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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P10568 | MYO1A_BOVIN | MTLLEGSVGVEDLVLLEPLEQESLIRNLQLRYEKKEIYTYIGNVLVSVNPYQQLPIYDLEFVAKYRDYTFYELKPHIYALANMAYQSLRDRDRDQCILITGESGAGKTEASKLVMSYVAAVCGKGEQVNSVKEQLLQSNPVLEAFGNAKTIRNNNSSRFGKYMDIEFDFKGFPLGGVITNYLLEKSRVVKQLEGERNFHIFYQLLAGADAQLLKALKLERDTGGYAYLNPDTSRVDGMDDDANFKVLQSAMTVIGFSDEEIRQVLEVAALVLKLGNVELINEFQANGVPASGIRDGRGVQEIGELVGLNSVELERALCSR... | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; endocytosis [GO:0006897]; microvillus assembly [GO:0030033]; sensory perception of sound [GO:0007605]; vesicle localization [GO:0051648]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; lateral plasma membrane [GO:0016328]; microvillus [GO:0005902]; myosin complex [GO:... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00612;PF00063;PF06017; | 1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Phosphorylated by ALPK1. {ECO:0000250|UniProtKB:Q9UBC5}. | null | null | null | null | null | null | FUNCTION: Involved in directing the movement of organelles along actin filaments. {ECO:0000305}. | Bos taurus (Bovine) |
P10569 | MYSC_ACACA | MAYTSKHGVDDMVMLTSISNDAINDNLKKRFAADLIYTYIGHVLISVNPYKQINNLYTERTLKDYRGKYRYELPPHVYALADDMYRTMLSESEDQCVIISGESGAGKTEASKKIMQYIAAVSGATGDVMRVKDVILEAFGNAKTIRNNNSSRFGKYMEIQFDLKGDPVGGRISNYLLEKSRVVYQTNGERNFHIFYQLLAARARRPEAKFGLQTPDYYFYLNQGKTYTVDGMDDNQEFQDTWNAMKVIGFTAEEQHEIFRLVTAILYLGNVQFVDDGKGGSTIADSRPVAVETALLYRTITTGEQGRGRSSVYSCPQDPL... | null | null | actin filament organization [GO:0007015]; cellular component assembly [GO:0022607]; endocytosis [GO:0006897]; vesicle transport along actin filament [GO:0030050] | cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; microvillus [GO:0005902]; myosin complex [GO:0016459]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146] | PF00063;PF06017;PF14604; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | null | null | null | null | null | null | FUNCTION: Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. | Acanthamoeba castellanii (Amoeba) |
P10586 | PTPRF_HUMAN | MAPEPAPGRTMVPLVPALVMLGLVAGAHGDSKPVFIKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEEQLPPGFPSIDMGPQLKVVEKARTATMLCAAGGNPDPEISWFKDFLPVDPATSNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVVRSANYTCVAISSLGMIEATAQVTVKALPK... | 3.1.3.48 | null | cell adhesion [GO:0007155]; cell migration [GO:0016477]; negative regulation of receptor binding [GO:1900121]; neuron projection regeneration [GO:0031102]; peptidyl-tyrosine dephosphorylation [GO:0035335]; regulation of axon regeneration [GO:0048679]; synaptic membrane adhesion [GO:0099560]; transmembrane receptor prot... | extracellular exosome [GO:0070062]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | cell adhesion molecule binding [GO:0050839]; chondroitin sulfate proteoglycan binding [GO:0035373]; heparin binding [GO:0008201]; protein tyrosine phosphatase activity [GO:0004725]; protein-containing complex binding [GO:0044877]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00041;PF07679;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}; | null | null | null | null | FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; FUNCTION: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. | Homo sapiens (Human) |
P10587 | MYH11_CHICK | MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKKLVWVPSEKHGFEAASIKEEKGDEVTVELQENGKKVTLSKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVINPYKQLPIYSEKIIDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFSYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHIFYYLIAGASEQMRNDLLLEGFNNYTFLSNGH... | null | null | actomyosin structure organization [GO:0031032]; cardiac muscle cell development [GO:0055013]; elastic fiber assembly [GO:0048251]; myofibril assembly [GO:0030239]; skeletal muscle myosin thick filament assembly [GO:0030241]; smooth muscle contraction [GO:0006939] | cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; magnesium ion binding [GO:0000287]; microfilament motor activity [GO:0000146]; myosin II binding [GO:0045159]; myosin light chain binding [GO:0032027]; structural constit... | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.58.530;3.30.70.1590;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;4.10.270.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Gallus gallus (Chicken) |
P10588 | NR2F6_HUMAN | MAMVTGGWGGPGGDTNGVDKAGGYPRAAEDDSASPPGAASDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRSIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQRGRIPHSLPGAVAASSGSPPGSALAAVASGGDLFPGQPVSELIAQLLRAEPYPAAAGRFGAGGGAAGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPVADQVALLRLSWSELFVLNAAQAALPLHTAPLLAAAGLHAAPMAAERAVAFMDQVRAFQEQVDKLGRLQVDSAEYGCLKAIALFTPDACGLSD... | null | null | cell differentiation [GO:0030154]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron development [GO:0048666] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-spec... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:18701084}. | null | null | null | null | null | FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal resp... | Homo sapiens (Human) |
P10589 | COT1_HUMAN | MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGAGEQQQQAGSGAPHTPQTPGQPGAPATPGTAGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLNGHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYS... | null | null | cell differentiation [GO:0030154]; negative regulation of neuron projection development [GO:0010977]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; signal transduction [GO:0007165] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; retinoic acid-responsive element binding [GO:0044323]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG. {ECO:00... | Homo sapiens (Human) |
P10591 | HSP71_YEAST | MSKAVGIDLGTTYSCVAHFANDRVDIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPSNTVFDAKRLIGRNFNDPEVQADMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRD... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; clathrin coat disassembly [GO:0072318]; cytoplasmic translation [GO:0002181]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; negative regulation of DNA-templated transcription [GO:0045892]; proteasome-mediated ubiquitin-de... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription repressor complex [GO:0017053] | 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]; tRNA binding [GO:0000049]; 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: Cytoplasm {ECO:0000269|PubMed:14562095}. Secreted, cell wall {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles. {ECO:0000269|PubMed:12761219}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10592 | HSP72_YEAST | MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRD... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of DNA-templated transcription [GO:0045892]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein folding [GO:0006457]; protein refolding [GO:0042026]; response to oxygen levels [GO:0070482]; SRP-dependen... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole membrane [GO:0000329]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription repressor complex [GO:0017053] | 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]; tRNA binding [GO:0000049]; 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: Cytoplasm. Secreted, cell wall. | null | null | null | null | null | FUNCTION: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles. {ECO:0000269|PubMed:12761219}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10599 | THIO_HUMAN | MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV | null | null | activation of protein kinase B activity [GO:0032148]; cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA bindin... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | protein homodimerization activity [GO:0042803]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]; protein-disulfide reductase activity [GO:0015035]; RNA binding [GO:0003723]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791] | PF00085; | 3.40.30.10; | Thioredoxin family | PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins. {ECO:0000269|PubMed:15246877, ECO:0000269|PubMed:16408020, ECO:00... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Cytoplasm {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Secreted {ECO:0000269|PubMed:1332947}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA) (PubMed:9108029... | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, an... | Homo sapiens (Human) |
P10600 | TGFB3_HUMAN | MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPL... | null | null | cell-cell junction organization [GO:0045216]; detection of hypoxia [GO:0070483]; digestive tract development [GO:0048565]; embryonic neurocranium morphogenesis [GO:0048702]; face morphogenesis [GO:0060325]; female pregnancy [GO:0007565]; frontal suture morphogenesis [GO:0060364]; in utero embryonic development [GO:0001... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; T-tubule... | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; transforming growth factor beta binding [GO:0050431]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor bet... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: Methy... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [L... | Homo sapiens (Human) |
P10605 | CATB_MOUSE | MWWSLILLSCLLALTSAHDKPSFHPLSDDLINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPKLPGRVAFGEDIDLPETFDAREQWSNCPTIGQIRDQGSCGSCWAFGAVEAISDRTCIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWSFWTKKGLVSGGVYNSHVGCLPYTIPPCEHHVNGSRPPCTGEGDTPRCNKSCEAGYSPSYKEDKHFGYTSYSVSNSVKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDMMGGHAIRILGWGVENGVPYWLAANSWNLDWGDNGFFKILRGENHCG... | 3.4.22.1 | null | cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; epithelial cell differentiation [GO:0030855]; neuron apoptotic process [GO:0051402]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; proteolysis involved in protein catabo... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; peptidase... | collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; kininogen binding [GO:0030984]; peptide binding [GO:0042277]; protein self-association [GO:0043621]; protein-containing complex binding [GO:0044877]; prot... | PF00112;PF08127; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:12782676}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:1278... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.; EC=3.4.... | null | null | null | null | FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). Has als... | Mus musculus (Mouse) |
P10606 | COX5B_HUMAN | MASRLLRGAGTLAAQALRARGPSGAAAMRSMASGGGVPTDEEQATGLEREIMLAAKKGLDPYNVLAPKGASGTREDPNLVPSISNKRIVGCICEEDNTSVVWFWLHKGEAQRCPRCGAHYKLVPQQLAH | null | null | cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; respiratory gaseous exchange by respiratory system [GO:0007585] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | cytochrome-c oxidase activity [GO:0004129]; metal ion binding [GO:0046872] | PF01215; | 2.60.11.10; | Cytochrome c oxidase subunit 5B family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Peripheral membrane protein {ECO:0000269|PubMed:30030519}; Matrix side {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P04037}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P10608 | ADRB2_RAT | MEPHGNDSDFLLAPNGSRAPGHDITQERDEAWVVGMAILMSVIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWNFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYVAITSPFKYQSLLTKNKARVVILMVWIVSGLTSFLPIQMHWYRATHKQAIDCYAKETCCDFFTNQAYAIASSIVSFYVPLVVMVFVYSRVFQVAKRQLQKIDKSEGRFHAQNLSQVEQDGRSGHGLRSSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIRANLIPKEVYILLNWLGYVNSA... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adrenergic receptor signaling pathway [GO:0071875]; associative learning [GO:0008306]; bone resorption [GO:0045453]; brown fat cell differentiation [GO... | apical plasma membrane [GO:0016324]; axon [GO:0030424]; caveola [GO:0005901]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; early endosome [GO:0005769]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; neuronal cell body membrane [GO:0032809]; neuron... | adenylate cyclase binding [GO:0008179]; amyloid-beta binding [GO:0001540]; B2 bradykinin receptor binding [GO:0031713]; beta2-adrenergic receptor activity [GO:0004941]; enzyme binding [GO:0019899]; epinephrine binding [GO:0051379]; G-protein alpha-subunit binding [GO:0001965]; identical protein binding [GO:0042802]; io... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB2 sub-subfamily | PTM: Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity). {ECO:0000250}.; PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which media... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07550}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early endosome {ECO:0000250|UniProtKB:P07550}. Golgi apparatus {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL at the cell membrane. Activated receptors are internalized into endosom... | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000250|UniProtKB:P07550}. | Rattus norvegicus (Rat) |
