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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P14779 | CPXB_PRIM2 | MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLN... | 1.14.14.1; 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:7578081}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10051560}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269... | metabolic process [GO:0008152]; response to hormone [GO:0009725] | cytosol [GO:0005829] | aromatase activity [GO:0070330]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity, acting on paired donors, with incorpo... | PF00667;PF00258;PF00175;PF00067; | 3.40.50.360;1.10.630.10;3.40.50.80;2.40.30.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:1169... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=250 uM for lauric acid at pH 7.4 at room temperature {ECO:0000269|PubMed:18020460}; KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone {ECO:0000269|PubMed:18020460}; KM=210 uM for N-beta-oxolauroyl-DL-homoserine {ECO:0000269|PubMed:18020460}; KM=140 uM for N-laur... | null | null | null | FUNCTION: Functions as a fatty acid monooxygenase (PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:16566047, PubMed:17077084, PubMed:1727637, PubMed:17868686, PubMed:18004886, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028, PubMed:3106359,... | Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19) (Bacillus megaterium) |
P14780 | MMP9_HUMAN | MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANY... | 3.4.24.35 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12051944}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12051944}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12051944}; Note=Binds 3 Ca(2+) ions per subunit.; | apoptotic process [GO:0006915]; cell migration [GO:0016477]; cellular response to cadmium ion [GO:0071276]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; embryo implantatio... | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; tertiary granule lumen [GO:1904724] | collagen binding [GO:0005518]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270] | PF00040;PF00045;PF00413; | 3.40.390.10;2.10.10.10;2.110.10.10; | Peptidase M10A family | PTM: Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9. {ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:1400481}.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1464361}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:2551898}. | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000269|PubMed:1480034}; | null | null | null | null | FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves N... | Homo sapiens (Human) |
P14784 | IL2RB_HUMAN | MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDTIPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDVQKWLSSPFPSSSFSPGGLAP... | null | null | cytokine-mediated signaling pathway [GO:0019221]; immunoglobulin mediated immune response [GO:0016064]; interleukin-15-mediated signaling pathway [GO:0035723]; interleukin-2-mediated signaling pathway [GO:0038110]; negative regulation of apoptotic process [GO:0043066]; positive regulation of phagocytosis [GO:0050766]; ... | cell surface [GO:0009986]; cytosol [GO:0005829]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; interleukin-2 receptor complex [GO:0005893]; membrane [GO:0016020]; plasma membrane [GO:0005886] | coreceptor activity [GO:0015026]; cytokine receptor activity [GO:0004896]; interleukin-15 receptor activity [GO:0042010]; interleukin-2 binding [GO:0019976]; interleukin-2 receptor activity [GO:0004911] | PF18707; | 2.60.40.10; | Type I cytokine receptor family, Type 4 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123770, ECO:0000269|PubMed:31040184, ECO:0000269|PubMed:31040185}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770, PubMed:31040185). {ECO:0000269|PubMed:15123770, ECO:0000... | Homo sapiens (Human) |
P14785 | CCNA_DROME | MASFQIHQDMSNKENPGIKIPAGVKNTKQPLAVIGGKAEKNALAPRANFAVLNGNNNVPRPAGKVQVFRDVRNLNVDENVEYGAKKSNVVPVVEQFKTFSVYEDNNDTQVAPSGKSLASLVDKENHDVKFGAGQKELVDYDLDSTPMSVTDVQSPMSVDRSILGVIQSSDISVGTETGVSPTGRVKELPPRNDRQRFLEVVQYQMDILEYFRESEKKHRPKPLYMRRQKDISHNMRSILIDWLVEVSEEYKLDTETLYLSVFYLDRFLSQMAVVRSKLQLVGTAAMYIAAKYEEIYPPEVGEFVFLTDDSYTKAQVLRME... | null | null | asymmetric neuroblast division [GO:0055059]; mitotic cell cycle [GO:0000278]; mitotic cell cycle phase transition [GO:0044772]; mitotic sister chromatid segregation [GO:0000070]; positive regulation of stem cell differentiation [GO:2000738]; regulation of chromatin binding [GO:0035561]; regulation of exit from mitosis ... | centrosome [GO:0005813]; cyclin A2-CDK2 complex [GO:0097124]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fusome [GO:0045169]; male germ cell nucleus [GO:0001673]; nucleus [GO:0005634]; spectrosome [GO:0045170]; synapse [GO:0045202] | cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF02984;PF00134; | 1.10.472.10; | Cyclin family, Cyclin AB subfamily | null | null | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the Cdk1 and Cdk2 protein kinases to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. | Drosophila melanogaster (Fruit fly) |
P14789 | LASA_PSEAE | MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20026068}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20026068}; | peptidoglycan catabolic process [GO:0009253]; protein secretion by the type II secretion system [GO:0015628]; protein transport by the Sec complex [GO:0043952]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01551; | 2.70.70.10; | Peptidase M23A family | PTM: Processing of pro-LasA can occur extracellularly and requires elastase (lasB) (PubMed:9642203). Secretion and processing may be linked (PubMed:8932318). {ECO:0000269|PubMed:8932318, ECO:0000269|PubMed:9642203}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179971, ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:2110137, ECO:0000269|PubMed:9642203}. Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway). {ECO:0000269|PubMed:9642203}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 9 {ECO:0000269|PubMed:20026068}; KM=61 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 8 {ECO:0000269|PubMed:20026068}; KM=105 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 7 {ECO:0000269|PubMed:20026068}; Note=kcat is... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9, inactive at pH 6 and below. {ECO:0000269|PubMed:20026068}; | null | FUNCTION: Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidoglycan), preferring Gly-Gly-|-X substrates where X is Ala or Gly (PubMed:11179971). Enhances the elastolytic but not proteolytic activity of elas... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P14791 | HMOX1_CHICK | METSQPHNAESMSQDLSELLKEATKEVHEQAENTPFMKNFQKGQVSLHEFKLVTASLYFIYSALEEEIERNKDNPVYAPVYFPMELHRKAALEKDLEYFYGSNWRAEIPCPEATQKYVERLHVVGKKHPELLVAHAYTRYLGDLSGGQVLKKIAQKALQLPSTGEGLAFFTFDGVSNATKFKQLYRSRMNALEMDHATKKRVLEEAKKAFLLNIQVFEALQKLVSKSQENGHAVQPKAELRTRSVNKSHENSPAAGKESERTSRMQADMLTTSPLVRWLLALGFIATTVAVGLFAM | 1.14.14.18 | null | heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; response to oxidative stress [GO:0006979] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872] | PF01126; | 1.20.910.10; | Heme oxygenase family | PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000250|UniProtKB:P09601}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. | CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:1724... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 uM for heme b {ECO:0000269|PubMed:2158889}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:2158889}; | null | FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:1996964, PubMed:2158889). Affords protection against programmed cell death an... | Gallus gallus (Chicken) |
P14824 | ANXA6_MOUSE | MAKIAQGAMYRGSVHDFPEFDANQDAEALYTAMKGFGSDKESILELITSRSNKQRQEICQNYKSLYGKDLIEDLKYELTGKFERLIVNLMRPLAYCDAKEIKDAISGVGTDEKCLIEILASRTNEQMHQLVAAYKDAYERDLESDIIGDTSGHFQKMLVVLLQGTRENDDVVSEDLVQQDVQDLYEAGELKWGTDEAQFIYILGNRSKQHLRLVFDEYLKTTGKPIEASIRGELSGDFEKLMLAVVKCIRSTPEYFAERLFKAMKGLGTRDNTLIRIMVSRSELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKALLKL... | null | null | apoptotic signaling pathway [GO:0097190]; calcium ion transport [GO:0006816]; growth plate cartilage chondrocyte differentiation [GO:0003418]; mitochondrial calcium ion homeostasis [GO:0051560]; negative regulation of sequestering of calcium ion [GO:0051283]; neural crest cell migration [GO:0001755]; plasma membrane re... | apical plasma membrane [GO:0016324]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; mit... | actin filament binding [GO:0051015]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cholesterol binding [GO:0015485]; chondroitin sulfate binding [GO:0035374]; GTP binding [GO:0005525]; identic... | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores. | Mus musculus (Mouse) |
P14832 | CYPH_YEAST | MSQVYFDVEADGQPIGRVVFKLYNDIVPKTAENFRALCTGEKGFGYAGSPFHRVIPDFMLQGGDFTAGNGTGGKSIYGGKFPDENFKKHHDRPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVVDGYDIVKKVESLGSPSGATKARIVVAKSGEL | 5.2.1.8 | null | ascospore formation [GO:0030437]; cellular response to starvation [GO:0009267]; DNA damage response [GO:0006974]; negative regulation of meiotic nuclear division [GO:0045835]; positive regulation of meiotic nuclear division [GO:0045836]; protein folding [GO:0006457]; protein metabolic process [GO:0019538]; protein tran... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Set3 complex [GO:0034967] | cyclosporin A binding [GO:0016018]; mRNA binding [GO:0003729]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family, PPIase A subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15643056}. Nucleus {ECO:0000269|PubMed:15643056}. Mitochondrion intermembrane space {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:8431466}; | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradatio... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14835 | PSBH_SYNY3 | MAQRTRLGDILRPLNSEYGKVVPGWGTTPVMGVFMALFLVFLLIILQIYNSSLILEGFSVDWAG | null | null | photosynthesis [GO:0015979]; protein stabilization [GO:0050821] | plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | phosphate ion binding [GO:0042301] | PF00737; | 1.20.5.880; | PsbH family | PTM: Phosphorylated in vitro in the presence or absence of light; phosphorylation is inhibited by oxidizing conditions, DCMU and zinc ions. {ECO:0000269|PubMed:8495743}. | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000269|PubMed:8495743}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:34937700}. | null | null | null | null | null | FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. May regulate electron transport between the quinone binding sites of the reaction center (PubMed:7626631, Ref.6). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to ... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
P14841 | CYTC_RAT | MASPLRSLMLLLAVLAVAWAGTSRPPPRLLGAPQEADASEEGVQRALDFAVSEYNKGSNDAYHSRAIQVVRARKQLVAGINYYLDVEMGRTTCTKSQTNLTNCPFHDQPHLMRKALCSFQIYSVPWKGTHTLTKSSCKNA | null | null | cellular response to hydrogen peroxide [GO:0070301]; cellular response to oxidative stress [GO:0034599]; defense response [GO:0006952]; embryo implantation [GO:0007566]; eye development [GO:0001654]; male gonad development [GO:0008584]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of... | axon [GO:0030424]; basement membrane [GO:0005604]; cell projection [GO:0042995]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; multivesicular body [GO:0005771]; neuronal cell body [GO:0043025]; nuclear membrane ... | amyloid-beta binding [GO:0001540]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; identical protein binding [GO:0042802]; peptidase inhibitor activity [GO:0030414]; protease binding [GO:0002020] | PF00031; | 3.10.450.10; | Cystatin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity. Known to inhibit cathepsin B, H, and L. | Rattus norvegicus (Rat) |
P14842 | 5HT2A_RAT | MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQK... | null | null | artery smooth muscle contraction [GO:0014824]; behavioral response to cocaine [GO:0048148]; chemical synaptic transmission [GO:0007268]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; G protein-... | axon [GO:0030424]; caveola [GO:0005901]; cell body fiber [GO:0070852]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; G protein-coupled serotonin receptor complex [GO:0098666]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; post... | 1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding [GO:0071886]; G protein-coupled serotonin receptor activity [GO:0004993]; Gq/11-coupled serotonin receptor activity [GO:0001587]; identical protein binding [GO:0042802]; neurotransmitter receptor activity [GO:0030594]; protein tyrosine kinase activator activity [GO:0... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11960784, ECO:0000269|PubMed:2300586, ECO:0000269|PubMed:2854054}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:11960784}. Cytoplasmic vesicle {ECO:0000269|PubMed:11960784}. Membrane, caveola {ECO:0000269|PubMed:11960784}. C... | null | null | null | null | null | FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change tha... | Rattus norvegicus (Rat) |
