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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O09000 | NCOA3_MOUSE | MSGLGESSLDPLAAESRKRKLPCDAPGQGLVYSGEKWRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISSDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYSILHEPRRKDFLNTYQNPQLMEFLGLMRTRDKKAPYILIVRMLMKTHDILEDVNASPETRQRYETMQCFALSQPRAMLEEGEDLQCCMICVARRVTAPFPSSPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEA... | 2.3.1.48 | null | cell dedifferentiation [GO:0043697]; cellular response to hormone stimulus [GO:0032870]; labyrinthine layer morphogenesis [GO:0060713]; mammary gland branching involved in thelarche [GO:0060744]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; negative regulation of st... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; histone acetyltransferase activity [GO:0004402]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor binding [GO:0016922]; nuclear receptor ... | PF07469;PF16279;PF16665;PF08815;PF00989;PF14598;PF08832; | 6.10.140.410;4.10.280.10;3.30.450.20; | SRC/p160 nuclear receptor coactivator family | PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function (By similarity). {ECO:0000250}.; PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by IKK complex. Regulated its function (By similarity). {ECO:0000... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; | null | null | null | null | FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptor... | Mus musculus (Mouse) |
O09005 | DEGS1_MOUSE | MGSRVSREEFEWVYTDQPHAARRKEILAKYPEIKSLMKPDHNLIWIVAMMLLVQLASFYLVKDLDWKWVIFWSYVFGSCLNHSMTLAIHEISHNFPFGHHKALWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADKIDVDIPTDFEGWFFCTTFRKFVWVILQPLFYAFRPLFINPKPITYLEIINTVIQITFDIIIYYVFGVKSLVYMLAATLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPMVRKIASEYYDDLPHYNSWIKVLYDFVTDDTISPYSRMKRPPKGNE... | 1.14.19.17; 5.2.1.- | null | ceramide biosynthetic process [GO:0046513]; fatty acid biosynthetic process [GO:0006633]; myelin maintenance [GO:0043217]; positive regulation of apoptotic process [GO:0043065] | endoplasmic reticulum membrane [GO:0005789]; mitochondrial membrane [GO:0031966] | retinol isomerase activity [GO:0050251]; sphingolipid delta-4 desaturase activity [GO:0042284] | PF00487;PF08557; | null | Fatty acid desaturase type 1 family, DEGS subfamily | PTM: Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels. {ECO:0000250|UniProtKB:O15121}. | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15121}. | CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI... | null | null | null | null | FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Catalyzes the equilibrium isomerization of retinols (By similarity). {ECO:0000250|UniProtKB:Q5F3C1, ECO:0000269|PubMed:11937514}. | Mus musculus (Mouse) |
O09008 | MFNG_MOUSE | MHCRLFRGMAGALFTLLCVGLLSLRYHSSLSQRMIQGALRLNQRNPGPLELQLGDIFIAVKTTWAFHRSRLDLLLDTWVSRIRQQTFIFTDSPDERLQERLGPHLVVTNCSAEHSHPALSCKMAAEFDAFLVSGLRWFCHVDDDNYVNPKALLQLLKTFPQDRDVYVGKPSLNRPIHASELQSKNRTKLVRFWFATGGAGFCINRQLALKMVPWASGSHFVDTSALIRLPDDCTVGYIIECKLGGRLQPSPLFHSHLETLQLLGAAQLPEQVTLSYGVFEGKLNVIKLPGPFSHEEDPSRFRSLHCLLYPDTPWCPLLAA... | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665, ECO:0000269|PubMed:16964258}; Note=Has some activity with cobalt, magnesium and calcium, but not zinc. {ECO:0000269|PubMed:16221665}; | blastocyst formation [GO:0001825]; marginal zone B cell differentiation [GO:0002315]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=3.3 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG... | Mus musculus (Mouse) |
O09009 | RFNG_MOUSE | MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHW... | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665}; Note=Has some activity with cobalt but not with magnesium, calcium and zinc. {ECO:0000269|PubMed:16221665}; | cell differentiation [GO:0030154]; negative regulation of Notch signaling pathway [GO:0045746]; nervous system development [GO:0007399]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=53.6 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=1.6 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 (PubMe... | Mus musculus (Mouse) |
O09010 | LFNG_MOUSE | MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQV... | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16221665}; Note=Manganese is the most effective. Can also use cobalt with lower efficiency. Has some activity with magnesium and calcium, but not zinc. {ECO:0000269|Pu... | compartment pattern specification [GO:0007386]; marginal zone B cell differentiation [GO:0002315]; negative regulation of Notch signaling pathway involved in somitogenesis [GO:1902367]; ovarian follicle development [GO:0001541]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of Notch signal... | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | PTM: A soluble form may be derived from the membrane form by proteolytic processing. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16385447}. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=78 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=20 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG... | Mus musculus (Mouse) |