P10611 | CP4A4_RABIT | MSVSALSPTRLPGSLSGLLQVAALLGLLLLLLKAAQLYLHRQWLLRALQQFPCPPFHWLLGHSREFQNDQELERIQKWVEKFPGACPWWLSGNKARLLVYDPDYLKVILGRSDPKAPRNYKLMTPWIGYGLLLLDGQTWFQHRRMLTPAFHYDILKPYVGLMVDSVQIMLDRWEQLISQDSSLEIFQHVSLMTLDTIMKCAFSYQGSVQLDRNSHSYIQAINDLNNLVFYRARNVFHQSDFLYRLSPEGRLFHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAKMENGSSLSDQDLRAEVDTFMF... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P51869}; | arachidonic acid metabolic process [GO:0019369]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651] | endoplasmic reticulum membrane [GO:0005789] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Catalyzes the omega- and (omega-1)-hydroxyla... | Oryctolagus cuniculus (Rabbit) |
P10612 | CP11A_PIG | MLARGLALRSVLVKGCQPFLSAPRECPGHPRVGTGEGACISTKTPRPFSEIPSPGDNGWINLYRFWKEKGTQKIHYHHVQNFQKYGPIYREKLGNLESVYIIDPEDVALLFKFEGPNPERYNIPPWVAYHQHYQKPVGVLLKKSGAWKKDRLVLNTEVMAPEAIKNFIPLLDTVSQDFVGVLHRRIKQQGSGKFSGDIREDLFRFAFESITNVIFGERLGMLEEIVDPEAQKFIDAVYQMFHTSVPMLNLPPDLFRLFRTKTWRDHVAAWDTIFNKAEKYTQNFYWDLRRKREFNNYPGILYRLLGNDKLLSEDVKANVT... | 1.14.15.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P05108}; | C21-steroid hormone biosynthetic process [GO:0006700]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; glucocorticoid biosynthetic process [GO:0006704] | mitochondrial inner membrane [GO:0005743] | cholesterol monooxygenase (side-chain-cleaving) activity [GO:0008386]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone; Xref=Rhea:RHEA:35739, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:16581, ChEBI:CH... | null | PATHWAY: Lipid metabolism; C21-steroid hormone metabolism. {ECO:0000250|UniProtKB:P05108}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05108}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones (PubMed:1773895, PubMed:2039527). Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hyd... | Sus scrofa (Pig) |
P10613 | CP51_CANAL | MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWRRDAAQKKISATYMKEIKSRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANLLIGILMGGQHTSASTSAWFL... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:28258218, ECO:0000269|PubMed:30126961}; | bile acid biosynthetic process [GO:0006699]; cell growth mode switching, budding to filamentous [GO:0036187]; cholesterol homeostasis [GO:0042632]; endosome organization [GO:0007032]; ergosterol biosynthetic process [GO:0006696]; membrane raft polarization [GO:0001766] | cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for lanosterol {ECO:0000269|PubMed:9559662}; KM=6.3 uM for lanosterol {ECO:0000269|PubMed:28258218}; KM=25 uM for 24,25-dihydrolanosterol {ECO:0000269|PubMed:9559662}; KM=11 uM for eburicol {ECO:0000269|PubMed:9559662}; KM=28.5 uM for obtusifoliol {ECO:000026... | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. {ECO:0000269|PubMed:28258218, ECO:0000269|PubMed:8647850}. | null | null | FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:10393548, PubMed:28258218, PubMed:8647850, PubMed:9559662). The third module or late... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
P10614 | CP51_YEAST | MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANLLIGVLMGGQHTSA... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:24613931}; | ergosterol biosynthetic process [GO:0006696] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000269|PubMed:16847258, ECO:0000269|PubMed:24613931}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 uM for lanosterol {ECO:0000269|PubMed:1872829}; KM=8.7 uM for eburicol {ECO:0000269|PubMed:1872829}; Vmax=11.8 nmol/min/nmol enzyme with lanosterol {ECO:0000269|PubMed:1872829}; Vmax=16.7 nmol/min/nmol enzyme with eburicol {ECO:0000269|PubMed:1872829}; | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. {ECO:0000269|PubMed:105731, ECO:0000269|PubMed:369554}. | null | null | FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:105731, PubMed:369554). The third module or late pathway involves the ergosterol syn... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10619 | PPGB_HUMAN | MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLR... | 3.4.16.5 | null | intracellular protein transport [GO:0006886]; negative regulation of chaperone-mediated autophagy [GO:1904715]; proteolysis [GO:0006508]; regulation of chaperone-mediated autophagy [GO:1904714]; regulation of protein stability [GO:0031647] | azurophil granule lumen [GO:0035578]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:0016020] | carboxypeptidase activity [GO:0004180]; enzyme activator activity [GO:0008047]; 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. {ECO:0000269|PubMed:190... | Homo sapiens (Human) |
P10620 | MGST1_HUMAN | MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAKKYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL | 2.5.1.18 | null | cellular response to lipid hydroperoxide [GO:0071449]; glutathione transport [GO:0034635] | azurophil granule membrane [GO:0035577]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886] | glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364] | PF01124; | 1.20.120.550; | MAPEG family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08011}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P08011}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P08011}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250|UniProtKB:P08011}. | Homo sapiens (Human) |
P10622 | RLA3_YEAST | MSDSIISFAAFILADAGLEITSDNLLTITKAAGANVDNVWADVYAKALEGKDLKEILSGFHNAGPVAGAGAASGAAAAGGDAAAEEEKEEEAAEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; positive regulation of protein kinase activity [GO:0045860]; translational elongation [GO:0006414] | cytosolic large ribosomal subunit [GO:0022625]; fungal-type vacuole [GO:0000324] | protein kinase activator activity [GO:0030295]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of ribosome [GO:0003735] | PF00428; | 1.10.10.1410; | Eukaryotic ribosomal protein P1/P2 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10627 | TWIST_DROME | MMSARSVSPKVLLDISYKPTLPNIMELQNNVIKLIQVEQQAYMQSGYQLQHQQQHLHSHQHHQQHHQQQHAQYAPLPSEYAAYGITELEDTDYNIPSNEVLSTSSNQSAQSTSLELNNNNTSSNTNSSGNNPSGFDGQASSGSSWNEHGKRARSSGDYDCQTGGSLVMQPEHKKLIHQQQQQQQQHQQQIYVDYLPTTVDEVASAQSCPGVQSTCTSPQSHFDFPDEELPEHKAQVFLPLYNNQQQQSQQLQQQQPHQQSHAQMHFQNAYRQSFEGYEPANSLNGSAYSSSDRDDMEYARHNALSSVSDLNGGVMSPACL... | null | null | actomyosin structure organization [GO:0031032]; developmental process [GO:0032502]; ectoderm and mesoderm interaction [GO:0007499]; gastrulation [GO:0007369]; gastrulation involving germ band extension [GO:0010004]; heart development [GO:0007507]; Malpighian tubule morphogenesis [GO:0007443]; mesoderm development [GO:0... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:3416836}. | null | null | null | null | null | FUNCTION: Involved in the establishment and dorsoventral patterning of germ layers in the embryo. {ECO:0000269|PubMed:3416836}. | Drosophila melanogaster (Fruit fly) |
P10628 | HXD4_MOUSE | MAMSSYMVNSKYVDPKFPPCEEYLQGGYLGEQGADYYGSGAQGADFQPSGLYPRPDFGEQPFGGGGPGPGSALPARGHGQEPSGPGSHYGAPGERCPAPPPAPLPGARACSQPTGPKQPPPGTALKQPAVVYPWMKKVHVNSVNPNYTGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQIKIWFQNRRMKWKKDHKLPNTKGRSSSSSSCSSSAAPGQHLQPMAKDHHTDLTTL | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; positive regulation of transcription by RNA polymerase II [GO:0045944]; stem cell differentiation [GO:0048863] | cell junction [GO:0030054]; nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Mus musculus (Mouse) |
P10632 | CP2C8_HUMAN | MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKVYGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRWKEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICSVVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALTRSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTETTSTTLRYGLLLLLKHPEVT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | epoxygenase P450 pathway [GO:0019373]; estrogen metabolic process [GO:0008210]; icosanoid biosynthetic process [GO:0046456]; lipid hydroxylation [GO:0002933]; long-chain fatty acid biosynthetic process [GO:0042759]; omega-hydroxylase P450 pathway [GO:0097267]; organic acid metabolic process [GO:0006082]; oxidative deme... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; estrogen 16-alpha-hydroxylase activity [GO:0101020]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donor... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for all-trans-retinoate (4-hydroxylation) {ECO:0000269|PubMed:11093772}; KM=5.4 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (epoxygenation) {ECO:0000269|PubMed:15766564}; KM=6 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (epoxygenation) {ECO:0000269|PubMed:15766... | PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:14559847}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000269|PubMed:15766564, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:7574697}.; PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:11093772}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11093772, PubMed:14559847, PubMed:15766564, PubMed:19965576, PubMed:7574697). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substr... | Homo sapiens (Human) |
P10633 | CP2D1_RAT | MELLNGTGLWSMAIFTVIFILLVDLMHRRHRWTSRYPPGPVPWPVLGNLLQVDLSNMPYSLYKLQHRYGDVFSLQKGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQGVILASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQAGQSINPKAMLNKALCNVIASLIFARRFEYEDPYLIRMVKLVEESLTEVSGFIPEVLNTFPALLRIPGLADKVFQGQKTFMALLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRMVVVDLFTAGMVTTATTLTWA... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to xenobiotic stimulus [GO:0009410]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P10634 | CP2DQ_RAT | MGLLIGDDLWAVVIFTAIFLLLVDLVHRHKFWTAHYPPGPVPLPGLGNLLQVDFENMPYSLYKLRSRYGDVFSLQIAWKPVVVINGLKAVRELLVTYGEDTADRPLLPIYNHLGYGNKSKGVVLAPYGPEWREQRRFSVSTLRDFGVGKKSLEQWVTEEAGHLCDTFAKEAEHPFNPSILLSKAVSNVIASLVYARRFEYEDPFFNRMLKTLKESFGEDTGFMAEVLNAIPILLQIPGLPGKVFPKLNSFIALVDKMLIEHKKSWDPAQPPRDMTDAFLAEMQKAKGNPESSFNDENLRLVVIDLFMAGMVTTSTTLSWA... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; female pregnancy [GO:0007565]; response to xenobiotic stimulus [GO:0009410]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P10635 | CP2D6_HUMAN | MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLL... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | alkaloid catabolic process [GO:0009822]; alkaloid metabolic process [GO:0009820]; arachidonic acid metabolic process [GO:0019369]; cholesterol metabolic process [GO:0008203]; coumarin metabolic process [GO:0009804]; estrogen metabolic process [GO:0008210]; heterocycle metabolic process [GO:0046483]; isoquinoline alkalo... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739] | anandamide 11,12 epoxidase activity [GO:0062188]; anandamide 14,15 epoxidase activity [GO:0062189]; anandamide 8,9 epoxidase activity [GO:0062187]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on pair... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for all-trans retinol {ECO:0000269|PubMed:10681376}; KM=1.3 uM for anandamide (oxidation to 20-HETE) {ECO:0000269|PubMed:18698000}; KM=2.1 uM for anandamide (oxidation to 8,9-EpETrE-EA) {ECO:0000269|PubMed:18698000}; KM=2.6 uM for anandamide (oxidation to 11,... | PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:10681376}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972997}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:21576599}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids, steroids and retinoids (PubMed:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075, PubMed:21576599). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molec... | Homo sapiens (Human) |
P10636 | TAU_HUMAN | MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEE... | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; amyloid fibril formation [GO:1990000]; astrocyte activation [GO:0048143]; axon development [GO:0061564]; axonal transport [GO:0098930]; axonal transport of mitochondrion [GO:0019896]; cell-cell signaling [GO:0007267]; cellula... | axolemma [GO:0030673]; axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extracellular region [GO:0005576]; glial cell projection [GO:0097386]; gro... | actin binding [GO:0003779]; apolipoprotein binding [GO:0034185]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; dynactin binding [GO:0034452]; enzyme binding [GO:0019899]; histone-dependent DNA binding [GO:0099077]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; lipopro... | PF00418; | null | null | PTM: Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10747907, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:26014385}. Cell membrane {ECO:0000269|PubMed:10747907}; Peripheral membrane protein {ECO:0000269|PubMed:10747907}; Cytoplasmic side {ECO:0000269|PubMed:10747907}. Cytoplasm, cytoskeleton {ECO:0000269|P... | null | null | null | null | null | FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both ... | Homo sapiens (Human) |