P14844 | CCL2_RAT | MQVSVTLLGLLFTVAACSIHVLSQPDAVNAPLTCCYSFTGKMIPMSRLENYKRITSSRCPKEAVVFVTKLKREICADPNKEWVQKYIRKLDQNQVRSETTVFYKIASTLRTSAPLNVNLTHKSEANASTLFSTTTSSTSVEVTSMTEN | null | null | animal organ regeneration [GO:0031100]; astrocyte cell migration [GO:0043615]; cellular response to ATP [GO:0071318]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to estradiol stimulus [GO:0071392]; cellular response to fatty acid [GO:0071398]; cellular response to fibroblast growth facto... | axon terminus [GO:0043679]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471] | CCR chemokine receptor binding [GO:0048020]; CCR2 chemokine receptor binding [GO:0031727]; chemokine activity [GO:0008009]; cytokine activity [GO:0005125]; G protein-coupled receptor binding [GO:0001664]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: Processing at the N-terminus can regulate receptor and target cell selectivity (By similarity). Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant (By similarity). {ECO:0000250|UniProtKB:P13500}.; PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P13500}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23955712}. | null | null | null | null | null | FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinoph... | Rattus norvegicus (Rat) |
P14846 | CARB_SALTY | MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA... | 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01210}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01210}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01210}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872] | PF02786;PF02787;PF02142; | 3.40.50.20;3.30.470.20;1.10.1030.10;3.40.50.1380; | CarB family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01210}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01210}. | null | null | FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P14847 | CRP_MOUSE | MEKLLWCLLIMISFSRTFGHEDMFKKAFVFPKESDTSYVSLEAESKKPLNTFTVCLHFYTALSTVRSFSVFSYATKKNSNDILIFWNKDKQYTFGVGGAEVRFMVSEIPEAPTHICASWESATGIVEFWIDGKPKVRKSLHKGYTVGPDASIILGQEQDSYGGDFDAKQSLVGDIGDVNMWDFVLSPEQISTVYVGGTLSPNVLNWRALNYKAQGDVFIKPQLWS | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 2 calcium ions per subunit. {ECO:0000250}; | acute-phase response [GO:0006953]; cellular response to calcium ion [GO:0071277]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of lipid storage [GO:0010888]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; negative regu... | extracellular space [GO:0005615]; filopodium [GO:0030175]; growth cone [GO:0030426] | calcium ion binding [GO:0005509]; cholesterol binding [GO:0015485]; complement component C1q complex binding [GO:0001849]; identical protein binding [GO:0042802]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein particle receptor binding [GO:0050750] | PF00354; | 2.60.120.200; | Pentraxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulati... | Mus musculus (Mouse) |
P14851 | PPIA_CRIGR | MVNPTVFFDISADGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL | 5.2.1.8 | null | activation of protein kinase B activity [GO:0032148]; apoptotic process [GO:0006915]; cell adhesion molecule production [GO:0060352]; cellular response to oxidative stress [GO:0034599]; endothelial cell activation [GO:0042118]; leukocyte chemotaxis [GO:0030595]; negative regulation of oxidative stress-induced intrinsic... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; midbody [GO:0030496]; nucleus [GO:0005634] | cyclosporin A binding [GO:0016018]; heparan sulfate binding [GO:1904399]; integrin binding [GO:0005178]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family, PPIase A subfamily | PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization (By similarity). PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity). Acetylation at Lys-125 favors the ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}. Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus {ECO:0000250|UniProtKB:P62937}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, ... | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000250|UniProtKB:P62937}; | null | null | null | null | FUNCTION: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity). ... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P14854 | CX6B1_HUMAN | MAEDMETKIKNYKTAPFDSRFPNQNQTRNCWQNYLDFHRCQKAMTAKGGDISVCEWYQRVYQSLCPTSWVTDWDEQRAEGTFPGKI | null | null | cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; substantia nigra development [GO:0021762] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | cytochrome-c oxidase activity [GO:0004129] | PF02297; | 1.10.10.140; | Cytochrome c oxidase subunit 6B family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Peripheral membrane protein {ECO:0000269|PubMed:30030519}; Intermembrane side {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:Q01519}. | 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) |
P14859 | PO2F1_HUMAN | MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGND... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978];... | PF00046;PF00157;PF19536; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-2 subfamily | PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:14612514, ECO:0000269|PubMed:1684878}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269|PubMed:10480874, ECO:000... | Homo sapiens (Human) |
P14866 | HNRPL_HUMAN | MSRRLLPRAEKRRRRLEQRQQPDEQRRRSGAMVKMAAAGGGGGGGRYYGGGSEGGRAPKRLKTDNAGDQHGGGGGGGGGAGAAGGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGP... | null | null | mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; RNA processing [GO:0006396] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; ribonucleoprotein granule [GO:0035770] | mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157]; RNA binding [GO:0003723]; transcription cis-regulatory region binding [GO:0000976] | PF00076;PF13893;PF11835; | 3.30.70.330; | null | PTM: Several isoelectric forms of the L protein are probably the results of post-translational modifications.; PTM: Phosphorylation at Ser-544 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel tran... | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:2687284, ECO:0000305|PubMed:26051023, ECO:0000305|PubMed:36537238}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodi... | null | null | null | null | null | FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprote... | Homo sapiens (Human) |
P14867 | GBRA1_HUMAN | MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVC... | null | null | chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; inhibitory synapse assembly [GO:1904862]; regulation of postsynaptic membrane potential [GO:0060078]; synaptic transmission, GABAergic [GO:0051932] | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; dendrite membrane [GO:0032590]; GABA receptor complex [GO:1902710]; GABA-A receptor complex [GO:1902711]; GABA-ergic synapse [GO:0098982]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynapti... | benzodiazepine receptor activity [GO:0008503]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; inhibitory extracellular ligand-gated monoatomic ion channel activity [GO:0005237]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membra... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRA1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P08219}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cell membrane {ECO:0000269|PubMed:2465923, ECO:0000269|PubMed:25489750}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cytoplasmic vesicle membrane {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:23909897, ECO:0000269|PubMed:29950725, ECO:0000269|PubMed:30602789}; | null | null | null | null | FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:23909897, PubMed:25489750, PubMed:29950725, PubMed:30602789). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of fi... | Homo sapiens (Human) |
P14868 | SYDC_HUMAN | MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQER... | 6.1.1.12 | null | aspartyl-tRNA aminoacylation [GO:0006422]; protein-containing complex assembly [GO:0065003]; translation [GO:0006412] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; synapse [GO:0045202] | aminoacylase activity [GO:0004046]; aspartate-tRNA ligase activity [GO:0004815]; ATP binding [GO:0005524]; RNA binding [GO:0003723] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. {ECO:0000250|UniProtKB:P15178}. | Homo sapiens (Human) |
P14869 | RLA0_MOUSE | MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLIIQQVFDNGSIYNPEVLDITEQALHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETEYTFPLTEKVKAFLADPSAFAAAAPAAAATTAAPAAAAAPAKAEAKEESEESDEDMGFGLFD | null | null | cellular response to interleukin-4 [GO:0071353]; cytoplasmic translation [GO:0002181]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; dendrite [GO:0030425]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; synapse [GO:0045202] | large ribosomal subunit rRNA binding [GO:0070180]; peptide binding [GO:0042277]; structural constituent of ribosome [GO:0003735] | PF00428;PF00466;PF17777; | 3.30.70.1730;3.90.105.20; | Universal ribosomal protein uL10 family | PTM: Ubiquitinated at Lys-264 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000250|UniProtKB:P05388}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05388}. Cytoplasm {ECO:0000250|UniProtKB:P05388}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P05388}. | null | null | null | null | null | FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. | Mus musculus (Mouse) |
P14873 | MAP1B_MOUSE | MATVVVEATEPEPSGSIGNPAASTSPSLSHRFLDSKFYLLVVVGETVTEEHLRRAIGNIELGIRSWDTNLIECNLDQELKLFVSRHSARFSPEVPGQKILHHRSDVLETVVLINPSDEAVSTEVRLMITDAARHKLLVLTGQCFENTGELILQSGSFSFQNFIEIFTDQEIGELLSTTHPANKASLTLFCPEEGDWKNSNLDRHNLQDFINIKLNSASILPEMEGLSEFTEYLSESVEVPSPFDILEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNMLINGGSERKSCFWKLIRHLDRVDSILLTHIGDDNLPGI... | null | null | axon extension [GO:0048675]; axonogenesis [GO:0007409]; cellular response to growth factor stimulus [GO:0071363]; cellular response to peptide hormone stimulus [GO:0071375]; dendrite development [GO:0016358]; developmental maturation [GO:0021700]; establishment of monopolar cell polarity [GO:0061162]; induction of syna... | apical dendrite [GO:0097440]; axon [GO:0030424]; basal dendrite [GO:0097441]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; growth cone [GO:0030426]; hippocampal mossy fiber [GO:0097457]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; neuronal cell body [GO:0043025];... | actin binding [GO:0003779]; cytoskeletal regulatory protein binding [GO:0005519]; microtubule binding [GO:0008017]; phospholipid binding [GO:0005543]; protein-containing complex binding [GO:0044877] | PF00414; | null | MAP1 family | PTM: LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B.; PTM: S-nitrosylation at Cys-2460 enhances interaction with microtubules, and may act as an effector modification f... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:21984824}. Cytoplasm {ECO:0000250}. Synapse {ECO:0000269|PubMed:21984824}. Cell projection, dendritic spine {ECO:0000269|PubMed:21984824}. Note=Colocalizes with DAPK1 in the microtubules and cortical actin fibers. {ECO:0000250}.; SUBCELLULAR LOCATION: [M... | null | null | null | null | null | FUNCTION: Required for proper microtubule dynamics. Plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule po... | Mus musculus (Mouse) |
P14881 | CRBA1_RAT | METQTVQRELETLPTTKMAQTNPMPGSMGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVECGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKITIFEKENFIGRQWEICDDYPSLQAMGWFNNEVGSMKIQCGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGTHAQTSQIQSIRRIQQ | null | null | camera-type eye development [GO:0043010]; lens development in camera-type eye [GO:0002088]; negative regulation of cytokine production [GO:0001818]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative... | null | identical protein binding [GO:0042802]; structural constituent of eye lens [GO:0005212] | PF00030; | 2.60.20.10; | Beta/gamma-crystallin family | PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. {ECO:0000250}.; PTM: The initiator methionine for isoform A1 is removed. The new N-terminal amino acid is then N-acetylated (By similarity). {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. | Rattus norvegicus (Rat) |
P14882 | PCCA_RAT | MAGLWVRTVALLAARRHWRRSSQQLLWTLKRAPRSSQQLLWTLKRAPVYSQQCLVVSRSLSSVEYEPKEKTFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTGAQAVHPGYGFLSENKEFAKCLAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVLKDADEAVRIAREIGYPVMIKASAGGGGKGMRIPWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPE... | 6.4.1.3 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000255|PROSITE-ProRule:PRU01066}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0... | amino acid catabolic process [GO:0009063]; fatty acid catabolic process [GO:0009062] | catalytic complex [GO:1902494]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]; propionyl-CoA carboxylase activity [GO:0004658]; urea carboxylase activity [GO:0004847] | PF02785;PF00289;PF00364;PF02786;PF18140; | 2.40.50.100;3.30.700.30;3.40.50.20;3.30.1490.20;3.30.470.20; | null | PTM: Acetylated. {ECO:0000250|UniProtKB:Q91ZA3}.; PTM: The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity. Biotinylation is catalyzed by HLCS. {ECO:0000250|UniProtKB:P05165}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P05165}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3; Evidence={ECO:0000250|UniProtKB:P... | null | PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3. {ECO:0000250|UniProtKB:P05165}. | null | null | FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylati... | Rattus norvegicus (Rat) |
