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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P05814 | CASB_HUMAN | MKVLILACLVALALARETIESLSSSEESITEYKQKVEKVKHEDQQQGEDEHQDKIYPSFQPQPLIYPFVEPIPYGFLPQNILPLAQPAVVLPVPQPEIMEVPKAKDTVYTKGRVMPVLKSPTIPFFDPQIPKLTDLENLHLPLPLLQPLMQQVPQPIPQTLALPPQPLWSVPQPKVLPIPQQVVPYPQRAVPVQALLLNQELLLNPTHQIYPVTQPLAPVHNPISV | null | null | calcium ion transport [GO:0006816]; lactation [GO:0007595]; negative regulation of cysteine-type endopeptidase activity [GO:2000117] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; enzyme inhibitor activity [GO:0004857] | PF00363; | null | Beta-casein family | PTM: Form 1-P is phosphorylated once; half of the molecules are phosphorylated on Ser-24, half on Ser-25. {ECO:0000269|PubMed:18847231, ECO:0000269|PubMed:6715339}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Important role in determination of the surface properties of the casein micelles. | Homo sapiens (Human) |
P05817 | D11_DICDI | MLNKLILLLILSSCLVLSVKSEVNVDCSLVRCAQPICKPHYRLNMTDSCCGRCEPCTDVACTLQVKYCQDGEVPTGCCPCTLPPTKPDCSLVKCARPVCKPYYRLNMTDSCCGRCEPCTGVACTLQIKYCKDGEVPTGCCPCTPQPTKKPDCSKVPCPKILKYCQEGELPTGCCPCTPQPTKKPDCSRVPCPKILKYCKEGELPTGCCPCTPQPTKKPDCSDVMCTMDIRYCKNGELPTGCCPCTPQETKVPDCSKAMCTMDIKYCKPGEKPFGCCPCRENLTQ | null | null | actin filament polymerization [GO:0030041]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-substrate adhesion [GO:0031589]; chemotaxis to folate [GO:0043326]; macropinocytosis [GO:0044351]; pattern specification process [GO:0007389]; sorocarp development [GO:0030587]; sor... | cell periphery [GO:0071944]; extracellular region [GO:0005576]; vesicle [GO:0031982] | null | null | null | null | null | null | null | null | null | null | null | null | Dictyostelium discoideum (Social amoeba) |
P05824 | RECN_ECOLI | MLAQLTISNFAIVRELEIDFHSGMTVITGETGAGKSIAIDALGLCLGGRAEADMVRTGAARADLCARFSLKDTPAALRWLEENQLEDGHECLLRRVISSDGRSRGFINGTAVPLSQLRELGQLLIQIHGQHAHQLLTKPEHQKFLLDGYANETSLLQEMTARYQLWHQSCRDLAHHQQLSQERAARAELLQYQLKELNEFNPQPGEFEQIDEEYKRLANSGQLLTTSQNALALMADGEDANLQSQLYTAKQLVSELIGMDSKLSGVLDMLEEATIQIAEASDELRHYCDRLDLDPNRLFELEQRISKQISLARKHHVSPE... | null | null | DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; recombinational interstrand cross-link repair [GO:0036298]; recombinational repair [GO:0000725]; response to ionizing radiation [GO:0010212]; response to radiation [GO:0009314]; response to UV [GO:0009411]; response to X-ray [GO:0010165]; SOS re... | bacterial nucleoid [GO:0043590]; cytosol [GO:0005829] | ATP binding [GO:0005524] | PF02463; | 3.40.50.300; | RecN family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21219465}. Note=In 70% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours. | null | null | null | null | null | FUNCTION: May be involved in recombinational repair of damaged DNA. | Escherichia coli (strain K12) |
P05825 | FEPA_ECOLI | MNKKIHSLALLVNLGIYGVAQAQEPTDTPVSHDDTIVVTAAEQNLQAPGVSTITADEIRKNPVARDVSKIIRTMPGVNLTGNSTSGQRGNNRQIDIRGMGPENTLILIDGKPVSSRNSVRQGWRGERDTRGDTSWVPPEMIERIEVLRGPAAARYGNGAAGGVVNIITKKGSGEWHGSWDAYFNAPEHKEEGATKRTNFSLTGPLGDEFSFRLYGNLDKTQADAWDINQGHQSARAGTYATTLPAGREGVINKDINGVVRWDFAPLQSLELEAGYSRQGNLYAGDTQNTNSDSYTRSKYGDETNRLYRQNYALTWNGGWD... | null | null | colicin transport [GO:0042914]; enterobactin transport [GO:0042930]; ferric-enterobactin import into cell [GO:0015685]; intracellular iron ion homeostasis [GO:0006879]; siderophore transmembrane transport [GO:0044718]; siderophore-dependent iron import into cell [GO:0033214] | cell envelope [GO:0030313]; cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495] | colicin transmembrane transporter activity [GO:0042912]; enterobactin binding [GO:1903981]; enterobactin transmembrane transporter activity [GO:0042931]; ferric-enterobactin transmembrane transporter activity [GO:0015620]; ligand-gated channel activity [GO:0022834]; protein domain specific binding [GO:0019904]; siderop... | PF07715;PF00593; | 2.40.170.20;2.170.130.10; | TonB-dependent receptor family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}. | null | null | null | null | null | FUNCTION: This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D. | Escherichia coli (strain K12) |
P05844 | POLS_IPNVJ | MSTSKATATYLRSIMLPENGPASIPDDITERHILKQETSSYNLEVSESGSGLLVCFPGAPGSRVGAHYRWNLNQTALEFDQWLETSQDLKKAFNYGRLISRKYDIQSSTLPAGLYALNGTLNAATFEGSLSEVESLTYNSLMSLTTNPQDKVNNQLVTKGITVLNLPTGFDKPYVRLEDETPQGPQSMNGARMRCTAAIAPRRYEIDLPSERLPTVAATGTPTTIYEGNADIVNSTAVTGDITFQLEAEPVNETRFDFILQFLGLDNDVPVVTVTSSTLVTADNYRGASAKFTQSIPTEMITKPITRVKLAYQLNQQTAI... | 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;3.30.230.110;6.10.250.1030;1.10.8.880;1.10.150.620;2.60.120.660; | null | PTM: Specific enzymatic cleavages yield mature proteins. 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, giving ri... | 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.; FUNCTION: The precursor of VP2 plays an important role ... | Infectious pancreatic necrosis virus (strain Jasper) (IPNV) |
P05852 | TSAD_ECOLI | MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATAD... | 2.3.1.234 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445}; | maintenance of translational fidelity [GO:1990145]; tRNA threonylcarbamoyladenosine modification [GO:0002949] | cytosol [GO:0005829]; EKC/KEOPS complex [GO:0000408] | glycosylation-dependent protein binding [GO:0140032]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; magnesium ion binding [GO:0000287]; N(6)-L-threonylcarbamoyladenine synthase activity [GO:0061711] | PF00814; | 3.30.420.40; | KAE1 / TsaD family | PTM: Can be proteolytically processed in vitro by TsaB. {ECO:0000269|PubMed:19376873}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445, ECO:0000269|PubMed:19376873}. | CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; ... | null | null | null | null | FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likel... | Escherichia coli (strain K12) |
P05854 | NEF_HV1H3 | MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWRYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB3) (HIV-1) |
P05855 | NEF_HV1B8 | MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIHHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPEKEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHMARELHPEYFKNC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate BH8) (HIV-1) |
P05856 | NEF_HV1MN | MGGKWSKRVTGWPTVRERMRRAEPAELAADGVGAASRDLEKHGALTSSNTAATNADCAWLEAQEEEEVGFPVKPQVPLRPMTYKAALDLSHFLKEKGGLDGLIYSQKRQDILDLWVYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKIEEANKGENNCLLHPMSQHGMDDPEREVLVWKSDSHLAFQHYARELHPEYYKNC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1) |
P05857 | NEF_HV1SC | MGGKWSKRSVVGWPTVRERMRKTEPAADGVGAASRDLEKHGAITSSNTPANNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAAVDLSHFLKEQGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLCFGWCFKLVPVKPEKIEEANEGENNSLLHPMSLHGMEDPEREVLEWRFDNRLAFHHMARDLHPEYYKDCLTSMCLQGTFRWGISREARLGGTGEWRALRCCI | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1) |
P05858 | NEF_HV1RH | MGGKWSKSKMGGWPAVRERMQKAEPAADGVGAASRDLEKHGTITSSNTAANNAACTWLEAQEDEDEEVGFPVRPQVPLRPMTFKAAVDLSHFLKEKGGLDGLVFSQKRQDILDLWVYHTQGYFPDWQNYTPGPGTRYPLTFGWCFKLVPVEPDKVEEATEGENNSLLHPICLHGMDDPEKEVLVWKFDSRLAFHHVAREKHPEYYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1) |
P05859 | NEF_HV1ZH | MGNKWSKGWPAVRERIRQTPPAPPAAEGVGAASQDLAKHGAISSSNTATNNPDCAWLEAQEESEEVGFPVRPQVPLRPMTFKGAFDLSFFLKEKGGLDGLIYSKKRQEILDLWVYHTQGFFPDWHNYTPGPGTRYPLCFGWCFKLVPVDPREVEEANTGENNCLLHPMSQHGMDDDEREVLMWKFDSSLARKHLAREMHPEFYKD | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype A (isolate Z321) (HIV-1) |
P05877 | ENV_HV1MN | MRVKGIRRNYQHWWGWGTMLLGLLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATQACVPTDPNPQEVELVNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNTTNTNNSTANNNSNSEGTIKGGEMKNCSFNITTSIRDKMQKEYALLYKLDIVSIDNDSTSYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAILKCNDKKFSGKGSCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVHLNESVQINCTRPNYNKRKRIHIGPGRAF... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1) |
P05878 | ENV_HV1SC | MRVKGSGRNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNIWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNLRNDTSTNATNTTSSNRGKMEGGEMTNCSFNITTSIRSKVQKEYALFYKLDVVPIDNTSYTLINCNTSVITQACPKVSFEPIPIHYCARWFAILNCNNKKFNGTGPCTNVSTVQCTHGIRPVVSTHLLLNGSLAEEEVVLRSENFTDNAKTIIVQLKEAVEINCTRPNNNTTRSIHIGPGRAFYATGD... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1) |
P05879 | ENV_HV1C4 | MAMRAKGIRKNCQHLWRWGTMLLGMLMICSAAANLWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTNPNPQEVVLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLNTNNTTNTTELSIIVVWEQRGKGEMRNCSFNITTSIRDKVQREYALFYKLDVEPIDDNKNTTNNTKYRLINCNTSVITQACPKVSFEPIPIHYCTPTGFALLKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTNNAKTIIVQLNVSVEINCTRPNNHTRKRVTL... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1) |
P05880 | ENV_HV1W2 | MRVKGIMRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTTLFCASDAKAYSTEAHNVWATHACVPTDPNPQEVILGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWKNTTIIGGGEVKNCSFNITTSRRDKVHKEYALFYKLDVVPIKGDNNSSRYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPYNNVRRSLSIGPGRAFRTREIIGI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22) (HIV-1) |
P05881 | ENV_HV1ZH | MKVKGIQGNWQNWWKWGTLILGLVIICSAAENLWVTVYYGVPVWKDAETTLFCASDAKAYDTEKHNVWATHACVPTDPNPQELSLGNVTEKFDMWKNNMVEQMHEDVISLWDQSLKPCVKLTPLCVTLSCHNITIKDNNTNVDTEMKEEIKNCSYNMTTELRDKQRKIYSLFYRLDIVPIGGNSSNGDSSKYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDEEFEGKGPCRNVSTVQCTHGIRPVVSTQLLLNGSLAEGEVRIRSENFTDNAKIIIVQLVKPVNITCMRPNNNTRKSISIGPGRAFFATG... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype A (isolate Z321) (HIV-1) |
P05882 | ENV_HV1Z8 | MRVMGIRMNYQHLWKWGIMLLGILMTCSVAEDLWVTVYYGVPVWKEATTTLFCASDAKSYEPEAHNIWATHACVPTDPNPREIEMENVTENFNMWKNNMVEQMHEDIISLWDQNLKPCVKLTPLCVTLNCTNAGGNKTTNGNNTTNQEEQMMEKGEMKNCSFNITTVISDKKKQVHALFYRLDVVPIDDDNSANTSNTNYTNYRLINCNTSAITQACPKVTFEPIPIHYCAPAGFAILKCKDKKFNGTGPCKKVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNVKTIIVHLNESVEINCTRPDNKITRQST... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype D (isolate Z84) (HIV-1) |