O09012 | PEX5_MOUSE | MAMRELVEGECGGANPLMKLATHFTQDKALRQEGLRPGPWPPGASAAETVSKPLGVGTEDELVSEFLQDQNATLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVAQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGDQEGSSTADRWYDEYHPEEDLQHTASDFVSKVDDPKLANSEFLKFVRQIGEGQVSLESAAGSGGAQAEQWAAEFIQQQGTSEAWVDQFTRPGNKIAALQVEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSA... | null | null | cell development [GO:0048468]; cellular lipid metabolic process [GO:0044255]; cellular response to reactive oxygen species [GO:0034614]; cerebral cortex cell migration [GO:0021795]; cerebral cortex neuron differentiation [GO:0021895]; endoplasmic reticulum organization [GO:0007029]; fatty acid beta-oxidation [GO:000663... | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | peroxisome matrix targeting signal-1 binding [GO:0005052]; peroxisome membrane targeting sequence binding [GO:0033328]; peroxisome targeting sequence binding [GO:0000268]; protein carrier chaperone [GO:0140597]; small GTPase binding [GO:0031267] | PF13432;PF13181; | 1.25.40.10; | Peroxisomal targeting signal receptor family | PTM: Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes. Monoubiquitination at Cys-11 is removed by USP9X in the c... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50542}. Peroxisome matrix {ECO:0000250|UniProtKB:P50542}. Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the dockin... | null | null | null | null | null | FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14... | Mus musculus (Mouse) |
O09014 | S15A4_RAT | MEGERAPLLGSRRAAAAAGVFAGRRAACGAVLLAELLERAAFYGVTANLVLFLNGAPFNWEGAQASQALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPRSRSFLCGDPHPELVRNCSAPFPNGTAVCPDAAARRCAPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFLTGYLIPTVCVAIAFLVFLCGQSVFITKPPDGSAFTDMFRILTYSCCSQRGGQRRSGEGLGVFQQSSKHSLFDSCKMSRGGPFTEDKVEDVKALVKI... | null | null | dipeptide import across plasma membrane [GO:0140206]; histidine transport [GO:0015817]; innate immune response [GO:0045087]; L-histidine transmembrane export from vacuole [GO:0089708]; mast cell homeostasis [GO:0033023]; peptidoglycan transport [GO:0015835]; positive regulation of innate immune response [GO:0045089]; p... | early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; membrane [GO:0016020] | dipeptide transmembrane transporter activity [GO:0071916]; L-histidine transmembrane transporter activity [GO:0005290]; peptide:proton symporter activity [GO:0015333]; peptidoglycan transmembrane transporter activity [GO:0015647] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91W98}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + L-histidine(out) = n H(+)(in) + L-histidine(in); Xref=Rhea:RHEA:76379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595; Evidence={ECO:0000269|PubMed:9092568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76380; Evidence={ECO:0000305|PubMed:9092568}; CATALYTIC ACTIVITY: Reaction=n... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for histidine (at pH 5.5) {ECO:0000269|PubMed:9092568}; | null | null | null | FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response (PubMed:9092568). Able to transport a variety of di- and tripeptides, including carnosine and some... | Rattus norvegicus (Rat) |
O09017 | NR2F6_RAT | MAMVTGGWGGPGGDTNGVDKAGGSYPRATEDDSASPPGATSDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRTIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQPGPIPHALPGPAACSPPGAAGVEPFAGPPVSELIAQLLRAEPYPAAGRFGGGGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPAADQVGLLRLSWSELFVLNAAQAPVPLHTAPLLAAAGLHAGPMAAERAVAFMDQVRAFQEQVDKLGRLQVDAAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQV... | null | null | cell differentiation [GO:0030154]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron development [GO:0048666] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal resp... | Rattus norvegicus (Rat) |
O09018 | COT2_RAT | MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGSQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVL... | null | null | anterior/posterior pattern specification [GO:0009952]; blood vessel morphogenesis [GO:0048514]; cell differentiation [GO:0030154]; female gonad development [GO:0008585]; fertilization [GO:0009566]; forebrain development [GO:0030900]; in utero embryonic development [GO:0001701]; interneuron migration [GO:1904936]; lymph... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; nuclear receptor activity [GO:0004879]; protein homodimerization activity [GO:0042803]; retinoic acid binding [GO:0001972]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding ... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity d... | Rattus norvegicus (Rat) |