P14891 | HMDH1_ARATH | MDLRRRPPKPPVTNNNNSNGSFRSYQPRTSDDDHRRRATTIAPPPKASDALPLPLYLTNAVFFTLFFSVAYYLLHRWRDKIRYNTPLHVVTITELGAIIALIASFIYLLGFFGIDFVQSFISRASGDAWDLADTIDDDDHRLVTCSPPTPIVSVAKLPNPEPIVTESLPEEDEEIVKSVIDGVIPSYSLESRLGDCKRAASIRREALQRVTGRSIEGLPLDGFDYESILGQCCEMPVGYIQIPVGIAGPLLLDGYEYSVPMATTEGCLVASTNRGCKAMFISGGATSTVLKDGMTRAPVVRFASARRASELKFFLENPEN... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; isoprenoid biosynthetic process [GO:0008299]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420] | PF00368; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | PTM: Inactivated by phosphorylation at Ser-577 by KIN10 activated form (PubMed:28263378). Probably also phosphorylated at additional sites (PubMed:10318703, PubMed:7588795). {ECO:0000269|PubMed:10318703, ECO:0000269|PubMed:28263378, ECO:0000269|PubMed:7588795}. | SUBCELLULAR LOCATION: [Isoform Short]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15618432, ECO:0000269|PubMed:8302869}; Multi-pass membrane protein {ECO:0000255}. Note=Also observed within spherical structures located along the endoplasmic reticulum strands. {ECO:0000269|PubMed:15618432, ECO:0000269|PubMed:830... | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003}; | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants. {ECO:0000269|PubMed:14871314, ECO:0000269|PubMed:17917299, ECO:0000269|PubMed:19041104, ECO:0000269|PubMed:19363204}. | Arabidopsis thaliana (Mouse-ear cress) |
P14894 | CONA_CANGL | MAISKKSSLFLPIFTFITMFLMVVNKVSSSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDANVIRNSTTIDFNAAYNADTIVAVELDTYPNTDIGDPNYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNEIPDIATVV | null | null | negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of cell division [GO:0051781]; positive regulation of mitotic nuclear division [GO:0045840]; regulation of defense response to virus [GO:0050688] | null | mannose binding [GO:0005537]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: The mature chain consists of residues 164-281 followed by 30-148. To form a mature chain the precursor undergoes further post-translational modification after removal of the signal sequence; cleavage after Asn at positions Asn-148, Asn-163, and Asn-281 is followed by transposition and ligation (By formation of a n... | null | null | null | null | null | null | FUNCTION: Glucose/D-mannose/rhamnose specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes that is inhibited by glucose. Inhibits HIV-1 reverse transcriptase with an IC(50) of 35 uM. Has a potent antiproliferative activity against L1210 leukemia ce... | Canavalia gladiata (Sword bean) (Dolichos gladiatus) |
P14900 | MURD_ECOLI | MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLNDEWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHLNHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEHNGVRWINDSK... | 6.3.2.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:1765076}; | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; UDP-N-acetylmuramoylalanine-D-glutamate ligase activity [GO:0008764] | PF02875;PF08245;PF21799; | 3.90.190.20;3.40.1190.10;3.40.50.720; | MurCDEF family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:4562... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.5 uM for UDP-N-acetylmuramoyl-L-alanine {ECO:0000269|PubMed:1765076}; KM=55 uM for D-glutamate {ECO:0000269|PubMed:1765076}; KM=138 uM for ATP/ Mg(2+) {ECO:0000269|PubMed:1765076}; Note=The optimum activity is at 11-16 mM for potassium phosphate and at 5 mM for M... | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000305|PubMed:1765076}; | null | FUNCTION: Cell wall formation (Probable). Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (PubMed:1765076). {ECO:0000269|PubMed:1765076, ECO:0000305}. | Escherichia coli (strain K12) |
P14901 | HMOX1_MOUSE | MERPQPDSMPQDLSEALKEATKEVHIQAENAEFMKNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEIIPCTPATQHYVKRLHEVGRTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQVMLTEEHKDQSPSQMASLRQRPASLVQDTAPAETPRGKPQISTSSSQTPLLQWVLTLSFLLATVAVGIYAM | 1.14.14.18 | null | angiogenesis [GO:0001525]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to cisplatin [GO:0072719]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; epithelial cell apoptotic process [GO:1904019]; erythr... | caveola [GO:0005901]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | arachidonic acid omega-hydroxylase activity [GO:0052869]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]; phospholipase D activity [GO:0004630]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:00... | PF01126; | 1.20.910.10; | Heme oxygenase family | PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000250|UniProtKB:P09601}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. | CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:1724... | null | null | null | null | FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (By similarity) Affords protection against programmed cell death and this cytoprotect... | Mus musculus (Mouse) |
P14902 | I23O1_HUMAN | MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFV... | 1.13.11.52 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:16477023, ECO:0000269|PubMed:25313323}; Note=Binds 1 heme group per subunit (PubMed:16477023, PubMed:25313323). In the active form, the heme iron is in its ferrous state Fe(+2). The catalytic cycle does not alter the oxidation state of the heme... | 'de novo' NAD biosynthetic process from tryptophan [GO:0034354]; female pregnancy [GO:0007565]; inflammatory response [GO:0006954]; kynurenic acid biosynthetic process [GO:0034276]; multicellular organismal response to stress [GO:0033555]; negative regulation of interleukin-10 production [GO:0032693]; negative regulati... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; smooth muscle contractile fiber [GO:0030485]; stereocilium bundle [GO:0032421] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; indoleamine 2,3-dioxygenase activity [GO:0033754]; metal ion binding [GO:0046872]; tryptophan 2,3-dioxygenase activity [GO:0004833] | PF01231; | 1.20.58.480; | Indoleamine 2,3-dioxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P28776, ECO:0000303|PubMed:25691885}. | CATALYTIC ACTIVITY: Reaction=D-tryptophan + O2 = N-formyl-D-kynurenine; Xref=Rhea:RHEA:14189, ChEBI:CHEBI:15379, ChEBI:CHEBI:57719, ChEBI:CHEBI:60051; EC=1.13.11.52; Evidence={ECO:0000269|PubMed:17671174}; CATALYTIC ACTIVITY: Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine; Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.23 uM for L-tryptophan {ECO:0000269|PubMed:18026683}; KM=4.6 mM for D-tryptophan {ECO:0000269|PubMed:18026683}; Note=Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.; | PATHWAY: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. | null | null | FUNCTION: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174). Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolle... | Homo sapiens (Human) |
P14904 | AMPL_YEAST | MEEQREILEQLKKTLQMLTVEPSKNNQIANEEKEKKENENSWCILEHNYEDIAQEFIDFIYKNPTTYHVVSFFAELLDKHNFKYLSEKSNWQDSIGEDGGKFYTIRNGTNLSAFILGKNWRAEKGVGVIGSHVDALTVKLKPVSFKDTAEGYGRIAVAPYGGTLNELWLDRDLGIGGRLLYKKKGTNEIKSALVDSTPLPVCRIPSLAPHFGKPAEGPFDKEDQTIPVIGFPTPDEEGNEPPTDDEKKSPLFGKHCIHLLRYVAKLAGVEVSELIQMDLDLFDVQKGTIGGIGKHFLFAPRLDDRLCSFAAMIALICYAK... | 3.4.11.22 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9ULA0, ECO:0000269|PubMed:3882418, ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147, ECO:0000269|PubMed:6352682, ECO:0000269|Ref.6}; Note=Binds 2 Zn(2+) ions per subunit. The average amount of Zn(2+) bound at physiological metal concentr... | cytoplasm to vacuole targeting by the Cvt pathway [GO:0032258]; proteolysis [GO:0006508] | Cvt complex [GO:0034270]; cytoplasm [GO:0005737]; fungal-type vacuole [GO:0000324] | identical protein binding [GO:0042802]; metalloaminopeptidase activity [GO:0070006]; zinc ion binding [GO:0008270] | PF02127; | 2.30.250.10;3.40.630.10; | Peptidase M18 family | PTM: Synthesized in a precursor form (prApe1) that has an amino-terminal propeptide. The N-terminal extension of the 61 kDa precursor is proteolytically processed in two sequential steps. The first step involves proteinase A (PrA/PEP4) and produces a 55 kDa unstable intermediate (iAPI). The second step involves protein... | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:24493041, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:8601598}. Note=Transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway. {ECO:0000269|PubMed:9151668, ECO:0000269|PubMed:9214379, ECO:0000269|PubMed:9412464}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.; EC=3.4.11.22; Evidence={ECO:0000269|PubMed:19185714, ECO:0000269|PubMed:363165, ECO:0000269|PubMed:3890752, ECO:0000269|PubMed:5147, ECO:0000269|PubMe... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8.5. {ECO:0000269|PubMed:5147}; | null | FUNCTION: Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the a... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14906 | SEC63_YEAST | MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDKNSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKGLTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVSRWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNN... | null | null | cytosol to endoplasmic reticulum transport [GO:0046967]; post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; post-translational protein targeting to membrane, translocation [GO:0031204]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614] | endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear inner membrane [GO:0005637]; rough endoplasmic reticulum membrane [GO:0030867]; Sec62/Sec63 complex [GO:0031207]; translocon complex [GO:0071256] | protein transmembrane transporter activity [GO:0008320]; RNA binding [GO:0003723] | PF00226; | 1.10.287.110; | null | PTM: Phosphotylated by casein kinase II. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Acts as a component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from S... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14907 | NSP1_YEAST | MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPTSNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGNANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFGSGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKP... | null | null | ncRNA export from nucleus [GO:0097064]; NLS-bearing protein import into nucleus [GO:0006607]; nucleocytoplasmic transport [GO:0006913]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein import into nucleus [GO:0006606]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from ... | nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore central transport channel [GO:0044613]; nuclear pore nuclear basket [GO:0044615] | phospholipid binding [GO:0005543]; structural constituent of nuclear pore [GO:0017056] | PF05064; | 1.20.5.170; | Nucleoporin NSP1/NUP62 family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. | null | null | null | null | null | FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14908 | MTF1_YEAST | MSVPIPGIKDISKLKFFYGFKYLWNPTVYNKIFDKLDLTKTYKHPEELKVLDLYPGVGIQSAIFYNKYCPRQYSLLEKRSSLYKFLNAKFEGSPLQILKRDPYDWSTYSNLIDEERIFVPEVQSSDHINDKFLTVANVTGEGSEGLIMQWLSCIGNKNWLYRFGKVKMLLWMPSTTARKLLARPGMHSRSKCSVVREAFTDTKLIAISDANELKGFDSQCIEEWDPILFSAAEIWPTKGKPIALVEMDPIDFDFDVDNWDYVTRHLMILKRTPLNTVMDSLGHGGQQYFNSRITDKDLLKKCPIDLTNDEFIYLTKLFME... | 2.1.1.- | null | mitochondrial transcription [GO:0006390]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; transcription initiation at mitochondrial promoter [GO:0006391] | mitochondrial DNA-directed RNA polymerase complex [GO:0034245]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | DNA binding [GO:0003677]; mitochondrial transcription factor activity [GO:0034246]; RNA binding [GO:0003723]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179] | PF00398; | 1.10.8.100;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, rRNA adenine N(6)-methyltransferase family | null | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}. | null | null | null | null | null | FUNCTION: Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14916 | URE23_HELPY | MKLTPKELDKLMLHYAGELAKKRKEKGIKLNYVEAVALISAHIMEEARAGKKTAAELMQEGRTLLKPDDVMDGVASMIHEVGIEAMFPDGTKLVTVHTPIEANGKLVPGELFLKNEDITINEGKKAVSVKVKNVGDRPVQIGSHFHFFEVNRCLDFDREKTFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVDRQADNESKKIALHRAKERGFHGAKSDDNYVKTIKE | 3.5.1.5 | null | urea catabolic process [GO:0043419] | urease complex [GO:0035550] | nickel cation binding [GO:0016151]; urease activity [GO:0009039] | PF00699;PF00547; | 2.10.150.10;3.30.280.10; | Urease gamma subunit family; Urease beta subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01955, ECO:0000269|PubMed:8641799}. Note=Also associates with the outer membrane upon autolysis of neighboring bacteria. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01955, ECO:0000269|PubMed:1612735, ECO:0000269|PubMed:2188975}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.48 mM for urea {ECO:0000269|PubMed:2188975}; Vmax=1.1 mmol/min/mg enzyme {ECO:0000269|PubMed:2188975}; | PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01955}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered solutions, the dodecameric complex is active at pH 3.0. {ECO:0000269|PubMed:11373617, ECO:0000269|PubMed:2188975}; | null | FUNCTION: Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach. {ECO:0000269|PubMed:8039935}. | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