P10637 | TAU_MOUSE | MADPRQEFDTMEDHAGDYTLLQDQEGDMDHGLKESPPQPPADDGAEEPGSETSDAKSTPTAEDVTAPLVDERAPDKQAAAQPHTEIPEGITAEEAGIGDTPNQEDQAAGHVTQGRREGQAPDLGTSDWTRQQVSSMSGAPLLPQGLREATCQPSGTRPEDIEKSHPASELLRRGPPQKEGWGQDRLGSEEEVDEDLTVDESSQDSPPSQASLTPGRAAPQAGSGSVCGETASVPGLPTEGSVPLPADFFSKVSAETQASQPEGPGTGPMEEGHEAAPEFTFHVEIKASTPKEQDLEGATVVGVPGEEQKAQTQGPSVGKG... | null | null | adult walking behavior [GO:0007628]; axo-dendritic transport [GO:0008088]; axon extension [GO:0048675]; axonogenesis [GO:0007409]; DNA damage response [GO:0006974]; intracellular transport [GO:0046907]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; microtubule cytoskeleton organiza... | axon [GO:0030424]; axonal growth cone [GO:0044295]; axoneme [GO:0005930]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; glial cell projection [GO:0097386]; growth cone [GO:0030426]; main a... | DNA binding [GO:0003677]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; Hsp90 protein binding [GO:0051879]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; protein phosphatase 2A binding [GO:0051721]; protein-containing complex binding [GO:0044877]; protein-folding chapero... | PF00418; | null | null | PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (a few sites per protei... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10636}. Cell membrane {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10636}. Cell projection, axon {ECO:0000250|U... | null | null | null | null | null | FUNCTION: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity i... | Mus musculus (Mouse) |
P10639 | THIO_MOUSE | MVKLIESKEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGEFSGANKEKLEASITEYA | null | null | cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA binding [GO:0043388]; positive regulation of peptidyl-cystei... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; protein homodimerization activity [GO:0042803]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]; protein-disulfide reductase activity [GO:0015035] | PF00085; | 3.40.30.10; | Thioredoxin family | PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm {ECO:0000250|UniProtKB:P10599}. Secreted {ECO:0000250|UniProtKB:P10599}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA). Predominantly in the cytoplasm in non irradiated cells. Radiation ... | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the respon... | Mus musculus (Mouse) |
P10643 | CO7_HUMAN | MKVISLFILVGFIGEFQSFSSASSPVNCQWDFYAPWSECNGCTKTQTRRRSVAVYGQYGGQPCVGNAFETQSCEPTRGCPTEEGCGERFRCFSGQCISKSLVCNGDSDCDEDSADEDRCEDSERRPSCDIDKPPPNIELTGNGYNELTGQFRNRVINTKSFGGQCRKVFSGDGKDFYRLSGNVLSYTFQVKINNDFNYEFYNSTWSYVKHTSTEHTSSSRKRSFFRSSSSSSRSYTSHTNEIHKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVD... | null | null | complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886] | null | PF21284;PF21330;PF18434;PF00057;PF01823;PF00084;PF00090; | 3.30.60.30;2.10.70.10;4.10.400.10;2.20.100.10; | Complement C6/C7/C8/C9 family | PTM: C7 has 28 disulfide bridges.; PTM: C-, N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:10551839, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C7 serves as a membrane anchor. | Homo sapiens (Human) |
P10644 | KAP0_HUMAN | MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGP... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cardiac muscle cell proliferation [GO:0060038]; cellular response to glucagon stimulus [GO:0071377]; intracellular signal transduction [GO:0035556]; mesoderm formation [GO:0001707]; negative regulation of activated T cell proliferat... | cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; nucleotide-activated protein kinase comp... | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23115245}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:20215566, ECO:0000269|PubMed:26405036}. | Homo sapiens (Human) |
P10645 | CMGA_HUMAN | MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGG... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation [GO:0086030]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative b... | chromaffin granule [GO:0042583]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; perinuclear region of cytoplasm [GO:0048471]; secretory granule [GO:0030141]; transport vesicle [GO:0030133] | null | PF01271; | null | Chromogranin/secretogranin protein family | PTM: Sulfated on tyrosine residues and/or contains sulfated glycans.; PTM: O-glycosylated with core 1 or possibly core 8 glycans (PubMed:19838169, PubMed:23234360, PubMed:9852066). Contains chondroitin sulfate (CS); CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH,... | SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:15326220). Displays antibacterial activity again... | Homo sapiens (Human) |
P10646 | TFPI1_HUMAN | MIYTMKKVHALWASVCLLLNLAPAPLNADSEEDEEHTIITDTELPPLKLMHSFCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNQNRFESLEECKKMCTRDNANRIIKTTLQQEKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQSTKVPSLFEFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGCGGNENNFTSKQECLRACKKGFIQRISKGGLIKTKRKRKKQRVKIAYEEIFVKNM | null | null | blood coagulation [GO:0007596]; cellular response to steroid hormone stimulus [GO:0071383]; negative regulation of blood coagulation [GO:0030195] | caveola [GO:0005901]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | endopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00014; | 4.10.410.10; | null | PTM: O-glycosylated. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592}. | SUBCELLULAR LOCATION: [Isoform Alpha]: Secreted.; SUBCELLULAR LOCATION: [Isoform Beta]: Microsome membrane {ECO:0000269|PubMed:22144186}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22144186}. | null | null | null | null | null | FUNCTION: Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma. | Homo sapiens (Human) |
P10648 | GSTA2_MOUSE | MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLYGKDMKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVFKF | 2.5.1.18 | null | glutathione metabolic process [GO:0006749]; response to bacterium [GO:0009617]; response to stilbenoid [GO:0035634]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | dinitrosyl-iron complex binding [GO:0035731]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; protein homodimerization activity [GO:0042803] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | null | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:9606968}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; Vmax=1295 nmol/min/mg enzyme for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; | null | null | null | FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. {ECO:0000269|PubMed:9606968}. | Mus musculus (Mouse) |
P10649 | GSTM1_MOUSE | MPMILGYWNVRGLTHPIRMLLEYTDSSYDEKRYTMGDAPDFDRSQWLNEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLARKHHLDGETEEERIRADIVENQVMDTRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYRMFEPKCLDAFPNLRDFLARFEGLKKISAYMKSSRYIATPIFSKMAHWSNK | 2.5.1.18 | null | cellular response to xenobiotic stimulus [GO:0071466]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; prostaglandin metabolic process [GO:0006693]; xenobiotic catabolic process [GO:0042178] | cytosol [GO:0005829]; extracellular region [GO:0005576]; myelin sheath [GO:0043209]; protein-containing complex [GO:0032991] | glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; nickel cation binding [GO:0016151]; protein kinase binding [GO:0019901]; steroid binding [GO:0005496] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P09488}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. {ECO:0000250|UniProtKB:P094... | Mus musculus (Mouse) |
P10651 | H33_SCHPO | MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPPTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS | null | null | DNA damage response [GO:0006974]; heterochromatin boundary formation [GO:0033696]; mitotic sister chromatid biorientation [GO:1990758]; rRNA transcription [GO:0009303] | chromosome, subtelomeric region [GO:0099115]; heterochromatin [GO:0000792]; mating-type region heterochromatin [GO:0031934]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | chromatin-protein adaptor activity [GO:0140463]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.; PTM: ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P10653 | TBB1_EMENI | MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGELFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVVDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAYSFRAVSVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGK... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; microtubule depolymerization [GO:0007019]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle disassembly [GO:0051228]; nuclear migration along microtubule [GO:0030473]; response ... | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; microtubule [GO:0005874]; spindle microtubule [GO:0005876]; tubulin complex [GO:0045298] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P10659 | METK1_YEAST | MAGTFLFTSESVGEGHPDKICDQVSDAILDACLAEDPHSKVACETAAKTGMIMVFGEITTKAQLDYQKIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGVHEEKDLEDIGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLAWLRPDTKTQVTVEYKDDHGRWVPQRIDTVVVSAQHADEITTEDLRAQLKSEIIEKVIPRDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLHVD... | 2.5.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P13444}; Note=Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate. {ECO:0000250|UniProtKB:P13444}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P13444}; Note=Binds 1 po... | methionine metabolic process [GO:0006555]; one-carbon metabolic process [GO:0006730]; S-adenosylmethionine biosynthetic process [GO:0006556] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; methionine adenosyltransferase activity [GO:0004478] | PF02773;PF02772;PF00438; | 3.30.300.10; | AdoMet synthase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000305|PubMed:3316224}; | null | PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000269|PubMed:3316224}. | null | null | FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000305|PubMed:3316224}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10664 | RL4A_YEAST | MSRPQVTVHSLTGEATANALPLPAVFSAPIRPDIVHTVFTSVNKNKRQAYAVSEKAGHQTSAESWGTGRAVARIPRVGGGGTGRSGQGAFGNMCRGGRMFAPTKTWRKWNVKVNHNEKRYATASAIAATAVASLVLARGHRVEKIPEIPLVVSTDLESIQKTKEAVAALKAVGAHSDLLKVLKSKKLRAGKGKYRNRRWTQRRGPLVVYAEDNGIVKALRNVPGVETANVASLNLLQLAPGAHLGRFVIWTEAAFTKLDQVWGSETVASSKVGYTLPSHIISTSDVTRIINSSEIQSAIRPAGQATQKRTHVLKKNPLKN... | null | null | cytoplasmic translation [GO:0002181] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; nucleus [GO:0005634] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF14374;PF00573; | 3.40.1370.10; | Universal ribosomal protein uL4 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:1544921}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:25936803}. Nucleus {ECO:0000269|PubMed:25936803}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10668 | COF1_PIG | MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPECAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL | null | null | actin filament fragmentation [GO:0030043]; actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; cytoskeleton organization [GO:0007010]; establishment of spindle localization [GO:0051293]; mitotic cytokinesis [GO:0000281]; positive regulation of embryonic development [GO:0040019]; regulation o... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; lamellipodium membrane [GO:0031258]; nuclear matrix [GO:0016363]; ruffle membrane [GO:0032587] | actin filament binding [GO:0051015] | PF00241; | 3.40.20.10; | Actin-binding proteins ADF family | PTM: Inactivated by phosphorylation on Ser-3 (PubMed:9078368). Phosphorylated on Ser-3 in resting cells (By similarity). Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal ... | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P23528}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P23528}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P23528}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23528}; Cytoplasmic side {ECO:0000250|UniProtKB:P23528}. Cell projection, lame... | null | null | null | null | null | FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:6509022, PubMed:9078368). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:9078368).... | Sus scrofa (Pig) |