P05883 | ENV_HV2NZ | MKGSKNQLLIAIVLASAYLIHCKQFVTVFYGIPAWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWNNTVTEQAVEDVWNLFETSIKPCVKLTPLCVAMNCTRNMTTWTGRTDTQNITIINDTSHARADNCTGLKEEEMIDCQFSMTGLERDKRKQYTEAWYSKDVVCDNNTSSQSKCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFAPNCSKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNNFYNLTMHCKRPGNKTVLPITFMSGFKFHSQPVI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: 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}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2) |
P05884 | ENV_SIVMK | MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKT... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: 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}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05885 | ENV_SIVM1 | MGCLGNQLLIAILLLSVYGIYCIQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNDDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDKWGLTKSSTTTASTTTTTTAKSVETRDIVNETSPCVVHDNCTGLEQEPMISCKFNMTGLKRDKKKEYNETWYSADLVCEQGNSTGNESRCYMNHCNTSVIQECCDKDYWDAIRCRYCAPPGYALLRCNDTNYSGFMPNCSKVVVSSCTRMMETQTSTWFRFNGTRAENRTYIYWHGRDNRTIISLNKHYNLTMKCRRPGNK... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: 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}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05886 | ENV_SIVVT | MRYTIITLGIIVIGIGIVLSKQWITVFYGIPVWKNSSVQAFCMTPTTSLWATTNCIPDDHDYTEVPLNITEPFEAWGDRNPLIAQAASNIHLLFEQTMKPCVKLSPLCIKMNCVELNSTRERATTPTTTPKSTGLPCVGPTSGENLQSCNASIIEREMEDEPASNCTFAMAGYVRDQKKNYYSVVWNDAEIYCKNKTNSTSKECYMIHCNDSVIKEACDKTYWDQLRLRYCAPAGYALLKCNDEDYNGYKQNCSNVSVVHCTGLMNTTVTTGLLLNGSYHENRTQIWQKHRVNNNTVLILFNKHYNLSVTCRRPGNKTVL... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: 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}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet) |
P05887 | GAG_HV1C4 | MGARASVLSGGELDRWEKIRLRPGGKKQYRLKHIVWASRKLERFAVNPGLLETSKGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFAALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPTPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1) |
P05888 | GAG_HV1MN | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHVVWASRELERFAINPGLLETSEGCRQILGQLQPSLQTGSEERKSLYNTVATLYCVHQKIKIKDTKEALEKIEEEQNKSKKKAQQAAADTGNRGNSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPAHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWM... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | sequence-specific DNA binding [GO:0043565]; structural molecule activity [GO:0005198]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1) |
P05889 | GAG_HV1W2 | MGARASVLSGGELDKWEKIRLRPGGKKKYRLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEKKDTKEALDKIEEEQNKCKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQATQEVKNWMTET... | null | null | viral process [GO:0016032] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF00540;PF00607;PF19317; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760; | Primate lentivirus group gag polyprotein family | PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22) (HIV-1) |
P05890 | GAG_HV1RH | MGARASVLSGGKLDKWEKIRLRPRGKKRYKLKHIVWASRELERFAVNPSLLETAEGCRQILGQLQPALQTGSEELKSLYNAVATLYCVHQNIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNGSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1) |
P05891 | GAG_HV2NZ | MGARNSVLRGKKADELEKIRLRPGGKKKYKLKHIVWAANELDRFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVQRHLVAETGTAEKMPNTSRPTAPPSGKNFPVQQVAGNYTHIPLSPGTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVAHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDINQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2) |
P05892 | GAG_SIVVT | MGAATSALNRRQLDQFEKIRLRPNGKKKYQIKHLIWAGKEMERFGLHERLLETEEGCKRIIEVLYPLEPTGSEGLKSLFNLVCVLYCLHKEQKVKDTEEAVATVRQHCHLVEKEKSATETSSGQKKNDKGIAAPPGCSQNFPAQQQGNAWVHVPLSPRTLNAWVKAVEEKKFGAEIVPMFQALSEGCTPYDINQMLNVLGDHQGALQIVKEIINEEAAQWDVTHPLPAGPLPAGQLRDPRGSDIAGTTSSVQEQLEWIYTANPRVDVGAIYRRWIILGLQKCVKMYNPVSVLDIRQGPKEPFKDYVDRFYKAIRAEQASG... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear ... | null | null | null | null | null | FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {EC... | Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet) |
P05893 | GAG_SIVMK | MGARNAVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTAETMPKTSRPTAPSSGRGGNYPVQQIGGNYVHLPLSPRTLNAWVKLIEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQPAPQQGQLREPSGSDIAGTTSSVDEQIQWMYRQQNPIPVGNIYRRWIQLRLQKCVRMYNPINILDVKQRPKEPFQSYVDRFYKSLRAEQTDAAVKNWMTQ... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | null | null | null | null | null | FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {EC... | Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05894 | GAG_SIVM1 | MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQ... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | null | null | null | null | null | FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {EC... | Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05895 | POL_SIVVT | MGAATSALNRRQLDKFEHIRLRPTGKKKYQIKHLIWAGKEMERFGLHERLLESEEGCKKIIEVLYPLEPTGSEGLKSLFNLVCVLFCVHKDKEVKDTEEAVAIVRQCCHLVEKERNAERNTTETSSGQKKNDKGVTVPPGGSQNFPAQQQGNAWIHVPLSPRTLNAWVKAVEEKKFGAEIVPMFQALSEGCTPYDINQMLNVLGDHQGALQIVKEIINEEAAQWDIAHPPPAGPLPAGQLRDPRGSDIAGTTSTVQEQLEWIYTANPRVDVGAIYRRWIILGLQKCVKMYNPVSVLDIRQGPKEAFKDYVDRFYKAIRAE... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural mo... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|P... | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet) |
P05896 | POL_SIVM1 | MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVMETGTAETMPKTSRPTAPFSGRGGNYPVQQIGGNYTHLPLSPRTLNAWVKLIEEKKFGAEVVSGFQALSEGCLPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQQAPQQGQLREPSGSDIAGTTSTVEEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQ... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural mo... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|P... | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05897 | POL_SIVMK | MGARNSVLSGKKADELEKIRLRPGGKKKYMLKHVVWAANELDRFGLAESLLENKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTAETMPKTSRPTAPSSGRGGNYPVQQIGGNYVHLPLSPRTLNAWVKLIEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIRDIINEEAADWDLQHPQPAPQQGQLREPSGSDIAGTTSSVDEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDAAVKNWMTQ... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural mo... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|P... | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Simian immunodeficiency virus (isolate K6W) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P05905 | TAT_HV1MN | MEPVDPRLEPWKHPGSQPKTACTTCYCKKCCFHCQVCFTKKALGISYGRKKRRQRRRAPEDSQTHQVSLPKQPAPQFRGDPTGPKESKKKVERETETHPVD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1) |
P05906 | TAT_HV1SC | MDPVDPRLEPWKHPGSQPKAACTSCYCKKCCFHCQVCFTTKGLGISYGRKKRRQRRRAPQDSQTHQVSLPKQPASQARGDPTGPKESKKKVERETETDPVD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1) |
P05907 | TAT_HV1C4 | MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFTKKALGISYGRKKRRQRRRAHQDSQNHQASLSKQPSSQTRGDPTGPKEPKKEVEREAETDPLD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1) |
P05908 | TAT_HV1RH | MEPVDPRLEPWKHPGSQPKTACNNCYCKKCCYHCQVCFLTKGLGISYGRKKRRQRRGPPQGSQTHQVSLSKQPTSQPRGDPTGPKESKEKVERETETDPAVQ | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1) |
P05919 | VPU_HV1H2 | MQPIPIVAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDVDDL | null | null | receptor catabolic process [GO:0032801]; suppression by virus of host tetherin activity [GO:0039587]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral release from host cell [GO:0019076] | host cell membrane [GO:0033644]; membrane [GO:0016020] | CD4 receptor binding [GO:0042609]; monoatomic cation channel activity [GO:0005261] | PF00558; | 1.10.195.10; | HIV-1 VPU protein family | PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4. {ECO:0000255|HAMAP-Rule:MF_04082}. | SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:8331740}. | null | null | null | null | null | FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... | Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) |
P05923 | VPU_HV1BR | MQPIQIAIAALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALVEMGVEMGHHAPWDIDDL | null | null | receptor catabolic process [GO:0032801]; suppression by virus of host tetherin activity [GO:0039587]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral release from host cell [GO:0019076] | host cell membrane [GO:0033644]; membrane [GO:0016020] | CD4 receptor binding [GO:0042609]; monoatomic cation channel activity [GO:0005261] | PF00558; | 1.10.195.10; | HIV-1 VPU protein family | PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4. {ECO:0000255|HAMAP-Rule:MF_04082, ECO:0000269|PubMed:1541298}. | SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082}. | null | null | null | null | null | FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P05928 | VPR_HV1BR | MEQAPEDQGPQREPHNEWTLELLEELKNEAVRHFPRIWLHGLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTQQRRARNGASRS | null | null | cell cycle [GO:0007049]; DNA-templated transcription [GO:0006351]; monoatomic ion transmembrane transport [GO:0034220]; protein homooligomerization [GO:0051260]; regulation of DNA-templated transcription [GO:0006355]; symbiont entry into host cell [GO:0046718]; symbiont-mediated arrest of host cell cycle during G2/M tr... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host extracellular space [GO:0043655]; virion component [GO:0044423] | null | PF00522; | 6.10.210.10;1.20.5.90; | HIV-1 VPR protein family | PTM: Phosphorylated on several residues by host. These phosphorylations regulate VPR activity for the nuclear import of the HIV-1 pre-integration complex. {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:10864665, ECO:0000269|PubMed:11860675}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may functio... | null | null | null | null | null | FUNCTION: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions. {ECO:0000... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P05933 | CALM_SCHPO | MTTRNLTDEQIAEFREAFSLFDRDQDGNITSNELGVVMRSLGQSPTAAELQDMINEVDADGNGTIDFTEFLTMMARKMKDTDNEEEVREAFKVFDKDGNGYITVEELTHVLTSLGERLSQEEVADMIREADTDGDGVINYEEFSRVISSK | null | null | ascospore formation [GO:0030437]; ascospore-type prospore-specific spindle pole body remodeling [GO:0031322]; mitotic spindle assembly [GO:0090307]; protein localization to meiotic spindle pole body [GO:1902441]; spindle pole body organization [GO:0051300] | cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; central plaque of mitotic spindle pole body [GO:0061493]; central plaque of spindle pole body [GO:0005823]; cytosol [GO:0005829]; division septum [GO:0000935]; growing cell tip [GO:0035838]; mating projection tip [GO:0043332]; meiotic spindle pole b... | calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234] | PF13499; | 1.10.238.10; | Calmodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9635188}. Note=In the growing tips and spindle pole body during interphase and in the septum during septation. Component of a ring structure that forms prior to septation. | null | null | null | null | null | FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P05937 | CALB1_HUMAN | MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN | null | null | cellular response to organic substance [GO:0071310]; cochlea development [GO:0090102]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; metanephric collecting duct development [GO:0072205]; metanephric connecting tubule development [GO:0072286]; metanephric distal convoluted tubule development [GO:00722... | axon [GO:0030424]; calyx of Held [GO:0044305]; cuticular plate [GO:0032437]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal c... | calcium ion binding [GO:0005509]; calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration [GO:0099567]; calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration [GO:0099534]; vitamin D binding [GO:0005499]; zinc ion binding [GO:0008270] | PF00036;PF13499; | 1.10.238.10; | Calbindin family | null | null | null | null | null | null | null | FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. | Homo sapiens (Human) |
P05942 | S10A4_RAT | MARPLEEALDVIVSTFHKYSGNEGDKFKLNKTELKELLTRELPSFLGRRTDEAAFQKLMNNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK | null | null | positive regulation of canonical NF-kappaB signal transduction [GO:0043123] | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | actin binding [GO:0003779]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; chemoattractant activity [GO:0042056]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; RAGE receptor binding [GO:0050786]; transition metal ion binding [GO:0046914] | PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000250|UniProtKB:P07091}. | null | null | null | null | null | FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By similarity). Mechanistically, promotes filam... | Rattus norvegicus (Rat) |
P05943 | S10AA_RAT | MPSQMEHAMETMMLTFHRFAGEKNYLTKEDLRVLMEREFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFLSLVAGLIIACNDYFVVHMKQKK | null | null | membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of plasminogen activation [GO:0010756]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-depende... | AnxA2-p11 complex [GO:1990665]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; RNA polymerase II transcription regulator complex [GO:0090575] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein homodimerization activity [GO:0042803]; transmembrane transporter binding [GO:0044325] | PF01023; | 1.10.238.10; | S-100 family | null | null | null | null | null | null | null | FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase. {ECO:0000250}. | Rattus norvegicus (Rat) |
P05959 | POL_HV1RH | MGARASVLSGGKLDKWEKIRLRPRGKKRYKLKHIVWASRELERFAVNPSLLETAEGCRQILGQLQPALQTGSEELKSLYNAVATLYCVHQNIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNGSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3) (HIV-1) |
P05960 | POL_HV1C4 | MGARASVLSGGELDRWEKIRLRPGGKKQYRLKHIVWASRKLERFAVNPGLLETSKGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEVRDTKEALDKIEEEQNKSKKKAQQAAADTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFAALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPTPVGEIYKRWIILGLNKIVRMYSPISILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 3.4.23.16 | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; lipid binding [GO:0008289]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid p... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451) (HIV-1) |
P05961 | POL_HV1MN | MGARASVLSGGELDRWENIRLRPGGKKKYKLKHVVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELKSLYNTVATLYCVHQKIEIKDTKEALEKIEEEQNKSKKKAQQAAADTGNRGNSSQVSQNYPIVQNIEGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPITPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNRT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1) |
P05962 | POL_HV2NZ | MGARNSVLRGKKADELEKIRLRPGGKKKYKLKHIVWAANELDRFGLAESLLESKEGCQKILTVLDPLVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVQRHLVAETGTAEKMPNTSRPTAPPSGKNFPVQQVAGNYTHIPLSPGTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVAHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDINQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate NIH-Z) (HIV-2) |
P05976 | MYL1_HUMAN | MAPKKDVKKPVAAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQDEFKEAFLLFDRTGDSKITLSQVGDVLRALGTNPTNAEVRKVLGNPSNEELNAKKIEFEQFLPMMQAISNNKDQATYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCINYEAFVKHIMSI | null | null | muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049] | contractile fiber [GO:0043292]; cytosol [GO:0005829]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | calcium ion binding [GO:0005509]; structural constituent of muscle [GO:0008307] | null | 1.10.238.10; | null | PTM: [Isoform MLC3]: Acetylated at position 2. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function. {ECO:0000269|PubMed:30215711}. | Homo sapiens (Human) |
P05979 | PGH1_SHEEP | MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMDTKGKKQLPDAEFLSRRFLLRRKFIPDPQSTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEH... | 1.14.99.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; | cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of blood pressure [GO:0008217]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]; protein homodimerization act... | PF03098; | 1.10.640.10;2.10.25.10; | Prostaglandin G/H synthase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000269|PubMed:7947975}; PhysiologicalDirection=le... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.1 uM for arachidonate {ECO:0000269|PubMed:7947975}; | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:7947975}. | null | null | FUNCTION: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response (PubMed:9448728). The cyclooxygenase ac... | Ovis aries (Sheep) |
P05980 | PGFS1_BOVIN | MDPKSQRVKLNDGHFIPVLGFGTYAPEEVPKSEALEATKFAIEVGFRHVDSAHLYQNEEQVGQAIRSKIADGTVKREDIFYTSKLWCNSLQPELVRPALEKSLQNLQLDYVDLYIIHSPVSLKPGNKFVPKDESGKLIFDSVDLCHTWEALEKCKDAGLTKSIGVSNFNHKQLEKILNKPGLKYKPVCNQVECHPYLNQSKLLEFCKSHDIVLVAYAALGAQLLSEWVNSNNPVLLEDPVLCAIAKKHKQTPALVALRYQVQRGVVVLAKSFNKKRIKENMQVFDFELTPEDMKAIDGLNRNIRYYDFQKGIGHPEYPFS... | 1.1.1.188 | null | daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; progesterone metabolic process [GO:0042448]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693] | cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; androsterone dehydrogenase activity [GO:0047023]; bile acid binding [GO:0032052]; ketosteroid monooxygenase activity [GO:0047086]; prostaglandin D2 11-ketoreductase activity [GO:0036131]; prostaglandin-F synthase activity [GO:0047017] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin D2; Xref=Rhea:RHEA:10140, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404, ChEBI:CHEBI:57406, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.188; | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. | null | null | FUNCTION: Catalyzes the reduction of PGD(2) and PGH(2) to PGF(2 alpha) and a stereoisomer, respectively. It has a broad substrate specificity and reduces also other carbonyl compounds. | Bos taurus (Bovine) |
P05981 | HEPS_HUMAN | MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISND... | 3.4.21.106 | null | basement membrane disassembly [GO:0034769]; cochlea morphogenesis [GO:0090103]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epitheli... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008]; serine-type peptidase activity [GO:0008236] | PF09272;PF00089; | 3.10.250.10;2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1885621}; Single-pass type II membrane protein {ECO:0000269|PubMed:1885621}. Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.; EC=3.4.21.106; Evidence={ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000305|PubMed:26673890}; | null | null | null | null | FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:15839837, PubMed:21875933). Plays a role in cell growth and maintenance of cell morphology (PubMed:21875933, PubMed:8346233). Plays a role in the proteolyti... | Homo sapiens (Human) |