P14920 | OXDA_HUMAN | MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHW... | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16616139, ECO:0000269|PubMed:17088322, ECO:0000269|PubMed:17303072, ECO:0000269|PubMed:18455394, ECO:0000269|PubMed:19438227, ECO:0000269|PubMed:20521334, ECO:0000269|PubMed:20603179, ECO:0000269|PubMed:23566269, ECO:0000269|PubMed:23631755, ECO:0... | D-alanine catabolic process [GO:0055130]; D-amino acid catabolic process [GO:0019478]; D-serine catabolic process [GO:0036088]; D-serine metabolic process [GO:0070178]; digestion [GO:0007586]; dopamine biosynthetic process [GO:0042416]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; proline catabo... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; presynaptic active zone [GO:0048786] | D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949]; identical protein binding [GO:0042802] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | PTM: Phosphorylated in the cerebellum; probably not by PRKACA, PRKCA or PRKCE. {ECO:0000269|PubMed:34041270}.; PTM: May be S-nitrosylated, which partially inactivates the enzyme. {ECO:0000269|PubMed:34041270}. | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:18544534, ECO:0000269|PubMed:20368421, ECO:0000269|PubMed:21679769, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:31799256, ECO:0000305|PubMed:17880399, ECO:0000305|PubMed:29274788}. Cytoplasm, cytosol {ECO:0000269|PubMed:1854453... | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:16616139, ECO:0000269|PubMed:17088322, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 mM for D-serine {ECO:0000269|PubMed:17088322, ECO:0000269|PubMed:17303072}; KM=7.5 mM for D-serine (at 25 degrees Celsius and at pH 8.5) {ECO:0000269|PubMed:16616139, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:31799256}; KM=7.41 mM for D-serine {ECO:000026... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5-10. {ECO:0000269|PubMed:29326945}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:29326945}; | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:16616139, PubMed:17088322, PubMed:17303072, PubMed:18544534, PubMed:20368421, PubMed:20567862, PubMed:20603179, PubMed:22203986, PubMed:23219954, PubMed:23391306, PubMed:25030849, PubMed:25701391, PubMed:29274788, Pu... | Homo sapiens (Human) |
P14921 | ETS1_HUMAN | MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPV... | null | null | cell differentiation [GO:0030154]; cell motility [GO:0048870]; immune response [GO:0006955]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; PML body organization [GO:0030578]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blo... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; nuclear receptor coactivato... | PF00178;PF19525;PF02198; | 1.10.150.50;1.10.10.10; | ETS family | PTM: Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which inhibits transcriptional activity. {ECO:0000250|UniProtKB:P27577}.; PTM: Ubiquitinated; which induces proteasomal degradation. {ECO:0000250|UniProtKB:P27577}.; PTM: Phosphorylation at Ser-251, Ser-282 and Ser-285 by CaMK2/CaMKII in response to calc... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:19377509}. Cytoplasm {ECO:0000269|PubMed:19377509}. Note=Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27. {ECO:0000269|PubMed:19377509}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angio... | Homo sapiens (Human) |
P14922 | CYC8_YEAST | MNPGGEQTIMEQPAQQQQQQQQQQQQQQQQAAVPQQPLDPLTQSTAETWLSIASLAETLGDGDRAAMAYDATLQFNPSSAKALTSLAHLYRSRDMFQRAAELYERALLVNPELSDVWATLGHCYLMLDDLQRAYNAYQQALYHLSNPNVPKLWHGIGILYDRYGSLDYAEEAFAKVLELDPHFEKANEIYFRLGIIYKHQGKWSQALECFRYILPQPPAPLQEWDIWFQLGSVLESMGEWQGAKEAYEHVLAQNQHHAKVLQQLGCLYGMSNVQFYDPQKALDYLLKSLEADPSDATTWYHLGRVHMIRTDYTAAYDAFQ... | null | null | chromatin remodeling [GO:0006338]; hyperosmotic response [GO:0006972]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polym... | MLL3/4 complex [GO:0044666]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | chromatin DNA binding [GO:0031490]; histone deacetylase binding [GO:0042826]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714] | PF00515;PF13432; | 1.25.40.10; | CYC8/SSN6 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Acts as a component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14923 | PLAK_HUMAN | MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMR... | null | null | bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; canonical Wnt signaling pathway [GO:0060070]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cellular response to indole-3-methanol [GO:0071681]; desmosome assembly [GO:0002159]; detection of mechanical stimulus [GO... | adherens junction [GO:0005912]; catenin complex [GO:0016342]; cell-cell junction [GO:0005911]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; extracell... | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; cell adhesion molecule binding [GO:0050839]; cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication [GO:0086083]; cytoskeletal protein-membrane anchor activity [GO:0106006]; DNA-binding transcription factor binding [... | PF00514; | 1.25.10.10; | Beta-catenin family | PTM: May be phosphorylated by FER. {ECO:0000269|PubMed:14517306}. | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:22781308}. Cell junction, desmosome {ECO:0000269|PubMed:22781308}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22781308}. Cell membrane {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:22781308}; Peripheral membrane protein {ECO:0000269|PubMed:2... | null | null | null | null | null | FUNCTION: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctio... | Homo sapiens (Human) |
P14925 | AMD_RAT | MAGRARSGLLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIM... | 1.14.17.3; 4.3.2.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds one Zn(2+) ion per subunit. {ECO:0000269|PubMed:19604476}; COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Note=Binds 2 Cu(2+) ions per subunit. {ECO:0000269|PubMed:10504734}; | fatty acid primary amide biosynthetic process [GO:0062112]; heart development [GO:0007507]; lactation [GO:0007595]; limb development [GO:0060173]; long-chain fatty acid metabolic process [GO:0001676]; maternal process involved in female pregnancy [GO:0060135]; mitotic chromosome condensation [GO:0007076]; ovulation cyc... | cell surface [GO:0009986]; chromatin [GO:0000785]; condensed chromosome [GO:0000793]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; secretory granule [GO:0030141]; trans-Golgi network [GO:00058... | calcium ion binding [GO:0005509]; chromatin binding [GO:0003682]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; L-ascorbic acid binding [GO:0031418]; peptidylamidoglycolate lyase activity [GO:0004598]; peptidylglycine monooxygenase activity [GO:0004504]; protein kinase binding [GO:0019901]; z... | PF03712;PF01082;PF01436; | 2.60.120.230;2.60.120.310;2.120.10.30; | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P10731}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10731}. Note=Secretory granules. {ECO:0000250|UniProtKB:P10731}. | 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... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.8 uM for [peptide]-C-terminal (2S)-2-hydroxyglycine {ECO:0000269|PubMed:19604476}; | null | null | 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 (By similarity). Alpha-amidation involves two sequential reactions... | Rattus norvegicus (Rat) |
P14927 | QCR7_HUMAN | MAGKQAVSASGKWLDGIRKWYYNAAGFNKLGLMRDDTIYEDEDVKEAIRRLPENLYNDRMFRIKRALDLNLKHQILPKEQWTKYEEENFYLEPYLKEVIRERKEREEWAKK | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidative phosphorylation [GO:0006119] | mitochondrial inner membrane [GO:0005743]; mitochondrial respirasome [GO:0005746]; mitochondrial respiratory chain complex III [GO:0005750] | null | PF02271; | 1.10.1090.10; | UQCRB/QCR7 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00128}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00128}; Matrix side {ECO:0000250|UniProtKB:P00128}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Homo sapiens (Human) |
P14930 | MSRAB_NEIGO | MKHRTFFSLCAKFGCLLALGACSPKIVDAGTATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGQAEKWAQDAKFSSANLITVASPGFLHEKKDGEFQKWYAGLNYPKLPVVTDNGGTIAQNLNISVYPSWALIGKDGDVQRIVKGSINEAQALALIRNPNADLGSLKHSFYKPDTQKKDSAIMNTRTIYLAGGCFWGLEAYFQRIDGVVDAVSGYANGNTENPSYEDVSYRHTGHAETVKVTYDADKLSLDDILQYYFRVVDPTSLNKQGNDTGTQYRSGVYYTDPAEKAVIAAALKREQQKYQLPL... | 1.8.4.11; 1.8.4.12 | null | protein modification process [GO:0036211]; protein repair [GO:0030091]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737] | L-methionine:thioredoxin-disulfide S-oxidoreductase activity [GO:0033744]; peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; peptide-methionine (S)-S-oxide reductase activity [GO:0008113] | PF01625;PF08534;PF01641; | 3.40.30.10;2.170.150.20;3.30.1060.10; | Thioredoxin family; MsrA Met sulfoxide reductase family; MsrB Met sulfoxide reductase family | null | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHE... | null | null | null | null | FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. {ECO:0000250}. | Neisseria gonorrhoeae |
P14942 | GSTA4_RAT | MEVKPKLYYFQGRGRMESIRWLLATAGVEFEEEFLETREQYEKLQKDGCLLFGQVPLVEIDGMLLTQTRAILSYLAAKYNLYGKDLKERVRIDMYADGTQDLMMMIIGAPFKAPQEKEESLALAVKRAKNRYFPVFEKILKDHGEAFLVGNQLSWADIQLLEAILMVEEVSAPVLSDFPLLQAFKTRISNIPTIKKFLQPGSQRKPPPDGHYVDVVRTVLKF | 2.5.1.18 | null | cellular response to lithium ion [GO:0071285]; glutathione metabolic process [GO:0006749]; response to herbicide [GO:0009635]; response to nicotine [GO:0035094]; response to zinc ion [GO:0010043]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737] | glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; organic cyclic compound binding [GO:0097159]; protein homodimerization activity [GO:0042803]; toxic substance binding [GO:0015643] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. | Rattus norvegicus (Rat) |
P14943 | EST2_RABIT | QDSASPIRNTHTGQVRGSLVHVEGTDAGVHTFLGIPFAKPPLGPLRFAPPEPAEAWSGVRDGTSLPAMCLQNLAIMDQDVLLLHFTPPSIPMSEDCLYLNIYSPAHAREGSDLPVMVWIHGGGLTMGMASMYDGSALAAFEDVVVVTIQYRLGVLGFFSTGDQHATGNHGYLDQVAALRWVQKNIAHFGGNPGRVTIFGESAGGTSVSSHVLSPMSQGLFHGAIMESLVALLPGLITSSSEVVSTVVANLSRCGQVDSETLVRCLRAKSEEEMLAITQVFMLIPGVVDGVFLPRHPEELLALADFQPVPSIIGINNDEYG... | 3.1.1.1; 3.1.1.84 | null | lipid metabolic process [GO:0006629] | endoplasmic reticulum lumen [GO:0005788] | carboxylesterase activity [GO:0106435] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O00748}. | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; CATALYTIC ACTIVITY: Reaction=cocaine + H2O = benzoa... | null | null | null | null | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (By similarity). {ECO:0000250|UniProtKB:O00748}. | Oryctolagus cuniculus (Rabbit) |
P14950 | ANX11_COLLI | MAVVSEFLKQAWFMENLEQECIKCTQCVHGVPQQTNFDPSADVVALEKAMTAKGVDEATIIDIMTTRTNAQRPRIKAAYHKAKGKSLEEAMKRVLKSHLEDVVVALLKTPAQFDAEELRACMKGHGTDEDTLIEILASRNNKEIREACRYYKEVLKRDLTQDIISDTSGDFQKALVSLAKADRCENPHVNDELAEKDARALYEAGEQKKGTDINVFVTVLTARSYPHSEVFQKYTKYSKHDMNKAVDMEMKGDIEKCLTALVKCATSKPAFFAEKLHMAMKGFGTQHRDLIRIMVSRHEVDMNEIKGYYKKMYGISLCQA... | null | null | alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to vascular endothelial growth factor stimulus ... | basolateral plasma membrane [GO:0016323]; cilium [GO:0005929]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phospholipase A2 inhibitor activity [GO:0019834] | PF00191; | 1.10.220.10; | Annexin family | PTM: In contrast to mammalian homologs, does not contain a tyrosine phosphorylation site in the N-terminal part. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Note=Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium. Found in the cytoplasm of type II pneumocytes and alveolar ... | null | null | null | null | null | FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity. | Columba livia (Rock dove) |
P14956 | CECB_DROME | MNFNKIFVFVALILAISLGNSEAGWLRKLGKKIERIGQHTRDASIQVLGIAQQAANVAATARG | null | null | antibacterial humoral response [GO:0019731]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to insect [GO:0002213]; humoral immune response [GO:0006959]; innate immune response [GO:0045087] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00272; | null | Cecropin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. | Drosophila melanogaster (Fruit fly) |
P14997 | VP2_POVBA | MGAALALLGDLVASVSEAAAATGFSVAEIAAGEAAAAIEVQIASLATVEGITTTSEAIAAIGLTPQTYAVIAGAPGAIAGFAALIQTVTGISSLAQVGYRFFSDWDHKVSTVGLYQQSGMALELFNPDEYYDILFPGVNTFVNNIQYLDPRHWGPSLFATISQALWHVIRDDIPAITSQELQRRTERFFRDSLARFLEETTWTIVNAPINFYNYIQDYYSNLSPIRPSMVRQVAEREGTHVNFGHTYSIDNADSIEEVTQRMDLRNKESVHSGEFIEKTIAPGGANQRTAPQWMLPLLLGLYGTVTPALEAYEDGPNQKK... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; protein complex oligomerization [GO:0051259]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; viral penetration into host nucleus [GO:0075732]; virion attachment to host cell [GO:0019062] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198] | PF00761; | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP4]: Host ... | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | BK polyomavirus (strain AS) (BKPyV) |
