO:0002933]; placenta development [GO:0001890] | endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231] | 16-hydroxypalmitate dehydrogenase activity [GO:0103002]; alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-hydroxylase activity [GO:0102033]; medium-chain fatty acid omega-hydroxylase ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3027069}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:3027069}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:10362749}; Note=kcat is 649 min-1 for dodecanoate. kcat is 230 min-1 for tetradecanoate. kcat is 60 min-1 for hexadecanoate. kcat is 1.4 min-1 for (9Z)-octadecenoate. kcat is 6 min-1 for (5Z,8Z,11Z,14Z... | null | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long-chain fatty acids (PubMed:10362749, PubMed:10620324, PubMed:3027069). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (PubMe... | Rattus norvegicus (Rat) |
P08518 | RPB2_YEAST | MSDLANSEKYYDEDPYGFEDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTLQDIICEDSTLILEQLAQHTTESDNISRKYEISFGKIYVTKPMVNESDGVTHALYPQEARLRNLTYSSGLFVDVKKRTYEAIDVPGRELKYELIAEESEDDSESGKVFIGRLPIMLRSKNCYLSEATESDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFKKAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSARTIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQMLEMLKPCVED... | 2.7.7.6 | null | RNA-templated transcription [GO:0001172]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367] | cytoplasmic stress granule [GO:0010494]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; ribonucleoside binding [GO:0032549]; RNA polymerase II activity [GO:0001055] | PF04563;PF04561;PF04565;PF04566;PF04567;PF00562;PF04560; | 2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10; | RNA polymerase beta chain family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08519 | APOA_HUMAN | MEHKEVVLLLLLFLKSAAPEQSHVVQDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRD... | 3.4.21.- | null | blood circulation [GO:0008015]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma lipoprotein particle [GO:0034358] | apolipoprotein binding [GO:0034185]; endopeptidase activity [GO:0004175]; endopeptidase inhibitor activity [GO:0004866]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF00051;PF00089; | 2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also det... | null | null | null | null | null | null | FUNCTION: Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. {ECO:0000269|PubMed:2531657}. | Homo sapiens (Human) |
P08523 | OMP_RAT | MAEDGPQKQQLDMPLVLDQDLTKQMRLRVESLKQRGEKKQDGEKLLRPAESVYRLDFIQQQKLQFDHWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPAAIFWRKEDSDAMDWNEADALEFGERLSDLAKIRKVMYFLITFGEGVEPANLKASVVFNQL | null | null | neurogenesis [GO:0022008]; sensory perception of smell [GO:0007608]; signal transduction [GO:0007165] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | peptide binding [GO:0042277] | PF06554; | 2.60.120.390; | Olfactory marker protein family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: May act as a modulator of the olfactory signal-transduction cascade. | Rattus norvegicus (Rat) |
P08524 | ERG20_YEAST | MASEKEIRRERFLNVFPKLVEELNASLLAYGMPKEACDWYAHSLNYNTPGGKLNRGLSVVDTYAILSNKTVEQLGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWYKVPEVGEIAINDAFMLEAAIYKLLKSHFRNEKYYIDITELFHEVTFQTELGQLMDLITAPEDKVDLSKFSLKKHSFIVTFKTAYYSFYLPVALAMYVAGITDEKDLKQARDVLIPLGEYFQIQDDYLDCFGTPEQIGKIGTDIQDNKCSWVINKALELASAEQRKTLDENYGKKDSVAEAKCKKIFNDLKIEQLYHEYEESIAK... | 2.5.1.1; 2.5.1.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; isoprenoid biosynthetic process [GO:0008299] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; vacuole [GO:0005773] | dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; isopentenyl-diphosphate delta-isomerase activity [GO:0004452]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:8096487}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:8096487}.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl ... | null | null | FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:8096487). ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosph... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08525 | QCR8_YEAST | MGPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLYSKAGREELERVNV | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | null | PF02939; | 1.20.5.210; | UQCRQ/QCR8 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08535 | HBB_LEPEU | MVHLSGEEKSAVTALWGKVNVEEVGGETLGRLLVVYPWTQRFFESFGDLSTASAVMGNPKVKAHGKKVLAAFSEGLSHLDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLVIVLSHHFGKEFTPQVQAAYQKVVAGVANALAHKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Lepus europaeus (European hare) |
