Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P16387 | ODPA_YEAST | MLAASFKRQPSQLVRGLGAVLRTPTRIGHVRTMATLKTTDKKAPEDIEGSDTVQIELPESSFESYMLEPPDLSYETSKATLLQMYKDMVIIRRMEMACDALYKAKKIRGFCHLSVGQEAIAVGIENAITKLDSIITSYRCHGFTFMRGASVKAVLAELMGRRAGVSYGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKNEDACSFTLYGDGASNQGQVFESFNMAKLWNLPVVFCCENNKYGMGTAASRSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWCLSGKGPLVLEYETYRYGGHSMSDPGTT... | 1.2.4.1 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; pseudohyphal growth [GO:0007124] | mitochondrial nucleoid [GO:0042645]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739] | pyruvate dehydrogenase (acetyl-transferring) activity [GO:0004739] | PF00676; | 3.40.50.970; | null | PTM: Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6. {ECO:0000269|PubMed:18180296}. | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16388 | KCNA1_MOUSE | MTVMSGENADEASTAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTIHRIDNTTVIYTSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLK... | null | null | axon development [GO:0061564]; brain development [GO:0007420]; cell communication by electrical coupling [GO:0010644]; cellular response to magnesium ion [GO:0071286]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; detection of mechanical stimulus involved in sensory perception of p... | anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; calyx of Held [GO:0044305]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; endopl... | delayed rectifier potassium channel activity [GO:0005251]; disordered domain specific binding [GO:0097718]; voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1905030]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane p... | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.1/KCNA1 sub-subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P10499}.; PTM: Palmitoylated on Cys-243; which may be required for membrane targeting. {ECO:0000250|UniProtKB:Q09470}.; PTM: Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (PubMed:22158511). Phosphorylation a... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:7517498}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:20392939, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:26269648, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541, ECO:0000269|PubM... | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:7517498, ECO:0000269|PubMed:9736643}; | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:10... | Mus musculus (Mouse) |
P16389 | KCNA2_HUMAN | MTVATGDPADEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGSGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQT... | null | null | cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; neuronal action potential [GO:0019228]; optic nerve structural organization [GO:0021633]; potassium ion export across plasma membrane [GO:0097623]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]... | axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; calyx of Held [GO:0044305]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; juxtaparanode region of axon [GO:0044224]; lamellipodium [GO:0030027]; lamellipodium membrane [GO:0031258]... | delayed rectifier potassium channel activity [GO:0005251]; kinesin binding [GO:0019894]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1905030]; voltage-gated... | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.2/KCNA2 sub-subfamily | PTM: Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (By similarity). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on tyrosine residues suppresses ion channel activity (By similarity). Phosphorylated on tyrosine residues in response ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11211111, ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:20220134, ECO:0000269|PubMed:23769686, ECO:0000269|PubMed:8495559}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P63142, ECO:0000305}. Membrane {ECO:0000250|UniProtKB:P63142}. Cell projection, axon {E... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels activate rapidly, i.e within a few msec, but inactivation is very slow, with only a marginal decrease in conductance over several seconds. The voltage-dependence of activation and inactivation and other channel characteristics vary dependi... | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective ch... | Homo sapiens (Human) |
P16390 | KCNA3_MOUSE | MTVVPGDHLLEPEAAGGGGGDPPQGGCGSGGGGGGCDRYEPLPPALPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASPSQDVFEAANNSTSGAPSGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIR... | null | null | corpus callosum development [GO:0022038]; optic nerve development [GO:0021554]; potassium ion transmembrane transport [GO:0071805]; protein homooligomerization [GO:0051260] | axon [GO:0030424]; calyx of Held [GO:0044305]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.3/KCNA3 sub-subfamily | PTM: N-glycosylation promotes the cell surface expression. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gr... | Mus musculus (Mouse) |
P16391 | HA12_RAT | MEAMAPRTLLLLLAAALAPTQTRAGSHSLRYFYTAVSRPGLGEPRFIAVGYVDDTEFVRFDSDAENPRMEPRARWMEREGPEYWEQQTRIAKEWEQIYRVDLRTLRGYYNQSEGGSHTIQEMYGCDVGSDGSLLRGYRQDAYDGRDYIALNEDLKTWTAADFAAQITRNKWERARYAERLRAYLEGTCVEWLSRYLELGKETLLRSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVEHEGLPKPLSQRWEPSPSTDSNMETTVIYVILGAV... | 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. | Rattus norvegicus (Rat) |
P16395 | ACM1_DROME | MEPVMSLALAAHGPPSILEPLFKTVTTSTTTTTTTTTSTTTTTASPAGYSPGYPGTTLLTALFENLTSTAASGLYDPYSGMYGNQTNGTIGFETKGPRYSLASMVVMGFVAAILSTVTVAGNVMVMISFKIDKQLQTISNYFLFSLAIADFAIGAISMPLFAVTTILGYWPLGPIVCDTWLALDYLASNASVLNLLIISFDRYFSVTRPLTYRAKRTTNRAAVMIGAAWGISLLLWPPWIYSWPYIEGKRTVPKDECYIQFIETNQYITFGTALAAFYFPVTIMCFLYWRIWRETKKRQKDLPNLQAGKKDSSKRSNSSD... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; cellular response to organonitrogen compound [GO:0071417]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling path... | dendrite [GO:0030425]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled amine receptor activity [GO:0008227]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. May have a role in the processing of olfactory ... | Drosophila melanogaster (Fruit fly) |
P16396 | SUBE_BACSU | MKNMSCKLVVSVTLFFSFLTIGPLAHAQNSSEKEVIVVYKNKAGKETILDSDADVEQQYKHLPAVAVTADQETVKELKQDPDILYVENNVSFTAADSTDFKVLSDGTDTSDNFEQWNLEPIQVKQAWKAGLTGKNIKIAVIDSGISPHDDLSIAGGYSAVSYTSSYKDDNGHGTHVAGIIGAKHNGYGIDGIAPEAQIYAVKALDQNGSGDLQSLLQGIDWSIANRMDIVNMSLGTTSDSKILHDAVNKAYEQGVLLVAASGNDGNGKPVNYPAAYSSVVAVSATNEKNQLASFSTTGDEVEFSAPGTNITSTYLNQYYA... | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252] | PF00082; | 3.30.70.80;3.40.50.200;1.10.10.1270; | Peptidase S8 family | PTM: May undergo two steps of processing in its passage through the cell membrane: removal of the N-terminal signal sequence and cleavage of the C-terminal domain (PubMed:16553828). Several active forms of Epr with molecular masses between 40 and 34 kDa were found in the medium of B.subtilis cultures (PubMed:2116590). ... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16553828, ECO:0000269|PubMed:2116590, ECO:0000269|PubMed:3142851}. Secreted, cell wall {ECO:0000269|PubMed:17666034}. Note=Secretion is crucial for the swarming motility. {ECO:0000269|PubMed:16553828}. | null | null | null | null | null | FUNCTION: Serine protease (PubMed:17666034, PubMed:2116590, PubMed:3142851). Involved in the production of the competence and sporulation stimulating factor CSF (PubMed:17666034). In addition, is essential for swarming motility (PubMed:11751842, PubMed:16553828, PubMed:19416356). Plays a key role in DegU-mediated swarm... | Bacillus subtilis (strain 168) |
P16401 | H15_HUMAN | MSETAPAETATPAPVEKSPAKKKATKKAAGAGAAKRKATGPPVSELITKAVAASKERNGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGATPKKAKKAAGAKKAVKKTPKKAKKPAAAGVKKVAKSPKKAKAAAKPKKATKSPAKPKAVKPKAAKPKAAKPKAAKPKAAKAKKAAAKKK | null | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; establishment of protein localization to chromatin [GO:0071169]; muscle organ development [GO:0007517]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome ass... | chromatin [GO:0000785]; chromosome [GO:0005694]; heterochromatin [GO:0000792]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter (By similarity). Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase. {ECO:0000250, EC... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621}. Chromosome. Note=Mainly localizes with heterochromatin (PubMed:15911621). Associates with actively transcribed chromatin and not heterochromatin (PubMed:10997781). {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621}. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Homo sapiens (Human) |
P16402 | H13_HUMAN | MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK | null | null | chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334] | chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and ... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Homo sapiens (Human) |
P16403 | H12_HUMAN | MSETAPAAPAAAPPAEKAPVKKKAAKKAGGTPRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKVKKAGGTKPKKPVGAAKKPKKAAGGATPKKSAKKTPKKAKKPAAATVTKKVAKSPKKAKVAKPKKAAKSAAKAVKPKAAKPKVVKPKKAAPKKK | null | null | chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334] | euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P15864}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Homo sapiens (Human) |
P16406 | AMPE_MOUSE | MNFAEEEPSKKYCIKGKHVAIICGVVVAVGLIVGLSVGLTRSCEQDTTPAPSQPPPEASTALPPQDQNVCPDSEDESGEWKNFRLPDFINPVHYDLEVKALMEEDRYTGIVTISVNLSKPTRDLWLHIRETKITKLPELRRPSGEQVPIRRCFEYKKQEYVVIQAAEDLAATSGDSVYRLTMEFKGWLNGSLVGFYKTTYMEDGQIRSIAATDHEPTDARKSFPCFDEPNKKSTYSISIIHPKEYSALSNMPEEKSEMVDDNWKKTTFVKSVPMSTYLVCFAVHRFTAIERKSRSGKPLKVYVQPNQKETAEYAANITQA... | 3.4.11.7 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q07075}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q07075}; | angiogenesis [GO:0001525]; cell migration [GO:0016477]; cell population proliferation [GO:0008283]; glomerulus development [GO:0032835]; peptide catabolic process [GO:0043171]; protein processing [GO:0016485]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217]; regulation of systemic arterial blood pre... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.; EC=3.4.11.7; Evidence={ECO:0000250|UniProtKB:Q07075}; | null | null | null | null | FUNCTION: Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. {ECO:0000250|UniProtKB:Q07075}. | Mus musculus (Mouse) |
P16409 | MYL3_RAT | MAPKKPEPKKDDAKTAAPKAAPAPAAAPAAAPEPERPKEAEFDASKIKIEFTPEQIEEFKEAFQLFDRTPKGEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPKQEELNSKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMAS | null | null | cardiac muscle contraction [GO:0060048]; muscle contraction [GO:0006936]; regulation of striated muscle contraction [GO:0006942]; regulation of the force of heart contraction [GO:0002026]; skeletal muscle tissue development [GO:0007519]; ventricular cardiac muscle tissue morphogenesis [GO:0055010] | A band [GO:0031672]; I band [GO:0031674]; myosin complex [GO:0016459]; myosin II complex [GO:0016460] | actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; cytoskeletal motor activity [GO:0003774] | null | 1.10.238.10; | null | PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Regulatory light chain of myosin. Does not bind calcium. | Rattus norvegicus (Rat) |
P16410 | CTLA4_HUMAN | MACLGFQRHKAQLNLATRTWPCTLLFFLLFIPVFCKAMHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNELTFLDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPEPCPDSDFLLWILAAVSSGLFFYSFLLTAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN | null | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; DNA damage response [GO:0006974]; immune response [GO:0006955]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of regulatory T cell differentiation [GO:0045590]; negative regulation of T cell proliferat... | clathrin-coated endocytic vesicle [GO:0045334]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636] | null | PF07686; | 2.60.40.10; | null | PTM: N-glycosylation is important for dimerization. {ECO:0000269|PubMed:11279502, ECO:0000269|PubMed:16002699, ECO:0000269|PubMed:21156796}.; PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter complex, blocks endocytosis, and leads to retention of CTLA4 on the cell surface. {ECO:0000269|PubMed:1084231... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18468488, ECO:0000269|PubMed:28484017}; Single-pass type I membrane protein {ECO:0000269|PubMed:18468488, ECO:0000269|PubMed:28484017}. Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the ce... | null | null | null | null | null | FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. {ECO:0000269|PubMed:16551244, ECO:0000269|PubMed:1714933}. | Homo sapiens (Human) |
P16422 | EPCAM_HUMAN | MAPPQVLAFGLLLAAATATFAAAQEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMNGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSMCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTRYQLDPKFITSILYENNVITIDLVQNSSQKTQNDVDIADVAYYFEKDVKGESLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKAGVIAVIVVVVIAVVAGIVVLVISRKKRMAKYEKAEIKEMGEMHRELNA | null | null | negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; signal transduction involved in regulation ... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886] | cadherin binding involved in cell-cell adhesion [GO:0098641]; protein-containing complex binding [GO:0044877] | PF21283;PF18635;PF00086; | 4.10.800.10; | EPCAM family | PTM: Hyperglycosylated in carcinoma tissue as compared with autologous normal epithelia. Glycosylation at Asn-198 is crucial for protein stability. {ECO:0000269|PubMed:11080501, ECO:0000269|PubMed:18508581, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000269|PubMed:15195135, ECO:0000269|PubMed:16054130, ECO:0000269|PubMed:19785009}; Single-pass type I membrane protein {ECO:0000269|PubMed:16054130}. Cell junction, tight junction {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the lateral cell membrane an... | null | null | null | null | null | FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and dif... | Homo sapiens (Human) |