P15005 | MCRB_ECOLI | MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAYGISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF... | 3.1.21.- | null | DNA catabolic process [GO:0006308]; DNA restriction-modification system [GO:0009307] | endonuclease complex [GO:1905348] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; double-stranded methylated DNA binding [GO:0010385]; endonuclease activity [GO:0004519]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; hemi-methylated DNA-binding [GO:0044729]; identical protein binding [GO:0042802]; res... | PF07728;PF12102; | 3.30.920.90;3.40.50.300; | null | null | null | null | null | null | null | null | FUNCTION: Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may ... | Escherichia coli (strain K12) |
P15007 | ENO_DROME | MSWTASVFLRTSTTSMKFLRLRWPLPRIPQNKSANVAPRFRSKSAVSQLSSGFKFVQIRKSTCDSNEMTIKAIKARQIYDSRGNPTVEVDLTTELGLFRAAVPSGASTGVHEALELRDNDKANYHGKSVLKAVGHVNDTLGPELIKANLDVVDQASIDNFMIKLDGTENKSKFGANAILGVSLAVAKAGAAKKGVPLYKHIADLAGNKEIILPVPAFNVINGGSHAGNKLAMQEFMILPTGATSFTEAMKMGSEVYHHLKNVIKAKFGLDATAVGDEGGFAPNIQSNKEALNLISDAIAKAGYTGKIEIGMDVAASEFYK... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. | null | null | null | Drosophila melanogaster (Fruit fly) |
P15018 | LIF_HUMAN | MKVLAAGVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF | null | null | blood vessel remodeling [GO:0001974]; cell morphogenesis [GO:0000902]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; fibroblast proliferation [GO:0048144]; gene expression [GO:0010467]; immune response [GO:0006955]; leukemia inhibitory factor signaling pathway [GO:0048861]; lung alveolus development [... | cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; leukemia inhibitory factor receptor binding [GO:0005146]; signaling receptor binding [GO:0005102] | PF01291; | 1.20.1250.10; | LIF/OSM family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. | Homo sapiens (Human) |
P15019 | TAL1_YEAST | MSEPAQKKQKVANNSLEQLKASGTVVVADTGDFGSIAKFQPQDSTTNPSLILAAAKQPTYAKLIDVAVEYGKKHGKTTEEQVENAVDRLLVEFGKEILKIVPGRVSTEVDARLSFDTQATIEKARHIIKLFEQEGVSKERVLIKIASTWEGIQAAKELEEKDGIHCNLTLLFSFVQAVACAEAQVTLISPFVGRILDWYKSSTGKDYKGEADPGVISVKKIYNYYKKYGYKTIVMGASFRSTDEIKNLAGVDYLTISPALLDKLMNSTEPFPRVLDPVSAKKEAGDKISYISDESKFRFDLNEDAMATEKLSEGIRKFSA... | 2.2.1.2 | null | carbohydrate metabolic process [GO:0005975]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, non-oxidative branch [GO:0009052] | cytosol [GO:0005829]; nucleus [GO:0005634] | transaldolase activity [GO:0004801] | PF00923; | 3.20.20.70; | Transaldolase family, Type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2; Evidence={ECO:0000269|PubMed:2185015, ECO:0000269|PubMed:8109173}... | null | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. {ECO:0000305|PubMed:2185015}. | null | null | FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. {ECO:0000269|PubMed:2185015}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15028 | FECB_ECOLI | MLAFIRFLFAGLLLVISHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVIPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQPLTVVK | null | null | intracellular iron ion homeostasis [GO:0006879]; iron import into cell [GO:0033212]; response to iron ion [GO:0010039]; siderophore-dependent iron import into cell [GO:0033214] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288] | null | PF01497; | 3.40.50.1980; | Bacterial solute-binding protein 8 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2651410, ECO:0000269|PubMed:2836368}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex FecBCDE involved in citrate-dependent Fe(3+) uptake (PubMed:17660286, PubMed:2651410). Binds both iron-free and iron-loaded citrate although it binds iron-loaded citrate with a higher affinity (PubMed:26600288). Binds different forms of Fe(3+)-citrate as well as citrate com... | Escherichia coli (strain K12) |
P15029 | FECD_ECOLI | MKIALVIFITLALAGCALLSLHMGVIPVPWRALLTDWQAGHEHYYVLMEYRLPRLLLALFVGAALAVAGVLIQGIVRNPLASPDILGVNHAASLASVGALLLMPSLPVMVLPLLAFAGGMAGLILLKMLAKTHQPMKLALTGVALSACWASLTDYLMLSRPQDVNNALLWLTGSLWGRDWSFVKIAIPLMILFLPLSLSFCRDLDLLALGDARATTLGVSVPHTRFWALLLAVAMTSTGVAACGPISFIGLVVPHMMRSITGGRHRRLLPVSALTGALLLVVADLLARIIHPPLELPVGVLTAIIGAPWFVWLLVRMR | null | null | intracellular iron ion homeostasis [GO:0006879]; iron import into cell [GO:0033212]; siderophore-dependent iron import into cell [GO:0033214] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | iron chelate transmembrane transporter activity [GO:0015603]; transmembrane transporter activity [GO:0022857] | PF01032; | 1.10.3470.10; | Binding-protein-dependent transport system permease family, FecCD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2651410}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex FecBCDE involved in citrate-dependent Fe(3+) uptake (PubMed:17660286, PubMed:2651410). Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000269|PubMed:17660286, ECO:0000269|PubMed:2651410, ECO:0000305}. | Escherichia coli (strain K12) |
P15030 | FECC_ECOLI | MTAIKHPVLLWGLPVAALIIIFWLSLFCYSAIPVSGADATRALLPGHTPTLPEALVQNLRLPRSLVAVLIGASLALAGTLLQTLTHNPMASPSLLGINSGAALAMALTSALSPTPIAGYSLSFIAACGGGVSWLLVMTAGGGFRHTHDRNKLILAGIALSAFCMGLTRITLLLAEDHAYGIFYWLAGGVSHARWQDVWQLLPVVVTAVPVVLLLANQLNLLNLSDSTAHTLGVNLTRLRLVINMLVLLLVGACVSVAGPVAFIGLLVPHLARFWAGFDQRNVLPVSMLLGATLMLLADVLARALAFPGDLPAGAVLALIG... | null | null | intracellular iron ion homeostasis [GO:0006879]; iron import into cell [GO:0033212]; siderophore-dependent iron import into cell [GO:0033214] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | iron chelate transmembrane transporter activity [GO:0015603]; transmembrane transporter activity [GO:0022857] | PF01032; | 1.10.3470.10; | Binding-protein-dependent transport system permease family, FecCD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2651410}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex FecBCDE involved in citrate-dependent Fe(3+) uptake (PubMed:17660286, PubMed:2651410). Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000269|PubMed:17660286, ECO:0000269|PubMed:2651410, ECO:0000305}. | Escherichia coli (strain K12) |
P15034 | AMPP_ECOLI | MSEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPEKLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRKGSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAMEKCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETSLRLYRPGTSILEVTGEVVR... | 3.4.11.9 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 manganese ions per subunit.; | protein homotetramerization [GO:0051289]; proteolysis [GO:0006508] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | aminopeptidase activity [GO:0004177]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235] | PF05195;PF00557; | 3.90.230.10;3.40.350.10; | Peptidase M24B family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; | null | null | null | null | null | Escherichia coli (strain K12) |
P15036 | ETS2_HUMAN | MNDFGIKNMDQVAPVANSYRGTLKRQPAFDTFDGSLFAVFPSLNEEQTLQEVPTGLDSISHDSANCELPLLTPCSKAVMSQALKATFSGFKKEQRRLGIPKNPWLWSEQQVCQWLLWATNEFSLVNVNLQRFGMNGQMLCNLGKERFLELAPDFVGDILWEHLEQMIKENQEKTEDQYEENSHLTSVPHWINSNTLGFGTEQAPYGMQTQNYPKGGLLDSMCPASTPSVLSSEQEFQMFPKSRLSSVSVTYCSVSQDFPGSNLNLLTNNSGTPKDHDSPENGADSFESSDSLLQSWNSQSSLLDVQRVPSFESFEDDCSQ... | null | null | ectodermal cell fate commitment [GO:0001712]; mesoderm development [GO:0007498]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primitive streak formation [GO:0090009]; regulation of transcription by RNA polymerase II [GO:0... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA binding [GO:0003677]; 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 glucocorticoid receptor binding [GO:0035259]; protein domai... | PF00178;PF19525;PF02198; | 1.10.150.50;1.10.10.10; | ETS family | PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a phosphodegron that targets ETS2 for proteasomal degradation. {ECO:0000269|PubMed:24218572}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor activating transcription. Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription. {ECO:0000269|PubMed:11909962}. | Homo sapiens (Human) |
P15037 | ETS2_MOUSE | MNDFGIKNMDQVAPVANSFRGTLKRQPAFDTFDGSLFAVLPSLSEDQTLQEVPTGLDSVSHDSASCELPLLTPCSKAVMSQALKATFSGFQKEQRRLGIPKNPWLWSEQQVCQWLLWATNEFSLVNVNLHQFGMNGQMLCNLGKERFLELAPDFVGDILWEHLEQMIKENQEKTEDQYEENSHLNAVPHWINSNTLGFSMEQAPYGMQAPNYPKDNLLDSMCPPSATPAALGSELQMLPKSRLNTVNVNYCSISQDFPSSNVNLLNNNSGKPKDHDSPENGGDSFESSDSLLRSWNSQSSLLDVQRVPSFESFEEDCSQS... | null | null | ectodermal cell fate commitment [GO:0001712]; mesoderm development [GO:0007498]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primitive streak formation [GO:0090009]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear glucocorticoid receptor binding [GO:0035259]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-r... | PF00178;PF19525;PF02198; | 1.10.150.50;1.10.10.10; | ETS family | PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a phosphodegron that targets ETS2 for proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor activating transcription. Binds specifically the GGA DNA motif in gene promoters and stimulates transcription of those genes (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P15042 | DNLJ_ECOLI | MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKNNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQ... | 6.5.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11781321}; | base-excision repair, DNA ligation [GO:0006288]; DNA ligation [GO:0006266]; DNA replication [GO:0006260] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403] | PF00533;PF01653;PF03120;PF03119;PF12826;PF14520; | 6.20.10.30;1.10.150.20;3.40.50.10190;3.30.470.30;1.10.287.610;2.40.50.140; | NAD-dependent DNA ligase family, LigA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000269|PubMed:11781321}; | null | null | null | null | FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Escherichia coli (strain K12) |
P15043 | RECQ_ECOLI | MAQAEVLNLESGAKQVLQETFGYQQFRPGQEEIIDTVLSGRDCLVVMPTGGGKSLCYQIPALLLNGLTVVVSPLISLMKDQVDQLQANGVAAACLNSTQTREQQLEVMTGCRTGQIRLLYIAPERLMLDNFLEHLAHWNPVLLAVDEAHCISQWGHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYMLMEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSKGISAAAYHAGLENNVRADVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY... | 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2164680}; Note=Requires Mg(2+) for helicase activity (PubMed:2164680). {ECO:0000269|PubMed:2164680}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14517231, ECO:0000312|PDB:1OYW, ECO:0000312|PDB:1OYY}; | DNA damage response [GO:0006974]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; SOS response [GO:0009432]; ... | bacterial nucleoid [GO:0043590]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; replisome [GO:0030894]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; single-stranded D... | PF00270;PF00271;PF00570;PF16124;PF09382; | 1.10.150.80;3.40.50.300;1.10.10.10; | Helicase family, RecQ subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:12771204, ECO:0000269|PubMed:2164680}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:C... | null | null | null | null | FUNCTION: An ATP-dependent DNA helicase which unwinds DNA in a 3'-5' direction (PubMed:12771204, PubMed:16084389, PubMed:2164680, PubMed:9553043). Involved in the RecF recombination pathway (PubMed:2993821). ATPase activity is stimulated by ssDNA but only very poorly by dsDNA (PubMed:2164680). Binds to and unwinds a wi... | Escherichia coli (strain K12) |
P15047 | ENTA_ECOLI | MDFSGKNVWVTGAGKGIGYATALAFVEAGAKVTGFDQAFTQEQYPFATEVMDVADAAQVAQVCQRLLAETERLDALVNAAGILRMGATDQLSKEDWQQTFAVNVGGAFNLFQQTMNQFRRQRGGAIVTVASDAAHTPRIGMSAYGASKAALKSLALSVGLELAGSGVRCNVVSPGSTDTDMQRTLWVSDDAEEQRIRGFGEQFKLGIPLGKIARPQEIANTILFLASDLASHITLQDIVVDGGSTLGA | 1.3.1.28 | null | enterobactin biosynthetic process [GO:0009239] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity [GO:0008667]; identical protein binding [GO:0042802] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-dihydroxybenzoate + H(+) + NADH; Xref=Rhea:RHEA:23824, ChEBI:CHEBI:15378, ChEBI:CHEBI:36654, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58764; EC=1.3.1.28; Evidence={ECO:0000269|PubMed:2144454}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 mM for methyl 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454}; KM=0.3 mM for 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454}; KM=1.7 mM for methyl-3-hydroxy-1,4... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the transient intermedi... | Escherichia coli (strain K12) |
P15054 | SRC_AVIS2 | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. | Avian sarcoma virus (strain PR2257) |
P15056 | BRAF_HUMAN | MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSA... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | animal organ morphogenesis [GO:0009887]; CD4-positive or CD8-positive, alpha-beta T cell lineage commitment [GO:0043369]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; cellular response to calcium ion [GO:0071277]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to xeno... | cell body [GO:0044297]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; MAP kinase kinase activity [GO:0004708]; MAP kinase kinase kinase activity [GO:0004709]; mitogen-activated protein kinase kinase binding [GO:0031434]; protein kinase activity [GO:0004672]; protein serine kinase activity ... | PF00130;PF07714;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Ser-365 by SGK1 inhibits its activity. {ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:1508179, ECO:0000269|PubMed:19710016, ECO:0000269|Ref.8}.; PTM: Methylation at Arg-671 decreases stability and kinase activity. {ECO:0000269|PubMed:21917714}.; PTM: Ubiquitinated by RNF149; which leads to pro... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:19710016}. Cell membrane {ECO:0000269|PubMed:19710016}. Note=Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:21441910, ECO:000026... | null | null | null | null | FUNCTION: Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway (PubMed:21441910, PubMed:29433126). Phosphorylates PFKFB2 (PubMed:36402789). May play a role in the postsyn... | Homo sapiens (Human) |