P05982 | NQO1_RAT | MAVRRALIVLAHAERTSFNYAMKEAAVEALKKKGWEVVESDLYAMNFNPLISRNDITGEPKDSENFQYPVESSLAYKEGRLSPDIVAEQKKLEAADLVIFQFPLYWFGVPAILKGWFERVLVAGFAYTYATMYDKGPFQNKKTLLSITTGGSGSMYSLQGVHGDMNVILWPIQSGILRFCGFQVLEPQLVYSIGHTPPDARVQVLEGWKKRLETVWEESPLYFAPSSLFDLNFQAGFLLKKEVQEEQKKNKFGLSVGHHLGKSIPADNQIKARK | 1.6.5.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:1703398}; | cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to metal ion [GO:0071248]; cellular response to oxidative stress [GO:0034599]; innate immune response [GO:0045087]; NADH oxidation [GO:0006116]; NADPH oxidation [GO:0070995]; negative regulation of apoptotic proc... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADPH dehydrogenase (quinone) activity [GO:0008753]; superoxide dismutase activity [GO:0004784] | PF02525; | 3.40.50.360; | NAD(P)H dehydrogenase (quinone) family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1703398}. | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630, ECO:0000269|PubMed:8999809}; PhysiologicalDirectio... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=85 uM for NADH {ECO:0000269|PubMed:7862630}; KM=39 uM for NADPH {ECO:0000269|PubMed:7862630}; KM=110 uM for NADH {ECO:0000269|PubMed:8999809}; KM=2.5 uM for menadione {ECO:0000269|PubMed:8999809}; KM=840 uM for 5-(aziridin-1-yl)-2,4-dinitrobenzamide {ECO:0000269|Pu... | null | null | null | FUNCTION: Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypass... | Rattus norvegicus (Rat) |
P05986 | KAPC_YEAST | MYVDPMNNNEIRKLSITAKTETTPDNVGQDIPVNAHSVHEECSSNTPVEINGRNSGKLKEEASAGICLVKKPMLQYRDTSGKYSLSDFQILRTLGTGSFGRVHLIRSNHNGRFYALKTLKKHTIVKLKQVEHTNDERRMLSIVSHPFIIRMWGTFQDSQQVFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVCLALEYLHSKDIIYRDLKPENILLDKNGHIKITDFGFAKYVPDVTYTLCGTPDYIAPEVVSTKPYNKSVDWWSFGVLIYEMLAGYTPFYNSNTMKTYENILNAELKFPPFFHPDAQDLLKKLITR... | 2.7.11.11 | null | mitochondrion organization [GO:0007005]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of cytoplasmic translation [GO:2000766]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265] | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05987 | KAPR_DICDI | MTNNISHNQKATEKVEAQNNNNITRKRRGAISSEPLGDKPATPLPNIPKTVETQQRLEQALSNNIMFSHLEEEERNVVFLAMVEVLYKAGDIIIKQGDEGDLFYVIDSGICDIYVCQNGGSPTLVMEVFEGGSFGELALIYGSPRAATVIARTDVRLWALNGATYRRILMDQTIKKRKLYEEFLEKVSILRHIDKYERVSLADALEPVNFQDGEVIVRQGDPGDRFYIIVEGKVVVTQETVPGDHSTSHVVSELHPSDYFGEIALLTDRPRAATVTSIGYTKCVELDRQRFNRLCGPIDQMLRRNMETYNQFLNRPPSSP... | null | null | c-di-GMP signaling [GO:0061939]; culmination involved in sorocarp development [GO:0031154]; positive regulation of gene expression [GO:0010628]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of gene expression [GO:0010468]; regulation of protein kinase ... | cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytosol [GO:0005829] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027; | 2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain but is not phosphorylated. The physiological significance of phosphorylations by other kinases is unclear. | null | null | null | null | null | null | null | Dictyostelium discoideum (Social amoeba) |
P05989 | ILVC_SALTY | MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPQGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADW... | 1.1.1.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:4388025}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287] | PF01450;PF07991; | 3.40.50.720; | Ketol-acid reductoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:4388025}; CATA... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:4388025}; | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methy... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P05990 | PYR1_DROME | MASTDCYLALEDGTVLPGYSFGYVPSENESKVGFGGEVVFQTGMVGYTEALTDRSYSGQILVLTYPLIGNYGVPAPDEDEHGLPLHFEWMKGVVQATALVVGEVAEEAFHWRKWKTLPDWLKQHKVPGIQDIDTRALTKKLREQGSMLGKIVYEKPPVEGLPKSSFVDPNVRNLAKECSVKERQVYGNPNGKGPRIAILDCGLKLNQLRCLLQRGASVTLLPWSARLEDEQFDALFLSNGPGNPESCDQIVQQVRKVIEEGQKPVFGICLGHQLLAKAIGCSTYKMKYGNRGHNLPCLHRATGRCLMTSQNHGYAVDLEQ... | 2.1.3.2; 3.5.1.2; 3.5.2.3; 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:2910... | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:000435... | PF01979;PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729; | 3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380; | CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P27708}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000250|UniProtKB:P27708}.; PATHWAY: Pyrimidine ... | null | null | FUNCTION: Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-d... | Drosophila melanogaster (Fruit fly) |
P05994 | PAPA4_CARPA | MAIICSFSKLLFVAICLFGHMSLSYCDFSIVGYSQDDLTSTERLIQLFNSWMLKHNKNYKNVDEKLYRFEIFKDNLKYIDERNKMINGYWLGLNEFSDLSNDEFKEKYVGSLPEDYTNQPYDEEFVNEDIVDLPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDKQSYGCNRGYQSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEGSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKSGGKGYILIKNSWGPGWGEN... | 3.4.22.25 | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.; EC=3.4.22.25; Evidence={ECO:0000269|PubMed:2404797}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 mM for Boc-Ala-Ala-Gly-NHPhNO(2) {ECO:0000269|PubMed:2404797}; KM=0.16 mM for Boc-Ala-Ala-Gly-NHMec {ECO:0000269|PubMed:2404797}; KM=0.08 mM for Boc-Ala-Ala-Ala-NHMec {ECO:0000269|PubMed:2404797}; Note=kcat is 22 sec(-1) with Boc-Ala-Ala-Gly-NHPhNO(2) as substr... | null | null | null | FUNCTION: Thiol protease with a substrate specificity very different from the other thiol proteases. {ECO:0000269|PubMed:2404797}. | Carica papaya (Papaya) |
P05997 | CO5A2_HUMAN | MMANWAEARPLLILIVLLGQFVSIKAQEEDEDEGYGEEIACTQNGQMYLNRDIWKPAPCQICVCDNGAILCDKIECQDVLDCADPVTPPGECCPVCSQTPGGGNTNFGRGRKGQKGEPGLVPVVTGIRGRPGPAGPPGSQGPRGERGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGLSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPVGPRGPQGLQGQQGGAGPTGPPGEPGDPGPMGPIGSRGPEGPPGKPGEDGEPGRNGNPGEVGFAGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEVGAPGSK... | null | null | cellular response to amino acid stimulus [GO:0071230]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; eye morphogenesis [GO:0048592]; negative regulation of endodermal cell differentiation [GO:1903225]; notochord development [GO:0030903]; ossification [GO:0001503]; skeletal s... | collagen type II trimer [GO:0005585]; collagen type V trimer [GO:0005588]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332] | PF01410;PF01391;PF00093; | 2.60.120.1000;6.20.200.20; | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1. {ECO:0000269|PubMed:21757687, ECO:0000269|PubMed:8181482}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specifi... | Homo sapiens (Human) |
P06002 | OPS1_DROME | MESFAVAAAQLGPHFAPLSNGSVVDKVTPDMAHLISPYWNQFPAMDPIWAKILTAYMIMIGMISWCGNGVVIYIFATTKSLRTPANLLVINLAISDFGIMITNTPMMGINLYFETWVLGPMMCDIYAGLGSAFGCSSIWSMCMISLDRYQVIVKGMAGRPMTIPLALGKIAYIWFMSSIWCLAPAFGWSRYVPEGNLTSCGIDYLERDWNPRSYLIFYSIFVYYIPLFLICYSYWFIIAAVSAHEKAMREQAKKMNVKSLRSSEDAEKSAEGKLAKVALVTITLWFMAWTPYLVINCMGLFKFEGLTPLNTIWGACFAKS... | null | null | adult locomotory behavior [GO:0008344]; cellular response to light stimulus [GO:0071482]; detection of UV [GO:0009589]; detection of visible light [GO:0009584]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; optomotor respo... | cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; inaD signaling complex [GO:0016027]; rhabdomere [GO:0016028]; rhabdomere membrane [GO:0033583]; subrhabdomeral cisterna [GO:0016029] | 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: Cell projection, rhabdomere membrane {ECO:0000269|PubMed:23226104}; Multi-pass membrane protein {ECO:0000305}. Note=Upon white light stimulation, is internalized into the rhabdomere membranes. {ECO:0000269|PubMed:23226104}. | 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) |
P06003 | PSBC_SPIOL | MKTLYSLRRFYPVETLFNGTLTLAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNVTLSPSIIFGCLLKSPFGGEGWIVSVDDLEDIIGGHVWIGVICILGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVR... | null | COFACTOR: Note=Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01496}; | photosynthetic electron transport in photosystem II [GO:0009772] | chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; metal ion binding [GO:0046872] | PF00421; | 1.10.10.670; | PsbB/PsbC family, PsbC subfamily | PTM: Over time a tryptophan in the fifth lumenal loop is converted to 2-hydroxy-2,3-dihydrotryptophan, 2-oxo-2,3-dihydrotryptophan, and kynurenine by oxidizing species from the active site. This oxidation targets the protein for turnover. {ECO:0000269|PubMed:12417747}. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:3121625}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496}. | null | null | null | null | null | FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gr... | Spinacia oleracea (Spinach) |
P06006 | PSBD_PEA | MTIALGKFTKDQNDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFAVGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDLTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNI... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which... | photosynthetic electron transport in photosystem II [GO:0009772] | chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxygen evolving activity [GO:0010242] | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:9407103}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01383}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P06008 | RCEH_BLAVI | MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVYELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAERAEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYFRYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSAYYAGGLLYATPERAESLL | null | COFACTOR: Name=a bacteriochlorophyll; Xref=ChEBI:CHEBI:38201; Note=Binds 4 bacteriochlorophylls per trimer.; COFACTOR: Name=a bacteriopheophytin; Xref=ChEBI:CHEBI:60411; Note=Binds 2 bacteriopheophytins per trimer.; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe cation per trimer.; COFACTOR: Name=Mg(... | photosynthesis, light reaction [GO:0019684] | plasma membrane light-harvesting complex [GO:0030077]; plasma membrane-derived chromatophore membrane [GO:0042717] | bacteriochlorophyll binding [GO:0042314]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156] | PF05239;PF03967; | 3.90.50.10;4.10.540.10; | Reaction center PuhA family | null | SUBCELLULAR LOCATION: Cellular chromatophore membrane; Single-pass membrane protein. | null | null | null | null | null | FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | Blastochloris viridis (Rhodopseudomonas viridis) |