P16435 | NCPR_HUMAN | MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTLTSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEHFNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHV... | 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:21808038}; Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:21808038}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:218... | cellular organofluorine metabolic process [GO:0090346]; electron transport chain [GO:0022900]; positive regulation of monooxygenase activity [GO:0032770]; response to hormone [GO:0009725]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADP binding [GO:0050661]; NADPH-hemoprotein reductase activity [GO:0003958] | PF00667;PF00258;PF00175; | 3.40.50.360;3.40.50.80;2.40.30.10; | NADPH--cytochrome P450 reductase family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:... | null | null | null | null | FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-Rule:MF_03212}. | Homo sapiens (Human) |
P16442 | BGAT_HUMAN | MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDHLQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLS... | 2.4.1.37; 2.4.1.40 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17259183}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:17259183}; | carbohydrate metabolic process [GO:0005975]; lipid glycosylation [GO:0030259]; protein glycosylation [GO:0006486] | extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; vesicle [GO:0031982] | antigen binding [GO:0003823]; fucosylgalactoside 3-alpha-galactosyltransferase activity [GO:0004381]; glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity [GO:0004380]; manganese ion binding [GO:0030145]; nucleotide binding [GO:0000166] | PF03414; | null | Glycosyltransferase 6 family | PTM: The soluble form derives from the membrane form by proteolytic processing. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein {ECO:0000269|PubMed:18513251}. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. | CATALYTIC ACTIVITY: Reaction=an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) + UDP; Xref=Rhea:RHEA:19021, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CH... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. | null | null | FUNCTION: This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP... | Homo sapiens (Human) |
P16444 | DPEP1_HUMAN | MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSK... | 3.4.13.19; 3.5.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:12144777}; Note=Binds 2 Zn(2+) ion per monomer. {ECO:0000269|PubMed:12144777}; | antibiotic metabolic process [GO:0016999]; cellular response to calcium ion [GO:0071277]; cellular response to nitric oxide [GO:0071732]; cellular response to xenobiotic stimulus [GO:0071466]; glutathione catabolic process [GO:0006751]; glutathione metabolic process [GO:0006749]; homocysteine metabolic process [GO:0050... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; microvillus membrane [GO:0031528]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | beta-lactamase activity [GO:0008800]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; dipeptidase activity [GO:0016805]; GPI anchor binding [GO:0034235]; metallodipeptidase activity [GO:0070573]; metalloexopeptidase activity [GO:0008235]; modified amino acid binding [GO:007234... | PF01244; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Peptidase M19 family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:28413640}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2168407}. Cell projection, microvillus membrane {ECO:0000269|PubMed:2168407}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2168407}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}. | CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073, ECO:0000269|PubMed:2303490, ECO:0000269|PubMed:32325220}; CATALYTIC ACTIVITY: Reaction=H2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.9 uM for imipenem {ECO:0000269|PubMed:6334084}; Vmax=44.5 umol/min/mg enzyme with imipenem as substrate {ECO:0000269|PubMed:6334084}; | null | null | null | FUNCTION: Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4 (PubMed:2303490, PubMed:31442408, PubMed:32325220, PubMed:6334084). Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation (PubMed:32325220). Possesses also beta lactamase activity a... | Homo sapiens (Human) |
P16446 | PIPNA_RAT | MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD | null | null | axonogenesis [GO:0007409]; phospholipid transport [GO:0015914] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | fatty-acyl-CoA binding [GO:0000062]; lipid binding [GO:0008289]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine transfer activity [GO:0120019]; phosphatidylcholine transporter activity [GO:0008525]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol transfer activity [GO:0008526]; phospholip... | PF02121; | 3.30.530.20; | PtdIns transfer protein family, PI transfer class I subfamily | PTM: Phosphorylated by PKC in a calcium and phosphatidylserine-dependent manner. {ECO:0000250|UniProtKB:P53810}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus {ECO:0000250|UniProtKB:P53810}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:7568025}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000305|PubMed:7568025}; CATALYTIC ACTIVITY... | null | null | null | null | FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes (PubMed:18636990, PubMed:7568025). Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions (By similarity). Preference order for PC is C16:1 > C1... | Rattus norvegicus (Rat) |
P16451 | ODPX_YEAST | MLSAISKVSTLKSCTRYLTKCNYHASAKLLAVKTFSMPAMSPTMEKGGIVSWKYKVGEPFSAGDVILEVETDKSQIDVEALDDGKLAKILKDEGSKDVDVGEPIAYIADVDDDLATIKLPQEANTANAKSIEIKKPSADSTEATQQHLKKATVTPIKTVDGSQANLEQTLLPSVSLLLAENNISKQKALKEIAPSGSNGRLLKGDVLAYLGKIPQDSVNKVTEFIKKNERLDLSNIKPIQLKPKIAEQAQTKAADKPKITPVEFEEQLVFHAPASIPFDKLSESLNSFMKEAYQFSHGTPLMDTNSKYFDPIFEDLVTLS... | null | null | acetyl-CoA biosynthetic process from pyruvate [GO:0006086] | mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]; structural molecule activity [GO:0005198] | PF00364; | 2.40.50.100;4.10.320.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | null | null | null | null | null | FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16452 | EPB42_HUMAN | MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVALTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWDFGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLIDEYYNEEGLQNGEGQR... | null | null | cell morphogenesis [GO:0000902]; erythrocyte maturation [GO:0043249]; hemoglobin metabolic process [GO:0020027]; multicellular organismal-level iron ion homeostasis [GO:0060586]; regulation of cell shape [GO:0008360]; spleen development [GO:0048536] | ankyrin-1 complex [GO:0170014]; cortical cytoskeleton [GO:0030863]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]; structural constituent of cytoskeleton [GO:0005200] | PF00927;PF01841;PF00868; | 2.60.40.10;3.90.260.10; | Transglutaminase superfamily, Transglutaminase family | PTM: Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42. {ECO:0000269|PubMed:8499466}. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of erythrocyte membranes. | 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) |
P16453 | DCHS_RAT | MMEPSEYHEYQARGKEMVDYICQYLSTVRERQVTPNVKPGYLRAQIPSSAPEEPDSWDSIFGDIEQIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNIMDWLAKMLGLPDFFLHHHPSSQGGGVLQRTVSESTLIALLAARKNKILEMKAHEPNADESSLNARLVAYASDQAHSSVEKAGLISLVKIKFLPVDDNFSLRGEALQKAIEEDKQQGLVPVFVCATLGTTGVCAFDKLSELGPICAREGLWLHVDAAYAGTAFLRPELRGFLKGIEYADSFTFNPSKWMMVHFDCTGFW... | 4.1.1.22 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | amino acid metabolic process [GO:0006520]; catecholamine biosynthetic process [GO:0042423]; histamine biosynthetic process [GO:0001694]; histamine metabolic process [GO:0001692]; histidine catabolic process [GO:0006548]; histidine metabolic process [GO:0006547] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025] | amino acid binding [GO:0016597]; histidine decarboxylase activity [GO:0004398]; identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170] | PF00282; | 3.90.1150.10;1.20.1340.10;3.40.640.10; | Group II decarboxylase family | PTM: May be post-translationally processed. | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-histidine = CO2 + histamine; Xref=Rhea:RHEA:20840, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57595, ChEBI:CHEBI:58432; EC=4.1.1.22; | null | PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1. | null | null | FUNCTION: Catalyzes the biosynthesis of histamine from histidine. {ECO:0000250}. | Rattus norvegicus (Rat) |
P16455 | MGMT_HUMAN | MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN | 2.1.1.63 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion.; | DNA dealkylation involved in DNA repair [GO:0006307]; DNA ligation [GO:0006266]; DNA repair [GO:0006281]; methylation [GO:0032259]; negative regulation of apoptotic process [GO:0043066]; positive regulation of double-strand break repair [GO:2000781] | membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-methyltransferase activity [GO:0009008]; metal ion binding [GO:0046872]; methylated-DNA-[protein]-cysteine S-methyltransferase activity [GO:0003908]; methyltransferase activity [GO:0008168] | PF01035;PF02870; | 3.30.160.70;1.10.10.10; | MGMT family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:85445,... | null | null | null | null | FUNCTION: Involved in the cellular defense against the biological effects of 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. This is a suicide reaction: the enzyme is irrever... | Homo sapiens (Human) |
P16456 | SELD_ECOLI | MSENSIRLTQYSHGAGCGCKISPKVLETILHSEQAKFVDPNLLVGNETRDDAAVYDLGNGTSVISTTDFFMPIVDNPFDFGRIAATNAISDIFAMGGKPIMAIAILGWPINKLSPEIAREVTEGGRYACRQAGIALAGGHSIDAPEPIFGLAVTGIVPTERVKKNSTAQAGCKLFLTKPLGIGVLTTAEKKSLLKPEHQGLATEVMCRMNIAGASFANIEGVKAMTDVTGFGLLGHLSEMCQGAGVQARVDYEAIPKLPGVEEYIKLGAVPGGTERNFASYGHLMGEMPREVRDLLCDPQTSGGLLLAVMPEAENEVKAT... | 2.7.9.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394}; | phosphorylation [GO:0016310]; selenocysteine biosynthetic process [GO:0016260]; tRNA seleno-modification [GO:0070329] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; selenide, water dikinase activity [GO:0004756] | PF00586;PF02769; | 3.90.650.10;3.30.1330.10; | Selenophosphate synthase 1 family, Class I subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate; Xref=Rhea:RHEA:18737, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16144, ChEBI:CHEBI:29317, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; EC=2.7.9.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00625, ECO:0... | null | null | null | null | FUNCTION: Synthesizes selenophosphate from selenide and ATP. {ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0000269|PubMed:2405383}. | Escherichia coli (strain K12) |
P16460 | ASSY_MOUSE | MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYEDRYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVTNIKDGTTRTTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAEL... | 6.3.4.5 | null | acute-phase response [GO:0006953]; arginine biosynthetic process [GO:0006526]; argininosuccinate metabolic process [GO:0000053]; aspartate metabolic process [GO:0006531]; cellular response to amine stimulus [GO:0071418]; cellular response to amino acid stimulus [GO:0071230]; cellular response to ammonium ion [GO:007124... | cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204] | amino acid binding [GO:0016597]; argininosuccinate synthase activity [GO:0004055]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; toxic substance binding [GO:0015643] | PF20979;PF00764; | 3.90.1260.10;3.40.50.620;1.20.5.470; | Argininosuccinate synthase family, Type 1 subfamily | PTM: Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases. {ECO:0000269|PubMed:28985504}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P00966}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; Evidence={ECO:0000250|UniPr... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. {ECO:0000250|UniProtKB:P00966}.; PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. {ECO:0000250|UniProtKB:P00966}. | null | null | FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynth... | Mus musculus (Mouse) |
P16462 | LTXA_AGGAC | MATTTLPNTKQQAAQFANSVADRAKENIDAAKEQLQKALDKLGKTGKKLTLYIPKNYKKGNGLTALIKAAQKLGIEVYHEGKDGPALTNGILNTGKKLLGLTERGLTLFAPELDKWIQGNKHLSNSVGSTGNLTKAIDKVQSVLGTLQAFLNTAFSGMDLDALIKARQNGKNVTDVQLAKASLNLINELIGTISSITNNVDTFSKQLNKLGEALGQVKHFGSFGDKLKNLPKLGNLGKGLGALSGVLSAISAALLLANKDADTATKAAAAAELTNKVLGNIGKAITQYLIAQRAAAGLSTTGPVAGLIASVVSLAISPLS... | null | null | killing of cells of another organism [GO:0031640] | cell outer membrane [GO:0009279]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; channel activity [GO:0015267]; toxin activity [GO:0090729] | PF00353;PF02382;PF08339; | 2.150.10.10; | RTX prokaryotic toxin (TC 1.C.11) family | PTM: Acylated at Lys-562 and Lys-687 by LtxC. This modification is required for full activity. Isolated methyl esters contain palmitoyl and palmitolyl fatty acyl groups with smaller quantities of myristic and stearic fatty acids. {ECO:0000269|PubMed:19450669, ECO:0000269|PubMed:21729247}. | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:1937819}; Peripheral membrane protein {ECO:0000269|PubMed:1937819}; Extracellular side {ECO:0000269|PubMed:1937819}. Secreted {ECO:0000269|PubMed:11035711}. Note=Leukotoxin expressed by the rough, adherent, clinical isolate CU1000N is cell associated. Howeve... | null | null | null | null | null | FUNCTION: Virulence factor that plays an important role in immune evasion. Lyses human lymphocytes and monocytes. Binds to the LFA-1 integrin on the surface of the host cell and to cholesterol-containing membranes, which probably results in large LtxA-LFA-1 clusters in lipid rafts. Shows also beta-hemolytic activity on... | Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans) |