P08536 | MET3_YEAST | MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHE... | 2.7.7.4 | null | hydrogen sulfide biosynthetic process [GO:0070814]; sulfate assimilation via adenylyl sulfate reduction [GO:0010134]; sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) [GO:0019379]; sulfur amino acid metabolic process [GO:0000096] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781] | PF01747;PF14306; | 3.40.50.620;3.40.50.300;3.10.400.10; | Sulfate adenylyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03106}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.65 mM for Sulfate {ECO:0000269|PubMed:14983089}; KM=0.082 mM for ATP {ECO:0000269|PubMed:14983089}; | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03106}. | null | null | FUNCTION: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids. {ECO:0000255|HAMAP-Rule:MF_03106}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08537 | TBA_XENLA | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVADITNACFEPANQMVKCDPRHGKYMACCLLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Xenopus laevis (African clawed frog) |
P08539 | GPA1_YEAST | MGCTVSTQTIGDESDPFLQNKRANDVIEQSLQLEKQRDKNEIKLLLLGAGESGKSTVLKQLKLLHQGGFSHQERLQYAQVIWADAIQSMKILIIQARKLGIQLDCDDPINNKDLFACKRILLKAKALDYINASVAGGSDFLNDYVLKYSERYETRRRVQSTGRAKAAFDEDGNISNVKSDTDRDAETVTQNEDADRNNSSRINLQDICKDLNQEGDDQMFVRKTSREIQGQNRRNLIHEDIAKAIKQLWNNDKGIKQCFARSNEFQLEGSAAYYFDNIEKFASPNYVCTDEDILKGRIKTTGITETEFNIGSSKFKVLDA... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; dopamine receptor signaling pathway [GO:0007212]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; nuclear migration involved in conjugation with cellular fusion [GO:0000743]; pheromone-dependent signal transduct... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886] | corticotropin-releasing hormone receptor 1 binding [GO:0051430]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta-subunit binding [GO:0031681]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(q) subfamily | PTM: N-myristoylation by NMT1 is pheromone-stimulated and required for palmitoylation of Cys-3. This lipid modification anchors the protein to membranes. Depalmitoylated by YLR118C/APT1. {ECO:0000269|PubMed:10712512, ECO:0000269|PubMed:1936988, ECO:0000269|PubMed:8415763, ECO:0000269|PubMed:8702760, ECO:0000269|PubMed:... | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Endosome membrane; Lipid-anchor; Cytoplasmic side. Note=Localizes predominantly to the plasma membrane in its inactive, GDP-bound form, and is directed to endosomes once in its active, GTP-bound form. Concentrates at the tip of the mating projections. | null | null | null | null | null | FUNCTION: Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) that mediates mating pheromone signal transduction. Binding of alpha-factor or a-factor to its cognate transmembrane receptor STE2 and STE3, respectively, allows the receptor to serve as a guanine nucleotide exchange factor (GE... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08542 | UDB17_RAT | MPGKWISALLLLQISCCFQSGNCGKVLVWPMEFSHWMNIKTILDELVQRGHEVTVLKPSAYYVLDPKKSPDLKFETFPTSVSKDELENYFIKLVDVWTYELQRDTCLSYSPLLQNMIDGFSDYYLSLCKDTVSNKQLMAKLQESKFDVLLSDPVAACGELIAEVLHIPFLYSLRFSPGYKIEKSSGRFILPPSYVPVILSGMGGPMTFIDRVKNMICTLYFDFWFHMFNAKKWDPFYSEILGRPTTLAETMGKAEMWLIRSYWDLEFPHPTLPNVDYIGGLQCRPPKPLPKDMEDFVQSSGEHGVVVFSLGSMVSSMTEE... | 2.4.1.17 | null | cellular glucuronidation [GO:0052695]; cellular response to ethanol [GO:0071361]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to growth hormone stimulus [GO:0071378]; cellular response to testosterone stimulus [GO:0071394]; estrogen metabolic process [GO:0008210]; response to lipopolysa... | endoplasmic reticulum membrane [GO:0005789] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75795}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:1692835, ECO:0000269|PubMed:18719240}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.2 uM for 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; KM=19.5 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; Vmax=8110 pmol/min/mg en... | null | null | null | FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:18719240). Catalyzes the glucuronidation ... | Rattus norvegicus (Rat) |