P06019 | REPC_BPMU | MKSNFIEKNNTEKSIWCSPQEIMAADGMPGSVAGVHYRANVQGWTKQKKEGVKGGKAVEYDVMSMPTKEREQVIAHLGLSTPDTGAQANEKQDSSELINKLTTTLINMIEELEPDEARKALKLLSKGGLLALMPLVFNEQKLYSFIGFSQQSIQTLMMLDALPEEKRKEILSKYGIHEQESVVVPSQEPQEVKKAV | null | null | latency-replication decision [GO:0098689]; viral latency [GO:0019042] | host cell cytoplasm [GO:0030430]; transcription repressor complex [GO:0017053] | DNA binding [GO:0003677] | PF02316; | 1.10.10.10; | Mulikevirus repressor c protein family | PTM: C-terminally truncated forms act as exceptionally stable repressors that prevent prophage induction. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Promotes latency by binding operators O1 and O2 in the enhancer/operator region, thereby repressing the transcription from the Pe (early) promoter and blocking the expression of the genes required for replication (lytic growth). Competes with DDE-recombinase A for binding to the internal activation sequence (... | Escherichia phage Mu (Bacteriophage Mu) |
P06022 | ACTC_BPMU | MQHDLFEHDPAIRQLIGHIDNIPAPELESRWPRSVVDLIDVLENELKRQNVSNPRELARKQAVALSCFLGGRQFYIPCGDTILTALRDDLLYCQFNGRNMEELRRQYRLSQPQIYQIIARQRKLHTRRHQPDLFSPETPK | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:19170593}; Note=Binding magnesium induces a conformational change that allows DNA-binding. {ECO:0000305|PubMed:19170593}; | null | host cell cytoplasm [GO:0030430] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF08765; | 1.10.10.60; | C/mor transcriptional regulatory family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Positive regulator of viral late genes transcription. Responsible for the transition from middle to late gene expression. Activates the Plys, PI, PP and Pmom late promoters thereby allowing the expression of viral endolysin and structural genes. Activates Pmom promoter by unwinding the DNA, thus realigning th... | Escherichia phage Mu (Bacteriophage Mu) |
P06028 | GLPB_HUMAN | MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAPVVIILIILCVMAGIIGTILLISYSIRRLIKA | null | null | null | ankyrin-1 complex [GO:0170014]; plasma membrane [GO:0005886] | null | PF01102; | 1.20.5.70; | Glycophorin-A family | PTM: The N-terminal extracellular domain is heavily glycosylated on serine and threonine residues. {ECO:0000269|PubMed:7681597}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane. {ECO:0000269|PubMed:35835865}. | Homo sapiens (Human) |
P06100 | NOT2_YEAST | MEKFGLKALVPLLKLEDKELSSTYDHSMTLGADLSSMLYSLGIPRDSQDHRVLDTFQSPWAETSRSEVEPRFFTPESFTNIPGVLQSTVTPPCFNSIQNDQQRVALFQDETLFFLFYKHPGTVIQELTYLELRKRNWRYHKTLKAWLTKDPMMEPIVSADGLSERGSYVFFDPQRWEKCQRDFLLFYNAIM | null | null | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; deadenylation-independent decapping of nuclear-transcribed mRNA [GO:0031087]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regula... | CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932] | null | PF04153; | 2.30.30.1020; | CNOT2/3/5 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889048}. Nucleus {ECO:0000269|PubMed:11889048}. | null | null | null | null | null | FUNCTION: Acts as a component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. NOT2 is required for the integrity of the complex. The NOT protein subcomplex negatively regulates the basal and activat... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06101 | CDC37_YEAST | MAIDYSKWDKIELSDDSDVEVHPNVDKKSFIKWKQQSIHEQRFKRNQDIKNLETQVDMYSHLNKRVDRILSNLPESSLTDLPAVTKFLNANFDKMEKSKGENVDPEIATYNEMVEDLFEQLAKDLDKEGKDSKSPSLIRDAILKHRAKIDSVTVEAKKKLDELYKEKNAHISSEDIHTGFDSSFMNKQKGGAKPLEATPSEALSSAAESNILNKLAKSSVPQTFIDFKDDPMKLAKETEEFGKISINEYSKSQKFLLEHLPIISEQQKDALMMKAFEYQLHGDDKMTLQVIHQSELMAYIKEIYDMKKIPYLNPMELSNV... | null | null | cell division [GO:0051301]; p38MAPK cascade [GO:0038066]; positive regulation of MAPK cascade [GO:0043410]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of cell cycle [GO:0051726]; spindle pole body duplication [GO:0030474] | cytoplasm [GO:0005737] | heat shock protein binding [GO:0031072]; protein kinase binding [GO:0019901]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF08564;PF08565;PF03234; | 1.20.58.610; | CDC37 family | PTM: Phosphorylation at Ser-14 is required for the interactions with HOG1 and SLT2 MAP kinases and is crucial for adaptation to stress conditions due to high osmolarity or cell wall perturbation. {ECO:0000269|PubMed:17220467}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall per... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06102 | NOT3_YEAST | MAHRKLQQEVDRVFKKINEGLEIFNSYYERHESCTNNPSQKDKLESDLKREVKKLQRLREQIKSWQSSPDIKDKDSLLDYRRSVEIAMEKYKAVEKASKEKAYSNISLKKSETLDPQERERRDISEYLSQMIDELERQYDSLQVEIDKLLLLNKKKKTSSTTNDEKKEQYKRFQARYRWHQQQMELALRLLANEELDPQDVKNVQDDINYFVESNQDPDFVEDETIYDGLNLQSNEAIAHEVAQYFASQNAEDNNTSDANESLQDISKLSKKEQRKLEREAKKAAKLAAKNATGAAIPVAGPSSTPSPVIPVADASKETE... | null | null | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; protein ubiquitination [GO:0016567] | CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932] | null | PF04153;PF04065; | 2.30.30.1020; | CNOT2/3/5 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus. | null | null | null | null | null | FUNCTION: Acts as a component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affe... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06103 | EIF3B_YEAST | MKNFLPRTLKNIYELYFNNISVHSIVSRNTQLKRSKIIQMTTETFEDIKLEDIPVDDIDFSDLEEQYKVTEEFNFDQYIVVNGAPVIPSAKVPVLKKALTSLFSKAGKVVNMEFPIDEATGKTKGFLFVECGSMNDAKKIIKSFHGKRLDLKHRLFLYTMKDVERYNSDDFDTEFREPDMPTFVPSSSLKSWLMDDKVRDQFVLQDDVKTSVFWNSMFNEEDSLVESRENWSTNYVRFSPKGTYLFSYHQQGVTAWGGPNFDRLRRFYHPDVRNSSVSPNEKYLVTFSTEPIIVEEDNEFSPFTKKNEGHQLCIWDIASG... | null | null | cytoplasmic translational initiation [GO:0002183]; formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413] | cytoplasmic stress granule [GO:0010494]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; multi-eIF complex [GO:0043614] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369] | PF08662;PF00076; | 3.30.70.330;2.130.10.10; | EIF-3 subunit B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06104 | UBC2_YEAST | MSTPARRRLMRDFKRMKEDAPPGVSASPLPDNVMVWNAMIIGPADTPYEDGTFRLLLEFDEEYPNKPPHVKFLSEMFHPNVYANGEICLDILQNRWTPTYDVASILTSIQSLFNDPNPASPANVEAATLFKDHKSQYVKRVKETVEKSWEDDMDDMDDDDDDDDDDDDDEAD | 2.3.2.23 | null | cytoplasm protein quality control by the ubiquitin-proteasome system [GO:0071629]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; DNA-templated transcription termination [GO:0006353]; double-strand break repair via homologous recombination [GO:0000724]; ERAD pathway [GO:0036503]; error-free postreplication... | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; HULC complex [GO:0033503]; MUB1-RAD6-UBR2 ubiquitin ligase complex [GO:1990304]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505]; RAD6-UBR2 ubiquitin ligase complex [GO:1990305]; UBR1-RAD6 ubiquitin ligase complex [GO:19903... | ATP binding [GO:0005524]; proteasome binding [GO:0070628]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}. Nucleus {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elon... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06105 | SC160_YEAST | MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKPAVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVAANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYL... | null | null | chemotropism [GO:0043577]; chromosome segregation [GO:0007059]; meiotic telomere clustering [GO:0045141]; nuclear division [GO:0000280]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; silent mating-type cassette heterochromatin formation [GO:0030466]; subtelomeric het... | chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole membrane [GO:0000329]; nuclear membrane [GO:0031965]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175]; nucleus [GO:0005634] | G-protein alpha-subunit binding [GO:0001965]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF00013; | 3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic surface of the ER-nuclear envelope membranes. | null | null | null | null | null | FUNCTION: Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER-nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06106 | CYSD_YEAST | MPSHFDTVQLHAGQENPGDNAHRSRAVPIYATTSYVFENSKHGSQLFGLEVPGYVYSRFQNPTSNVLEERIAALEGGAAALAVSSGQAAQTLAIQGLAHTGDNIVSTSYLYGGTYNQFKISFKRFGIEARFVEGDNPEEFEKVFDERTKAVYLETIGNPKYNVPDFEKIVAIAHKHGIPVVVDNTFGAGGYFCQPIKYGADIVTHSATKWIGGHGTTIGGIIVDSGKFPWKDYPEKFPQFSQPAEGYHGTIYNEAYGNLAYIVHVRTELLRDLGPLMNPFASFLLLQGVETLSLRAERHGENALKLAKWLEQSPYVSWVS... | 2.5.1.47; 2.5.1.49 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:7765825, ECO:0000269|PubMed:795806}; | cysteine biosynthetic process [GO:0019344]; cysteine biosynthetic process from serine [GO:0006535]; L-homocysteine biosynthetic process [GO:0071269]; methionine metabolic process [GO:0006555]; sulfate assimilation [GO:0000103]; transsulfuration [GO:0019346] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | cysteine synthase activity [GO:0004124]; O-acetylhomoserine aminocarboxypropyltransferase activity [GO:0003961]; O-acetylhomoserine sulfhydrylase activity [GO:0051009]; pyridoxal phosphate binding [GO:0030170] | PF01053; | 3.90.1150.10;3.40.640.10; | Trans-sulfuration enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}. | CATALYTIC ACTIVITY: Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307, ECO:0000269|PubMed:776582... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.7 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:7765825}; KM=6.67 mM for O-acetyl-L-homoserine (at pH 7.8 in Tris-HCl buffer) {ECO:0000269|PubMed:4609980}; KM=5.12 mM for O-acetyl-L-serine (at pH 7.8 in potassium phosphate buffer) {ECO:0000269|PubMed:4609980};... | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine. {ECO:0000305|PubMed:12586406, ECO:0000305|PubMed:1732168}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 (for O-acetylhomoserine sulfhydrylase activity in Tris-HCl buffer) and 8.4 (for both O-acetylhomoserine sulfhydrylase and O-acetylserine sulfhydrylase activities in barbital-HCl buffer). {ECO:0000269|PubMed:4609980, ECO:0000269|PubMed:4947307}; | null | FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:36379252, PubMed:36455053, PubMed:4609980, PubMed:7765825, PubMed:795806). Required to efficiently reduce toxic levels of hydrogen sulfide generated when the sulfate assimilation pathway (S... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06115 | CATT_YEAST | MNVFGKKEEKQEKVYSLQNGFPYSHHPYASQYSRPDGPILLQDFHLLENIASFDRERVPERVVHAKGGGCRLEFELTDSLSDITYAAPYQNVGYKCPGLVRFSTVGGESGTPDTARDPRGVSFKFYTEWGNHDWVFNNTPVFFLRDAIKFPVFIHSQKRDPQSHLNQFQDTTIYWDYLTLNPESIHQITYMFGDRGTPASWASMNAYSGHSFIMVNKEGKDTYVQFHVLSDTGFETLTGDKAAELSGSHPDYNQAKLFTQLQNGEKPKFNCYVQTMTPEQATKFRYSVNDLTKIWPHKEFPLRKFGTITLTENVDNYFQE... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | hydrogen peroxide catabolic process [GO:0042744]; response to hydrogen peroxide [GO:0042542]; response to reactive oxygen species [GO:0000302] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06126 | CD1A_HUMAN | MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSNSSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCELHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLSDTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSVGFIILAVIVPLLLLIGLALW... | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723] | PF07654;PF16497; | 2.60.40.10;3.30.500.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:11600221, ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:11231314};... | null | null | null | null | null | FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:16272286, ECO:0000269|PubMed:18178838}. | Homo sapiens (Human) |
P06127 | CD5_HUMAN | MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQ... | null | null | apoptotic signaling pathway [GO:0097190]; cell recognition [GO:0008037]; T cell costimulation [GO:0031295] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023] | PF00530; | 3.10.250.10; | null | PTM: Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: May act as a receptor in regulating T-cell proliferation. | Homo sapiens (Human) |
P06129 | BTUB_ECOLI | MIKKASLLTACSVTAFSAWAQDTSPDTLVVTANRFEQPRSTVLAPTTVVTRQDIDRWQSTSVNDVLRRLPGVDITQNGGSGQLSSIFIRGTNASHVLVLIDGVRLNLAGVSGSADLSQFPIALVQRVEYIRGPRSAVYGSDAIGGVVNIITTRDEPGTEISAGWGSNSYQNYDVSTQQQLGDKTRVTLLGDYAHTHGYDVVAYGNTGTQAQTDNDGFLSKTLYGALEHNFTDAWSGFVRGYGYDNRTNYDAYYSPGSPLLDTRKLYSQSWDAGLRYNGELIKSQLITSYSHSKDYNYDPHYGRYDSSATLDEMKQYTVQW... | null | null | cobalamin transport [GO:0015889]; monoatomic ion transmembrane transport [GO:0034220] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; pore complex [GO:0046930]; transmembrane transporter complex [GO:1902495] | ABC-type vitamin B12 transporter activity [GO:0015420]; calcium ion binding [GO:0005509]; porin activity [GO:0015288]; protein domain specific binding [GO:0019904]; siderophore uptake transmembrane transporter activity [GO:0015344] | PF07715;PF00593; | 2.40.170.20;2.170.130.10; | TonB-dependent receptor family, BtuB (TC 1.B.14.3.1) subfamily | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:12595710, ECO:0000269|PubMed:12652322, ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:12595710, ECO:0000269|PubMed:12652322, ECO:00002... | null | null | null | null | null | FUNCTION: Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space (PubMed:4579869). It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. {ECO:0000255|HAMAP-Rule:MF_01531, ECO:0000269|PubMed:10485884, ECO:0000... | Escherichia coli (strain K12) |
P06132 | DCUP_HUMAN | MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQL... | 4.1.1.37 | null | heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; porphyrin-containing compound catabolic process [GO:0006787]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynth... | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | uroporphyrinogen decarboxylase activity [GO:0004853] | PF01208; | 3.20.20.210; | Uroporphyrinogen decarboxylase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37; Evidence={ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:18004775, ECO:0000269|PubMed:... | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. {ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11719352, ECO:0000269|PubMed:14633982, ECO:0000269|PubMed:21668429}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:18004775}; | null | FUNCTION: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway (PubMed:11069625, PubMed:11719352, PubMed:14633982, PubMed:18004775, PubMed:21668429). Isomer I or isomer III of uroporphy... | Homo sapiens (Human) |
P06133 | UD2B4_HUMAN | MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSASISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFNDILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAIEKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVLGRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNTSEER... | 2.4.1.17 | null | cellular glucuronidation [GO:0052695]; estrogen metabolic process [GO:0008210] | endoplasmic reticulum membrane [GO:0005789] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8333863}; 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:18719240, ECO:0000269|PubMed:23288867... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.77 uM for 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; KM=57.8 uM for calcitriol (when assaying glucuronidation at position 25) {ECO:0000269|PubMed:18177842}; Vmax=135 pmol/min/mg enzyme for the form... | 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, PubMed:23288867). Essential for... | Homo sapiens (Human) |
P06134 | ADA_ECOLI | MKKATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVSFYANASEALAAGFRPCKRCQPEKANAQQHRLDKITHACRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLRESLAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQFRHGGENLAVRYALADCELGRCLVAESERGICAILLGDDDATLISELQQMFPAADNAPADLMFQQHVREVIASLNQRDTPLTLPLDIRGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIIIP... | 2.1.1.63; 2.1.1.n11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | DNA damage response [GO:0006974]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA demethylation [GO:0080111]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893] | null | DNA-binding transcription factor activity [GO:0003700]; methylated-DNA-[protein]-cysteine S-methyltransferase activity [GO:0003908]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF02805;PF01035;PF12833;PF02870; | 3.40.10.10;1.10.10.60;3.30.160.70;1.10.10.10; | MGMT family | null | null | CATALYTIC ACTIVITY: Reaction=(2'-deoxyribonucleoside 5'-methylphosphotriester)-DNA + L-cysteinyl-[protein] = 2'-deoxyribonucleotide-DNA + H(+) + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56324, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:14462, Rhea:RHEA-COMP:14463, ChEBI:CHEBI:15378, ChEBI:CHEBI:29... | null | null | null | null | FUNCTION: Involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme (Cys-321). Also sp... | Escherichia coli (strain K12) |
P06136 | FTSQ_ECOLI | MSQAALNTRNSEEEVSSRRNNGTRLAGILFLLTVLTTVLVSGWVVLGWMEDAQRLPLSKLVLTGERHYTRNDDIRQSILALGEPGTFMTQDVNIIQTQIEQRLPWIKQVSVRKQWPDELKIHLVEYVPIARWNDQHMVDAEGNTFSVPPERTSKQVLPMLYGPEGSANEVLQGYREMGQMLAKDRFTLKEAAMTARRSWQLTLNNDIKLNLGRGDTMKRLARFVELYPVLQQQAQTDGKRISYVDLRYDSGAAVGWAPLPPEESTQQQNQAQAEQQ | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093] | cell division site [GO:0032153]; divisome complex [GO:1990586]; FtsQBL complex [GO:1990587]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802] | PF03799;PF08478; | 3.40.50.11690;3.10.20.310; | FtsQ/DivIB family, FtsQ subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520, ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918, ECO:0000269|PubMed:9882666}; Single-pass ty... | null | null | null | null | null | FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly. {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:17185541, EC... | Escherichia coli (strain K12) |
P06140 | HA1B_RABIT | MGSIPPRTLLLLLAGALTLKDTQAGSHSMRYFYTSVSRPGLGEPRFIIVGYVDDTQFVRFDSDAASPRMEQRAPWMGQVEPEYWDQQTQIAKDTAQTFRVNLNTALRYYNQSAAGSHTFQTMFGCEVWADGRFFHGYRQYAYDGADYIALNEDLRSWTAADTAAQNTQRKWEAAGEAERHRAYLERECVEWLRRYLEMGKETLQRADPPKAHVTHHPASDREATLRCWALGFYPAEISLTWQRDGEDQTQDTELVETRPGGDGTFQKWAAVVVPSGEEQRYTCRVQHEGLPEPLTLTWEPPAQPTALIVGIVAGVLGVLL... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Oryctolagus cuniculus (Rabbit) |
P06149 | DLD_ECOLI | MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEK... | 1.1.5.12 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233}; | aerobic respiration [GO:0009060]; anaerobic respiration [GO:0009061]; lactate oxidation [GO:0019516]; respiratory electron transport chain [GO:0022904]; transmembrane transport [GO:0055085] | cytoplasmic side of plasma membrane [GO:0009898]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; plasma membrane [GO:0005886] | D-lactate dehydrogenase (quinone) activity [GO:0102029]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor [GO:0016901]; quinone binding [GO:0048038] | PF01565;PF09330; | 3.30.465.10;3.30.70.610;3.30.1370.20;3.30.43.10; | Quinone-dependent D-lactate dehydrogenase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMe... | CATALYTIC ACTIVITY: Reaction=(R)-lactate + a quinone = a quinol + pyruvate; Xref=Rhea:RHEA:51468, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.12; Evidence={ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:7578233}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for D-lactate {ECO:0000269|PubMed:2185834}; | null | null | null | FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. {ECO:0000269|PubMed:2... | Escherichia coli (strain K12) |