P16467 | PDC5_YEAST | MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKLLETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQFPVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYSYKTKNIVEFHSDHIKIRNAT... | 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:0000250|UniProtKB:P06169}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P06169}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|Uni... | 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 | null | 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:2185016}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2; Xref=Rhea:RHEA:54356, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.1 mM for pyruvate {ECO:0000269|PubMed:22904058}; KM=1.2 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058}; KM=1.5 mM for 2-oxopentanoate {ECO:0000269|PubMed:22904058}; KM=0.67 mM for phenylpyruvate {ECO:0000269|PubMed:22904058}; Vmax=1.3 umol/min/mg enzyme for ... | PATHWAY: Fermentation; ethanol fermentation.; PATHWAY: Amino-acid degradation; Ehrlich pathway. | null | null | FUNCTION: Second most abundant 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 p... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16469 | LOX15_PIG | MGLYRVRVSTGSSFYAGSQNQVQLWLVGQHGEAALGWCLRPARGKETEFSVDVSEYLGPLLFVKLRKRHLLQDDAWFCNWISVQGPGANGDEFRFPCYRWVEGDRILSLPEGTARTVVDDPQGLFKKHREEELAERRKLYRWGNWKDGLILNIASTGIHDLPVDERFLEDKRIDFEASLAKGLADLAVKDSLNVLMSWNSLDSFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGTNPMLLRHSVELPARLKFPPGMEELQAQLEKELQGGTLFEADFSLLDGIKANVILCSQQYLAVPLVMLKLQPDGKLLPMVIQLQ... | 1.13.11.-; 1.13.11.12; 1.13.11.31; 1.13.11.33 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8305485}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8305485}; | apoptotic cell clearance [GO:0043277]; arachidonic acid metabolic process [GO:0019369]; bone mineralization [GO:0030282]; cellular response to calcium ion [GO:0071277]; cellular response to interleukin-13 [GO:0035963]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabol... | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; plasma membrane [GO:0005886] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P16050}. Cell membrane {ECO:0000250|UniProtKB:P16050}; Peripheral membrane protein {ECO:0000250|UniProtKB:P16050}. Lipid droplet {ECO:0000250|UniProtKB:P16050}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates ... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:17493578, ECO:0000269|PubMed:8305485}; PhysiologicalDirection=left-to-righ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.8 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:17493578}; KM=8 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine {ECO:0000269|PubMed:17493578}; KM=9 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine {ECO:0000269|PubMed:17493578}; KM=7.8 uM for N-(... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:8305485}. | null | null | FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:17493578, PubMed:18311922, PubMed:19324874, PubMed:8305485). It inserts peroxyl groups at C12 or C15 of arachidonat... | Sus scrofa (Pig) |
P16471 | PRLR_HUMAN | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPPVPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDS... | null | null | activation of Janus kinase activity [GO:0042976]; activation of transmembrane receptor protein tyrosine kinase activity [GO:0007171]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cytokine-mediated signaling pathway [GO:0019221]; embryo implantation [GO:0007566]; lactation... | cell surface [GO:0009986]; endosome lumen [GO:0031904]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | cytokine binding [GO:0019955]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; peptide hormone binding [GO:0017046]; prolactin receptor activity [GO:0004925]; protein kinase binding [GO:0019901] | PF09067; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:12580759}; Single-pass type I membrane protein {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:12580759}.; SUBCELLULAR LOCATION: [Isoform 7]: Secreted. | null | null | null | null | null | FUNCTION: This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prola... | Homo sapiens (Human) |
P16473 | TSHR_HUMAN | MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNS... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; cellular response to glycoprotein [GO:1904588]; cellular response to thyrotropin-releasing hormone [GO:1905229]; G protein-coupled receptor sign... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | G protein-coupled peptide receptor activity [GO:0008528]; protein-containing complex binding [GO:0044877]; signaling receptor activity [GO:0038023]; thyroid-stimulating hormone receptor activity [GO:0004996] | PF00001;PF13306; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family, FSH/LSH/TSH subfamily | PTM: Glycosylated. {ECO:0000269|PubMed:11847099}.; PTM: Sulfated. Sulfation on Tyr-385 plays a role in thyrotropin receptor binding and activation. {ECO:0000269|PubMed:11847099}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11847099}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:11847099}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin (PubMed:11847099, PubMed:12045258). Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin (PubMed:12045258). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (P... | Homo sapiens (Human) |
P16474 | BIP_YEAST | MFFNRLSAGKLLVPLSVVLYALFVVILPLQNSFHSSNVLVRGADDVENYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKDIKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALS... | 3.6.4.10 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; detection of unfolded protein [GO:0002235]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; fungal-type cell wall beta-glucan biosynthetic process [GO:0070880]; karyogamy involved in conjugation with cellular fusion [G... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; luminal surveillance complex [GO:0034099]; membrane [GO:0016020]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-transporting ATPase activity [GO:0015450]; unfolded protein binding [GO:0051082] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:2661018}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P11021}; | null | null | null | null | FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. {ECO:0000269|PubMed:16002399}... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16493 | GP_HANTH | MGIWKWLVMASLVWPVLTLRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQNSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIP... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; signal transduction [GO:0007165]; symbiont-mediated suppression of host TRAF-mediated signal transduction [GO:0039527]; virion attachment to host cell [GO:0019062]; virus-mediated perturba... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase. {ECO:0000250|UniProtKB:P08668}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum memb... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity)... | Hantaan virus (strain Hojo) (Hojo virus) (Korean hemorrhagic fever virus) |
P16499 | PDE6A_HUMAN | MGEVTAEEVEKFLDSNIGFAKQYYNLHYRAKLISDLLGAKEAAVDFSNYHSPSSMEESEIIFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRLFNVHKDAVLEDCLVMPDQEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEVPPYSGPRTPDGREINFYKVID... | 3.1.4.35 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250}; | cAMP-mediated signaling [GO:0019933]; retina development in camera-type eye [GO:0060041]; visual perception [GO:0007601] | photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:20940301}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:20940301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000305|PubMed:20940301}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 3',5'-cyclic GMP (with the chimera containing the N-terminal regulatory GAF domains of PDE6C and the C-terminal catalytic domain of PDE6A) {ECO:0000269|PubMed:20940301}; | null | null | null | FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (PubMed:20940301). This protein participates in processes of transmission and amplification of the visual signal. {ECO:0000269|PubMed:20940301}. | Homo sapiens (Human) |
P16501 | IGF1A_XENLA | METNNNLSTQLFKCYFCDILKLKMHKMSCIHLLYLVLCFLTLTHSAAAGPETLCGAELVDTLQFVCGDRGFYFSKPTGYGSNNRRSHHRGIVDECCFQSCDFRRLEMYCAPAKQAKSARSVRTQRHTDMPKAQKEVHPKNTSRGNTGSRGFRM | null | null | cell population proliferation [GO:0008283]; head morphogenesis [GO:0060323]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of Wnt signaling path... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Promotes head development by inhibiting Wnt signaling during embryogenesis (PubMed:11709186, PubMed:11944947). Acts as a ligand for IGF1R. Binds to the ... | Xenopus laevis (African clawed frog) |
P16517 | GP167_BPPH2 | MEAILMIGVLALCVIFLLSGRNNKKKQEARELEDYLEDLNKRVVQRTQILSELNEVISNRSIDKTVNLSACEVAVLDLYEQSNIRIPSDIIEDLVNQRLQSEQEVLNYIETQRTYWKLENQKKLYRGSLK | null | null | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693] | host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | DNA binding [GO:0003677] | PF06720; | 1.10.8.600; | Phi29likevirus gp16.7 family | null | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255, ECO:0000269|PubMed:11169113}; Single-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:11169113}. | null | null | null | null | null | FUNCTION: Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11169113, PubMed:11741949). Required for the redistribution of replicating vir... | Bacillus phage phi29 (Bacteriophage phi-29) |
P16519 | NEC2_HUMAN | MKGGCVSQWKAAAGFLFCVMVFASAERPVFTNHFLVELHKGGEDKARQVAAEHGFGVRKLPFAEGLYHFYHNGLAKAKRRRSLHHKQQLERDPRVKMALQQEGFDRKKRGYRDINEIDINMNDPLFTKQWYLINTGQADGTPGLDLNVAEAWELGYTGKGVTIGIMDDGIDYLHPDLASNYNAEASYDFSSNDPYPYPRYTDDWFNSHGTRCAGEVSAAANNNICGVGVAYNSKVAGIRMLDQPFMTDIIEASSISHMPQLIDIYSASWGPTDNGKTVDGPRELTLQAMADGVNKGRGGKGSIYVWASGDGGSYDDCNCD... | 3.4.21.94 | null | enkephalin processing [GO:0034230]; insulin processing [GO:0030070]; islet amyloid polypeptide processing [GO:0034231]; nervous system development [GO:0007399]; peptide hormone processing [GO:0016486]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508] | dendrite [GO:0030425]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]; secretory granule [GO:0030141]; transport vesicle [GO:0030133] | serine-type endopeptidase activity [GO:0004252] | PF01483;PF00082;PF16470; | 2.60.120.260;3.30.70.850;3.40.50.200; | Peptidase S8 family, Furin subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Secreted {ECO:0000269|PubMed:28719828}. Note=Localized in the secretion granules. | CATALYTIC ACTIVITY: Reaction=Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.; EC=3.4.21.94; | null | null | null | null | FUNCTION: Serine endopeptidase which is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells. {ECO:0000269|PubMed:28719828, ECO:0000269|PubMed:9287128}. | Homo sapiens (Human) |
P16520 | GBB3_HUMAN | MGEMEQLRQEAEQLKKQIADARKACADVTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDFNLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEAICTGSDDASCRLFDLRADQELICFSHESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSMKSERVGILSGHDNRVSCLGV... | null | null | cell volume homeostasis [GO:0006884]; G protein-coupled receptor signaling pathway [GO:0007186]; regulation of blood pressure [GO:0008217]; regulation of cholesterol metabolic process [GO:0090181]; regulation of fat cell differentiation [GO:0045598]; regulation of gene expression [GO:0010468]; regulation of glucose met... | cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886] | GTPase activity [GO:0003924]; GTPase binding [GO:0051020]; signaling receptor complex adaptor activity [GO:0030159]; spectrin binding [GO:0030507] | PF00400; | 2.130.10.10; | WD repeat G protein beta family | null | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | Homo sapiens (Human) |
P16521 | EF3A_YEAST | MSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVPEHFFGELAKGIKDKKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICTNAGNKDKEIQSVASETLISIVNAVNPVAIKALLPHLTNAIVETNKWQEKIAILAAISAMVDAAKDQVALRMPELIPVLSETMWDTKKEVKAAATAAMTKATETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSNFATIADPEAREVTLRALKTLRRV... | 3.6.4.- | null | negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; translational elongation [GO:0006414]; translational termination [GO:0006415] | cytoplasmic stress granule [GO:0010494]; cytosolic ribosome [GO:0022626]; ribosome [GO:0005840] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; rRNA binding [GO:0019843]; translation elongation factor activity [GO:0003746] | PF17947;PF00005; | 1.20.1390.20;2.40.50.990;1.25.10.10;3.40.50.300; | ABC transporter superfamily, ABCF family, EF3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269, ECO:0000269|PubMed:7657623, ECO:0000269|PubMed:7957240}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.126 mM for ATP {ECO:0000269|PubMed:7957240}; KM=0.125 mM for GTP {ECO:0000269|PubMed:7957240}; Vmax=15.2 umol/min/mg enzyme with ATP as substrate {ECO:0000269|PubMed:7957240}; | PATHWAY: Protein biosynthesis; polypeptide chain elongation. {ECO:0000305}. | null | null | FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:29300771, PubMed:6456269, PubMed:7657623). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacy... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16522 | CDC23_YEAST | MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEF... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein ubiquitination [GO:0016567]; regulation of meiotic cell cycle [GO:0051445]; regulation of mitotic cell cycle [GO:00... | anaphase-promoting complex [GO:0005680]; kinetochore [GO:0000776] | cyclin binding [GO:0030332] | PF04049;PF13414;PF13181; | 1.25.40.10; | APC8/CDC23 family | PTM: Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form. {ECO:0000269|PubMed:10871279}. | SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with the kinetochore. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16528 | ICLR_ECOLI | MVAPIPAKRGRKPAVATAPATGQVQSLTRGLKLLEWIAESNGSVALTELAQQAGLPNSTTHRLLTTMQQQGFVRQVGELGHWAIGAHAFMVGSSFLQSRNLLAIVHPILRNLMEESGETVNMAVLDQSDHEAIIIDQVQCTHLMRMSAPIGGKLPMHASGAGKAFLAQLSEEQVTKLLHRKGLHAYTHATLVSPVHLKEDLAQTRKRGYSFDDEEHALGLRCLAACIFDEHREPFAAISISGPISRITDDRVTEFGAMVIKAAKEVTLAYGGMR | null | null | glyoxylate cycle [GO:0006097]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF09339;PF01614; | 3.30.450.40;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Regulation of the glyoxylate bypass operon (aceBAK), which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase. Glyoxylate disrupts the interaction with the promoter by favoring the inactive dimeric form. Pyruvate enhances promoter binding by stabilizing the tetr... | Escherichia coli (strain K12) |