P10669 | FST_PIG | MVRPKHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPTSSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPESKSEEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSIS... | null | null | cell differentiation [GO:0030154]; negative regulation of activin receptor signaling pathway [GO:0032926]; regulation of BMP signaling pathway [GO:0030510] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | activin binding [GO:0048185] | PF09289;PF21333;PF07648; | 3.30.60.30;3.90.290.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:8340384}.; PTM: FS-303 may be derived from mature isoform 1 by post-translational proteolytic cleavage. It is the most abundant form in ovaries (PubMed:8340384). {ECO:0000269|PubMed:8340384}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). | Sus scrofa (Pig) |
P10674 | FAS1_DROME | MLNAAALLLALLCAANAAAAADLADKLRDDSELSQFYSLLESNQIANSTLSLRSCTIFVPTNEAFQRYKSKTAHVLYHITTEAYTQKRLPNTVSSDMAGNPPLYITKNSNGDIFVNNARIIPSLSVETNSDGKRQIMHIIDEVLEPLTVKAGHSDTPNNPNALKFLKNAEEFNVDNIGVRTYRSQVTMAKKESVYDAAGQHTFLVPVDEGFKLSARSSLVDGKVIDGHVIPNTVIFTAAAQHDDPKASAAFEDLLKVTVSFFKQKNGKMYVKSNTIVGDAKHRVGVVLAEIVKANIPVSNGVVHLIHRPLMIIDTTVTQF... | null | null | axon guidance [GO:0007411]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; macroautophagy [GO:0016236]; neuron recog... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | cell adhesion molecule binding [GO:0050839] | PF02469; | 2.30.180.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: Neural cell adhesion molecule. | Drosophila melanogaster (Fruit fly) |
P10676 | NINAC_DROME | MMYLPYAQLPDPTDKFEIYEEIAQGVNAKVFRAKELDNDRIVALKIQHYDEEHQVSIEEEYRTLRDYCDHPNLPEFYGVYKLSKPNGPDEIWFVMEYCAGGTAVDMVNKLLKLDRRMREEHIAYIIRETCRAAIELNRNHVLHRDIRGDNILLTKNGRVKLCDFGLSRQVDSTLGKRGTCIGSPCWMAPEVVSAMESREPDITVRADVWALGITTIELADGKPPFADMHPTRAMFQIIRNPPPTLMRPTNWSQQINDFISESLEKNAENRPMMVEMVEHPFLTELIENEDEMRSDIAEMLELSRDVKTLYKEPELFVDRG... | 2.7.11.1 | null | adaptation of rhodopsin mediated signaling [GO:0016062]; cytoskeleton organization [GO:0007010]; deactivation of rhodopsin mediated signaling [GO:0016059]; dsRNA transport [GO:0033227]; intracellular protein transport [GO:0006886]; phosphorylation [GO:0016310]; photoreceptor cell maintenance [GO:0045494]; phototransduc... | cytoplasm [GO:0005737]; inaD signaling complex [GO:0016027]; myosin III complex [GO:0042385]; nucleus [GO:0005634]; rhabdomere [GO:0016028]; rhabdomere membrane [GO:0033583] | actin binding [GO:0003779]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol binding [GO:0035091]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00612;PF00063;PF00069; | 1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;1.10.510.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family; Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25822849}. Cytoplasm, cytoskeleton. Nucleus {ECO:0000269|PubMed:25822849}. Membrane {ECO:0000269|PubMed:25822849}; Peripheral membrane protein {ECO:0000305}. Cell projection, rhabdomere membrane {ECO:0000269|PubMed:25822849}; Peripheral membrane protein {ECO:0000305}.... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Required for photoreceptor cell function. The ninaC proteins combines putative serine/threonine-protein kinase and myosin activities (PubMed:2449973). Essential for the expression and stability of the rtp protein in the photoreceptors (PubMed:20107052). The rtp/ninaC complex is required for stability of inad ... | Drosophila melanogaster (Fruit fly) |
P10683 | GALA_RAT | MARGSVILLAWLLLVATLSATLGLGMPTKEKRGWTLNSAGYLLGPHAIDNHRSFSDKHGLTGKRELPLEVEEGRLGSVAVPLPESNIVRTIMEFLSFLHLKEAGALDSLPGIPLATSSEDLEQS | null | null | cAMP-mediated signaling [GO:0019933]; feeding behavior [GO:0007631]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of lymphocyte proliferation [GO:0050672]; nervous system development [GO:0007399]; neuropeptide signaling pathway [GO:0007218]; parental behavior [GO:0060746]; posi... | extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; secretory granule [GO:0030141] | G protein-coupled receptor binding [GO:0001664]; galanin receptor activity [GO:0004966]; galanin receptor binding [GO:0031763]; neuropeptide hormone activity [GO:0005184]; type 1 galanin receptor binding [GO:0031764]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF01296;PF06540; | null | Galanin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07480, ECO:0000250|UniProtKB:P22466}. | null | null | null | null | null | FUNCTION: Endocrine hormone of the central and peripheral nervous systems that binds and activates the G protein-coupled receptors GALR1, GALR2, and GALR3. This small neuropeptide may regulate diverse physiologic functions including contraction of smooth muscle of the gastrointestinal and genitourinary tract, growth ho... | Rattus norvegicus (Rat) |
P10686 | PLCG1_RAT | MAGVGTPCANGCGPSAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDFEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNTLRTGERPELCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPE... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:7531435}; | calcium ion transport [GO:0006816]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; epidermal growth factor receptor signaling pathway [GO:0007173]; in utero embryonic development [GO:0001701]; inositol trisphosphate biosynthetic ... | cell projection [GO:0042995]; cell-cell junction [GO:0005911]; clathrin-coated vesicle [GO:0030136]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587... | calcium ion binding [GO:0005509]; calcium-dependent phospholipase C activity [GO:0050429]; glutamate receptor binding [GO:0035254]; guanyl-nucleotide exchange factor activity [GO:0005085]; insulin receptor binding [GO:0005158]; neurotrophin TRKA receptor binding [GO:0005168]; phosphatidylinositol phospholipase C activi... | PF00168;PF00169;PF00388;PF00387;PF00017;PF00018; | 2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30;3.30.505.10;2.30.30.40; | null | PTM: Ubiquitinated by CBLB in activated T-cells. {ECO:0000250|UniProtKB:Q62077}.; PTM: Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phos... | SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250|UniProtKB:P19174}. Cell projection, ruffle {ECO:0000250|UniProtKB:P19174}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000250|UniProtKB:P19174}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=13.8 umol/min/mg enzyme toward phosphatidylinositol {ECO:0000269|PubMed:7531435}; Vmax=0.6 umol/min/mg enzyme toward 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) {ECO:0000269|PubMed:7531435}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:7531435}; | null | FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:7531435). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, ... | Rattus norvegicus (Rat) |
P10687 | PLCB1_RAT | MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQ... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; | activation of meiosis involved in egg activation [GO:0060466]; cellular response to fluoride [GO:1902618]; cellular response to glyceraldehyde [GO:1905631]; cellular response to ionomycin [GO:1904637]; cellular response to vasopressin [GO:1904117]; cerebral cortex development [GO:0021987]; fat cell differentiation [GO:... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; postsynaptic cytosol [GO:0099524]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; lamin binding [GO:0005521]; phosphatidylinositol phospholipase C activity [GO:0004435]; phosphatidylinositol-4,5-bisphosphate binding [GO:000554... | PF06631;PF09279;PF17787;PF00388;PF00387;PF08703; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | PTM: Palmitoylated. Palmitoylation at Cys-17 by ZDHHC21 regulates the signaling activity of PLCB1 and the function of the endothelial barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation. {ECO:0000250|UniProtKB:Q9Z1B3}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors. Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3}. | Rattus norvegicus (Rat) |
P10688 | PLCD1_RAT | MDSGRDFLTLHGLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQL... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound to the C2 domain.; | angiogenesis [GO:0001525]; G protein-coupled receptor signaling pathway [GO:0007186]; labyrinthine layer blood vessel development [GO:0060716]; lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G pr... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial membrane [GO:0031966] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; enzyme binding [GO:0019899]; GTPase activating protein binding [GO:0032794]; inositol 1,4,5 trisphosphate binding [GO:0070679]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidyl... | PF00168;PF09279;PF16457;PF00388;PF00387; | 2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (PubMed:16000311). Essential for trophoblast and placental development (By similarity). Binds phosphatidylinositol 4,5-bis... | Rattus norvegicus (Rat) |
P10696 | PPBN_HUMAN | MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALLLLSR... | 3.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05187}; Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P05187}; Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187}; COFACTOR: Name=Ca(2+); Xref=C... | dephosphorylation [GO:0016311] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | alkaline phosphatase activity [GO:0004035]; metal ion binding [GO:0046872] | PF00245; | 3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:1939159}; | null | null | null | null | FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. {ECO:0000269|PubMed:1939159}. | Homo sapiens (Human) |
P10711 | TCEA1_MOUSE | MEDEVVRIAKKMDKMVQKKNAAGALDLLKELKNIPMTLELLQSTRIGMSVNALRKQSTDEEVTSLAKSLIKSWKKLLDGPSTDKDPEEKKKEPAISSQNSPEAREESSSSSNVSSRKDETNARDTYVSSFPRAPSTSDSVRLKCREMLAAALRTGDDYVAIGADEEELGSQIEEAIYQEIRNTDMKYKNRVRSRISNLKDAKNPNLRKNVLCGNIPPDLFARMTAEEMASDELKEMRKNLTKEAIREHQMAKTGGTQTDLFTCGKCKKKNCTYTQVQTRSADEPMTTFVVCNECGNRWKFC | null | null | DNA-templated transcription [GO:0006351]; erythrocyte differentiation [GO:0030218]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; transcription elongation by RNA polymerase II [GO:0006368] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; zinc ion binding [GO:0008270] | PF08711;PF01096;PF07500; | 2.20.25.10;1.20.930.10;1.10.472.30; | TFS-II family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-... | Mus musculus (Mouse) |
P10719 | ATPB_RAT | MLSLVGRVASASASGALRGLNPLAALPQAHLLLRTAPAGVHPARDYAAQSSAAPKAGTATGQIVAVIGAVVDVQFDEGLPPILNALEVQGRESRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSA... | 7.1.2.2 | null | angiogenesis [GO:0001525]; ATP biosynthetic process [GO:0006754]; cellular response to interleukin-7 [GO:0098761]; cellular response to peptide [GO:1901653]; cold acclimation [GO:0009631]; lipid metabolic process [GO:0006629]; liver development [GO:0001889]; negative regulation of cell adhesion involved in substrate-bo... | cell surface [GO:0009986]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, ... | ADP binding [GO:0043531]; angiostatin binding [GO:0043532]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; lipoprotein particle receptor activity [GO:0030228]; MHC class I protein binding [GO:0042288]; proton-transporting ATP synthase activity, rotational mechanism [GO... | PF00006;PF02874; | 2.40.10.170;3.40.50.300; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829}. | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000269|PubMed:9736690}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722; Eviden... | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Rattus norvegicus (Rat) |
P10720 | PF4V_HUMAN | MSSAARSRLTRATRQEMLFLALLLLPVVVAFARAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQALLYKKIIKEHLES | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; inflammatory response [GO:0006954]; neutrophil chemotaxis [GO:0030593] | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | PTM: The N-terminal processed forms of platelet factor 4 variant seems to be produced by proteolytic cleavage. The most abundant form is Platelet factor 4 variant(5-74). | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibitor of angiogenesis. Inhibitor of endothelial cell chemotaxis (in vitro). {ECO:0000269|PubMed:15459074}. | Homo sapiens (Human) |
P10721 | KIT_HUMAN | MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMIN... | 2.7.10.1 | null | actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; digestive tract development [GO:0048565]; ectopic germ cell programmed... | acrosomal vesicle [GO:0001669]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [... | PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. {ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding enhances autophosphorylation. Isoform... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20601678}. Note=Detected in the cytoplasm of spermatozoa, especially in the equ... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KIT... | Homo sapiens (Human) |