P08543 | RIR1_HHV11 | MASRPAASSPVEARAPVGGQEAGGPSAATQGEAAGAPLAHGHHVYCQRVNGVMVLSDKTPGSASYRISDNNFVQCGSNCTMIIDGDVVRGRPQDPGAAASPAPFVAVTNIGAGSDGGTAVVAFGGTPRRSAGTSTGTQTADVPTEALGGPPPPPRFTLGGGCCSCRDTRRRSAVFGGEGDPVGPAEFVSDDRSSDSDSDDSEDTDSETLSHASSDVSGGATYDDALDSDSSSDDSLQIDGPVCRPWSNDTAPLDVCPGTPGPGADAGGPSAVDPHAPTPEAGAGLAADPAVARDDAEGLSDPRPRLGTGTAYPVPLELTP... | 1.17.4.1 | null | deoxyribonucleotide biosynthetic process [GO:0009263]; DNA replication [GO:0006260]; release from viral latency [GO:0019046] | ribonucleoside-diphosphate reductase complex [GO:0005971] | ATP binding [GO:0005524]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748] | PF02867;PF00317; | 3.20.70.20; | Ribonucleoside diphosphate reductase large chain family | null | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;... | null | null | null | null | FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme that provides the precursors necessary for viral DNA synthesis (By similarity). Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucle... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P08544 | POLG_TMEVB | MACKHGYPDVCPICTAVDATPGFEYLLMADGEWYPTDLLCVDLDDDVFWPSDTSNQSQTMDWTDVPLIRDIVMEPQGNSSSSDKSNSQSSGNEGVIINNFYSNQYQNSIDLSASGGNAGDAPQTNGQLSNILGGAANAFATMAPLLLDQNTEEMENLSDRVASDKAGNSATNTQSTVGRLCGYGKSHHGEHPASCADTATDKVLAAERYYTIDLASWTTSQEAFSHIRIPLPHVLAGEDGGVFGATLRRHYLCKTGWRVQVQCNASQFHAGSLLVFMAPEFYTGKGTKTGTMEPSDPFTMDTEWRSPQGAPTGYRYDSRT... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; ... | PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cyto... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail t... | Theiler's murine encephalomyelitis virus (strain BeAn 8386) (TMEV) |
P08545 | POLG_TMEVG | MACKHGYPDVCPICTAVDATPDFEYLLMADGEWFPTDLLCVDLDDDVFWPSDTSTQPQTMEWTDVPLVCDTVMEPQGNASSSDKSNSQSSGNEGVIINNFYSNQYQNSIDLSASGGNAGDAPQNNGQLSSILGGAANAFATMAPLLMDQNTEEMENLSDRVASDKAGNSATNTQSTVGRLCGYGKSHHGEHPTSCADAATDKVLAAERYYTIDLASWTTSQEAFSHIRIPLPHVLAGEDGGVFGATLRRHYLCKTGWRVQVQCNASQFHAGSLLVFMAPEFYTGKGTKSGTMEPSDPFTMDTTWRSPQSAPTGYRYDRQA... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytop... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; ... | PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:C0MHL9}. Host cyto... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals f... | Theiler's murine encephalomyelitis virus (strain GDVII) (TMEV) |
P08551 | NFL_MOUSE | MSSFGYDPYFSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEI... | null | null | anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cerebral cortex development [GO:0021987]; hippocampus development [GO:0021766]; intermediate filament bundle assembly [GO:0045110]; intermediate filament organization [GO:0045109]; intermediate filament... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; intermediate filament [GO:0005882]; myelin sheath [GO:0043209]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; postsynaptic intermediate f... | identical protein binding [GO:0042802]; phospholipase binding [GO:0043274]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic inte... | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000269|PubMed:18687884}. | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:22723690}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22723690}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690). {ECO:0000269|Pu... | Mus musculus (Mouse) |
P08553 | NFM_MOUSE | MSYTLDSLGNPSAYRRVTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYKRSALAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRR... | null | null | axo-dendritic transport [GO:0008088]; intermediate filament bundle assembly [GO:0045110]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament polymerization or depolymerization [GO:0045105]; microtubule cytoskeleton organization [GO:0000226]; neurofilament bundle assembly [GO:0033693]; n... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intermediate filament [GO:0005882]; myelin sheath [GO:0043209]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; postsynaptic intermediate fil... | protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; structural constituent of cytoskeleton [GO:0005200]; toxic substance binding [GO:0015643] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a maj... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22723690}. Cell projection, axon {ECO:0000269|PubMed:22723690}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690). {ECO:0000269|Pu... | Mus musculus (Mouse) |