P16545 | IGF1_PIG | MGKISSLPTQLFKCCFCDFLKVKMHITSSSHLFYLALCLLSFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKAQKEVHLKNTSRGSSGNKNYRM | null | null | cell population proliferation [GO:0008283]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; ... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bon... | Sus scrofa (Pig) |
P16546 | SPTN1_MOUSE | MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEKWIQEKLQVASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASETIRTRLMELHRQWELLLEKMREKGIKLLQAQKLVQYLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDLAAHEERVNEVSQFAAKLIQEQHPEEELIKTKQDEVNAAWQRLKGLALQRQGKLFGAAEVQRFNRDVDETIGWIKEKEQLMASDDFGRDLASVQALLRKHEGLERDLAALEDKVKALCAEADR... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693] | cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cortical cytoskeleton [GO:0030863]; cuticular plate [GO:0032437]; cytosol [GO:0005829]; fascia adherens [GO:0005916]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; myeli... | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; protein-containing complex binding [GO:0044877]; spectrin binding [GO:0030507] | PF13499;PF08726;PF00018;PF00435; | 1.20.5.170;1.20.58.60;1.10.238.10;2.30.30.40; | Spectrin family | PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | Mus musculus (Mouse) |
P16549 | FMO1_PIG | MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYPDFPFPEDYPNYVPNSHFLEYLRMYANQFNLLKCIQFKTKVCSVTKHEDFNTTGQWDVVTLCEGKQESAVFDAVMVCTGFLTNPYLPLDSFPGINTFKGQYFHSRQYKHPDIFKDKSVLVVGMGNSGTDIAVEASHLAKKVFLSTTGGAWVISRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVNWLIAKKMNSWFNHANYGLIPEDRIQLREPVLNDELPGRIITGKVLIKPSIKEVKENSVVFNSSPEEE... | 1.14.13.148; 1.14.13.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q01740}; | NADPH oxidation [GO:0070995]; organic acid metabolic process [GO:0006082]; taurine biosynthetic process [GO:0042412]; toxin metabolic process [GO:0009404] | endoplasmic reticulum membrane [GO:0005789] | flavin adenine dinucleotide binding [GO:0050660]; hypotaurine dehydrogenase activity [GO:0047822]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661]; trimethylamine monooxygenase activity [GO:0034899] | PF00743; | 3.50.50.60; | FMO family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7758472}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + hypotaurine + NADPH + O2 = H2O + NADP(+) + taurine; Xref=Rhea:RHEA:69819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57853, ChEBI:CHEBI:58349, ChEBI:CHEBI:507393; EC=1.14.13.8; Evidence={ECO:0000250|UniProtKB:Q01740}; PhysiologicalDirectio... | null | null | null | null | FUNCTION: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (PubMed:7758472). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytop... | Sus scrofa (Pig) |
P16550 | APA1_YEAST | MSIPADIASLISDKYKSAFDNGNLKFIQTETTKTKDPKTSMPYLISHMPSLIEKPERGQTPEGEDPLGKPEEELTVIPEFGGADNKAYKLLLNKFPVIPEHTLLVTNEYQHQTDALTPTDLLTAYKLLCALDNEESDKRHMVFYNSGPASGSSLDHKHLQILQMPEKFVTFQDRLCNGKEHFLPTFNTEPLQDAKVSFAHFVLPMPESEETVDEDLLAMCYISILQRALTFFQDWLNENPELKKSYNLMLTKEWICVVPRSKAFSDEMKIGFNSTGYCGMILTKNDEVFSKITEKPELINDILLECGFPNTSGQKPNEYN... | 2.7.7.5; 2.7.7.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:2174863}; | nucleoside catabolic process [GO:0009164]; nucleotide biosynthetic process [GO:0009165] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; bis(5'-nucleosyl)-tetraphosphatase activity [GO:0008796]; sulfate adenylyltransferase (ADP) activity [GO:0004780] | PF19327;PF09830; | 3.30.428.70; | ATP adenylyltransferase family | PTM: The N-terminus is blocked. {ECO:0000305|PubMed:2556364}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate + phosphate; Xref=Rhea:RHEA:16577, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=2.7.7.53; Evidence={ECO:0000269|PubMed:2174863, ECO:0000269|PubMed:2556364, ECO:0000269|PubMed:2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39.3 uM for Ap4A {ECO:0000269|PubMed:23628156}; Note=kcat is 81.2 sec(-1) with Ap4A as substrate. {ECO:0000269|PubMed:23628156}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23628156}; | null | FUNCTION: Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catal... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16554 | NUMB_DROME | MGNSSSHTHEPLERGFTRGKFGDVKNGKSASFRFSKKSPKKMDRLRRSFRDSFRRRKDRVPESSKPHQWQADEEAVRSATCSFSVKYLGCVEVFESRGMQVCEEALKVLRQSRRRPVRGLLHVSGDGLRVVDDETKGLIVDQTIEKVSFCAPDRNHERGFSYICRDGTTRRWMCHGFLACKDSGERLSHAVGCAFAVCLERKQRRDKECGVTMTFDTKNSTFTRTGSFRQQTLTERLAMATVGTNERSVDGPGSAMPGPPAATVKPFNPFAIERPHATPNMLERQSSFRLSTIGSQSPFKRQMSLRINDLPSNADRQRAF... | null | null | asymmetric neuroblast division [GO:0055059]; centrosome localization [GO:0051642]; embryonic heart tube development [GO:0035050]; enteroendocrine cell differentiation [GO:0035883]; glial cell migration [GO:0008347]; Malpighian tubule tip cell differentiation [GO:0061382]; muscle cell fate specification [GO:0042694]; ne... | basal part of cell [GO:0045178]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; Notch binding [GO:0005112] | PF06311;PF00640; | 2.30.29.30; | null | PTM: Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex. {ECO:0000269|PubMed:26481050}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2752427}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:26481050}. Note=In larval brain, shows asymmetric localization and asymmetrically sized divisions in type II secondary neuroblasts. {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Required in determination of cell fate during sensory organ formation in embryos (PubMed:2752427). Restricts developmental potential and promote maturation of intermediary neuronal progenitor (INP) cells probably acting as an antagonist of Notch signaling (PubMed:18342578, PubMed:24550111, PubMed:28899667). {... | Drosophila melanogaster (Fruit fly) |
P16559 | TCMN_STRGA | MAARTDNSIVVNAPFELVWDVTNDIEAWPELFSEYAEAEILRQDGDGFDFRLKTRPDANGRVWEWVSHRVPDKGSRTVRAHRVETGPFAYMNLHWTYRAVAGGTEMRWVQEFDMKPGAPFDNAHMTAHLNTTTRANMERIKKIIEDRHREGQRTPASVLPTELHAQQLLLLAASGRLARIVHVLTELRIADLLADGPRHVAELAKETDTHELSLYRVLRSAASVGVFAEGPVRTFSATPLSDGLRTGNPDGVLPLVKYNNMELTRRPYDEIMHSVRTGEPAFRRVFGSSFFEHLEANPEAGEFFERFMAHWSRRLVLDGL... | 2.1.1.-; 2.3.1.235 | null | antibiotic biosynthetic process [GO:0017000]; methylation [GO:0032259] | null | O-methyltransferase activity [GO:0008171] | PF00891;PF03364; | 1.10.287.1350;3.30.530.20;3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=8 H(+) + 10 malonyl-CoA = 10 CO2 + 10 CoA + 2 H2O + tetracenomycin F2; Xref=Rhea:RHEA:21348, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:77982; EC=2.3.1.235; Evidence={ECO:0000269|PubMed:9609708}; PhysiologicalDirection=left-to-... | null | PATHWAY: Antibiotic biosynthesis; tetracenomycin C biosynthesis. {ECO:0000269|PubMed:1548230, ECO:0000269|PubMed:9609708}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for methyltransferase activity. {ECO:0000269|PubMed:8692863}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermal resistance is enhanced at low protein and high salt concentrations, is pH-dependent and denaturation is irreversible. {ECO:0000269|PubMed:34139289}; | FUNCTION: Involved in the biosynthesis of tetracenomycin C (TCM C) (PubMed:1548230, PubMed:9609708). Part of a type II polyketide synthase (PKS) that catalyzes the synthesis of tetracenomycin F2 (TCM F2), a precursor of TCM C, from malonyl-CoA (PubMed:8248801, PubMed:9609708). The TcmN N-terminal domain, when coupled w... | Streptomyces glaucescens |
P16568 | BICD_DROME | MSSASNNGPSADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLFS... | null | null | cellular macromolecule localization [GO:0070727]; germarium-derived egg chamber formation [GO:0007293]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; microtubule anchoring at microtubule organizing center [GO:0072393]; mRNA transport [GO:0051028]; oocyte axis sp... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; presynapse [GO:0098793] | clathrin heavy chain binding [GO:0032050]; cytoskeletal anchor activity [GO:0008093]; dynactin binding [GO:0034452]; dynein complex binding [GO:0070840]; small GTPase binding [GO:0031267] | PF09730; | 6.10.250.2470; | BicD family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: This protein is essential for differentiation. It may play a role in localizing of Nanos (a maternal determinant) activity in oocytes. During oogenesis, plays a specific role, together with Rab6 but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in oskar mRNA localization a... | Drosophila melanogaster (Fruit fly) |
P16573 | CEAM1_RAT | MELASARLLRGQIPWRGLLLTASLLTYWSPLTTAQVTVDAVPPNVVEEKSVLLLAHNLPQEFQVFYWYKGTTLNPDSEIARYIRSDNMSKTGPAYSGRETIYSNGSLFFQNVNKTDERAYTLSVFDQQFNPIQTSVQFRVYPALQKPNVTGNNSNPMEGEPFVSLMCEPYTNNTSYLWSRNGESLSEGDRVTFSEGNRTLTLLNVRRTDKGYYECEARNPATFNRSDPFNLDVIYGPDAPVISPPDIYLHQGSNLNLSCHADSNPPAQYFWLINEKLQTSSQELFISNITTNNSGTYACFVNNTVTGLSRTTVKNITVFE... | null | null | bile acid and bile salt transport [GO:0015721]; blood vessel development [GO:0001568]; cell adhesion [GO:0007155]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cell-cell junction organization [GO:0045216]; cellular response to insulin stimulus [GO:0032869]; common myeloid progenitor cell prol... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; brush border membrane [GO:0031526]; cell junction [GO:0030054]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; external side of plasma membrane [GO:0009897]; extracellular... | actin binding [GO:0003779]; bile acid transmembrane transporter activity [GO:0015125]; calmodulin binding [GO:0005516]; filamin binding [GO:0031005]; granulocyte colony-stimulating factor receptor binding [GO:0005130]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein dimerization activity [G... | PF00047;PF13895;PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, CEA family | PTM: [Isoform 1]: Phosphorylated on serine and tyrosine (PubMed:8420979). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:15467833, PubMed:16054098, PubMed:7626603, PubMed:9712832). Phosphorylated at Ser-503; mediates acti... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458, ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8536699, ECO:0000269|PubMed:9003371, ECO:0000269|PubMed:9712832}; Single-pass type I membrane protein. Lateral cell membrane {ECO:0000269|PubMed:7774714}. Apical cell... | null | null | null | null | null | FUNCTION: [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:2373740, PubMed:8454589). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:11850617). Its coinhibitory recept... | Rattus norvegicus (Rat) |
P16575 | BVGS_BORPE | MPAPHRLYPRSLICLAQALLAWALLAWAPAQASQELTLVGKAAVPDVEVALDGDDWRWLARKRVLTLGVYAPDIPPFDVTYGERYEGLTADYMAIIAHNLGMQAKVLRYPTREQALSALESGQIDLIGTVNGTDGRQQSLRLSVPYAADHPVIVMPIGARHVPASNLAGQRLAVDINYLPKETLARAYPQATLHYFPSSEQALAAVAYGQADVFIGDALTTSHLVSQSYFNDVRVVAPAHIATGGESFGVRADNTRLLRVVNAVLEAIPPSEHRSLIYRWGLGSSISLDFAHPAYSAREQQWMADHPVVKVAVLNLFAPF... | 2.7.13.3 | null | regulation of DNA-templated transcription [GO:0006355] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF01627;PF00989;PF00072;PF00497; | 1.10.287.130;3.40.50.2300;3.30.565.10;1.20.120.160;3.30.450.20;3.40.190.10; | null | PTM: Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals. | Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) |
P16580 | GLNA_CHICK | MATSASSHLSKAIKHMYMKLPQGEKVQAMYIWIDGTGEHLRCKTRTLDHEPKSLEDLPEWNFDGSSTFQAEGSNSDMYLRPAAMFRDPFRKDPNKLVLCEVFKYNRQSADTNLRHTCRRIMDMVSNQHPWFGMEQEYTLLGTDGHPFGWPSNCFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKIGGTNAEVMPAQWEFQVGPCEGIEMGDHLWIARFILHRVCEDFGVIVSFDPKPIPGNWNGAGCHTNFSTKNMREDGGLKHIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSSIHEFSAGVANRG... | 4.1.1.15; 6.3.1.2 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:19895308}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19895308}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19895308}; | glutamine biosynthetic process [GO:0006542] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; glutamate decarboxylase activity [GO:0004351]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12965260}. Mitochondrion {ECO:0000269|PubMed:4401992}. Note=In the liver found in mitochondria, in brain and retina in the cytoplasm (PubMed:12965260, PubMed:4401992). In retinal cells found in the outer part of the inner nuclear layer and in the bacillary layer of th... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:19895308}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:19895308). When expressed in liver, it may be involved in detoxifying intramitochondrially generated ammonia (PubMed:4401992). Also acts as glutamate decarboxylase by catalyzing the production of 4-a... | Gallus gallus (Chicken) |
P16581 | LYAM2_HUMAN | MIASQFLSALTLVLLIKESGAWSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVWVWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTAACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSYNSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPWNTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHS... | null | null | actin filament-based process [GO:0030029]; activation of phospholipase C activity [GO:0007202]; calcium-mediated signaling [GO:0019722]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; inflammatory response [GO:0006954]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migr... | caveola [GO:0005901]; clathrin-coated pit [GO:0005905]; cortical cytoskeleton [GO:0030863]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; oligosaccharide binding [GO:0070492]; phospholipase binding [GO:0043274]; sialic acid binding [GO:0033691]; transmembrane signaling receptor activity [GO:0004888] | PF00008;PF00059;PF00084; | 2.10.70.10;3.10.100.10; | Selectin/LECAM family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12649084, ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis. {ECO:0000269|PubMed:1689848, ECO:0000269|PubMed:28011641}. | Homo sapiens (Human) |