P15057 | LYS_BPCP1 | MVKKNDLFVDVSSHNGYDITGILEQMGTTNTIIKISESTTYLNPCLSAQVEQSNPIGFYHFARFGGDVAEAEREAQFFLDNVPMQVKYLVLDYEDDPSGDAQANTNACLRFMQMIADAGYKPIYYSYKPFTHDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLLDDEEDDKPKTAGTWKQDSKGWWFRRNNGSFPYNKWEKIGGVWYYFDSKGYCLTSEWLKDNEKWYYLKDNGAMATGWVLVGSEWYYMDDSGAMVTGWVKYKNNWYYMTNERGNMVSNEFIKSGKGWYFMNTNG... | 3.2.1.17 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659] | null | lysozyme activity [GO:0003796] | PF01473;PF19127;PF01183; | 2.10.270.10;3.20.20.80;2.20.120.10; | Glycosyl hydrolase 25 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Strictly depends on the presence of choline-containing cell walls for activity. | Streptococcus phage Cp-1 (Bacteriophage Cp-1) |
P15064 | RASG_DICDI | MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVTIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSFDEIASFREQILRVKDKDRVPMIVVGNKCDLESDRQVTTGEGQDLAKSFGSPFLETSAKIRVNVEEAFYSLVREIRKDLKGDSKPEKGKKKRPLKACTLL | 3.6.5.2 | null | actin filament organization [GO:0007015]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; aggregation involved in sorocarp development [GO:0031152]; asexual reproduction [GO:0019954]; cell morphogenesis [GO:0000902]; cell-substrate adhesion [GO:0031589]; cellular response to cGMP... | cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cytoplasmic side of plasma membrane [GO:0009898]; lipid droplet [GO:0005811]; macropinosome [GO:0044354]; pathogen-containing vacuole [GO:0140220]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | adenylate cyclase activator activity [GO:0010856]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanylate cyclase activator activity [GO:0030250]; kinase binding [GO:0019900]; phosphatidylinositol 3-kinase binding [GO:0043548]; phosphatidylinositol 3... | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000305|PubMed:18948008}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:18948008}. | Dictyostelium discoideum (Social amoeba) |
P15066 | JUND_MOUSE | METPFYGEEALSGLAAGASSVAGATGAPGGGGFAPPGRAFPGAPPTSSMLKKDALTLSLAEQGAAGLKPGSATAPSALRPDGAPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSTQFLYPKVAASEEQEFAEGFVKALEDLHKQSQLGAATAATSGAPAPPAPADLAATPGATETPVYANLSSFAGGAGPPGGAATVAFAAEPVPFPPPPGALGPPPPPHPPRLAALKDEPQTVPDVPSFGDSPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQ... | null | null | cellular response to calcium ion [GO:0071277]; gene expression [GO:0010467]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast development [GO:0002076]; positive regulation of macrophage activation [GO:0043032]; positive regulation of osteoblast differentiation [GO:0045669]; positive re... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:001989... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is inhibited in the presence of MEN1. {ECO:0000250|UniProtKB:P17535}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor binding AP-1 sites (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing its transcriptional activity (By similarity). {ECO:0000... | Mus musculus (Mouse) |
P15067 | GLGX_ECOLI | MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASAC... | 3.2.1.196 | null | DNA damage response [GO:0006974]; glycogen catabolic process [GO:0005980] | null | amylo-alpha-1,6-glucosidase activity [GO:0004135]; glycogen debranching enzyme activity [GO:0004133] | PF00128;PF02922;PF18390; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.; EC=3.2.1.196; Evidence={ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}; | null | PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.6 to 6.4. {ECO:0000269|PubMed:779849}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:779849}; | FUNCTION: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. Shows only very little activity with native glycogen. {ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}. | Escherichia coli (strain K12) |
P15072 | POLG_FMDVT | MNTTDCFIAVVNAIREIRALFLPRTTGKMEFTLHDGEKKVFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLEAIKQLEELTGLELREGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFMKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNEGWKANVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTF... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.; PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of ... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate -/Germany/C1Oberbayen/1960 serotype C) (FMDV) |
P15073 | ENV_MCFF | MEGPAFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPRNQGPCYDSSVVSSGIQGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGIDPVTRFSLTRQVLNIGPRLPIGPNPVITGQLPPSRPVQIRLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAGPPYYEG... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Mink cell focus-forming murine leukemia virus |
P15083 | PIGR_RAT | MRLSLFALLVTVFSGVSTQSPIFGPQDVSSIEGNSVSITCYYPDTSVNRHTRKYWCRQGANGYCATLISSNGYLSKEYSGRASLINFPENSTFVINIAHLTQEDTGSYKCGLGTTNRGLFFDVSLEVSQVPEFPNDTHVYTKDIGRTVTIECRFKEGNAHSKKSLCKKRGEACEVVIDSTEYVDPSYKDRAILFMKGTSRDIFYVNISHLIPSDAGLYVCQAGEGPSADKNNADLQVLEPEPELLYKDLRSSVTFECDLGREVANDAKYLCRKNKETCDVIINTLGKRDPAFEGRILLTPRDDNGRFSVLITGLRKEDAG... | null | null | detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc receptor signaling pathway [GO:0038093]; immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor [GO:0002415]; receptor cl... | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; recycling endosome membrane [GO:0055038]; secretory IgA immunoglobulin complex [GO:0071751] | epidermal growth factor receptor binding [GO:0005154]; polymeric immunoglobulin binding [GO:0001790]; polymeric immunoglobulin receptor activity [GO:0001792] | PF07686; | 2.60.40.10; | null | PTM: N-glycosylated. N-glycosylation is required for anchoring IgA molecules to mucus, but is not necessary for Ig binding. {ECO:0000250|UniProtKB:P01833}. | SUBCELLULAR LOCATION: [Polymeric immunoglobulin receptor]: Cell membrane {ECO:0000250|UniProtKB:P01833}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secretory component]: Secreted {ECO:0000250|UniProtKB:P01833}. | null | null | null | null | null | FUNCTION: [Polymeric immunoglobulin receptor]: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, ... | Rattus norvegicus (Rat) |
P15085 | CBPA1_HUMAN | MRGLLVLSVLLGAVFGKEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPGSPIDVRVPFPSIQAVKIFLESHGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYATYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILDTLDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQLLMYPYGYKT... | 3.4.17.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:18566513}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18566513}; | leukotriene metabolic process [GO:0006691]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to cadmium ion [GO:0046686] | extracellular space [GO:0005615] | metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF00246;PF02244; | 3.30.70.340;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9UI42}. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1; Evidence={ECO:0000269|PubMed:20385563, ECO:0000269|PubMed:8806703}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = glycine + leukotriene F4; Xref=Rhea:RHEA:50740, ChEBI:CHEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.4 uM for 3-(2-furyl)acryloyl-Phe-Phe (at 25 degrees Celsius) {ECO:0000269|PubMed:20385563}; KM=166 uM for 3-(2-furyl)acryloyl-Phe-Trp (at 25 degrees Celsius) {ECO:0000269|PubMed:20385563}; KM=15.7 uM for 3-(2-furyl)acryloyl-Phe-Leu (at 25 degrees Celsius) {ECO:0... | null | null | null | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (PubMed:20385563, PubMed:8806703). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond (By similarity). {ECO:0000250|UniProtKB:P0... | Homo sapiens (Human) |
P15086 | CBPB1_HUMAN | MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKL... | 3.4.17.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12162965}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12162965}; | proteolysis [GO:0006508] | cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615] | carboxypeptidase activity [GO:0004180]; metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF00246;PF02244; | 3.30.70.340;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00732}. Zymogen granule lumen {ECO:0000250|UniProtKB:P55261}. | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:20600119}; | null | null | null | null | null | Homo sapiens (Human) |
P15087 | CBPE_RAT | MAGRGGRVLLALCAALVAGGWLLAAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQRGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNLKKIVDQNSKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGTAHEYSSCPDDAIFQSLARAYSSFNPVMSDPNRPPCRKNDDDSSFVDGTTNGGAWY... | 3.4.17.10 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | cardiac left ventricle morphogenesis [GO:0003214]; enkephalin processing [GO:0034230]; insulin processing [GO:0030070]; negative regulation of branching morphogenesis of a nerve [GO:2000173]; peptide catabolic process [GO:0043171]; peptide hormone processing [GO:0016486]; peptide hormone secretion [GO:0030072]; peptide... | dendrite [GO:0030425]; dense core granule [GO:0031045]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667]; synaptic membrane [GO:0097060]; tr... | carboxypeptidase activity [GO:0004180]; cell adhesion molecule binding [GO:0050839]; cobalt ion binding [GO:0050897]; metallocarboxypeptidase activity [GO:0004181]; neurexin family protein binding [GO:0042043]; protein domain specific binding [GO:0019904]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:14597614}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:14597614}; Peripheral membrane protein {ECO:0000269|PubMed:14597614}. Secreted {ECO:0000269|PubMed:14597614}. Note=Associated with the secretory granule membran... | CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; | null | null | null | null | FUNCTION: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. {ECO:0000250|UniProtKB:Q00493}. | Rattus norvegicus (Rat) |
P15088 | CBPA3_HUMAN | MRLILPVGLIATTLAIAPVRFDREKVFRVKPQDEKQADIIKDLAKTNELDFWYPGATHHVAANMMVDFRVSEKESQAIQSALDQNKMHYEILIHDLQEEIEKQFDVKEDIPGRHSYAKYNNWEKIVAWTEKMMDKYPEMVSRIKIGSTVEDNPLYVLKIGEKNERRKAIFTDCGIHAREWVSPAFCQWFVYQATKTYGRNKIMTKLLDRMNFYILPVFNVDGYIWSWTKNRMWRKNRSKNQNSKCIGTDLNRNFNASWNSIPNTNDPCADNYRGSAPESEKETKAVTNFIRSHLNEIKVYITFHSYSQMLLFPYGYTSKL... | 3.4.17.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | angiotensin maturation [GO:0002003]; proteolysis [GO:0006508] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; transport vesicle [GO:0030133] | metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF00246;PF02244; | 3.30.70.340;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1; | null | null | null | null | null | Homo sapiens (Human) |
P15090 | FABP4_HUMAN | MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA | null | null | brown fat cell differentiation [GO:0050873]; cellular response to lithium ion [GO:0071285]; cellular response to tumor necrosis factor [GO:0071356]; cholesterol homeostasis [GO:0042632]; fatty acid transport [GO:0015908]; long-chain fatty acid transport [GO:0015909]; negative regulation of DNA-templated transcription [... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lipid droplet [GO:0005811]; nucleus [GO:0005634] | fatty acid binding [GO:0005504]; hormone receptor binding [GO:0051427]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P... | null | null | null | null | null | FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. {ECO:0000250|UniProtKB:P04117}. | Homo sapiens (Human) |
P15101 | DOPO_BOVIN | MQVPSPSVREAASMYGTAVAVFLVILVAALQGSAPAESPFPFHIPLDPEGTLELSWNISYAQETIYFQLLVRELKAGVLFGMSDRGELENADLVVLWTDRDGAYFGDAWSDQKGQVHLDSQQDYQLLRAQRTPEGLYLLFKRPFGTCDPNDYLIEDGTVHLVYGFLEEPLRSLESINTSGLHTGLQRVQLLKPSIPKPALPADTRTMEIRAPDVLIPGQQTTYWCYVTELPDGFPRHHIVMYEPIVTEGNEALVHHMEVFQCAAEFETIPHFSGPCDSKMKPQRLNFCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRF... | 1.14.17.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:2620060, ECO:0000269|PubMed:4525162}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:4525162}; | dopamine catabolic process [GO:0042420]; norepinephrine biosynthetic process [GO:0042421]; octopamine biosynthetic process [GO:0006589] | chromaffin granule lumen [GO:0034466]; chromaffin granule membrane [GO:0042584]; extracellular space [GO:0005615]; secretory granule lumen [GO:0034774]; secretory granule membrane [GO:0030667]; transport vesicle membrane [GO:0030658] | copper ion binding [GO:0005507]; dopamine beta-monooxygenase activity [GO:0004500]; L-ascorbic acid binding [GO:0031418] | PF03712;PF01082;PF03351; | 2.60.120.230;2.60.120.310; | Copper type II ascorbate-dependent monooxygenase family | PTM: Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form. {ECO:0000269|PubMed:2620060}.; PTM: N-glycosylated. {ECO:0000269|PubMed:1693949, ECO:0000269|PubMed:2295597, ECO:0000269|PubMed:4525162}. | SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic vesicle, secretory vesicle lumen. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000269|PubMed:843373, ECO:0000305|PubMed:2620060}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type II m... | CATALYTIC ACTIVITY: Reaction=dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:19117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:59905, ChEBI:CHEBI:72587; EC=1.14.17.1; Evidence={ECO:0000269|PubMed:2620060, ECO:000026... | null | PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1. {ECO:0000269|PubMed:2620060}. | null | null | FUNCTION: Catalyzes the hydroxylation of dopamine to noradrenaline (also known as norepinephrine), and is thus vital for regulation of these neurotransmitters. {ECO:0000269|PubMed:2620060}. | Bos taurus (Bovine) |