P06150 | LDH_THECA | MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATPFAHPVWVRAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVVPRVLEAAPEAVLLVATNPVDVMTQVAYRLSALPPGRVVGSGTILDTARFRALLAEHLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRALSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVYTVSAFTPEVEGVLEVSLSLPRILGAGGVEGTVYPSLSPEEREALRRSAEILKEAAFALGF | 1.1.1.27 | null | glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089] | cytoplasm [GO:0005737] | L-lactate dehydrogenase activity [GO:0004459] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}. | CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:25258319, ECO:0000269|PubMed:3377774, ECO:0000269|Re... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.02 mM for pyruvate (in the presence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:3377774}; KM=0.03 mM for NADH (in the presence and in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:3377774}; KM=0.04 mM for pyruvate (in the presenc... | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}. | null | null | FUNCTION: Catalyzes the conversion of lactate to pyruvate. {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:25258319, ECO:0000269|PubMed:3377774, ECO:0000269|PubMed:6499843, ECO:0000269|Ref.4, ECO:0000305|PubMed:3533539}. | Thermus caldophilus |
P06151 | LDHA_MOUSE | MATLKDQLIVNLLKEEQAPQNKITVVGVGAVGMACAISILMKDLADELALVDVMEDKLKGEMMDLQHGSLFLKTPKIVSSKDYCVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPHCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWVLGEHGDSSVPVWSGVNVAGVSLKSLNPELGTDADKEQWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGINEDVFLSVPCILGQNGISDVVKVTLTPEEEARLKKSA... | 1.1.1.27 | null | cellular response to extracellular stimulus [GO:0031668]; glucose catabolic process to lactate via pyruvate [GO:0019661]; lactate biosynthetic process from pyruvate [GO:0019244]; lactate metabolic process [GO:0006089]; liver development [GO:0001889]; NAD metabolic process [GO:0019674]; positive regulation of apoptotic ... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; sperm fibrous sheath [GO:0035686] | identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; lactate dehydrogenase activity [GO:0004457]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000250|UniProtKB:P00338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; Evidence={ECO... | null | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}. | null | null | FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000250|UniProtKB:P00338}. | Mus musculus (Mouse) |
P06159 | NCAP_PI3H4 | MLSLFDTFNARRQENITKSAGGAIIPGQKNTVSIFALGPTITDDNEKMTLALLFLSHSLDNEKQHAQRAGFLVSLLSMAYANPELYLTTNGSNADVKYVIYMIEKDLKRQKYGGFVVKTREMIYEKTTEWIFGSDLDYDQETMLQNGRNNSTIEDLVHTFGYPSCLGALIIQIWIVLVKAITSISGLRKGFFTRLEAFRQDGTVQAGLVLSGDTVDQIGSIMRSQQSLVTLMVETLITMNTSRNDLTTIEKNIQIVGNYIRDAGLASFFNTIRYGIETRMAALTLSTLRPDINRLKALMELYLSKGPRAPFICILRDPIH... | null | null | null | helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF00973; | null | Paramyxoviruses nucleocapsid family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm. | null | null | null | null | null | FUNCTION: Forms the helical nucleocapsid (NC) in a ratio of 1 N per 6 ribonucleotides, protecting the genome from nucleases (Probable). The encapsidated genomic RNA serves as template for transcription and replication; encapsidation by N is coupled to RNA synthesis (PubMed:10846069). Forms the encapsidation complex wit... | Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human parainfluenza 3 virus (strain NIH 47885)) |
P06168 | ILV5_YEAST | MLRTQAARLICNSRVITAKRTFALATRAAAYSRPAARFVKPMITTRGLKQINFGGTVETVYERADWPREKLLDYFKNDTFALIGYGSQGYGQGLNLRDNGLNVIIGVRKDGASWKAAIEDGWVPGKNLFTVEDAIKRGSYVMNLLSDAAQSETWPAIKPLLTKGKTLYFSHGFSPVFKDLTHVEPPKDLDVILVAPKGSGRTVRSLFKEGRGINSSYAVWNDVTGKAHEKAQALAVAIGSGYVYQTTFEREVNSDLYGERGCLMGGIHGMFLAQYDVLRENGHSPSEAFNETVEEATQSLYPLIGKYGMDYMYDACSTTA... | 1.1.1.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; mitochondrial genome maintenance [GO:0000002]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739] | double-stranded DNA binding [GO:0003690]; ketol-acid reductoisomerase activity [GO:0004455]; metal ion binding [GO:0046872] | PF01450;PF07991; | 3.40.50.720; | Ketol-acid reductoisomerase family | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000305|PubMed:3027658}; PhysiologicalDirection=right-to-left;... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000305|PubMed:3027658}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000305|PubMed:3027658}. | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes the second common step in the parallel biosynthesis of isoleucine and valine. Converts alpha-aceto-alpha-hydroxybutyrate (AHB) to alpha,beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-acetolactate (AL) to alpha,beta-dihydroxy-iso... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06169 | PDC1_YEAST | MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNAT... | 4.1.1.-; 4.1.1.43; 4.1.1.72; 4.1.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10651824}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:10651824}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:10651824}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000269|PubMed... | aromatic amino acid family catabolic process to alcohol via Ehrlich pathway [GO:0000949]; branched-chain amino acid catabolic process [GO:0009083]; glycolytic fermentation to ethanol [GO:0019655]; L-phenylalanine catabolic process [GO:0006559]; pyruvate metabolic process [GO:0006090]; tryptophan catabolic process [GO:0... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | branched-chain-2-oxoacid decarboxylase activity [GO:0047433]; indolepyruvate decarboxylase activity [GO:0047434]; magnesium ion binding [GO:0000287]; phenylpyruvate decarboxylase activity [GO:0050177]; pyruvate decarboxylase activity [GO:0004737]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | PTM: Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1. {ECO:0000269|PubMed:10545125, ECO:0000269|PubMed:9298649}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; Evidence={ECO:0000269|PubMed:4687392}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2; Xref=Rhea:RHEA:54356, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 mM for pyruvate {ECO:0000269|PubMed:22904058}; KM=1 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058}; KM=1.5 mM for 2-oxopentanoate {ECO:0000269|PubMed:22904058}; Vmax=1.5 umol/min/mg enzyme for pyruvate {ECO:0000269|PubMed:22904058}; Vmax=0.5 umol/min/mg en... | PATHWAY: Fermentation; ethanol fermentation.; PATHWAY: Amino-acid degradation; Ehrlich pathway. | null | null | FUNCTION: Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for b... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06181 | LIG8_PHACH | MAFKQLFAAISLALLLSAANAAAVIEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFVQKHGVTPGDFIAFAGRVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHTVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSRTACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQS... | 1.11.1.14 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:16593451}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:16593451}; | cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lignin catabolic process [GO:0046274]; response to reactive oxygen species [GO:0000302] | null | diarylpropane peroxidase activity [GO:0016690]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141;PF11895; | 1.10.520.10;1.10.420.10; | Peroxidase family, Ligninase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O; Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591, ChEBI:CHEBI:86963; EC=1.11.1.14; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for H(2)O(2) {ECO:0000269|PubMed:2303054}; KM=116 uM for (3,4-dimethoxyphenyl)methanol {ECO:0000269|PubMed:3240864}; KM=30 uM for H(2)O(2) {ECO:0000269|PubMed:16593451}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3. {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054}; | null | FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054}. | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
P06186 | PRGR_RABIT | MTELKAKEPRAPHVAGGAPSPTEVGSQLLGRPDPGPFQGSQTSEASSVVSAIPISLDGLLFPRPCQGQNPPDGKTQDPPSLSDVEGAFPGVEAPEGAGDSSSRPPEKDSGLLDSVLDTLLAPSGPGQSHASPATCEAISPWCLFGPDLPEDPRAAPATKGVLAPLMSRPEDKAGDSSGTAAAHKVLPRGLSPSRQLLLPSSGSPHWPAVKPSPQPAAVQVDEEDSSESEGTVGPLLKGQPRALGGTAAGGGAAPVASGAAAGGVALVPKEDSRFSAPRVSLAEQDAPVAPGRSPLATSVVDFIHVPILPLNHAFLATRTR... | null | null | glandular epithelial cell maturation [GO:0002071]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:0042326]; ovulation from ovarian follicle [GO:0001542]; paracrine signaling ... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATPase binding [GO:0051117]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; estrogen response element binding [GO:0034056]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]... | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-293 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-387. Phosphorylation on Ser-102 and Ser-344 also requires induction by hormone. Basal phosphorylation on Ser-82, Ser-191 ... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependen... | Oryctolagus cuniculus (Rabbit) |