P10724 | ALR_GEOSE | MNDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDGQKAPIVGRICMDQCMIRLP... | 5.1.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:12741835, ECO:0000269|PubMed:15807525, ECO:0000269|PubMed:9063881, ECO:0000269|PubMed:9671513}; | D-alanine biosynthetic process [GO:0030632]; peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829] | alanine racemase activity [GO:0008784]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family | null | null | CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:12203980, ECO:0000269|PubMed:12741835}; | null | PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}. | null | null | FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine. {ECO:0000269|PubMed:10502689, ECO:0000269|PubMed:12203980}. | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P10731 | AMD_BOVIN | MAGFRSLLVLLLVFPSGCVGFRSPLSVFKRFKETTRSFSNECLGTTRPVIPIDSSDFALDIRMPGVTPKQSDTYFCMSVRLPMDEEAFVIDFKPRASMDTVHHMLLFGCNMPASTGNYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPPGGKVVNSDISCHYKKYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFTGEGRTEVTHIGGTSSDEMCNLYIMYYMEA... | 1.14.17.3; 4.3.2.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P14925}; Note=Binds one Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14925}; COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:2059626}; Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000250|UniProtKB:P14925}; | fatty acid primary amide biosynthetic process [GO:0062112]; peptide amidation [GO:0001519] | extracellular region [GO:0005576]; secretory granule membrane [GO:0030667]; transport vesicle membrane [GO:0030658] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; L-ascorbic acid binding [GO:0031418]; peptidylamidoglycolate lyase activity [GO:0004598]; peptidylglycine monooxygenase activity [GO:0004504]; zinc ion binding [GO:0008270] | PF03712;PF01082;PF01436; | 2.60.120.230;2.60.120.310;2.120.10.30; | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:2059626}; Single-pass membrane protein {ECO:0000269|PubMed:2059626}. Note=Secretory granules. {ECO:0000269|PubMed:2059626}. | CATALYTIC ACTIVITY: Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:C... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimally active at acidic pHs. {ECO:0000269|PubMed:2059626}; | null | FUNCTION: Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:2059626). Alpha-amidation involves two sequential reaction... | Bos taurus (Bovine) |
P10733 | SEVE_DICDI | MIKNRKLDITSTNVAGIGTDLDKKCRLDAASTEAQWKGVGQAPGLKIWRIENFKVVPVPESSYGKFYDGDSYIILHTFKEGNSLKHDIHFFLGTFTTQDEAGTAAYKTVELDDFLGGAPIQYRQCQSYESPSFLSLFPKYFILSGGVESGFNHVKPTEYKPRLLHISGDKNAKVAEVPLATSSLNSGDCFLLDAGLTIYQFNGSKSSPQEKNKAAEVARAIDAERKGLPKVEVFCETDSDIPAEFWKLLGGKGAIAAKHETAPTKSEKVLYKLSDASGSLKFSEVSRGKINKSSLKSEDVFIIDLGNEIYTWIGSKSSPN... | null | null | actin filament bundle assembly [GO:0051017]; actin filament fragmentation [GO:0030043]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; phagocytic vesicle [GO:0045335] | actin filament binding [GO:0051015]; actin filament severing activity [GO:0003789]; actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00626; | 3.40.20.10; | Villin/gelsolin family | null | null | null | null | null | null | null | FUNCTION: Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner. | Dictyostelium discoideum (Social amoeba) |
P10734 | KNIR_DROME | MNQTCKVCGEPAAGFHFGAFTCEGCKSFFGRSYNNISTISECKNEGKCIIDKKNRTTCKACRLRKCYNVGMSKGGSRYGRRSNWFKIHCLLQEHEQAAAAAGKAPPLAGGVSVGGAPSASSPVGSPHTPGFGDMAAHLHHHHQQQQQQQVPRHPHMPLLGYPSYLSDPSAALPFFSMMGGVPHQSPFQLPPHLLFPGYHASAAAAAASAADAAYRQEMYKHRQSVDSVESQNRFSPASQPPVVQPTSSARQSPIDVCLEEDVHSVHSHQSSASLLHPIAIRATPTTPTSSSPLSFAAKMQSLSPVSVCSIGGETTSVVPV... | null | null | epithelial cell migration, open tracheal system [GO:0007427]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]; regulation of mitotic nuclear division [GO:0007088]; regulation of... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; zinc ion binding [GO:0008270] | PF00105; | 3.30.50.10; | Nuclear hormone receptor family, NR0 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:8670869}. | null | null | null | null | null | FUNCTION: Transcriptional repressor. Binds to multiple sites in the eve stripe 3 enhancer element. Plays an essential role in the segmentation process both by refining the expression patterns of gap genes and by establishing pair-rules stripes of gene expression. {ECO:0000269|PubMed:8670869}. | Drosophila melanogaster (Fruit fly) |
P10745 | RET3_HUMAN | MMREWVLLMSVLLCGLAGPTHLFQPSLVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSSLNDPRLVISYEPSTPEPPPQVPALTSLSEEELLAWLQRGLRHEVLEGNVGYLRVDSVPGQEVLSMMGEFLVAHVWGNLMGTSALVLDLRHCTGGQVSGIPYIISYLHPGNTILHVDTIYNRPSNTTTEIWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRKLRIGESDFFFTVPVSRSLGPLGGGSQTWEGSGVLPCVGTPAEQALEKALAIL... | null | null | lipid metabolic process [GO:0006629]; proteolysis [GO:0006508]; retinoid metabolic process [GO:0001523]; visual perception [GO:0007601] | cone matrix sheath [GO:0090658]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561] | retinal binding [GO:0016918]; retinoid binding [GO:0005501]; retinol binding [GO:0019841]; serine-type peptidase activity [GO:0008236] | PF03572;PF11918; | 3.30.750.44; | Peptidase S41A family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix. Note=Interphotoreceptor matrix that permeates the space between the retina and the contiguous layer of pigment epithelium cells. | null | null | null | null | null | FUNCTION: IRBP shuttles 11-cis and all trans retinoids between the retinol isomerase in the pigment epithelium and the visual pigments in the photoreceptor cells of the retina. | Homo sapiens (Human) |
P10746 | HEM4_HUMAN | MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLIFTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCGNAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNLNSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVSCTAESPTPQALATGIRKALQPHGCC | 4.2.1.75 | null | cellular response to amine stimulus [GO:0071418]; cellular response to arsenic-containing substance [GO:0071243]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; protoporphyrinogen IX biosynthetic proce... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | folic acid binding [GO:0005542]; uroporphyrinogen-III synthase activity [GO:0004852] | PF02602; | 3.40.50.10090; | Uroporphyrinogen-III synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydroxymethylbilane = H2O + uroporphyrinogen III; Xref=Rhea:RHEA:18965, ChEBI:CHEBI:15377, ChEBI:CHEBI:57308, ChEBI:CHEBI:57845; EC=4.2.1.75; Evidence={ECO:0000269|PubMed:11689424, ECO:0000269|PubMed:18004775}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 uM for hydroxymethylbilane; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:18004775}; | null | FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins (PubMed:11689424, PubMed:18004775). Porphyrins act as cofactors for a multitude of enzymes that perform a va... | Homo sapiens (Human) |
P10747 | CD28_HUMAN | MLRLLLALNLFPSIQVTGNKILVKQSPMLVAYDNAVNLSCKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYSKTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPPYLDNEKSNGTIIHVKGKHLCPSPLFPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS | null | null | apoptotic signaling pathway [GO:0097190]; CD4-positive, alpha-beta T cell proliferation [GO:0035739]; cell surface receptor signaling pathway [GO:0007166]; humoral immune response [GO:0006959]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; negative thymic T ... | cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; immunological synapse [GO:0001772]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636] | coreceptor activity [GO:0015026]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; protein kinase binding [GO:0019901] | PF15910; | 2.60.40.10; | null | PTM: CD40LG induces tyrosine phosphorylation of isoform 3. {ECO:0000269|PubMed:15067037}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell surface {ECO:0000269|PubMed:15067037}. | null | null | null | null | null | FUNCTION: Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation (PubMed:8617933). Isoform 3 enhances CD40L-mediated activation of NF-kapp... | Homo sapiens (Human) |
P10749 | IL1B_MOUSE | MATVPELNCEMPPFDSDENDLFFEVDGPQKMKGCFQTFDLGCPDESIQLQISQQHINKSFRQAVSLIVAVEKLWQLPVSFPWTFQDEDMSTFFSFIFEEEPILCDSWDDDDNLLVCDVPIRQLHYRLRDEQQKSLVLSDPYELKALHLNGQNINQQVIFSMSFVQGEPSNDKIPVALGLKGKNLYLSCVMKDGTPTLQLESVDPKQYPKKKMEKRFVFNKIEVKSKVEFESAEFPNWYISTSQAEHKPVFLGNNSGQDIIDFTMESVSS | null | null | astrocyte activation [GO:0048143]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mechanical stimulus [GO:0071260]; cellular response to organic substance [GO:0071310]; cellular response to xenobiotic stimulus [GO:0071466]; cytokine-mediated ... | cytosol [GO:0005829]; extracellular space [GO:0005615]; lysosome [GO:0005764]; secretory granule [GO:0030141]; vesicle [GO:0031982] | cytokine activity [GO:0005125]; integrin binding [GO:0005178]; interleukin-1 receptor binding [GO:0005149]; protein domain specific binding [GO:0019904]; receptor ligand activity [GO:0048018] | PF00340;PF02394; | 2.80.10.50; | IL-1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17284521}. Secreted {ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000269|PubMed:17641058}. Note=The precursor is cytosolic. In response to inflammasome-activating sig... | null | null | null | null | null | FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 d... | Mus musculus (Mouse) |
P10754 | RHIT_MOUSE | MSADSQSIAATENEEKSHEVPGNVQHCGDMLSGQEETVPLGTSQESTHIKAEPEEPHSEGASREDRTPGTQRWMSPCPGPKDKGPFLPGGVVPSPWTPVLSRGGRTRERKMAAALLTAWSQMPVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNGLALGAVEMGKVVPALAVATLEDTKSIRTRARWAPGEDPKCGQHVASGPGTKLTRDTGKAGQLKPAPSESRPLKTPEDSGPEKPSEGEEALKSGEEGLVPDGDTGKKTYKCEQCGKGFSWHSHLVTHRRTHTGEKPYTCTDCGKRFGRSSHLIQHQIIHTGEK... | null | null | embryo development [GO:0009790]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of hydrogen peroxide biosynthetic process [GO:0010729]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; regulation of tr... | mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription r... | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional repressor that binds to the promoter region of Mpv17l isoform M-LP short and regulates its age-dependent and heat-induced expression (PubMed:20231359). By regulating Mpv17l expression, contributes to the regulation of genes involved in H(2)O(2) metabolism and the mitochondrial apoptotic cascad... | Mus musculus (Mouse) |
P10758 | LITH_RAT | MTRNKYFILLSCLMVLSPSQGQEAEEDLPSARITCPEGSNAYSSYCYYFMEDHLSWAEADLFCQNMNSGYLVSVLSQAEGNFLASLIKESGTTAANVWIGLHDPKNNRRWHWSSGSLFLYKSWDTGYPNNSNRGYCVSVTSNSGYKKWRDNSCDAQLSFVCKFKA | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to chemokine [GO:1990869]; cellular response to gastrin [GO:1990878]; disruption of cell wall in another organism [GO:0044278]; gene expression [GO:0010467]; liver regeneration [GO:0097421]; midgut development [GO:00... | basal part of cell [GO:0045178]; collagen-containing extracellular matrix [GO:0062023]; dendrite membrane [GO:0032590]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuronal cell body membrane [GO:0032809]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; zymogen gra... | growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; molecular function inhibitor activity [GO:0140678]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; phosphatase binding [GO:0019902]; protein phosphatase binding [GO:0019903]; signaling receptor activity [GO:0038023];... | PF00059; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. | Rattus norvegicus (Rat) |
P10759 | AMPD1_RAT | MPLFKLTGQGKQIDDAMRSFAEKVFASEVKDEGGRHEISPFDVDEICPISLREMQAHIFHMENLSMSMDGRRKRRFQGRKTVNLSIPQSETSSTKLSHIEEFISSSPTYESVPDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVAIESFYPVFTPPPKKGEDPFRREDLPANLGYHLKMKGGVIYIYPDEAAASRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIK... | 3.5.4.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | AMP metabolic process [GO:0046033]; GMP salvage [GO:0032263]; IMP biosynthetic process [GO:0006188]; IMP salvage [GO:0032264]; response to organic substance [GO:0010033] | cytosol [GO:0005829] | AMP deaminase activity [GO:0003876]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; myosin heavy chain binding [GO:0032036] | PF19326; | 4.10.800.20;3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:11102975, ECO:0000269|PubMed:9133604}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; ... | null | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. {ECO:0000305|PubMed:11102975, ECO:0000305|PubMed:9133604}. | null | null | FUNCTION: AMP deaminase plays a critical role in energy metabolism. {ECO:0000305|PubMed:11102975, ECO:0000305|PubMed:9133604}. | Rattus norvegicus (Rat) |