P08556 | RASN_MOUSE | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRLKKLNSSDDGTQGCMGSPCVLM | 3.6.5.2 | null | defense response to protozoan [GO:0042832]; negative regulation of skeletal muscle tissue development [GO:0048642]; positive regulation of angiogenesis [GO:0045766]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of type II interferon production [GO:0032729]; Ras protein signal transd... | Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. Depalmitoylated by ABHD17A, ABHD17B and ABHD17C. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01111}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma membrane and the Golgi ... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01116}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000250|UniProtKB:P01111}. | Mus musculus (Mouse) |
P08557 | CIRCN_BPMU | MFEDALNAVNAVRDKTGGGRKTTGKGTFRNVPFLVIEEQKQAGGRRLVKREYPLRDTGGVNDLGKKLRSRTFSACILNSNAETARDEAGALMDALDAPGSGELVHPDFGTVDVMVDSWECRTKADELNYYAFTVTVYPSLQDTAPDAETDTSAAVPAQAVAVTGSLGDTLSSVWQTVKDGTAAATAVMEAVTGVIDDISDAVDNLGVTQTVSGLMGSLSAMKGSVTSLINQPAMLASSLMGALSGVSSLCDTRTAFSTWNRLAQRFERRHAATAGRQGTITTSYNSPVAEKNIATLNYVMLAAAQTYRAEAASQALTAAL... | null | null | evasion of DNA end degradation by host [GO:0099016]; symbiont entry into host cell [GO:0046718]; viral genome circularization [GO:0099009]; viral tail assembly [GO:0098003]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | DNA binding [GO:0003677] | PF07157; | null | null | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27555589, ECO:0000269|PubMed:8599204}. Host cytoplasm {ECO:0000305|PubMed:8599204}. Note=Baseplate protein. {ECO:0000269|PubMed:27555589}. | null | null | null | null | null | FUNCTION: Required for tail assembly of phage Mu and responsible for circularizing the viral DNA after it has been ejected into the host cell. Following infection, the circularized DNA can be isolated as a supercoiled, non-covalent protein-DNA complex, in which the protein N is bound to the ends of the DNA. Protects li... | Escherichia phage Mu (Bacteriophage Mu) |
P08559 | ODPA_HUMAN | MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLL... | 1.2.4.1 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:19081061}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; glucose metabolic process [GO:0006006]; tricarboxylic acid cycle [GO:0006099] | mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; pyruvate dehydrogenase complex [GO:0045254] | pyruvate dehydrogenase (acetyl-transferring) activity [GO:0004739]; pyruvate dehydrogenase (NAD+) activity [GO:0034604] | PF00676; | 3.40.50.970; | null | PTM: Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation. {ECO:0000269|PubMed:11486000, ECO:0000269|PubMed:17474719,... | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}. | Homo sapiens (Human) |
P08563 | POLS_RUBVM | MASTTPITMEDLQKALEAQSRALRAGLAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDTAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPMPPQPPRA... | 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 Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF05750;PF05748;PF05749; | 2.60.98.30;3.30.67.20;2.60.40.2650;3.10.50.50; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidas... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000269|PubMed:28575072}. Host cytoplasm {ECO:0000269|PubMed:25056903}. Host mitochondrion {ECO:0000269|PubMed:10823864}. Note=The capsid protein is concentrated around Golgi region (PubMed:11160697). In the virion, it is probably associated to the viral membrane (Pub... | null | null | null | null | null | FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter (PubMed:28575072). The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from hos... | Rubella virus (strain M33) (RUBV) |
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