P15103 | GLNA_BOVIN | MATSASSHLNKGIKQVYMALPQGDKVQAMYIWIDGTGEGLRCKTRTLDSEPKCIEELPEWNFDGSSTFQSEGSNSDMYLVPAAMFRDPFRKDPNKLVFCEVFKYNRKPAETNLRHTCKRIMDMVSNQRPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGIKIGGTNAEVMPAQWEFQIGPCEGIDMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRG... | 2.3.1.225; 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P09606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15104}; | angiogenesis [GO:0001525]; glutamine biosynthetic process [GO:0006542]; protein palmitoylation [GO:0018345]; regulation of endothelial cell migration [GO:0010594]; regulation of sprouting angiogenesis [GO:1903670] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872]; protein-cysteine S-palmitoyltransferase activity [GO:0019706] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000250|UniProtKB:P15104}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P15104}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000250|UniProtKB:P15104}; Lipid-anchor {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol, with a fraction associated wit... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P15104}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of th... | Bos taurus (Bovine) |
P15104 | GLNA_HUMAN | MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRS... | 2.3.1.225; 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P09606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18005987}; | angiogenesis [GO:0001525]; cell population proliferation [GO:0008283]; cellular response to starvation [GO:0009267]; glutamate catabolic process [GO:0006538]; glutamine biosynthetic process [GO:0006542]; protein palmitoylation [GO:0018345]; regulation of endothelial cell migration [GO:0010594]; regulation of protein lo... | cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; glial cell projection [GO:0097386]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-cysteine S-palmitoyltransferase activity [GO:0019706] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000305|PubMed:30158707}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30158707, ECO:0000269|PubMed:36289327}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000269|PubMed:30158707}; Lipid-anchor {ECO:0000269|PubMed:30158707}. Note=Mainly localizes in the cytosol, with... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:16267323, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, w... | Homo sapiens (Human) |
P15105 | GLNA_MOUSE | MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSEGSNSDMYLHPVAMFRDPFRKDPNKLVLCEVFKYNRKPAETNLRHICKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKITGTNAEVMPAQWEFQIGPCEGIRMGDHLWIARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKCIEEAIDKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRG... | 2.3.1.225; 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P09606}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15104}; | ammonia assimilation cycle [GO:0019676]; angiogenesis [GO:0001525]; cell population proliferation [GO:0008283]; cellular response to starvation [GO:0009267]; glutamate metabolic process [GO:0006536]; glutamine biosynthetic process [GO:0006542]; positive regulation of epithelial cell proliferation [GO:0050679]; positive... | axon terminus [GO:0043679]; cell body [GO:0044297]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; glial cell projection [GO:0097386]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein-c... | ATP binding [GO:0005524]; dynein light chain binding [GO:0045503]; glutamate binding [GO:0016595]; glutamine synthetase activity [GO:0004356]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; nickel cation binding [GO:0016151]; protein-cysteine S-palmitoylt... | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000250|UniProtKB:P15104}.; PTM: Ubiquitinated by ZNRF1. {ECO:0000269|PubMed:20107048}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P15104}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000250|UniProtKB:P15104}; Lipid-anchor {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol, with a fraction associated wit... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P15104}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (By similarity). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of th... | Mus musculus (Mouse) |
P15107 | SOD1B_XENLA | MVKAVCVLAGSGDVKGVVHFEQQDEGAVSVEGKIEGLTDGLHGFHIHVFGDNTNGCMSAGSHFNPENKNHGAPGDTDRHVGDLGNVTAEGGVAQFKITDSLISLKGPNSIIGRTAVVHEKADDLGKGGNDESLKTGNAGGRLACGVIGYSP | 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.; | null | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | 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. | Xenopus laevis (African clawed frog) |
P15108 | HSC82_YEAST | MAGETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPKQLETEPDLFIRITPKPEEKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKNNEDEQYIWESNAGGSFTVTLDEVNERIGRGTVLRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLLVTKEVEKEVPIPEEEKKDEEKKDEDDKKPKLEEVDEEEEEKKPKTKKVKEEVQELEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIP... | null | null | box C/D snoRNP assembly [GO:0000492]; cellular response to heat [GO:0034605]; proteasome assembly [GO:0043248]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; response to oxygen levels [GO:0070482]; telomere maintenance [GO:0000723] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15116 | CADH2_MOUSE | MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLPKDVHEGQPLLNVKFSNCNRKRKVQYESSEPADFKVDEDGTVYAVRSFPLTAEQAKFLIYAQDKETQEKWQVAVNLSREPTLTEEPMKEPHEIEEIVFPRQLAKHSGALQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNM... | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; brain morphogenesis [GO:0048854]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell morphogenes... | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; ... | alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; gamma-catenin binding [GO:0045295]; identical protein binding [GO:0042802]; nitric-oxide synthase binding [GO:0050998]; protein kinase binding [GO:0019901]... | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: Cleaved by MMP24 (PubMed:19805319, PubMed:24952463). Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa (PubMed:24952463). Cleavage in neural stem cells by MM... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17988630, ECO:0000269|PubMed:26403541, ECO:0000269|PubMed:9655503}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Cell junction {ECO:0000269|PubMed:26750727}. Cell junction, adherens junction {ECO:00002... | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell (PubMed:11433297, PubMed:17988630, PubMed:25253890, PubMed:2762814, PubMed:9655503). Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts ... | Mus musculus (Mouse) |
P15121 | ALDR_HUMAN | MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF | 1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54 | null | C21-steroid hormone biosynthetic process [GO:0006700]; carbohydrate metabolic process [GO:0005975]; cellular hyperosmotic salinity response [GO:0071475]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; epithelial cell maturation [GO:0002070]; fructose biosynthetic process [GO:00... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; electron transfer activity [GO:0009055]; glyceraldehyde oxidoreductase activity [GO:0043795]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; L-glucuronate reductase activity [GO:0047939]; NADP-retinol dehydro... | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21; Evidence={ECO:0000269|PubMed:8245005}; CATALYTIC ACTIVITY: Reaction=al... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:12732097}; KM=76000 uM for glucose {ECO:0000269|PubMed:12732097}; KM=14 uM for pyridine-3-carbaldehyde {ECO:0000269|PubMed:12732097}; KM=10 uM for all-trans-retinal {ECO:0000269|PubMed:12732097}; KM=12 uM for 9-cis-r... | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the pol... | Homo sapiens (Human) |
P15122 | ALDR_RABIT | MATHLVLYNGAKMPILGLGTWKSPPGQVTEAVKTAIDLGYRHIDCAHVYQNENEVGVALQEKLKEQVVKREELFIVSKLWCTSHDKSLVKGACQKTLNDLKLDYLDLYLIHWPTGFKHGSEYFPLDAAGNVIPSDTDFLDTWEAMEGLVDEGLVKSIGVSNFNHLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIADKHKKTTAQVLIRFPMQRNLVVIPKSVTPARIAENFQVFDFELSSEDMTTLLSYNRNWRVCALVSCASHKDYPFHAEF | 1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54 | null | retinoid metabolic process [GO:0001523] | cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; NADP-retinol dehydrogenase activity [GO:0052650]; prostaglandin H2 endoperoxidase reductase activity [GO:0036130]; retinal dehydrogenase activity [GO:0001758] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21; Evidence={ECO:0000250|UniProtKB:P15121}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.; FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displa... | Oryctolagus cuniculus (Rabbit) |
P15127 | INSR_RAT | MGSGRGCETTAVPLLMAVAVAGGTAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDYVEDNYIVLNKDDNEECGDVCPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHKECLGNCSEPDDPTKCVACRNFYLDGQCVETCPPPYYHFQDWRCVNFSFCQDLHYKCRNSRKPGCHQYVIHNNKCIPECPSGYTM... | 2.7.10.1 | null | adrenal gland development [GO:0030325]; amyloid-beta clearance [GO:0097242]; animal organ morphogenesis [GO:0009887]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; cellular response to zinc ion starvation [GO:0034224]; cerebellum development [GO:0021549]; ... | axon [GO:0030424]; caveola [GO:0005901]; dendrite membrane [GO:0032590]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; insulin receptor complex [GO:0005899]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO... | 3-phosphoinositide-dependent protein kinase binding [GO:0043423]; amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; cargo receptor activity [GO:0038024]; GTP binding [GO:0005525]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-li... | PF00041;PF00757;PF17870;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. {ECO:0000250|UniProtKB:P06213}.; PTM: Autophosphorylated on tyrosine residues in response to insulin. Phosphor... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15208}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000250|UniProtKB:P15208}. Lysosome {ECO:0000250|UniProtKB:P15208}. Note=Binding of insulin to INSR induces internalization and lysosomal degradation of the receptor, a means for dow... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as ... | Rattus norvegicus (Rat) |
P15129 | CP4B1_RAT | MVLNFLSPSLSRLGLWASVVILMVIVLKLFSLLLRRQKLARAMDSFPGPPTHWLFGHALEIQKLGSLDKVVSWAQQFPHAHPLWFGQFVGFLNIYEPDYAKAVYSRGDPKAADVYDFFLQWIGKGLLVLDGPKWFQHRKLLTPGFHYDVLKPYVAIFAESTRMMLDKWEKKASENKSFDIFCDVGHMALDTLMKCTFGKGDSGLGHRDNSYYLAVSDLTLLMQQRIDSFQYHNDFIYWLTPHGRRFLRACKIAHDHTDEVIRQRKAALQDEKERKKIQQRRHLDFLDILLGVRDESGIKLSDAELRAEVDTFMFEGHDTT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P51869}; | biphenyl metabolic process [GO:0018879] | endoplasmic reticulum membrane [GO:0005789] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; heterocyclic compound binding [GO:1901363]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | 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) |
P15133 | E3RDA_ADE02 | MIPRVLILLTLVALFCACSTLAAVAHIEVDCIPPFTVYLLYGFVTLILICSLVTVVIAFIQFIDWVCVRIAYLRHHPQYRDRTIADLLRIL | null | null | null | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; membrane [GO:0016020] | null | PF03376; | null | Adenoviridae E3-RID-alpha family | PTM: The signal peptide is only cleaved partially by host signal peptidase. This results in two forms of the protein, one uncleaved with two transmembrane regions, and one cleaved with one transmembrane region (PubMed:1531278). {ECO:0000269|PubMed:1531278}. | SUBCELLULAR LOCATION: [Pre-early 3 receptor internalization and degradation alpha protein]: Host membrane; Multi-pass membrane protein. Host endoplasmic reticulum.; SUBCELLULAR LOCATION: [Early 3 receptor internalization and degradation alpha protein]: Host membrane; Single-pass type I membrane protein. Host endoplasmi... | null | null | null | null | null | FUNCTION: Prevents infected cell apoptosis induced by the host immune system. Acts by down-regulating a number of cell surface receptors in the tumor necrosis factor (TNF) receptor superfamily, namely FAS, TNFRSF10A/TRAIL receptor 1, and TNFRSF10B/TRAIL receptor 2. Down-regulation of these death receptors protects aden... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