P10760 | SAHH_RAT | MADKLPYKVADIGLAAWGRKALDIAENEMPGLMRMREMYSASKPLKGARIAGCLHMTVETAVLIETLVALGAEVRWSSCNIFSTQDHAAAAIAKAGIPVFAWKGETDEEYLWCIEQTLHFKDGPLNMILDDGGDLTNLIHTKHPQLLSGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACKEGNIFVTTTGCVDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVN... | 3.13.2.1 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF, ECO:0007744|PDB... | chronic inflammatory response to antigenic stimulus [GO:0002439]; circadian sleep/wake cycle [GO:0042745]; one-carbon metabolic process [GO:0006730]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]; S-adenosylhomocysteine catabolic process [GO:0019510]; S-adenosylmethionine cycle [GO:0033353] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; melanosome [GO:0042470]; nucleus [GO:0005634] | adenosylhomocysteinase activity [GO:0004013]; adenosylselenohomocysteinase activity [GO:0098604]; adenyl nucleotide binding [GO:0030554]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; protein self-association [GO:0043621] | PF05221;PF00670; | 3.40.50.1480;3.40.50.720; | Adenosylhomocysteinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23526}. Melanosome {ECO:0000250|UniProtKB:P23526}. Nucleus {ECO:0000250|UniProtKB:P23526}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23526}. | CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; Evidence={ECO:0000269|PubMed:11927587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709; Evidence={ECO:0000... | null | PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. {ECO:0000305|PubMed:11927587}. | null | null | FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form adenosine and homocysteine (PubMed:11927587). Binds copper ions (By similarity). {ECO:0000250|UniProtKB:P50247, ECO:0000269|PubMed:11927587}. | Rattus norvegicus (Rat) |
P10761 | ZP3_MOUSE | MASSYFLFLCLLLCGGPELCNSQTLWLLPGGTPTPVGSSSPVKVECLEAELVVTVSRDLFGTGKLVQPGDLTLGSEGCQPRVSVDTDVVRFNAQLHECSSRVQMTKDALVYSTFLLHDPRPVSGLSILRTNRVEVPIECRYPRQGNVSSHPIQPTWVPFRATVSSEEKLAFSLRLMEENWNTEKSAPTFHLGEVAHLQAEVQTGSHLPLQLFVDHCVATPSPLPDPNSSPYHFIVDFHGCLVDGLSESFSAFQVPRPRPETLQFTVDVFHFANSSRNTLYITCHLKVAPANQIPDKLNKACSFNKTSQSWLPVEGDADIC... | null | null | binding of sperm to zona pellucida [GO:0007339]; blastocyst formation [GO:0001825]; egg coat formation [GO:0035803]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; negative regulation of DNA-templated transcription [GO:0045892]; oocyte development [GO:0048599]; positive regulation of acros... | collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | acrosin binding [GO:0032190]; carbohydrate binding [GO:0030246]; receptor ligand activity [GO:0048018]; structural constituent of egg coat [GO:0035804] | PF00100; | 2.60.40.4100;2.60.40.3210; | ZP domain family, ZPC subfamily | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.; PTM: O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy. {ECO:0000269|PubMed:12799386}.; PTM: Cys-320, Cys-322, Cys-323 an... | SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000269|PubMed:19052627}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19052627}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona ... | Mus musculus (Mouse) |
P10763 | IGF1_SHEEP | MGKISSLPTQLFKCCFCDFLKQVKMPVTSSSHLFYLALCLLAFSSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKAAKSARSVRAQRHTDMPKAQKEVHLKNTSRGSAGNKNYRM | 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] | 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... | Ovis aries (Sheep) |
P10764 | IGF2_SHEEP | MGITAGKSMLALLAFLAFASCCYAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCAAPAKSERDVSASTTVLPDDFTAYPVGKFFQSDTWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHGGASSEASSD | null | null | embryonic placenta development [GO:0001892]; embryonic placenta morphogenesis [GO:0060669]; glucose metabolic process [GO:0006006]; in utero embryonic development [GO:0001701]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ossifi... | extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539] | PF08365;PF00049; | 1.10.100.10; | Insulin family | PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000250|UniProtKB:P01344}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in ad... | Ovis aries (Sheep) |
P10767 | FGF6_HUMAN | MALGQKLFITMSRGAGRLQGTLWALVFLGILVGMVVPSPAGTRANNTLLDSRGWGTLLSRSRAGLAGEIAGVNWESGYLVGIKRQRRLYCNVGIGFHLQVLPDGRISGTHEENPYSLLEISTVERGVVSLFGVRSALFVAMNSKGRLYATPSFQEECKFRETLLPNNYNAYESDLYQGTYIALSKYGRVKRGSKVSPIMTVTHFLPRI | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; myoblast differentiation [GO:0045445]; positive regulation of cell division [GO:0051781]; positive regulation of c... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; sarcolemma [GO:0042383] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. {ECO:0000269|PubMed:8663044}. | Homo sapiens (Human) |
P10768 | ESTD_HUMAN | MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLNA | 3.1.1.56; 3.1.2.12 | null | formaldehyde catabolic process [GO:0046294] | cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062] | carboxylic ester hydrolase activity [GO:0052689]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802]; methylumbelliferyl-acetate deacetylase activity [GO:0047374]; S-formylglutathione hydrolase activity [GO:0018738] | PF00756; | 3.40.50.1820; | Esterase D family | null | SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle. | CATALYTIC ACTIVITY: Reaction=H2O + S-formylglutathione = formate + glutathione + H(+); Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12; Evidence={ECO:0000269|PubMed:4768551}; CATALYTIC ACTIVITY: Reaction=4-methylumbelliferyl acetate + H2O ... | null | null | null | null | FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}. | Homo sapiens (Human) |
P10771 | H24_CAEEL | MSDSAVVAAAVEPKVPKAKAAKAAKPTKVAKAKAPVAHPPYINMIKEAIKQLKDRKGASKQAILKFISQNYKLGDNVIQINAHLRQALKRGVTSKALVQAAGSGANGRFRVPEKAAAAKKPAAAKKPAAAKKPAAAKKATGEKKAKKPAAAKPKKAATGDKKVKKAKSPKKVAKPAAKKVAKSPAKKAAPKKIAKPAAKKAAKPAAKA | null | null | chromosome condensation [GO:0030261]; defense response to Gram-positive bacterium [GO:0050830]; negative regulation of DNA recombination [GO:0045910]; negative regulation of gene expression [GO:0010629]; nucleosome assembly [GO:0006334]; regulation of gene expression [GO:0010468] | chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleosome [GO:0000786]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; H3K27me3 modified histone binding [GO:0061628]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: Methylation at lysine 14 is necessary to regulate male tail development. {ECO:0000269|PubMed:23028351}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22083954}. Chromosome {ECO:0000269|PubMed:22083954, ECO:0000305|PubMed:3202838}. Cytoplasm {ECO:0000269|PubMed:22083954}. Note=Cytoplasmic localization is observed after infection with Gram-positive bacterium B.thuringiensis. {ECO:0000269|PubMed:22083954}. | null | null | null | null | null | FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures (Probable) (PubMed:23028351). Probably does not act as global transcriptional repressor (PubMed:23028351). Acting in concert with chromobox protein homologs hpl-1 and hpl-2, involved in reproduction, somatic gonad... | Caenorhabditis elegans |
P10790 | FABPH_BOVIN | MVDAFVGTWKLVDSKNFDDYMKSLGVGFATRQVGNMTKPTTIIEVNGDTVIIKTQSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHVQKWNGQETSLVREMVDGKLILTLTHGTAVCTRTYEKQA | null | null | long-chain fatty acid transport [GO:0015909] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634] | long-chain fatty acid binding [GO:0036041] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion matrix. | null | null | null | null | null | FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.; FUNCTION: MDGI reversibly inhibits proliferation of mammary carcinoma cells. | Bos taurus (Bovine) |
P10791 | SODC_DROVI | MVVKAVCVINGDAKGTVFFEQEGEGCPVKVTGEVTGLAKGQHGFHVHEFGDNTNGCMSSGPHFNPYQKEHGAPTDENRHLGDLGNIIANGDGPTPVNICDCKITLLGANSIIGRTVVVHADPDDLGKGGHELSKTTGNAGARIGCGVIGIAKI | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 1 copper ion per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | determination of adult lifespan [GO:0008340]; regulation of autophagy of mitochondrion [GO:1903146]; regulation of synaptic plasticity [GO:0048167]; regulation of terminal button organization [GO:2000331] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | copper ion binding [GO:0005507]; protein homodimerization activity [GO:0042803]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Drosophila virilis (Fruit fly) |
P10795 | RBS1A_ARATH | MASSMLSSATMVASPAQATMVAPFNGLKSSAAFPATRKANNDITSITSNGGRVNCMQVWPPIGKKKFETLSYLPDLTDSELAKEVDYLIRNKWIPCVEFELEHGFVYREHGNSPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECKKEYPNAFIRIIGFDNTRQVQCISFIAYKPPSFTG | null | null | photorespiration [GO:0009853]; photosynthesis [GO:0015979]; reductive pentose-phosphate cycle [GO:0019253]; response to cold [GO:0009409]; ribulose bisphosphate carboxylase complex assembly [GO:0110102] | apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast membrane [GO:0031969]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; cytosolic ribosome [GO:0022626]; mitochondrion [GO:0005739]; thylakoid [GO:0009579]; thylakoid lumen [GO:0031977] | copper ion binding [GO:0005507]; mRNA binding [GO:0003729]; ribulose-bisphosphate carboxylase activity [GO:0016984]; salicylic acid binding [GO:1901149] | PF12338;PF00101; | 3.30.190.10; | RuBisCO small chain family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:12766230}; Peripheral membrane protein {ECO:0000269|PubMed:12766230}. Plastid, chloroplast stroma {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:28839179}. | null | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not ca... | Arabidopsis thaliana (Mouse-ear cress) |
P10809 | CH60_HUMAN | MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIAT... | 5.6.1.7 | null | 'de novo' protein folding [GO:0006458]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic mitochondrial changes [GO:0008637]; B cell activation [GO:0042113]; B cell proliferation [GO:0042100]; biological process involved in interaction with symbiont [GO:0051702]; c... | cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; coated vesicle [GO:0030135]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lipopolysaccharide receptor complex [GO:0046696]; membrane [GO:0016020]; migrasome [G... | apolipoprotein A-I binding [GO:0034186]; apolipoprotein binding [GO:0034185]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; DNA replication origin binding [GO:0003688]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; high-den... | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria... | Homo sapiens (Human) |
P10810 | CD14_MOUSE | MERVLGLLLLLLVHASPAPPEPCELDEESCSCNFSDPKPDWSSAFNCLGAADVELYGGGRSLEYLLKRVDTEADLGQFTDIIKSLSLKRLTVRAARIPSRILFGALRVLGISGLQELTLENLEVTGTAPPPLLEATGPDLNILNLRNVSWATRDAWLAELQQWLKPGLKVLSIAQAHSLNFSCEQVRVFPALSTLDLSDNPELGERGLISALCPLKFPTLQVLALRNAGMETPSGVCSALAAARVQLQGLDLSHNSLRDAAGAPSCDWPSQLNSLNLSFTGLKQVPKGLPAKLSVLDLSYNRLDRNPSPDELPQVGNLSL... | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive re... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lipopolysaccharide receptor complex [GO:0046696]; membrane raft [GO:0045121] | lipopolysaccharide binding [GO:0001530]; lipopolysaccharide immune receptor activity [GO:0001875]; lipoteichoic acid binding [GO:0070891] | PF00560; | 3.80.10.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:8612135}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P08571}. Secreted {ECO:0000250|UniProtKB:P08571}. Membrane raft {ECO:0000250|UniProtKB:P08571}. Golgi apparatus {ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem... | null | null | null | null | null | FUNCTION: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:16148141). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activat... | Mus musculus (Mouse) |
P10814 | SOMA_SALSA | MGQVFLLMPVLLVSCFLSQGAAMENQRLFNIAVNRVQHLHLMAQKMFNDFEGTLLPDERRQLNKIFLLDFCNSDSIVSPIDKLETQKSSVLKLLHISFRLIESWEYPSQTLTISNSLMVRNSNQISEKLSDLKVGINLLIKGSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL | null | null | animal organ development [GO:0048513]; calcium ion homeostasis [GO:0055074]; growth hormone receptor signaling pathway [GO:0060396]; hyperosmotic salinity response [GO:0042538]; hypotonic salinity response [GO:0042539]; magnesium ion homeostasis [GO:0010960]; photoperiodism [GO:0009648]; positive regulation of growth [... | extracellular space [GO:0005615] | growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation. | Salmo salar (Atlantic salmon) |