P16582 | LSHR_PIG | MRRRSLALRLLLALLLLPPPLPQTLLGAPCPEPCSCRPDGALRCPGPRAGLSRLSLTYLPIKVIPSQAFRGLNEVVKIEISQSDSLEKIEANAFDNLLNLSEILIQNTKNLVYIEPGAFTNLPRLKYLSICNTGIRKLPDVTKIFSSEFNFILEICDNLHITTVPANAFQGMNNESITLKLYGNGFEEIQSHAFNGTTLISLELKENAHLKKMHNDAFRGARGPSILDISSTKLQALPSYGLESIQTLIATSSYSLKKLPSREKFTNLLDATLTYPSHCCAFRNLPTKEQNFSFSIFKNFSKQCESTARRPNNETLYSAI... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to luteinizing hormone stimulus [GO:0071373]; cognition [GO:0050890]; development of secondary male sexual characteristics [GO:0046544]; hormone-mediated signaling pathway [GO:0009755]; luteinizing hormone signalin... | centriolar satellite [GO:0034451]; plasma membrane [GO:0005886] | choriogonadotropin hormone binding [GO:0038106]; choriogonadotropin hormone receptor activity [GO:0035472]; G protein-coupled peptide receptor activity [GO:0008528]; luteinizing hormone receptor activity [GO:0004964] | PF00001;PF13306; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family, FSH/LSH/TSH subfamily | PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}. | null | null | null | null | null | FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. {ECO:0000250|UniProtKB:P22888}. | Sus scrofa (Pig) |
P16591 | FER_HUMAN | MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQ... | 2.7.10.2 | null | actin cytoskeleton organization [GO:0030036]; adherens junction assembly [GO:0034333]; adherens junction disassembly [GO:0120179]; cell adhesion [GO:0007155]; cell-cell adhesion mediated by cadherin [GO:0044331]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to react... | adherens junction [GO:0005912]; cell cortex [GO:0005938]; cell projection [GO:0042995]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; epidermal growth factor receptor binding [GO:0005154]; lipid binding [GO:0008289]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein phosphatase 1 binding [GO:0008157]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | PTM: Autophosphorylated. {ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21518868}.; PTM: Polyubiquitinated; this leads to proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Note=Associated with the chromatin. Detected on microtubules in polarized and ... | 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=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream o... | Homo sapiens (Human) |
P16598 | IL1A_RAT | MAKVPDLFEDLKNCYSENEEYSSAIDHLSLNQKSFYDASYGSLHENCTDKFVSLRTSETSKMSTFTFKESRVVVSATSNKGKILKKRRLSFNQPFTEDDLEAIAHDLEETIQPRSAPHSFQNNLRYKLIRIVKQEFIMNDSLNQNIYVDMDRIHLKAASLNDLQLEVKFDMYAYSSGGDDSKYPVTLKVSNTQLFVSAQGEDKPVLLKEIPETPKLITGSETDLIFFWEKINSKNYFTSAAFPELLIATKEQSQVHLARGLPSMIDFQIS | null | null | cellular response to heat [GO:0034605]; cellular response to lipopolysaccharide [GO:0071222]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; cytokine-mediated signaling pathway [GO:0019221]; ectopic germ cell programmed cell death [GO:0035234]; extrinsic apoptotic signaling ... | cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | copper ion binding [GO:0005507]; cytokine activity [GO:0005125]; interleukin-1 receptor binding [GO:0005149] | PF00340;PF02394; | 2.80.10.50; | IL-1 family | PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000250|UniProtKB:P01583}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000250|UniProtKB:P01583}.; PTM: Phosphorylat... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that use... | null | null | null | null | null | FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 r... | Rattus norvegicus (Rat) |
P16599 | TNFA_RAT | MSTESMIRDVELAEEALPKKMGGLQNSRRCLCLSLFSFLLVAGATTLFCLLNFGVIGPNKEEKFPNGLPLISSMAQTLTLRSSSQNSSDKPVAHVVANHQAEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLIYSQVLFKGQGCPDYVLLTHTVSRFAISYQEKVSLLSAIKSPCPKDTPEGAELKPWYEPMYLGGVFQLEKGDLLSAEVNLPKYLDITESGQVYFGVIAL | null | null | animal organ morphogenesis [GO:0009887]; antiviral innate immune response [GO:0140374]; apoptotic signaling pathway [GO:0097190]; calcium-mediated signaling [GO:0019722]; cellular extravasation [GO:0045123]; cellular response to amino acid stimulus [GO:0071230]; cellular response to amyloid-beta [GO:1904646]; cellular ... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | cytokine activity [GO:0005125]; death receptor agonist activity [GO:0038177]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; receptor ligand activity [GO:0048018]; transcription cis-regulatory region binding [GO:0000976]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secre... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:00... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain c... | Rattus norvegicus (Rat) |
P16603 | NCPR_YEAST | MPFGIDNTDFTVLAGLVLAVLLYVKRNSIKELLMSDDGDITAVSSGNRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADVENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLRYNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDYMAWKDSILEVLKDELHLDEQEAKFTSQFQYTVLNEITDSMSLGEPSAHYLPSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSSNDRNCIHSEFDLSGSNIKYSTGDHLAVWPSNPLEKVEQ... | 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:9468503}; Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:9468503}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:94685... | ergosterol biosynthetic process [GO:0006696]; response to hormone [GO:0009725] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADP binding [GO:0050661]; NADPH dehydrogenase activity [GO:0003959]; NADPH-hemoprotein reductase activity [GO:0003958] | PF00667;PF00258;PF00175; | 3.40.50.360;3.40.50.80;2.40.30.10; | NADPH--cytochrome P450 reductase family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family | PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85. {ECO:0000269|PubMed:15082539}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9468503}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212, ECO... | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.59 uM for cytochrome c {ECO:0000269|PubMed:11485306}; KM=1.46 uM for NADPH {ECO:0000269|PubMed:11485306}; Note=The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH. {ECO:0000269|PubMed:11485306}; | null | null | null | FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane. {ECO:0000255|HAMAP-Rule:MF_03212, ECO:00... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16604 | POLG_SVDVH | MGAQVSTQKTGAHETSLSAAGNSVIHYTNINYYKDAASNSANRQDFTQDPGKFTEPVKDIMVKSMPALNSPSAEECGYSDRVRSITLGNSTITTQECANVVVGYGVWPTYLKDEEATAEDQPTQPDVATCRFYTLESVMWQQSSPGWWWKFPDALSNMGLFGQNMQYHYLGRAGYTIHVQCNASKFHQGCLLVVCVPEAEMGCATLANKPDPKSLSKGEIANMFESQNSTGETAVQANVINAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYINSVPMDNMFRHNNFTLMVIPFAPLSYSTGATTYVPITVTVAPMCAE... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Swine vesicular disease virus (strain H/3 '76) (SVDV) |
P16610 | NK2R_RAT | MGTRAIVSDANILSGLESNATGVTAFSMPGWQLALWATAYLALVLVAVTGNATVIWIILAHERMRTVTNYFIINLALADLCMAAFNATFNFIYASHNIWYFGRAFCYFQNLFPITAMFVSIYSMTAIAADRYMAIVHPFQPRLSAPSTKAIIAGIWLVALALASPQCFYSTITVDEGATKCVVAWPNDNGGKMLLLYHLVVFVLIYFLPLLVMFGAYSVIGLTLWKRAVPRHQAHGANLRHLQAKKKFVKAMVLVVLTFAICWLPYHLYFILGTFQEDIYYHKFIQQVYLALFWLAMSSTMYNPIIYCCLNHRFRSGFRL... | null | null | intestine smooth muscle contraction [GO:0014827]; negative regulation of luteinizing hormone secretion [GO:0033685]; operant conditioning [GO:0035106]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of m... | plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; sperm head [GO:0061827]; sperm midpiece [GO:0097225] | substance K receptor activity [GO:0016497] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: This is a receptor for the tachykinin neuropeptide substance K (neurokinin A). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance K > neuromedin-K > substance P. | Rattus norvegicus (Rat) |
P16612 | VEGFA_RAT | MNFLLSWVHWTLALLLYLHHAKWSQAAPTTEGEQKAHEVVKFMDVYQRSYCRPIETLVDIFQEYPDEIEYIFKPSCVPLMRCAGCCNDEALECVPTSESNVTMQIMRIKPHQSQHIGEMSFLQHSRCECRPKKDRTKPEKKSVRGKGKGQKRKRKKSRFKSWSVHCEPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR | null | null | angiogenesis [GO:0001525]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; apoptotic process [GO:0006915]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; blood vessel remodeling [GO:0001974]; bone trabecula formation [GO:0060346]... | adherens junction [GO:0005912]; basement membrane [GO:0005604]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]; secretory granule [GO:0030141]; VEGF-A complex [GO:1990150]; vesicle [GO:0031982] | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; fibronectin binding [GO:0001968]; growth factor activity [GO:0008083]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; platelet-derived growth factor receptor binding [GO:0005161]; receptor l... | PF00341;PF14554; | 2.10.90.10;2.10.160.10; | PDGF/VEGF growth factor family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=VEGF-A120 is acidic and freely secreted. VEGF-A164 is more basic, has heparin-binding properties and, although a significant proportion remains cell-associated, most is freely secreted. VEGF-A188 is very basic, it is cell-associated after secretion and is bound avidly ... | null | null | null | null | null | FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. May play a role i... | Rattus norvegicus (Rat) |
P16613 | PACA_SHEEP | MTMCSGARLALLVYGILMHSSVYGSPAASGLRFPGIRPENEAYDEDGNPQQDFYDSEPPGVGSPASALRDAYALYYPAEERDVAHGILDKAYRKVLDQLSARRYLQTLMAKGLGGTPGGGADDDSEPLSKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIPYL | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP-mediated signaling [GO:0019933]; insulin secretion [GO:0030073]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; ... | extracellular region [GO:0005576]; neuron projection [GO:0043005]; perikaryon [GO:0043204] | neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; pituitary adenylate cyclase activating polypeptide activity [GO:0016521] | PF00123; | 6.10.250.590; | Glucagon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and ne... | Ovis aries (Sheep) |
P16615 | AT2A2_HUMAN | MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 7.2.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607}; | autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cardiac muscle hypertrophy in response to stress [GO:... | calcium ion-transporting ATPase complex [GO:0090534]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; longitudinal sarcoplasmic reticulum [GO:0014801]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet dense tubular network membrane [GO:0031095]; ribbon synapse [GO:0097470];... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; lncRNA binding [GO:0106222]; P-type calcium transporter activity [GO:0005388]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039];... | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000269|PubMed:16399855}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12804600}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|Un... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:28890335}; PhysiologicalDirection=left-to-right; ... | null | null | null | null | FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation m... | Homo sapiens (Human) |
P16617 | PGK1_RAT | MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAAELKSLLGKDVLFLKDCVGSEVENACANPAAGTVILLENLRFHVEEEGKGKDASGNKVKAEPAKIDAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLYDEEGAKIVKDLMAKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGTES... | 2.7.2.3 | null | canonical glycolysis [GO:0061621]; cellular response to hypoxia [GO:0071456]; epithelial cell differentiation [GO:0030855]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of angiogenesis [GO:0016525]; phosphorylation [GO:0016310]; plasminogen activation [GO:0031639] | cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane raft [GO:0045121] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618]; protein-disulfide reductase (NAD(P)) activity [GO:0047134] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; Evidence={ECO:0000250|UniProtKB:P00558}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}. | null | null | FUNCTION: Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a rol... | Rattus norvegicus (Rat) |
P16619 | CL3L1_HUMAN | MQVSTAALAVLLCTMALCNQVLSAPLAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPSVIFLTKRGRQVCADPSEEWVQKYVSDLELSA | null | null | cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; eosinophil chemotaxis [GO:0048245]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory r... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: The N-terminal processed forms LD78-beta(3-70) and LD78-beta(5-70) are produced by proteolytic cleavage after secretion from peripheral blood monocytes. The cleavage to yield LD78-beta(3-70) is probably achieved by DPP4. {ECO:0000269|PubMed:10961862}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemotactic for lymphocytes and monocytes. Is a ligand for CCR1, CCR3 and CCR5. Is an inhibitor of HIV-1-infection. The processed form LD78-beta(3-70) shows a 20-fold to 30-fold higher chemotactic activity and is a very potent inhibitor of HIV-1-infection. LD78-beta(3-70) is also a ligand for CCR1, CCR3 and C... | Homo sapiens (Human) |
P16620 | PTP69_DROME | MALLYRRMSMLLNIILAYIFLCAICVQGSVKQEWAEIGKNVSLECASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTCTAQTGQNHSTEFQVRPYLPSKVLQSTPDRIKRKIKQDVMLYCLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKCTVFDDTGLEITSKEITLFVMEVPQVSIDFAKAVGANKIYLNWTVNDGNDPIQKFFITLQEAGTPTFTYHKDFINGSHTSYILDHFKPNTTYFLRIVGKNSIGNGQP... | 3.1.3.48 | null | axon guidance [GO:0007411]; cell adhesion [GO:0007155]; defasciculation of motor neuron axon [GO:0007415]; dendrite morphogenesis [GO:0048813]; fasciculation of sensory neuron axon [GO:0097155]; motor neuron axon guidance [GO:0008045]; peptidyl-tyrosine dephosphorylation [GO:0035335]; synaptic target inhibition [GO:001... | axon [GO:0030424]; cell surface [GO:0009986]; plasma membrane [GO:0005886] | protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00041;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Possible cell adhesion receptor. | Drosophila melanogaster (Fruit fly) |