P15144 | AMPN_HUMAN | MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNV... | 3.4.11.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22932899}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22932899}; | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667] | aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; metallopeptidase activity [GO:0008237]; peptide binding [GO:0042277]; signaling receptor activity [GO:0038023]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:9056417}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:00... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564851, ECO:0000269|PubMed:9056417}; Single-pass type II membrane protein {ECO:0000305|PubMed:1350662}. Note=Also found as a soluble form. {ECO:0000269|PubMed:7902291}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; E... | null | null | null | null | FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May a... | Homo sapiens (Human) |
P15145 | AMPN_PIG | MAKGFYISKALGILGILLGVAAVATIIALSVVYAQEKNKNAEHVPQAPTSPTITTTAAITLDQSKPWNRYRLPTTLLPDSYNVTLRPYLTPNADGLYIFKGKSIVRLLCQEPTDVIIIHSKKLNYTTQGHMVVLRGVGDSQVPEIDRTELVELTEYLVVHLKGSLQPGHMYEMESEFQGELADDLAGFYRSEYMEGNVKKVLATTQMQSTDARKSFPCFDEPAMKATFNITLIHPNNLTALSNMPPKGSSTPLAEDPNWSVTEFETTPVMSTYLLAYIVSEFQSVNETAQNGVLIRIWARPNAIAEGHGMYALNVTGPIL... | 3.4.11.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22876187}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22876187}; | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: Sulfated. {ECO:0000269|PubMed:3121301}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000250|UniProtKB:P15144}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7913510}; Single-pass type II membrane protein {ECO:0000305|PubMed:7913510}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; E... | null | null | null | null | FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May a... | Sus scrofa (Pig) |
P15146 | MTAP2_RAT | MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGG... | null | null | axonogenesis [GO:0007409]; cellular response to organic substance [GO:0071310]; central nervous system neuron development [GO:0021954]; dendrite development [GO:0016358]; dendrite morphogenesis [GO:0048813]; establishment of cell polarity [GO:0030010]; microtubule bundle formation [GO:0001578]; microtubule cytoskeleton... | actin cytoskeleton [GO:0015629]; apical dendrite [GO:0097440]; apical distal dendrite [GO:0150014]; axon hillock [GO:0043203]; axon initial segment [GO:0043194]; basal dendrite [GO:0097441]; CA3 pyramidal cell dendrite [GO:0097442]; cell body [GO:0044297]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendrite cytopla... | actin binding [GO:0003779]; calmodulin binding [GO:0005516]; dystroglycan binding [GO:0002162]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901] | PF08377;PF00418; | null | null | PTM: Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Isoform 3/MAP2c is probably phosphorylated by PKA at Ser-319, Ser-350 and Ser-382 and by FYN at Tyr-67. The interaction with KNDC1 enhance... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:P20357}. | null | null | null | null | null | FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. | Rattus norvegicus (Rat) |
P15149 | CP2A2_RAT | MLDTGLLLVVILASLSVMFLVSLWQQKIRERLPPGPTPLPFIGNYLQLNMKDVYSSITQLSERYGPVFTIHLGPRRIVVLYGYDAVKEALVDQAEEFSGRGELPTFNILFKGYGFSLSNVEQAKRIRRFTIATLRDFGVGKRDVQECILEEAGYLIKTLQGTCGAPIDPSIYLSKTVSNVINSIVFGNRFDYEDKEFLSLLEMIDEMNIFAASATGQLYDMFHSVMKYLPGPQQQIIKVTQKLEDFMIEKVRQNHSTLDPNSPRNFIDSFLIRMQEEKYVNSEFHMNNLVMSSLGLLFAGTGSVSSTLYHGFLLLMKHPD... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | coumarin metabolic process [GO:0009804]; epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; 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... | 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: Highly active in the 15-alpha-hydroxylation of testosterone. | Rattus norvegicus (Rat) |
P15150 | C11B1_BOVIN | MALWAKARVRMAGPWLSLHEARLLGTRGAAAPKAVLPFEAMPRCPGNKWMRMLQIWKEQSSENMHLDMHQTFQELGPIFRYDVGGRHMVFVMLPEDVERLQQADSHHPQRMILEPWLAYRQARGHKCGVFLLNGPQWRLDRLRLNPDVLSLPALQKYTPLVDGVARDFSQTLKARVLQNARGSLTLDIAPSVFRYTIEASTLVLYGERLGLLTQQPNPDSLNFIHALEAMLKSTVQLMFVPRRLSRWMSTNMWREHFEAWDYIFQYANRAIQRIYQELALGHPWHYSGIVAELLMRADMTLDTIKANTIDLTAGSVDTTA... | 1.14.15.4; 1.14.15.5 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P19099}; | aldosterone biosynthetic process [GO:0032342]; 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] | corticosterone 18-monooxygenase activity [GO:0047783]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 11-beta-monooxygenase activity [GO:0004507] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-hydroxysteroid + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 uM for 21-hydroxyprogesterone {ECO:0000305|PubMed:10491169}; | PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000250|UniProtKB:P15538}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P15538}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the biosynthesis of aldosterone and other adrenal corticoids. Differing from other species (such as human, rat and mice), it is able to catalyze three sequential oxidative reactions of 11-deoxycorticosterone (21-hydroxyprogesterone), namely 11-beta hydroxylation,... | Bos taurus (Bovine) |
P15151 | PVR_HUMAN | MARAMAAAWPLLLVALLVLSWPPPGTGDVVVQAPTQVPGFLGDSVTLPCYLQVPNMEVTHVSQLTWARHGESGSMAVFHQTQGPSYSESKRLEFVAARLGAELRNASLRMFGLRVEDEGNYTCLFVTFPQGSRSVDIWLRVLAKPQNTAEVQKVQLTGEPVPMARCVSTGGRPPAQITWHSDLGGMPNTSQVPGFLSGTVTVTSLWILVPSSQVDGKNVTCKVEHESFEKPQLLTVNLTVYYPPEVSISGYDNNWYLGQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTLICNVTNALGA... | null | null | acrosome assembly [GO:0001675]; coreceptor-mediated virion attachment to host cell [GO:0046814]; cytoskeleton organization [GO:0007010]; establishment of mitochondrion localization [GO:0051654]; fusion of virus membrane with host plasma membrane [GO:0019064]; heterophilic cell-cell adhesion via plasma membrane cell adh... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886] | cell adhesion molecule binding [GO:0050839]; signaling receptor activity [GO:0038023]; virus receptor activity [GO:0001618] | PF08205;PF07686; | 2.60.40.10; | Nectin family | PTM: N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.; PTM: Phosphorylated by Src kinases on tyrosine residues in the ITIM motif upon ligation. Interaction with TIGIT is required for Phosphorylation. {ECO:0000269|PubMed:15194502, ... | SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Delta]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Beta]: Secreted.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72 nM for VTN; | null | null | null | FUNCTION: Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secr... | Homo sapiens (Human) |
P15153 | RAC2_HUMAN | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRACSLL | null | null | actin filament organization [GO:0007015]; bone resorption [GO:0045453]; cell projection assembly [GO:0030031]; chemotaxis [GO:0006935]; cortical cytoskeleton organization [GO:0030865]; engulfment of apoptotic cell [GO:0043652]; erythrocyte enucleation [GO:0043131]; establishment or maintenance of cell polarity [GO:0007... | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; mitochondrial outer membrane [GO:0005741]; NADPH oxidase complex [GO:0043020]; nuclear envelope [GO:0005635]; phagocytic vesicle memb... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rac and leads to actin disassembly. {ECO:0000269|PubMed:24141704}. | SUBCELLULAR LOCATION: Cytoplasm. Note=Membrane-associated when activated. | null | null | null | null | null | FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the prod... | Homo sapiens (Human) |
P15163 | HBA_LEPWE | VLSPADKTNVKTTWDKIGGHAGEYGGEALERTFMAFPTTKTYFPHFDLSPGSAQVKTHGKKVADALTTAVSHIDDLPGALSALSDLHAYKLRVDPVNFKLLSHCLLVTLACHHPADFTPAVHASLDKFFSAVSTVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Leptonychotes weddellii (Weddell seal) (Otaria weddellii) |
P15167 | VM1AD_CROAT | MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKELFSKDYSETHYSPDGRKITTNPSVEDHCYYRGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLELSDSEAHAVFKLENVEKEDEAPKMCGVTQNWESYEPIKKASDLNLNPDQQNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTAIELDEETLGLAPLGTMCDPKLSIGIVQDH... | 3.4.24.42 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | collagen catabolic process [GO:0030574]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF01562;PF01421; | 3.40.390.10; | Venom metalloproteinase (M12B) family, P-I subfamily | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1.; EC=3.4.24.42; | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). {ECO:0000269|PubMed:2817904}. | Crotalus atrox (Western diamondback rattlesnake) |
P15169 | CBPN_HUMAN | MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEEL... | 3.4.17.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | bradykinin catabolic process [GO:0010815]; peptide metabolic process [GO:0006518]; protein catabolic process [GO:0030163]; protein processing [GO:0016485]; response to glucocorticoid [GO:0051384] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal basic amino acid, preferentially lysine.; EC=3.4.17.3; | null | null | null | null | FUNCTION: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. | Homo sapiens (Human) |
P15170 | ERF3A_HUMAN | MELSEPIVENGETEMSPEESWEHKEEISEAEPGGGSLGDGRPPEESAHEMMEEEEEIPKPKSVVAPPGAPKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSNERYEECKEKLVPFLKKVGFNPKKDIHFMPCSGLTGANLKEQSDFCPWYIGLPFIPYLDNLPNFNRSVDGPIRLPIVDKYKDMGTVVLGK... | 3.6.5.- | null | G1/S transition of mitotic cell cycle [GO:0000082]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; protein methylation [GO:0006479]; regulation of translational termination [GO:0006449]; translation [GO:0006412]; translational termination [GO:0006415] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; translation release factor complex [GO:0018444] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]; translation release factor activity [GO:0003747] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily | null | null | 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:0000269|PubMed:16777602, ECO:0000305|PubMed:15987998}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=... | null | null | null | null | FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:15987998, PubMed:19417105, PubMed:2511002, PubMed:27863242). GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP c... | Homo sapiens (Human) |
P15172 | MYOD1_HUMAN | MELLSPPLRDVDLTAPDGSLCSFATTDDFYDDPCFDSPDLRFFEDLDPRLMHVGALLKPEEHSHFPAAVHPAPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAAFYAPGPLPPGRGGEHYSGDSDASSPRSNCSDGMMDYSGPPSGARRRNCYEGAYYNEAPSEPRPGKSAAVSSLDCLSSIVERISTESPAAPALLLADVPSESPPRRQEAAAPSEGESSGDPTQSPDAAPQCPAGANPNPIYQVL | null | null | cellular response to estradiol stimulus [GO:0071392]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to oxygen levels [GO:0071453]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; muscle cell fate commitment [GO:0042693]; muscle organ ... | chromatin [GO:0000785]; euchromatin [GO:0000791]; myofibril [GO:0030016]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase ... | PF01586;PF00010;PF12232; | 4.10.280.10; | null | PTM: Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation. {ECO:0000269|PubMed:12037670}.; PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function (By similarity). ... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with ... | Homo sapiens (Human) |
P15173 | MYOG_HUMAN | MELYETSPYFYQEPRFYDGENYLPVHLQGFEPPGYERTELTLSPEAPGPLEDKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPGVPSECSSHSASCSPEWGSALEFSANPGDHLLTADPTDAHNLHSLTSIVDSITVEDVSVAFPDETMPN | null | null | cell cycle [GO:0007049]; cellular response to estradiol stimulus [GO:0071392]; cellular response to growth factor stimulus [GO:0071363]; cellular response to lithium ion [GO:0071285]; cellular response to tumor necrosis factor [GO:0071356]; muscle cell fate commitment [GO:0042693]; negative regulation of cell populatio... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667] | chromatin DNA binding [GO:0031490]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]... | PF01586;PF00010; | 4.10.280.10; | null | PTM: Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skel... | Homo sapiens (Human) |
P15180 | SYKC_YEAST | MSQQDNVKAAAEGVANLHLDEATGEMVSKSELKKRIKQRQVEAKKAAKKAAAQPKPASKKKTDLFADLDPSQYFETRSRQIQELRKTHEPNPYPHKFHVSISNPEFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIVGVEGYVGRTQPKKGGEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYE... | 6.1.1.6 | null | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; lysine-tRNA ligase activity [GO:0004824]; mRNA binding [GO:0003729]; tRNA binding [GO:0000049] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15198 | PHOSP_RABVA | MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNDAHLQGEPIEVDNLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSEDKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGWVALANSKKFQLLVEADKLSKIMQDDLNRYTSC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host J... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA-dependent RNA polymerase activity [GO:0003968] | PF03012; | 6.10.140.1560;1.20.120.820; | Lyssavirus protein P family | PTM: Phosphorylated by host PKC and by an unknown kinase. {ECO:0000250}. | SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P5]: Host nuc... | null | null | null | null | null | FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by bin... | Rabies virus (strain PM1503/AVO1) (RABV) |
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