P10815 | CG23_SCHPO | MTTRRLTRQHLLANTLGNNDENHPSNHIARAKSSLHSSENSLVNGKKATVSSTNVPKKRHALDDVSNFHNKEGVPLASKNTNVRHTTASVSTRRALEEKSIIPATDDEPASKKRRQPSVFNSSVPSLPQHLSTKSHSVSTHGVDAFHKDQATIPKKLKKDVDERVVSKDIPKLHRDSVESPESQDWDDLDAEDWADPLMVSEYVVDIFEYLNELEIETMPSPTYMDRQKELAWKMRGILTDWLIEVHSRFRLLPETLFLAVNIIDRFLSLRVCSLNKLQLVGIAALFIASKYEEVMCPSVQNFVYMADGGYDEEEILQAE... | null | null | cell division [GO:0051301]; meiotic nuclear division [GO:0140013]; mitotic cell cycle phase transition [GO:0044772]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of ascospore formation [GO:0075297]; negative regulation of meiotic cell cycle [GO:0051447]; positive regulation of G2/M transiti... | chromatin [GO:0000785]; chromosome, telomeric repeat region [GO:0140445]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; meiotic spindle [GO:0072687]; mitotic spindle [GO:0072686]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole body [GO:0044732]; new mitotic spindle... | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF02984;PF00134; | 1.10.472.10; | Cyclin family, Cyclin AB subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:2534559}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition (PubMed:2847913, PubMed:2908246). Interacts with the cdc2 protein kinase to form MPF (PubMed:8455610). G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis (PubMed:2534559). Involved in the reorganization ... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P10819 | SAHH_DICDI | MTKLHYKVKDISLAAWGRKEIEIAENEMPGLMTLRKKYGPAQILKGARIAGCLHMTIQTAVLIETLTALGAQVQWSSCNIFSTQDQAAAAIAATGVPVYAWKGETEEEYNWCVEQTIVFQDGQPLNMILDDGGDLTNLVHEKYPQFLAGIKGISEETTTGVHNLYKMFKEGKLKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQSLSKMGARVLVTEIDPINALQACMDGYQIVTMETAAPLSNIFVTTTGCRDIVRGEHFAVMKEDAIVCNIGHFDCEIDVAWLNANAKKDTV... | 3.13.2.1 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Note=Binds 1 NAD(+) per subunit.; | establishment or maintenance of cell polarity [GO:0007163]; one-carbon metabolic process [GO:0006730]; S-adenosylmethionine cycle [GO:0033353] | actin rod [GO:0031002]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335] | adenosylhomocysteinase activity [GO:0004013]; cAMP binding [GO:0030552] | PF05221;PF00670; | 3.40.50.1480;3.40.50.720; | Adenosylhomocysteinase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine; Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1; | null | PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. | null | null | FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. | Dictyostelium discoideum (Social amoeba) |
P10820 | PERF_MOUSE | MATCLFLLGLFLLLPRPVPAPCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQAT... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0000269|PubMed:35148176}; | circadian rhythm [GO:0007623]; defense response to tumor cell [GO:0002357]; defense response to virus [GO:0051607]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; immune response to tumor cell [GO:0002418]; immunological synapse formation [GO:0001771]; killing of cells of another organism [GO:0... | cytolytic granule [GO:0044194]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endosome lumen [GO:0031904]; extracellular space [GO:0005615]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; pore-forming activity [GO:0140911]; wide pore channel activity [GO:0022829] | PF00168;PF01823; | 2.60.40.150; | Complement C6/C7/C8/C9 family | PTM: N-glycosylated. The glycosylation sites are facing the interior of the pore. {ECO:0000269|PubMed:21037563}. | SUBCELLULAR LOCATION: Cytolytic granule {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:8164737}. Secreted {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:3261391}. Cell membrane {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176}; Multi-pass membrane protein {ECO:0000269|PubMed:1944... | null | null | null | null | null | FUNCTION: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells (PubMed:19446473, PubMed:21037563, PubMed:26306037, PubMed:2783478, PubMed:3261391, PubMed:35148176, PubMed:35705808, PubMed:7520535, PubMed:7526382, PubMed:7972104,... | Mus musculus (Mouse) |
P10823 | GPA2_YEAST | MGLCASSEKNGSTPDTQTASAGSDNVGKAKVPPKQEPQKTVRTVNTANQQEKQQQRQQQPSPHNVKDRKEQNGSINNAISPTATANTSGSQQINIDSALRDRSSNVAAQPSLSDASSGSNDKELKVLLLGAGESGKSTVLQQLKILHQNGFSEQEIKEYIPLIYQNLLEIGRNLIQARTRFNVNLEPECELTQQDLSRTMSYEMPNNYTGQFPEDIAGVISTLWALPSTQDLVNGPNASKFYLMDSTPYFMENFTRITSPNYRPTQQDILRSRQMTSGIFDTVIDMGSDIKMHIYDVGGQRSERKKWIHCFDNVTLVIFC... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; ascospore formation [GO:0030437]; glucose mediated signaling pathway [GO:0010255]; hexose mediated signaling [GO:0009757]; invasive growth in response to glucose limitation [GO:0001403]; protein kinase A signaling [GO:0010737]; pseu... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterotrimeric G-protein complex [GO:0005834]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(q) subfamily | PTM: Myristoylation at Gly-2 and palmitoylation at Cys-4 are required for membrane localization and function of the protein. {ECO:0000269|PubMed:16030250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}; Lipid-anchor {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}; Cytoplasmic side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}. | null | null | null | null | null | FUNCTION: Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and hapl... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10824 | GNAI1_RAT | MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIY... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to forskolin [GO:1904322]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of synaptic transmission [GO:0050805]; positive regulat... | cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | D2 dopamine receptor binding [GO:0031749]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase act... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | PTM: Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation. {ECO:0000269|PubMed:26253820}.; PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. {ECO:0000269|PubMed:26253820}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:21158412}; Peripheral membrane protein {ECO:0000305|PubMed:24596087, ECO:0000305|PubMed:25037222}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center... | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling ... | Rattus norvegicus (Rat) |
P10826 | RARB_HUMAN | MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPATIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLE... | null | null | apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; embryonic digestive tract development [GO:0048566]; embryonic eye morphogenesis [GO:0048048]; embryonic hindlimb morphogenesis [GO:0035116]; glandular epithelial cell developmen... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; heterocyclic compound binding [GO:1901363]; nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor activity [GO:0004879]; nuclear retinoid X receptor binding [GO:0046965]; protein-containing com... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.; SUBCELLULAR LOCATION: [Isoform Beta-1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-2]: Nucleus.; SUBCELLULAR LOCATION: [Isoform Beta-4]: Cytoplasm. | null | null | null | null | null | FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) c... | Homo sapiens (Human) |
P10827 | THA_HUMAN | MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQ... | null | null | cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; erythrocyte differentiation [GO:0030218]; female courtship behavior [GO:0008050]; hormone-mediated signaling pathway [GO:0009755]; learning or memory [GO:0007611]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of DNA-tem... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; general transcription initiation factor binding [GO:0140296]; nuclear receptor activity [GO:0004879]; protein domain specific binding [GO:001990... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus.; SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm {ECO:0000250|UniProtKB:P63058}. Nucleus {ECO:0000250|UniProtKB:P63058}. Note=When overexpressed found in the cytoplasm where it colocalizes with TACC1. {ECO:0000250|UniProtKB:P63058}. | null | null | null | null | null | FUNCTION: [Isoform Alpha-1]: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. {ECO:0000269|PubMed:12699376, ECO:0000269|PubMed:14673100, ECO:0000269|PubMed:18237438, ECO:0000269|PubMed:19926848}.; F... | Homo sapiens (Human) |
P10828 | THB_HUMAN | MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVR... | null | null | cell differentiation [GO:0030154]; cellular response to thyroid hormone stimulus [GO:0097067]; DNA-templated transcription [GO:0006351]; female courtship behavior [GO:0008050]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of female receptivity [GO:0007621]; negative regulation of transcript... | chromatin [GO:0000785]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. {ECO:0000269|PubMed:12699376, ECO:0000269|PubMed:14673100, ECO:0000269|PubMed:16781732, ECO:0000269|PubMed:17418816, ECO:0000269|PubMed:182... | Homo sapiens (Human) |
P10829 | KPCG_RABIT | MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRTVPSLCGVDHTERRGRLQLEIRAPTSDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P05129}; | negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of proteasomal protein catabolic process [GO:1901799]; negative regulation of protein ubiquitination [GO:0031397]; phosphorylation [GO:0016310]; regulation of circadian rhythm [GO:0042752]; regulation of response to food [GO:0032095]; res... | cytosol [GO:0005829]; dendrite [GO:0030425]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; zinc ion binding [GO:0008270] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4. {ECO:0000250|UniProtKB:P63318}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P05129}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63318}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Transl... | 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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to op... | Oryctolagus cuniculus (Rabbit) |
P10830 | KPCE_RABIT | MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKVAGLKKQETPDEVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR... | 2.7.11.13 | null | cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; phosphorylation [GO:0016310]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cytokinesis [GO:0032467]; positive regulation of epithelial... | cell periphery [GO:0071944]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; diacylglycerol-dependent, calcium-independent serine/threonine kinase activity [GO:0004699]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on Thr-565 by PDPK1 triggers autophosphorylation on Ser-728. Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P16054}. Nucleus {ECO:0000250|UniProtKB:P16054}. Note=Translocated to plasma membrane in epithelial c... | 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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion chann... | Oryctolagus cuniculus (Rabbit) |
P10833 | RRAS_MOUSE | MSSGAASGTGRGRPRGGGPGPRDPPPGETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICTVDGIPARLDILDTAGQEEFGAMREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLRLNVDEAFEQLVRAVRKYQEQELPPSPPSAPRKKDGGCPCVLL | 3.6.5.- | null | cell migration [GO:0016477]; face morphogenesis [GO:0060325]; leukocyte differentiation [GO:0002521]; negative regulation of Schwann cell migration [GO:1900148]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matr... | cytosol [GO:0005829]; plasma membrane [GO:0005886] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: S-palmitoylated by ZDHHC19, leading to increased association with membranes and with rafts/caveolae as well as enhanced cell viability. {ECO:0000250|UniProtKB:P10301}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P62070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6207... | null | null | null | null | FUNCTION: Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity. {ECO:0000250|UniProtKB:P10301}. | Mus musculus (Mouse) |
P10842 | MATPI_SCHPM | MKRVAVLLKTVMCEFLKCDYNGYDRIISLLRRILTLICTPNLNGLTIKRVIDSMQSLEYIKQTCNFKLQMCISSMAFKRNNALQNCNHYAWCDDHCSDIGRPMTTVRGQCSKCTKPHLMRWLLLHYDNPYPSNSEFYDLSAATGLTRTQLRNWFSNRRR | null | null | animal organ morphogenesis [GO:0009887]; cellular response to pheromone [GO:0071444]; mating type determination [GO:0007531]; negative regulation of conjugation with zygote [GO:0140538]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prote... | chromatin [GO:0000785]; nucleus [GO:0005634]; Pi Mi complex [GO:0062071] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF05920; | 1.10.10.60; | TALE/M-ATYP homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Required for meiosis, but plays no role in conjugation. {ECO:0000269|PubMed:2900761}. | Schizosaccharomyces pombe (Fission yeast) |