P16621 | LAR_DROME | MGLQMTAARPIAALSLLVLSLLTWTHPTIVDAAHPPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPVRAGRDDAPYECVAENGVGDAVSADATLTIYEGDKTPAGFPVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKATNLYVKVRRVPPTFSRPPETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQESANYTCIAASTLGQIDSVSVVKVQS... | 3.1.3.48 | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; axon target recognition [GO:0007412]; cell adhesion [GO:0007155]; centripetally migrating follicle cell migration [GO:0060269]; hematopoietic stem cell homeostasis [GO:0061484]; motor neuron axon guidance [GO:0008045]; negative regulation of homophilic cell adhes... | axon [GO:0030424]; basal plasma membrane [GO:0009925]; cell leading edge [GO:0031252]; cell surface [GO:0009986]; focal adhesion [GO:0005925]; receptor complex [GO:0043235] | heparin binding [GO:0008201]; insulin receptor binding [GO:0005158]; protein tyrosine phosphatase activity [GO:0004725]; SAM domain binding [GO:0032093]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00041;PF07679;PF13927;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Possible cell adhesion receptor (Probable). It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) (PubMed:2554325). It controls motor axon guidance (PubMed:8598047). In the developing eye, has a role in normal axonal targeting of the R7 photoreceptor, where it negatively regulates bdl (PubM... | Drosophila melanogaster (Fruit fly) |
P16622 | HEMH_YEAST | MLSRTIRTQGSFLRRSQLTITRSFSVTFNMQNAQKRSPTGIVLMNMGGPSKVEETYDFLYQLFADNDLIPISAKYQKTIAKYIAKFRTPKIEKQYREIGGGSPIRKWSEYQATEVCKILDKTCPETAPHKPYVAFRYAKPLTAETYKQMLKDGVKKAVAFSQYPHFSYSTTGSSINELWRQIKALDSERSISWSVIDRWPTNEGLIKAFSENITKKLQEFPQPVRDKVVLLFSAHSLPMDVVNTGDAYPAEVAATVYNIMQKLKFKNPYRLVWQSQVGPKPWLGAQTAEIAEFLGPKVDGLMFIPIAFTSDHIETLHEID... | 4.98.1.1 | null | heme biosynthetic process [GO:0006783] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ferrochelatase activity [GO:0004325] | PF00762; | 3.40.50.1400; | Ferrochelatase family | PTM: The leader peptide may be processed in two proteolytic steps, first between Ser-23 and Phe-24, second and by a different protease, to yield the mature protein. | SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Note=It is bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane. | CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1; | null | PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. | null | null | FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16627 | HS71L_MOUSE | MAANKGMAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQSDMKLWPFQVINEAGKPKVMVSYKGEKKAFYPEEISSMVLTKMKETAEAFLGHNVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGSHGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVE... | null | null | binding of sperm to zona pellucida [GO:0007339]; cell differentiation [GO:0030154]; chaperone cofactor-dependent protein refolding [GO:0051085]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein refolding [GO:0042026]; spermatogenesis [GO:0007283] | blood microparticle [GO:0072562]; cell body [GO:0044297]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982]; zona pellucida receptor complex [GO:0002199] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | null | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Mus musculus (Mouse) |
P16636 | LYOX_RAT | MRFAWTVLFLGQLQFCPLLRCAPQAPREPPAAPGAWRQTIQWENNGQVFSLLSLGAQYQPQRRRDSSATAPRADGNAAAQPRTPILLLRDNRTASARARTPSPSGVAAGRPRPAARHWFQVGFSPSGAGDGASRRAANRTASPQPPQLSNLRPPSHVDRMVGDDPYNPYKYSDDNPYYNYYDTYERPRSGSRHRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLE... | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:16432278}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:P33072}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250}; | aorta development [GO:0035904]; ascending aorta development [GO:0035905]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; bone mineralization [GO:0030282]; cell chemotaxis [GO:0060326]; cellular response to chemokine [GO:1990869]; cellular response to organic substance [GO:0071310]; coll... | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | collagen binding [GO:0005518]; copper ion binding [GO:0005507]; molecular adaptor activity [GO:0060090]; protein-lysine 6-oxidase activity [GO:0004720]; small molecule binding [GO:0036094] | PF01186; | null | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.; PTM: Proteolytically cleaved by BMP1 which removes the propeptide (By similarity). Also proteolytically cleaved by AD... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28301}. Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:... | null | null | null | null | FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:16432278). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity). {ECO:0000250|UniProtKB:P283... | Rattus norvegicus (Rat) |
P16638 | ACLY_RAT | MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDTKAQKLLVGVDEKLNAEDIKRHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA... | 2.3.3.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53396}; | acetyl-CoA biosynthetic process [GO:0006085]; acetyl-CoA metabolic process [GO:0006084]; citrate metabolic process [GO:0006101]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP citrate synthase activity [GO:0003878]; metal ion binding [GO:0046872] | PF16114;PF00285;PF02629;PF00549; | 3.30.470.110;1.10.580.10;1.10.230.10;3.40.50.720;3.40.50.261; | Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family | PTM: Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity (By similarity). Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454 (PubMed:12107176, PubMed:2176822). Phosphorylation on Ser-454 is decreased by prior phosphorylation on... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53396}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8; Evidence={ECO:0000269|PubMed:9116495}; PhysiologicalDire... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=155 uM for citrate {ECO:0000269|PubMed:9116495}; KM=103 uM for ATP {ECO:0000269|PubMed:9116495}; KM=15 uM for CoA {ECO:0000269|PubMed:9116495}; Vmax=1.9 umol/h/ug enzyme {ECO:0000269|PubMed:9116495}; | null | null | null | FUNCTION: Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis. {ECO:0000269|PubMed:9116495}. | Rattus norvegicus (Rat) |
P16646 | PMP22_MOUSE | MLLLLLGILFLHIAVLVLLFVSTIVSQWLVGNGHTTDLWQNCTTSALGAVQHCYSSSVSEWLQSVQATMILSVIFSVLALFLFFCQLFTLTKGGRFYITGFFQILAGLCVMSAAAIYTVRHSEWHVNTDYSYGFAYILAWVAFPLALLSGIIYVILRKREL | null | null | actin cytoskeleton organization [GO:0030036]; adult locomotory behavior [GO:0008344]; adult walking behavior [GO:0007628]; aggresome assembly [GO:0070842]; autophagy [GO:0006914]; axon development [GO:0061564]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differ... | bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; compact myelin [GO:0043218]; integrin complex [GO:0008305]; laminin complex [GO:0043256]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | cytoskeletal motor activity [GO:0003774] | PF00822; | 1.20.140.150; | PMP-22/EMP/MP20 family | PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation. {ECO:0000269|PubMed:35178836}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01453}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01453}. | null | null | null | null | null | FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. | Mus musculus (Mouse) |
P16649 | TUP1_YEAST | MTASVSNTQNKLNELLDAIRQEFLQVSQEANTYRLQNQKDYDFKMNQQLAEMQQIRNTVYELELTHRKMKDAYEEEIKHLKLGLEQRDHQIASLTVQQQRQQQQQQQVQQHLQQQQQQLAAASASVPVAQQPPATTSATATPAANTTTGSPSAFPVQASRPNLVGSQLPTTTLPVVSSNAQQQLPQQQLQQQQLQQQQPPPQVSVAPLSNTAINGSPTSKETTTLPSVKAPESTLKETEPENNNTSKINDTGSATTATTTTATETEIKPKEEDATPASLHQDHYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTND... | null | null | carbon catabolite repression of transcription from RNA polymerase II promoter by glucose [GO:0000433]; DNA damage response [GO:0006974]; hyperosmotic response [GO:0006972]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive r... | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; mediator complex binding [GO:0036033]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; transcription corepressor activity [GO:0003714] | PF08581;PF00400; | 1.20.5.340;2.130.10.10; | WD repeat TUP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Acts as a component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16655 | DIVIB_BACSU | MNPGQDREKIVNIEERIPKIKEQRKQKANRRLISFIMLFFIMVLIIVYLQTPISKVSTISVTGNENVSKKEIIDLSDINSGDTEFWSLDKQKTEKKIQQNKLVKKAEISKSLPNKINIAIEEYKAIAYLEKDDVYYEVLENGSVLPNEVTPDDAGPILVNWTNAKKRSQMAKQLDALSNSLKQSISEIYYTPVKMDENRIKLYMNDGYVVTASIKTFADRMKTYPSIISQLSSNKKGIIHLEVATYFEEFGKNDKAAKKEDEN | null | null | FtsZ-dependent cytokinesis [GO:0043093]; sporulation resulting in formation of a cellular spore [GO:0030435] | cell division site [GO:0032153]; plasma membrane [GO:0005886] | null | PF03799;PF08478; | 3.40.50.10960;3.10.20.310; | FtsQ/DivIB family, DivIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00912, ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00912, ECO:0000269|PubMed:10852898, ECO:0000269|PubMed:18208530}. Note=Localizes to the division septum. Localization requires ... | null | null | null | null | null | FUNCTION: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. Plays an essential role in division at high temperatures, maybe by protecting FtsL from degradation or by promoting formation of the FtsL-DivIC complex. May modulate the transpeptidase activity of PBP-... | Bacillus subtilis (strain 168) |
P16658 | SEN2_YEAST | MSKGRVNQKRYKYPLPIHPVDDLPELILHNPLSWLYWAYRYYKSTNALNDKVHVDFIGDTTLHITVQDDKQMLYLWNNGFFGTGQFSRSEPTWKARTEARLGLNDTPLHNRGGTKSNTETEMTLEKVTQQRRLQRLEFKKERAKLERELLELRKKGGHIDEENILLEKQRESLRKFKLKQTEDVGIVAQQQDISESNLRDEDNNLLDENGDLLPLESLELMPVEAMFLTFALPVLDISPACLAGKLFQFDAKYKDIHSFVRSYVIYHHYRSHGWCVRSGIKFGCDYLLYKRGPPFQHAEFCVMGLDHDVSKDYTWYSSIA... | 4.6.1.16 | null | tRNA-type intron splice site recognition and cleavage [GO:0000379] | endomembrane system [GO:0012505]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; tRNA-intron endonuclease complex [GO:0000214] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; tRNA-intron endonuclease activity [GO:0000213] | PF01974; | 3.40.1350.10; | TRNA-intron endonuclease family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12925762}. Endomembrane system {ECO:0000269|PubMed:12925762}; Peripheral membrane protein {ECO:0000269|PubMed:12925762}. Mitochondrion outer membrane {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:12925762, EC... | CATALYTIC ACTIVITY: Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16; | null | null | null | null | FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearin... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16659 | SYP_ECOLI | MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRNELSSYKQLPLNFYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVVFSDTSDYAANIELAEAIAPKEPRAAATQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAVEGSSFPQVALLVRGDHELNEVKAEKLPQVASPLT... | 6.1.1.15 | null | aminoacyl-tRNA metabolism involved in translational fidelity [GO:0106074]; prolyl-tRNA aminoacylation [GO:0006433] | cytosol [GO:0005829] | Ala-tRNA(Pro) hydrolase activity [GO:0043906]; ATP binding [GO:0005524]; proline-tRNA ligase activity [GO:0004827] | PF03129;PF00587;PF04073; | 3.40.50.800;3.90.960.10; | Class-II aminoacyl-tRNA synthetase family, ProS type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215; EC=6.1.1.15; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for proline {ECO:0000269|PubMed:10922054, ECO:0000269|PubMed:11408489, ECO:0000269|PubMed:12130657}; KM=140 mM for alanine {ECO:0000269|PubMed:10922054, ECO:0000269|PubMed:11408489, ECO:0000269|PubMed:12130657}; KM=0.17 mM for cysteine {ECO:0000269|PubMed:1... | null | null | null | FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has... | Escherichia coli (strain K12) |
P16661 | ALG1_YEAST | MFLEIPRWLLALIILYLSIPLVVYYVIPYLFYGNKSTKKRIIIFVLGDVGHSPRICYHAISFSKLGWQVELCGYVEDTLPKIISSDPNITVHHMSNLKRKGGGTSVIFMVKKVLFQVLSIFKLLWELRGSDYILVQNPPSIPILPIAVLYKLTGCKLIIDWHNLAYSILQLKFKGNFYHPLVLISYMVEMIFSKFADYNLTVTEAMRKYLIQSFHLNPKRCAVLYDRPASQFQPLAGDISRQKALTTKAFIKNYIRDDFDTEKGDKIIVTSTSFTPDEDIGILLGALKIYENSYVKFDSSLPKILCFITGKGPLKEKYMK... | 2.4.1.142 | null | oligosaccharide-lipid intermediate biosynthetic process [GO:0006490]; protein glycosylation [GO:0006486]; protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | beta-1,4-mannosyltransferase activity [GO:0019187]; chitobiosyldiphosphodolichol beta-mannosyltransferase activity [GO:0004578]; mannosyltransferase activity [GO:0000030] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 33 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29939232}; Single-pass membrane protein {ECO:0000269|PubMed:29939232}. | CATALYTIC ACTIVITY: Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865, Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:5818... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:15044395, ECO:0000269|PubMed:29939232}. | null | null | FUNCTION: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER. {ECO:0000269|PubMed:15044395, ECO:0000269|PubMed:29939232}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16662 | UD2B7_HUMAN | MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEER... | 2.4.1.17 | null | androgen metabolic process [GO:0008209]; cellular glucuronidation [GO:0052695]; estrogen metabolic process [GO:0008210]; lipid metabolic process [GO:0006629]; xenobiotic metabolic process [GO:0006805] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | glucuronosyltransferase activity [GO:0015020] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10702251}; 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:10702251, ECO:0000269|PubMed:15470161... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:15472229}; KM=33 uM for the formation of 2-hydroxy-17beta-estradiol (when assaying glucuronidation at position 2) {ECO:0000269|PubMed:15472229}; KM=33 uM for 2-h... | 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:10702251, PubMed:15470161, PubMed:1547222... | Homo sapiens (Human) |