P06191 | ALR2_SALTY | MTRPIQASLDLQVMKQNLAIVRRAAPEARVWSVVKANAYGHGIERVWSALGATDGFAMLNLEEAITLRERGWKGPILMLEGFFHAQDLEAYDTYRLTTCIHSNWQLKALQNARLNAPLDIYVKVNSGMNRLGFQPERAQTVWQQLRAMRNVGEMTLMSHFAQADHPEGIGEAMRRIALATEGLQCAYSLSNSAATLWHPQAHYDWVRPGIILYGASPSGQWRDIADTGLKPVMTLSSEIIGVQTLSAGERVGYGGGYSVTQEQRIGIVAAGYADGYPRHAPTGTPVLVDGIRTRTVGTVSMDMLAVDLTPCPQAGIGTPV... | 5.1.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6391537, ECO:0000269|PubMed:6439236}; | D-alanine biosynthetic process [GO:0030632]; peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829] | alanine racemase activity [GO:0008784]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family | null | null | CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000269|PubMed:6391537}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for D-alanine {ECO:0000269|PubMed:6391537}; KM=8.2 mM for L-alanine {ECO:0000269|PubMed:6391537}; | null | null | null | FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. {ECO:0000269|PubMed:6391537}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P06197 | PIS_YEAST | MSSNSTPEKVTAEHVLWYIPNKIGYVRVITAALSFFVMKNHPTAFTWLYSTSCLLDALDGTMARKYNQVSSLGAVLDMVTDRSSTAGLMCFLCVQYPQWCVFFQLMLGLDITSHYMHMYASLSAGKTSHKSVGEGESRLLHLYYTRRDVLFTICAFNELFYAGLYLQLFSNSATFGKWTTIISFPGYVFKQTANVVQLKRAALILADNDAKNANEKNKTY | 2.7.8.11 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q59RA2}; Note=Divalent metal cations; Mn(2+) or Mg(2+). {ECO:0000250|UniProtKB:Q59RA2}; | phosphatidylinositol biosynthetic process [GO:0006661] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity [GO:0003881]; metal ion binding [GO:0046872] | PF01066; | 1.20.120.1760; | CDP-alcohol phosphatidyltransferase class-I family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25687304}; Multi-pass membrane protein {ECO:0000305|PubMed:25687304}. Mitochondrion outer membrane {ECO:0000269|PubMed:16823961}; Multi-pass membrane protein {ECO:0000269|PubMed:16823961}. | CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; Evidence={ECO:0000305|PubMed:25687304}; | null | null | null | null | FUNCTION: Catalyzes the synthesis of phosphatidylinositol (PtdIns). {ECO:0000269|PubMed:25687304}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06199 | ACM2_PIG | MNNSTNSSNSGLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQEPVSPSLVQGRIVKPNNNNMPGSDEALEHNKIQNGKAPRDAVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENS... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM2 sub-subfamily | PTM: Phosphorylated in response to agonist treatment. {ECO:0000269|PubMed:9228066}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20976005, ECO:0000305|PubMed:3107123, ECO:0000305|PubMed:9228066}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Phosphorylation in response to agonist binding promotes receptor... | 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 adenylate cyclase inhibition. {ECO:0000269|PubMed:9228066}. | Sus scrofa (Pig) |
P06202 | OPPA_SALTY | MSNITKKSLIAAGILTALIAASAATAADVPAGVQLADKQTLVRNNGSEVQSLDPHKIEGVPESNVSRDLFEGLLISDVEGHPSPGVAEKWENKDFKVWTFHLRENAKWSDGTPVTAHDFVYSWQRLADPNTASPYASYLQYGHIANIDDIIAGKKPATDLGVKALDDHTFEVTLSEPVPYFYKLLVHPSVSPVPKSAVEKFGDKWTQPANIVTNGAYKLKNWVVNERIVLERNPQYWDNAKTVINQVTYLPISSEVTDVNRYRSGEIDMTYNNMPIELFQKLKKEIPNEVRVDPYLCTYYYEINNQKAPFNDVRVRTALK... | null | null | peptide transport [GO:0015833]; protein transport [GO:0015031] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; outer membrane-bounded periplasmic space [GO:0030288] | peptide transmembrane transporter activity [GO:1904680] | PF00496; | 3.40.190.10; | Bacterial solute-binding protein 5 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2821267, ECO:0000269|PubMed:3525163}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex OppABCDF involved in the uptake of oligopeptides, including the cell wall murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate (PubMed:2821267, PubMed:3301822). Plays an important nutritional role and is involved in the recycling of cell wall peptides (PubMed:28... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P06208 | LEU1_YEAST | MVKESIIALAEHAASRASRVIPPVKLAYKNMLKDPSSKYKPFNAPKLSNRKWPDNRITRAPRWLSTDLRDGNQSLPDPMSVEQKKEYFHKLVNIGFKEIEVSFPSASQTDFDFTRYAVENAPDDVSIQCLVQSREHLIKRTVEALTGAKKATIHTYLATSDMFREIVFNMSREEAISKAVEATKLVRKLTKDDPSQQATRWSYEFSPECFSDTPGEFAVEICEAVKKAWEPTEENPIIFNLPATVEVASPNVYADQIEYFATHITEREKVCISTHCHNDRGCGVAATELGMLAGADRVEGCLFGNGERTGNVDLVTVAMN... | 2.3.3.13 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P9WQB3, ECO:0000250|UniProtKB:Q9JZG1}; | amino acid biosynthetic process [GO:0008652]; leucine biosynthetic process [GO:0009098] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | 2-isopropylmalate synthase activity [GO:0003852]; metal ion binding [GO:0046872] | PF00682;PF08502; | 3.30.160.270;3.20.20.70; | Alpha-IPM synthase/homocitrate synthase family, LeuA type 2 subfamily | null | SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:3275644}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:3275644}. | CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; Evidence={ECO:0000269|PubMed:3275644}; PhysiologicalDirection... | null | PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000305|PubMed:3275644}. | null | null | FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000269|PubMed:10790691, ECO:0000269|PubMed:3275644}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P06209 | POLG_POL32 | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYKDSASNAASKQDYSQDPSKFTEPLKDVLIKTAPALNSPNVEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATSRFYTLDTVMWGKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGSLGVFAIPEFCLAGDSDTQRYTSYANANPGEKGGKFYAQFNKDTAVTSPKREFCPVDYLLGCGVLIGNAFVFPHQIINLRTNNSATLVLPYVNALSIDSMVKHNNWGIAILPLSPLDFAQDSSVEIPITVT... | 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]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; suppression by virus of host mRNA export from nucleus [GO:0... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;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... | Poliovirus type 3 (strain 23127) |
P06210 | POLG_POL2L | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFAQDPSKFTEPIKDVLIKTAPTLNSPNIEACGYSDRVMQLTLGNSTITTQEAANSVVAYGRWPEYIKDSEANPVDQPTEPDVAACRFYTLDTVTWRKESRGWWWKLPDALKDMGLFGQNMFYHYLGRAGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSTTHMFTKYENANPGEKGGEFKGSFTLDTNATNPARNFCPVDYLFGSGVLAGNAFVYPHQIINLRTNNCATLVLPYVNSLSIDSMTKHNNWGIAILPLAPLDFATESSTEIPITLT... | 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]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; suppression by virus of host mRNA export from nucleus [GO:0... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;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... | Poliovirus type 2 (strain Lansing) |
P06211 | ESR1_RAT | MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPAVFNYPEGAAYEFNAAAAAAAAGASAPVYGQSSITYGPGSEAAAFGANSLGAFPQLNSVSPSPLMLLHPPPHVSPFLHPHGHQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSSEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGTSGDMRAANLWPSPLVIKHTKKNSPALSLTADQM... | null | null | androgen metabolic process [GO:0008209]; antral ovarian follicle growth [GO:0001547]; baculum development [GO:1990375]; cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; cellular response to wortmannin [GO:1904568]; decidualization [GO:0046697]; epithelial cell d... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; T-tubule [GO:0030315]; terminal bouton [GO:0043195];... | 14-3-3 protein binding [GO:0071889]; ATPase binding [GO:0051117]; beta-catenin binding [GO:0008013]; calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; estrogen res... | PF12743;PF00104;PF02159;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-123 by PPP5C inhibits its transactivation activity (By similarity). Phosphorylated by LMTK3 (in vitro) (By similarity). {ECO:0000250|UniProtKB:P03372}.; PTM: Ubiquitinated; regulated by LAT... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated. {E... | null | null | null | null | null | FUNCTION: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... | Rattus norvegicus (Rat) |
P06212 | ESR1_CHICK | MTMTLHTKASGVTLLHQIQGTELETLSRPQLKIPLERSLSDMYVESNKTGVFNYPEGATYDFGTTAPVYGSTTLSYAPTSESFGSSSLAGFHSLNNVPPSPVVFLQTAPQLSPFIHHHSQQVPYYLENEQGSFGMREAAPPAFYRPSSDNRRHSIRERMSSTNEKGSLSMESTKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGEMMKQKRQREEQDSRNGEASSTELRAPTLWTSPLVVKHNKKNSPALSLTAEQMVSALLEAEPPI... | null | null | cellular response to estrogen stimulus [GO:0071391]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of gene expression [GO:0010628]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | estrogen response element binding [GO:0034056]; Hsp90 protein binding [GO:0051879]; nuclear estrogen receptor activity [GO:0030284]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270] | PF12743;PF00104;PF02159;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. | Gallus gallus (Chicken) |
P06213 | INSR_HUMAN | MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYT... | 2.7.10.1 | null | activation of protein kinase activity [GO:0032147]; activation of protein kinase B activity [GO:0032148]; adrenal gland development [GO:0030325]; amyloid-beta clearance [GO:0097242]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; dendritic spine maintenance... | axon [GO:0030424]; caveola [GO:0005901]; dendrite membrane [GO:0032590]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; insulin receptor complex [GO:0005899]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body ... | amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; cargo receptor activity [GO:0038024]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding... | PF00041;PF00757;PF17870;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. {ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1934... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15208}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000250|UniProtKB:P15208}. Lysosome {ECO:0000250|UniProtKB:P15208}. Note=Binding of insulin to INSR induces internalization and lysosomal degradation of the receptor, a means for dow... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as ... | Homo sapiens (Human) |
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