P10844 | BXB_CLOBO | MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIY... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10932256, ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:17167418}; Note=Binds 1 zinc ion per subunit, to the LC (PubMed:10932256, PubMed:1429690, PubMed:17167418). {ECO:0000269|PubMed:10932256, ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:17... | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | lipid binding [GO:0008289]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | SUBCELLULAR LOCATION: [Botulinum neurotoxin type B]: Secreted {ECO:0000269|PubMed:3139097}. Host synapse, host presynaptic cell membrane {ECO:0000269|PubMed:14504267}. Note=Colocalizes with its SYT1 receptor, probably in synaptic vesicles (PubMed:14504267). At pH 4.4 in the presence of ganglioside GT1b becomes a membra... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000269|PubMed:1331807}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.2 uM for over-expressed human VAMP1 {ECO:0000269|PubMed:22289120}; KM=29.9 uM for over-expressed human VAMP2 {ECO:0000269|PubMed:22289120}; KM=11.6 uM for over-expressed human VAMP3 {ECO:0000269|PubMed:22289120}; Note=kcat is 3.96, 4.68 and 3.50 sec(-1) for over... | null | null | null | FUNCTION: [Botulinum neurotoxin type B]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neur... | Clostridium botulinum |
P10852 | 4F2_MOUSE | MSQDTEVDMKDVELNELEPEKQPMNAADGAAAGEKNGLVKIKVAEDETEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALYRIGDLQAFVGRDAGGIAGLKSHLEYLSTLKVKGLVLGPIHKNQKDEINETDLKQINPTLGSQEDFKDLLQSAKKKSIHIILDLTPNYQGQNAWFLPAQADIVATKMKEALSSWLQDGVDGFQFRDVGKLMNAPLYLAEWQNITKNLSEDRLLIAGTESSDLQQIVNILESTSDLLLTSSYLSNSTFTGERTESLVTRFLNAT... | null | null | carbohydrate metabolic process [GO:0005975]; isoleucine transport [GO:0015818]; L-alanine import across plasma membrane [GO:1904273]; L-histidine transport [GO:1902024]; L-leucine import across plasma membrane [GO:1903801]; leucine transport [GO:0015820]; methionine transport [GO:0015821]; neutral amino acid transport ... | amino acid transport complex [GO:1990184]; anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; apical pole of neuron [GO:0044225]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; neuronal... | aromatic amino acid transmembrane transporter activity [GO:0015173]; double-stranded RNA binding [GO:0003725]; exogenous protein binding [GO:0140272]; L-alanine transmembrane transporter activity [GO:0015180]; L-leucine transmembrane transporter activity [GO:0015190]; neutral L-amino acid secondary active transmembrane... | PF00128;PF16028; | 3.20.20.80;2.60.40.1180; | SLC3A transporter family | PTM: Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions. {ECO:0000250|UniProtKB:P08195}.; PTM: N-glycosylated; N-glycosylation is crucial for trafficking and stability of SLC3A2 to the plasma membrane. {ECO:0000250|UniProtKB:P08195}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P08195}. Cell membrane {ECO:0000269|PubMed:9915839}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08195}. Cell junction {ECO:0000269|PubMed:9915839}. Lysosome membrane {ECO:0000250|UniProtKB:P08195}. Melanosome {ECO:0000250|UniProtKB:P081... | null | null | null | null | null | FUNCTION: Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10734121, PubMed:110... | Mus musculus (Mouse) |
P10853 | H2B1F_MOUSE | MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | null | null | chromatin organization [GO:0006325]; protein localization to CENP-A containing chromatin [GO:0061644] | CENP-A containing nucleosome [GO:0043505]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specif... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
P10854 | H2B1M_MOUSE | MPEPTKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | null | null | null | nucleoplasm [GO:0005654]; nucleosome [GO:0000786] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specif... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Mus musculus (Mouse) |
P10855 | CCL3_MOUSE | MKVSTTALAVLLCTMTLCNQVFSAPYGADTPTACCFSYSRKIPRQFIVDYFETSSLCSQPGVIFLTKRNRQICADSKETWVQEYITDLELNA | null | null | astrocyte cell migration [GO:0043615]; calcium ion transport [GO:0006816]; calcium-mediated signaling [GO:0019722]; cell activation [GO:0001775]; cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II inter... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; kinase activity [GO:0016301]; phospholipase activator activity [GO:0016004]; protein kinase activity [GO:0004672] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). {ECO:0000250|UniPr... | Mus musculus (Mouse) |
P10856 | STP1_MOUSE | MSTSRKLKTHGMRRGKNRAPHKGVKRGGSKRKYRKSVLKSRKRGDDASRNYRSHL | null | null | chromatin remodeling [GO:0006338]; flagellated sperm motility [GO:0030317]; heterochromatin formation [GO:0031507]; negative regulation of DNA-templated transcription [GO:0045892]; nucleosome disassembly [GO:0006337]; positive regulation of protein processing [GO:0010954]; sexual reproduction [GO:0019953]; single stran... | male germ cell nucleus [GO:0001673]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677] | PF02079; | null | Nuclear transition protein 1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion o... | null | null | null | null | null | FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:10781074, PubMed:15083521, PubMed:15163613, PubMed:15189834, PubMed:28366643). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, whi... | Mus musculus (Mouse) |
P10860 | DHE3_RAT | MYRRLGEVLLLSRAGPAALGSAAADSAALLGWARGQPSAVPQPGLTPVARRHYSEAATDREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRENEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGLGDKTFVVQGFGNVGLHSMRYL... | 1.4.1.3 | null | cerebellum development [GO:0021549]; glutamate biosynthetic process [GO:0006537]; glutamate catabolic process [GO:0006538]; glutamine metabolic process [GO:0006541]; long-term memory [GO:0007616]; positive regulation of insulin secretion [GO:0032024]; response to aluminum ion [GO:0010044]; tricarboxylic acid metabolic ... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; enzyme binding [GO:0019899]; glutamate dehydrogenase (NAD+) activity [GO:0004352]; glutamate dehydrogenase (NADP+) activity [GO:0004354]; glutamate dehydrogenase [NAD(P)+] activity [GO:0004353]; GTP binding [GO:0005525]; leucine binding [GO:0070728]; NAD+ binding [GO:... | PF00208;PF02812; | 1.10.287.140;3.40.50.10860;3.40.50.720; | Glu/Leu/Phe/Val dehydrogenases family | PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer. {ECO:0000250|UniProtKB:P00367}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P00367}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00367}. Note=Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P00367}. | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; Evidence={ECO:0000250|UniProtKB:P00367}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (By similarity). Plays a role in insulin homeostasis (By similarity). May be involved ... | Rattus norvegicus (Rat) |
P10861 | UCP1_BOVIN | MVGHTESDVPPTMAVKIFSAGVAACVADIITFPLDTAKVRLQVGSAIQGECLISSAIRYKGVLGTIITLAKTEGPVKLYSGLPAGLQRQISFASLRIGLYDTVQEFFTTGKEASLGSKISAGLMTGGVAVFIGQPTEVVKVRLQAQSHLHGPKPRYTGTYNAYRIIATTEGLTGLWKGTTPNLTRNVIINCTELVTYDLMKEALVKNKLLADDVPCHFVSAVVAGFCTTVLSSPVDVVKTRFVNSSPGQYTSVPNCAMMMLTREGPSAFFKGFVPSFLRLGSWNIIMFVCFEQLKQELMKSRHTMDCAT | null | null | adaptive thermogenesis [GO:1990845]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen species [GO:0034614]; mitochondrial transmembrane transport [GO:1990542]; proton transmembrane transport [GO:1902600]; regulation of reactive oxygen... | mitochondrial inner membrane [GO:0005743] | cardiolipin binding [GO:1901612]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; purine ribonucleotide binding [GO:0032555] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P25874}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/... | Bos taurus (Bovine) |
P10862 | RAD18_YEAST | MDHQITTASDFTTTSIPSLYQLDTLLRCHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCLFEFRESLLRSEFLVSEIIQSYTSLRSSLLDALRIPKPTPVPENEEVPGPENSSWIELISESESDSVNAADDDLQIVATSERKLAKRSMTDILPLSSKPSKRNFAMFRSERIKKKSKPNEQMAQCPICQQFYPLKALEKTHLDECLTLQSLGKKPKISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGETSHVDKYLNSMMSAEHQRLPKINFTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYEMLWNSNFC... | 2.3.2.27 | null | DNA duplex unwinding [GO:0032508]; error-free postreplication DNA repair [GO:0042275]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; postreplication repair [GO:0006301]; protein monoubiquitination [GO:0006513] | chromatin [GO:0000785]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505] | metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]; ubiquitin protein ligase activity [GO:0061630] | PF02037;PF13923; | 3.30.160.60;3.30.40.10; | RAD18 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10880451}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach m... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10863 | TIR1_YEAST | MAYTKIALFAAIAALASAQTQDQINELNVILNDVKSHLQEYISLASDSSSGFSLSSMPAGVLDIGMALASATDDSYTTLYSEVDFAGVSKMLTMVPWYSSRLEPALKSLNGDASSSAAPSSSAAPTSSAAPSSSAAPTSSAASSSSEAKSSSAAPSSSEAKSSSAAPSSSEAKSSSAAPSSSEAKSSSAAPSSTEAKITSAAPSSTGAKTSAISQITDGQIQATKAVSEQTENGAAKAFVGMGAGVVAAAAMLL | null | null | fungal-type cell wall organization [GO:0031505] | cell periphery [GO:0071944]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole [GO:0000324]; side of membrane [GO:0098552] | structural constituent of cell wall [GO:0005199] | PF00399;PF00660; | null | SRP1/TIP1 family | PTM: O-glycosylated. {ECO:0000305}.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan ... | SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). | null | null | null | null | null | FUNCTION: Component of the cell wall. Required for anaerobic growth. {ECO:0000269|PubMed:11292809}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P10867 | GGLO_RAT | MVHGYKGVQFQNWAKTYGCSPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQITVEAGILLADLHPQLDEHGLAMSNLGAVSDVTVAGVIGSGTHNTGIKHGILATQVVALTLMTADGEVLECSESRNADVFQAARVHLGCLGIILTVTLQCVPQFHLQETSFPSTLKEVLDNLDSHLKRSEYFRFLWFPHTENVSIIYQDHTNKAPSSASNWFWDYAIGFYLLEFLLWTSTYLPCLVGWINRFFFWMLFNCKKESSNLSHKIFTYECRFKQHVQDWAIPREKTKEAL... | 1.1.3.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | L-ascorbic acid biosynthetic process [GO:0019853] | endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739] | D-arabinono-1,4-lactone oxidase activity [GO:0003885]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; L-gulono-1,4-lactone dehydrogenase activity [GO:0080049]; L-gulonolactone oxidase activity [GO:0050105]; oxidoreductase activity [GO:0016491] | PF04030;PF01565; | 3.30.465.10;3.30.70.2520;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate; Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8; | null | PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step 4/4. | null | null | FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate. {ECO:0000269|PubMed:8459881}. | Rattus norvegicus (Rat) |
P10868 | GAMT_RAT | MSSSAASPLFAPGEDCGPAWRAAPAAYDTSDTHLQILGKPVMERWETPYMHSLAAAAASRGGRVLEVGFGMAIAASRVQQAPIKEHWIIECNDGVFQRLQNWALKQPHKVVPLKGLWEEEAPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKTHAFRLLKPGGILTYCNLTSWGELMKSKYTDITAMFEETQVPALLEAGFQRENICTEVMALVPPADCRYYAFPQMITPLVTKH | 2.1.1.2 | null | animal organ morphogenesis [GO:0009887]; creatine biosynthetic process [GO:0006601]; embryonic liver development [GO:1990402]; methylation [GO:0032259]; regulation of multicellular organism growth [GO:0040014]; S-adenosylhomocysteine metabolic process [GO:0046498]; S-adenosylmethionine metabolic process [GO:0046500]; s... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | guanidinoacetate N-methyltransferase activity [GO:0030731]; identical protein binding [GO:0042802]; protein arginine N5-methyltransferase activity [GO:0019702]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | null | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, RMT2 methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947, ChEBI:CHEBI:59789; EC=2.1.1.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00892}; | null | PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 2/2. | null | null | FUNCTION: Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development. {ECO:0000250|UniProtKB:Q14353}. | Rattus norvegicus (Rat) |
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