P16664 | RGP1_YEAST | MRAHRIDTFLIRENIKLEIIHESNSYFGGEHISIAFRFKHLGSQHELFNYKEKLLTVDKAVEEKLEQQAKVQDDGEGTMENQTWSLKSLLGAFKRTGEPEESVDVDNMKMLNESKMLREKIQKQMYFHQPVTLISGYVQISGVFQYDSEVISESKFKQDEVKMVGLDIVPGHTTNSVLALEDGEHFKGKRNLTNYLNSDYTNVTNGLLFSESGSRGRTGTYNERTLMISNDTSIKTLPLLLIPQTLLFSEISLEPGEVRTFYFKSTKLPKDICPSYSSSKVASINYTLEVGADVLSDDNIEKFSNRVPITIAPYISSNAE... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; retrograde transport, endosome to Golgi [GO:0042147] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; guanyl-nucleotide exchange factor complex [GO:0032045]; Ric1-Rgp1 guanyl-nucleotide exchange factor complex [GO:0034066] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF08737; | null | RGP1 family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11689439}. | null | null | null | null | null | FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of e... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16671 | CD36_HUMAN | MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISK... | null | null | amyloid fibril formation [GO:1990000]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; apoptotic cell clearance [GO:0043277]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to amyloid-beta [GO:1904646]; cellular resp... | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; caveola [GO:0005901]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endocytic vesicle membrane [GO:0030666]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:000... | amyloid-beta binding [GO:0001540]; fatty acid binding [GO:0005504]; high-density lipoprotein particle binding [GO:0008035]; lipid binding [GO:0008289]; lipoprotein particle binding [GO:0071813]; lipoteichoic acid immune receptor activity [GO:0070892]; long-chain fatty acid transporter activity [GO:0005324]; low-density... | PF01130; | null | CD36 family | PTM: N-glycosylated and O-glycosylated with a ratio of 2:1. {ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2468669}.; PTM: Palmitoylated by ZDHHC5 (PubMed:32958780). Palmitoylation is required for proper localization at the plasma membrane (PubMed:32958780, Pu... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:32958780, ECO:0000269|PubMed:37461827}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:16880211}. Golgi apparatus {ECO:0000269|PubMed:16880211}. Apical cell membrane {ECO:0000250|UniProtKB:Q08857}. Note=Up... | CATALYTIC ACTIVITY: Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248, ChEBI:CHEBI:17968; Evidence={ECO:0000269|PubMed:21395585}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249; Evidence={ECO:0000269|PubMed:21395585}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);... | null | null | null | null | FUNCTION: Multifunctional glycoprotein that acts as a receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and ... | Homo sapiens (Human) |
P16675 | PPGB_MOUSE | MPGTALSPLLLLLLLSWASRNEAAPDQDEIDCLPGLAKQPSFRQYSGYLRASDSKHFHYWFVESQNDPKNSPVVLWLNGGPGCSSLDGLLTEHGPFLIQPDGVTLEYNPYAWNLIANVLYIESPAGVGFSYSDDKMYVTNDTEVAENNYEALKDFFRLFPEYKDNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLASYEQNDNSLVYFAYYHGLLGNRLWTSLQTHCCAQNKCNFYDNKDPECVNNLLEVSRIVGKSGLNIYNLYAPCAGGVPGRHRYEDTLVVQDFGNIFTRLPLKRRFPEALMRSGDKVR... | 3.4.16.5 | null | negative regulation of chaperone-mediated autophagy [GO:1904715]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647] | lysosome [GO:0005764]; mitochondrion [GO:0005739] | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.1820; | Peptidase S10 family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074, ECO:0000255|PROSITE-ProRule:PRU10075}; | null | null | null | null | FUNCTION: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. | Mus musculus (Mouse) |
P16686 | PHNH_ECOLI | MTLETAFMLPVQDAQHSFRRLLKAMSEPGVIVALHQLKRGWQPLNIATTSVLLTLADNDTPVWLSTPLNNDIVNQSLRFHTNAPLVSQPEQATFAVTDEAISSEQLNALSTGTAVAPEAGATLILQVASLSGGRMLRLTGAGIAEERMIAPQLPECILHELTERPHPFPLGIDLILTCGERLLAIPRTTHVEVC | 2.7.8.37 | null | organic phosphonate catabolic process [GO:0019700]; organic phosphonate metabolic process [GO:0019634]; organic phosphonate transport [GO:0015716] | alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex [GO:0061694]; carbon phosphorus lyase complex [GO:1904176] | alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity [GO:0061693]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF05845; | 3.40.50.11310; | PhnH family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate; Xref=Rhea:RHEA:34679, ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:68684, ChEBI:CHEBI:68823; EC=2.7.8.37; Evidence={ECO:0000269|PubMed:22089136}; | null | null | null | null | FUNCTION: Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. {ECO:0000269|PubMed:22089136}. | Escherichia coli (strain K12) |
P16687 | PHNI_ECOLI | MYVAVKGGEKAIDAAHALQESRRRGDTDLPELSVAQIEQQLNLAVDRVMTEGGIADRELAALALKQASGDNVEAIFLLRAYRTTLAKLAVSEPLDTTGMRLERRISAVYKDIPGGQLLGPTYDYTHRLLDFTLLANGEAPTLTTADSEQQPSPHVFSLLARQGLAKFEEDSGAQPDDITRTPPVYPCSRSSRLQQLMRGDEGYLLALAYSTQRGYGRNHPFAGEIRSGYIDVSIVPEELGFAVNVGELLMTECEMVNGFIDPPGEPPHFTRGYGLVFGMSERKAMAMALVDRALQAPEYGEHATGPAQDEEFVLAHADNV... | 2.7.8.37 | null | organic phosphonate catabolic process [GO:0019700]; organic phosphonate metabolic process [GO:0019634]; organic phosphonate transport [GO:0015716] | alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex [GO:0061694]; carbon phosphorus lyase complex [GO:1904176] | alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity [GO:0061693] | PF05861; | null | PhnI family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate; Xref=Rhea:RHEA:34679, ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:68684, ChEBI:CHEBI:68823; EC=2.7.8.37; Evidence={ECO:0000269|PubMed:22089136}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = adenine + D-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for GTP (in the presence of PhnI alone) {ECO:0000269|PubMed:22089136}; KM=95 uM for ATP (in the presence of PhnI alone) {ECO:0000269|PubMed:22089136}; KM=80 uM for GTP (in the presence of PhnI, PhnG, PhnH and PhnL) {ECO:0000269|PubMed:22089136}; KM=56 uM for ... | null | null | null | FUNCTION: Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively. {ECO:0000269|PubMed:2208913... | Escherichia coli (strain K12) |
P16688 | PHNJ_ECOLI | MANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTGGIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDATVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYGVMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPALQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYLDEVVLDDAGNRMFVCSDTDYCRQQSEAKNQ | 4.7.1.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:22089136}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:22089136}; | organic phosphonate catabolic process [GO:0019700]; organic phosphonate metabolic process [GO:0019634]; organic phosphonate transport [GO:0015716] | alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex [GO:0061694]; carbon phosphorus lyase complex [GO:1904176] | 4 iron, 4 sulfur cluster binding [GO:0051539]; alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity [GO:0098848]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF06007; | null | PhnJ family | null | null | CATALYTIC ACTIVITY: Reaction=AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine = 5'-deoxyadenosine + A + alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H(+) + L-methionine + methane; Xref=Rhea:RHEA:34707, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:16183, ChEBI:CHEBI:17319, ChEBI:C... | null | null | null | null | FUNCTION: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP). {ECO:0000269|PubMed:22089136}. | Escherichia coli (strain K12) |
P16692 | PHNP_ECOLI | MSLTLTLTGTGGAQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGLHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNNQPQVMVMDCSHPPRADAPRNHCDLNTVLALNQVIRSPRVILTHISHQFDAWLMENALPSGFEVGFDGMEIGVA | 3.1.4.55 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19366688}; Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:19366688}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19366688}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19366688}; | organic phosphonate catabolic process [GO:0019700] | null | 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase activity [GO:0103043]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803] | PF12706; | 3.60.15.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H2O = alpha-D-ribose 1,5-bisphosphate + H(+); Xref=Rhea:RHEA:34795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:68687, ChEBI:CHEBI:68688; EC=3.1.4.55; Evidence={ECO:0000269|PubMed:21341651}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate. {ECO:0000269|PubMed:19366688, ECO:0000269|PubMed:21341651}. | Escherichia coli (strain K12) |
P16703 | CYSM_ECOLI | MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTEYLPGIFNASLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDRGDRYLSTGVFGEEHFSQGAGI | 2.5.1.47 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | cysteine biosynthetic process [GO:0019344]; cysteine biosynthetic process from serine [GO:0006535]; cysteine biosynthetic process via S-sulfo-L-cysteine [GO:0019345]; iron-sulfur cluster assembly [GO:0016226]; L-cysteine catabolic process to pyruvate [GO:0019450] | cytoplasm [GO:0005737] | cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; | null | PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. | null | null | FUNCTION: Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | Escherichia coli (strain K12) |
P16710 | PG143_VACCW | MGAAVTLNRIKIAPGIADIRDKYMELGFNYPEYNRAVKFAEESYTYYYETSPGEIKPKFCLIDGMSIDHCSSFIVPEFAKQYVLIHGEPCSSFKFRPGSLIYYQNEVTPEYIKDLKHATDYIASGQRCHFIKKDYLLGDSDSVAKCCSKTNTKHCPKIFNNNYKTEHCDDFMTGFCRNDPGNPNCLEWLRAKRKPAMSTYSDICSKHMDARYCSEFIRIIRPDYFTFGDTALYVFCNDHKGNRNCWCANYPKSNSGDKYLGPRVCWLHECTDESRDRKWLYYNQDVQRTRCKYVGCTINVNSLALKNSQAELTSNCTRTT... | null | null | DNA-templated transcription termination [GO:0006353]; membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787] | PF03003; | null | Orthopoxvirus OPG143 family | PTM: Most cysteines are linked by disulfide bonds. They are created by the viral disulfide bond formation pathway, a poxvirus-specific redox pathway that operates on the cytoplasmic side of the MV membranes. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Component of the mature virion (MV) membrane (Probable). The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. {ECO:0000269|PubMed:9188589, ECO:0000305}. | null | null | null | null | null | FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation). {ECO:0000269|PubMed:16352530, ECO:0000269|PubMed:22278246}. | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P16753 | SCAF_HCMVA | MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACDIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAE... | 3.4.21.97 | null | proteolysis [GO:0006508]; viral release from host cell [GO:0019076] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252] | PF00716; | 3.20.16.10; | Herpesviridae capsid scaffolding protein family | PTM: Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release and tail site. {ECO:0000255|HAMAP-Rule:MF_04008}. | SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}. | CATALYTIC ACTIVITY: Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008}; | null | null | null | null | FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and s... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P16766 | UL35_HCMVA | MAQGSRAPSGPPLPVLPVDDWLNFRVDLFGDEHRRLLLEMLTQGCSNFVGLLNFGVPSPVYALEALVDFQVRNAFMKVKPVAQEIIRICILANHYRNSRDVLRDLRTQLDVLYSDPLKTRLLRGLIRLCRAAQTGVKPEDISVHLGADDVTFGVLKRALVRLHRVRDALGLRASPEAEARYPRLTTYNLLFHPPPFTTVEAVDLCAENLSDVTQRRNRPLRCLTSIKRPGSRTLEDALNDMYLLLTLRHLQLRHALELQMMQDWVVERCNRLCDALYFCYTQAPETRQTFVTLVRGLELARQHSSPAFQPMLYNLLQLLT... | null | null | DNA-templated viral transcription [GO:0039695]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virus-mediated perturbation of host defe... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | null | PF04637; | null | Herpesviridae pp85 family | null | SUBCELLULAR LOCATION: [Isoform UL35]: Virion tegument {ECO:0000269|PubMed:15452216}. Host nucleus {ECO:0000269|PubMed:11836424, ECO:0000269|PubMed:21489587, ECO:0000269|PubMed:22072767, ECO:0000269|PubMed:32466380}. Host cytoplasm {ECO:0000269|PubMed:21489587, ECO:0000269|PubMed:32466380}. Note=Found in nuclear bodies.... | null | null | null | null | null | FUNCTION: [Isoform UL35]: Plays important role in immediate-early gene expression through interaction with UL82. Forms nuclear bodies in host nucleus, independently of PML. In turn, UL35 nuclear bodies associate with and remodel PML bodies (PubMed:21489587, PubMed:22072767). Through interaction with host DCAF1, causes ... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P16778 | VGLI_HCMVA | MSPVYVNLLGSVGLLAFWYFSYRWIQRKRLEDPLPPWLRKKKACALTRRSRHRLRRQHGVIDGENSETERSVDLVAALLAEAGEESVTEDTEREDTEEEREDEEEENEARTPEVNPIDAEGLSGLAREACEALKKALRRHRFLWQRRQRARMLQHNGPQQSHHAAVFCRVHGLRGFQVSVWLLLTLLWSTGHGVSVRCTYHGTDVNRTSNTTSMNCHLNCTRNHTQIYNGPCLGTEARLPLNVTFNQSRRKWHSVMLKFGFQYHLEGWFPLRVLNESREINVTEVHGEVACFRNDTNVTVGQLTLNFTGHSYVLRAIAHT... | null | null | null | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrial membrane [GO:0044191]; host cell peroxisome [GO:0120149]; membrane [GO:0016020] | null | PF07413; | null | Immediate early glycoprotein family | null | SUBCELLULAR LOCATION: [Isoform gpUL37]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane protein {ECO:0000255}. Host Golgi apparatus membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000269|PubMed:20504938}; Single-... | null | null | null | null | null | FUNCTION: [Isoform vMIA]: Multifunctional transmembrane protein that plays several key roles in viral replication. Rapidely traffics from the host endoplasmic reticulum to the outer mitochondrial membrane where it acts to inhibit host immune response, block apoptotic signaling, regulate calcium flux, and induce mitocho... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P16788 | UL97_HCMVA | MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDF... | 2.7.11.1 | null | phosphorylation [GO:0016310]; viral process [GO:0016032] | virion component [GO:0044423] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF06734; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, HCMV ganciclovir subfamily | PTM: Autophosphorylates on serine and threonine residues. {ECO:0000269|PubMed:10196346, ECO:0000269|PubMed:31548682}. | SUBCELLULAR LOCATION: Virion. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:25339763}; CATALYTIC... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that plays important roles in several processes including nuclear viral egress, viral replication or regulation of host cell cycle progression (PubMed:25339763, PubMed:31291580, PubMed:31548682). Participates in the acquisition of tegument during virion morphogenesis in the nuc... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P16790 | VPAP_HCMVA | MDRKTRLSEPPTLALRLKPYKTAIQQLRSVIRALKENTTVTFLPTPSLILQTVRSHCVSKITFNSSCLYITDKSFQPKTINNSTPLLGNFMYLTSSKDLTKFYVQDISDLSAKISMCAPDFNMEFSSACVHGQDIVRESENSAVHVDLDFGVVADLLKWIGPHTRVKRNVKKAPCPTGTVQILVHAGPPAIKFILTNGSELEFTANNRVSFHGVKNMRINVQLKNFYQTLLNCAVTKLPCTLRIVTEHDTLLYVASRNGLFAVENFLTEEPFQRGDPFDKNYVGNSGKSRGGGGGGGSLSSLANAGGLHDDGPGLDNDLM... | null | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication [GO:0006260]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nucleus [GO:0042025]; virion component [GO:0044423] | DNA binding [GO:0003677]; DNA polymerase processivity factor activity [GO:0030337] | PF03325; | 3.70.10.10; | Herpesviridae polymerase accessory protein family | PTM: Phosphorylated by UL97 on serine residues, phosphorylation seems important for UL44 nuclear entry but does not directly affect its role in replication. {ECO:0000269|PubMed:21784501}.; PTM: Sumoylated. Sumoylation on Lys-410 increases viral DNA replication. {ECO:0000269|PubMed:33967989}. | SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000269|PubMed:20739543, ECO:0000269|PubMed:21784501, ECO:0000269|PubMed:30867312}. | null | null | null | null | null | FUNCTION: Accessory subunit of the DNA polymerase that plays an essential role in viral DNA replication and acts by increasing the processivity of polymerization (PubMed:20538862, PubMed:20739543, PubMed:33967989). Forms dimers that binds to double-stranded DNA and UL54 specifically to stimulates long chain DNA synthes... | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P16853 | GP_HANTL | MGIWKWLVMASLVWPVLTLRNVYDMKIECPHTVSFGENSVIGYVELPPMPLADTAQLVPESSCSMDNHQSLNTITKYTQVSWRGKADQSQSSQTSFETVSTEVDLKGTCVLKHKMVEESYRSRKSITCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERTYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEETATYSIVGPANAKVPHSASSDTLSLIAFSGIP... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; signal transduction [GO:0007165]; symbiont-mediated suppression of host TRAF-mediated signal transduction [GO:0039527]; virion attachment to host cell [GO:0019062]; virus-mediated perturba... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase. {ECO:0000250|UniProtKB:P08668}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum memb... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity)... | Hantaan virus (strain Lee) (Lee virus) (Korean hemorrhagic fever virus) |
P16858 | G3P_MOUSE | MVKVGVNGFGRIGRLVTRAAICSGKVEIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPTNIKWGEAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSN... | 1.2.1.12; 2.6.99.- | null | cAMP-mediated signaling [GO:0019933]; canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycolytic process [GO:0006096]; innate immune response [GO:0045087]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of translatio... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; glutamatergic synapse [GO:0098978]; late endosome lumen [GO:0031906]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density, intracel... | enzyme binding [GO:0019899]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with ph... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with C... | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PR... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:19903941). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceral... | Mus musculus (Mouse) |
P16860 | ANFB_HUMAN | MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH | null | null | blood vessel diameter maintenance [GO:0097746]; body fluid secretion [GO:0007589]; cardiac conduction system development [GO:0003161]; cell surface receptor signaling pathway [GO:0007166]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; negative regulation of angiogenesis [GO:0016525]; neg... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | diuretic hormone activity [GO:0008613]; hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; signaling receptor binding [GO:0005102] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-102 to produce brain natriuretic peptide 32 and NT-proBNP (PubMed:10880574, PubMed:20489134, PubMed:21314817, PubMed:21482747, PubMed:21763278). This likely occurs after it has been secreted into the blood, either during c... | SUBCELLULAR LOCATION: [NT-proBNP]: Secreted {ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:25339504}. Note=Detected in blood. {ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:25339504}.; SUBCELLULAR LOCATION: [proBNP(3-108)]: Secreted {ECO:0000269|PubMed:17367664}. Note=Detected in blood. {ECO:0000269|PubMed:17367664... | null | null | null | null | null | FUNCTION: [Brain natriuretic peptide 32]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed:1672777, PubMed:17372040, PubMed:1914098, PubMed:9458824). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to... | Homo sapiens (Human) |
P16861 | PFKA1_YEAST | MQSQDSCYGVAFRSIITNDEALFKKTIHFYHTLGFATVKDFNKFKHGENSLLSSGTSQDSLREVWLESFKLSEVDASGFRIPQQEATNKAQSQGALLKIRLVMSAPIDETFDTNETATITYFSTDLNKIVEKFPKQAEKLSDTLVFLKDPMGNNITFSGLANATDSAPTSKDAFLEATSEDEIISRASSDASDLLRQTLGSSQKKKKIAVMTSGGDSPGMNAAVRAVVRTGIHFGCDVFAVYEGYEGLLRGGKYLKKMAWEDVRGWLSEGGTLIGTARSMEFRKREGRRQAAGNLISQGIDALVVCGGDGSLTGADLFRH... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453] | 6-phosphofructokinase complex [GO:0005945]; cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365;PF18468; | 3.10.180.90;3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:18313953}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16962558}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:6219673}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for ATP (without effector) {ECO:0000269|PubMed:6219673}; KM=0.3 mM for ATP (with 1 mM AMP) {ECO:0000269|PubMed:6219673}; KM=0.31 mM for ATP (with 20 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:6219673}; KM=1.65 mM for fructose 6-phosphate (without eff... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11221662, ECO:0000269|PubMed:147195, ECO:0000269|PubMed:3000145, ECO:0000269|PubMed:3007939, ECO:0000269|PubMed:6211191, EC... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16862 | PFKA2_YEAST | MTVTTPFVNGTSYCTVTAYSVQSYKAAIDFYTKFLSLENRSSPDENSTLLSNDSISLKILLRPDEKINKNVEAHLKELNSITKTQDWRSHATQSLVFNTSDILAVKDTLNAMNAPLQGYPTELFPMQLYTLDPLGNVVGVTSTKNAVSTKPTPPPAPEASAESGLSSKVHSYTDLAYRMKTTDTYPSLPKPLNRPQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVMEGYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEFKKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEWPSLIEE... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; vacuolar acidification [GO:0007035]; vacuolar proto... | 6-phosphofructokinase complex [GO:0005945]; cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]; mRNA binding [GO:0003729] | PF00365; | 3.40.50.450;3.10.180.10;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:18313953}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16962558}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:6219673}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for ATP (without effector) {ECO:0000269|PubMed:6219673}; KM=0.3 mM for ATP (with 1 mM AMP) {ECO:0000269|PubMed:6219673}; KM=0.31 mM for ATP (with 20 uM fructose 2,6-bisphosphate) {ECO:0000269|PubMed:6219673}; KM=1.65 mM for fructose 6-phosphate (without eff... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11221662, ECO:0000269|PubMed:3000145, ECO:0000269|PubMed:3007939, ECO:0000269|PubMed:40590, ECO:0000269|PubMed:6211191, ECO... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16863 | CXA1_XENLA | MGDWSALGRLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFVCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSTPTLLYLAHVFYLMRKEEKLNRKEEELKMVQNEGGNVDMHLKQIEIKKFKYGLEEHGKVKMRGGLLRTYIISILFKSVFEVGFIIIQWYMYGFSLSAIYTCKRDPCPHQVDCFLSRPTEKTIFIWFMLIVSIVSLALNIIELFYVTYKSIKDGIKGKKDPFSATNDAVISGKECGSPKYAYFNGCSSPTAPMSPPGYKLVTGERNPSSCRNYNKQASEQNWANYSAEQNRMGQA... | null | null | cell communication by electrical coupling [GO:0010644]; cell-cell signaling [GO:0007267]; heart development [GO:0007507]; microtubule-based transport [GO:0099111]; neural crest cell migration [GO:0001755]; positive regulation of transcription by RNA polymerase II [GO:0045944] | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; connexin complex [GO:0005922]; intercalated disc [GO:0014704]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | gap junction hemi-channel activity [GO:0055077] | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}... | null | null | null | null | null | FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Plays an essential role in gap junction communication in the ventricles. {ECO:0000250|UniProtKB:O57474, ECO:0000250|UniProtKB:... | Xenopus laevis (African clawed frog) |
P16869 | FHUE_ECOLI | MLSTQFNRDNQYQAITKPSLLAGCIALALLPSAAFAAPATEETVIVEGSATAPDDGENDYSVTSTSAGTKMQMTQRDIPQSVTIVSQQRMEDQQLQTLGEVMENTLGISKSQADSDRALYYSRGFQIDNYMVDGIPTYFESRWNLGDALSDMALFERVEVVRGATGLMTGTGNPSAAINMVRKHATSREFKGDVSAEYGSWNKERYVADLQSPLTEDGKIRARIVGGYQNNDSWLDRYNSEKTFFSGIVDADLGDLTTLSAGYEYQRIDVNSPTWGGLPRWNTDGSSNSYDRARSTAPDWAYNDKEINKVFMTLKQQFAD... | null | null | cellular response to hydroxyurea [GO:0072711]; ferric-hydroxamate import into cell [GO:0015687]; intracellular iron ion homeostasis [GO:0006879]; siderophore transmembrane transport [GO:0044718] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495] | high-affinity ferric iron transmembrane transporter activity [GO:0015092]; siderophore uptake transmembrane transporter activity [GO:0015344]; siderophore-iron transmembrane transporter activity [GO:0015343]; signaling receptor activity [GO:0038023] | 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, ECO:0000305|PubMed:31098021}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}. | null | null | null | null | null | FUNCTION: Involved in the active transport across the outer membrane of iron complexed with linear hydroxamate siderophores coprogen, rhodotorulic acid and ferrioxamine B. Binds Fe-coprogen with high affinity, rhodotorulic acid to a lesser extent, and weakly to ferrioxamine B. Selective for planar siderophores. Does no... | Escherichia coli (strain K12) |
P16870 | CBPE_HUMAN | MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWY... | 3.4.17.10 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | cardiac left ventricle morphogenesis [GO:0003214]; insulin processing [GO:0030070]; neuropeptide signaling pathway [GO:0007218]; peptide hormone secretion [GO:0030072]; peptide metabolic process [GO:0006518]; protein localization to membrane [GO:0072657]; protein localization to secretory granule [GO:0033366]; protein ... | extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; transport vesicle membrane [GO:0030658] | carboxypeptidase activity [GO:0004180]; cell adhesion molecule binding [GO:0050839]; metallocarboxypeptidase activity [GO:0004181]; neurexin family protein binding [GO:0042043]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q00493}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15087}. Secreted {ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretor... | CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; | null | null | null | null | FUNCTION: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. {ECO:0000250|UniProtKB:Q00493}. | Homo sapiens (Human) |
P16871 | IL7RA_HUMAN | MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEV... | null | null | B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; cell morphogenesis [GO:0000902]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; gene expression [GO:0010467]; hemopoiesis [GO:0030097]; i... | clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | antigen binding [GO:0003823]; cytokine receptor activity [GO:0004896]; interleukin-7 receptor activity [GO:0004917] | PF00041;PF18447; | 2.60.40.1870;2.60.40.10; | Type I cytokine receptor family, Type 4 subfamily | PTM: N-glycosylated IL-7Ralpha binds IL7 300-fold more tightly than the unglycosylated form. {ECO:0000269|PubMed:19141282}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:31748347}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted. | null | null | null | null | null | FUNCTION: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP). | Homo sapiens (Human) |
P16872 | IL7RA_MOUSE | MMALGRAFAIVFCLIQAVSGESGNAQDGDLEDADADDHSFWCHSQLEVDGSQHLLTCAFNDSDINTANLEFQICGALLRVKCLTLNKLQDIYFIKTSEFLLIGSSNICVKLGQKNLTCKNMAINTIVKAEAPSDLKVVYRKEANDFLVTFNAPHLKKKYLKKVKHDVAYRPARGESNWTHVSLFHTRTTIPQRKLRPKAMYEIKVRSIPHNDYFKGFWSEWSPSSTFETPEPKNQGGWDPVLPSVTILSLFSVFLLVILAHVLWKKRIKPVVWPSLPDHKKTLEQLCKKPKTSLNVSFNPESFLDCQIHEVKGVEARDEV... | null | null | B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; cell morphogenesis [GO:0000902]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; gene expression [GO:0010467]; hemopoiesis [GO:0030097]; lymph node development [GO:0048535]; negative regulatio... | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | cytokine receptor activity [GO:0004896] | PF00041;PF18447; | 2.60.40.1870;2.60.40.10; | Type I cytokine receptor family, Type 4 subfamily | PTM: N-glycosylated IL-7Ralpha binds IL7 300-fold more tightly than the unglycosylated form. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP). | Mus musculus (Mouse) |
P16879 | FES_MOUSE | MGFSSELCSPQGHGAVQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSWSSGPDSPVSQSWAEITSQTENLSRVLRQHAEDLNSGPLSKLSVLIRERQHLRKTYNEQWQQLQQELTKTHSQDIEKLKTQYRTLVRDSTQARRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHHHHHRFMLPGLLQSLQDLHEEMAGILKDILQEYLEISSLVQDDVASIHRELAAAAARIQPEFEYLGFLRQYGSTPDVPPCVTFDESLLEDGEQLEPGELQLNELTLESVQHTLTSVTDELAVA... | 2.7.10.2 | null | cardiac muscle cell proliferation [GO:0060038]; cell adhesion [GO:0007155]; cellular response to vitamin D [GO:0071305]; centrosome cycle [GO:0007098]; chemotaxis [GO:0006935]; microtubule bundle formation [GO:0001578]; myoblast proliferation [GO:0051450]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regula... | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; immunoglobulin receptor binding [GO:0034987]; microtubule binding [GO:0008017]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol binding [GO:0035091]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | PTM: Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Distr... | 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=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-strea... | Mus musculus (Mouse) |
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