O09027 | ACKR2_RAT | MPTIASPLPLATTGPENGSSIYDYDYLDDVTVLVCSKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSVPQRRRMIELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVVSTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKTRFRNLLLIVMVWITALAVSVPEMVFVKVHQTLDGVWHCYADFGGHATIWKLYLRFQMNLLGFLFPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVVVFFLLWFPYNLTLFLHSLLDLHVFGNCKISHRLDYMLQVTESLAFSHCCFTPVLYAFSSHSFR... | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; signal transduction [GO:0007165] | actin filament [GO:0005884]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000250}. | SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, ... | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... | Rattus norvegicus (Rat) |
O09028 | GBRP_RAT | MSYSLYLAFVCLNLLAQRMCIQGNQFNVEVSRSDKLSLPGFENLTAGYNKFLRPNFGGDPVRIALTLDIASISSISESNMDYTATIYLRQRWTDPRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVTCNMDLSKYPMDTQTCKLQLESWGYDGNDVEFSWLRGNDSVRGLENLRLAQYTIQQYFTLVTVSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLESVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGA... | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | 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, GABRP sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:17003036}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000269|PubMed:17003036}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:17003036}; | null | null | null | null | FUNCTION: Pi subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA) (PubMed:17003036). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha ... | Rattus norvegicus (Rat) |
O09032 | ELAV4_RAT | MEWNGLKMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGAATDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQ... | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; associative learning [GO:0008306]; cellular response to nerve growth factor stimulus [GO:1990090]; cerebral cortex neuron differentiation [GO:0021895]; dendrite morphogenesis [GO:0048813]; learning [GO:0007612]; locomotory behavior [GO:0007626]; mRNA processing [GO:00063... | apical dendrite [GO:0097440]; axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; perikaryon [GO:0043204]; postsynapse [GO:0098794]; ribonucleoprotein complex [GO:1990904]; ribosom... | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; pre-mRNA intronic pyrimidine-rich binding [GO:0097158] | PF00076; | 3.30.70.330; | RRM elav family | PTM: Methylated by CARM1, which leads to reduced RNA-binding activity and enhanced interaction with SMN (By similarity). Methylation at Arg-248 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state (PubMed:165080... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11948657, ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747, ECO:0000269|PubMed:16554442}. Perikaryon {ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:25692578}. Cell projection, axon {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs (PubMed:10982410, PubMed:16508003, PubMed:17577668). Plays a role in the regulation of mRNA stability, alternative splicing and translation (PubMed:10982410, PubMed:16508003, PubMed:17577668). Binds to AU-rich element (ARE) s... | Rattus norvegicus (Rat) |
O09037 | REG3A_MOUSE | MLPHLVLNSISWMLLSCLLFVFQVQGEDFQKEVPSPRTSCPMGYKAYRSHCYALVMTPKSWFQADLVCQKRPSGHLVSILSGGEASFVSSLVNGRVDNYQDIWIGLHDPTMGQQPNGGGWEWSNSDVLNYLNWDGDPSSTVNRGHCGSLTASSGFLKWGDYYCDGTLPFVCKFKQ | null | null | acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; disruption of cell wall in another organism [GO:0044278]; negative regulation of keratinocyte differentiation [GO:0045617]; positive regulation of cell population proliferation [GO:0008284]; positive... | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000250|UniProtKB:Q06141}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q06141}. Note=Found in the apical region of pancreatic acinar cells. {ECO:0000250|UniProtKB:Q06141}. | null | null | null | null | null | FUNCTION: Bactericidal C-type lectin. The lack of the EPN motif may explain its inability to bind peptidoglycan. {ECO:0000269|PubMed:20382864}.; FUNCTION: Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Secreted by different cell types to activate its... | Mus musculus (Mouse) |
O09039 | SH2B3_MOUSE | MNEPTVQPSRTSSAPASPASPRGWSDFCEQHAAAAARELARQYWLFARAHPQPPRADLVSLQFAELFQRHFCREVRESLAGPPGHDYRATAPPRPALPKARSSEDLGPRPACALQHLRRGLRQLFRRRSAGELPGATSDTNDIDTTAASRPGPARKLLPWGLREPPTEALKEVVLRYSLADEAAMDSGARWQRGRLVLRSPGPGHSHFLQLFDPPKSSKPKLQEACSSIREVRPCTRLEMPDNLYTFVLKVQDQTDIIFEVGDEQQLNSWLAELRASTGLGLEHPDTELPLSLAAEPGPARSPRGSTDSLDQGASPGVLL... | null | null | cellular response to chemokine [GO:1990869]; cellular response to interleukin-3 [GO:0036016]; embryonic hemopoiesis [GO:0035162]; erythrocyte development [GO:0048821]; hematopoietic stem cell differentiation [GO:0060218]; hemopoiesis [GO:0030097]; intracellular signal transduction [GO:0035556]; megakaryocyte developmen... | plasma membrane [GO:0005886] | phosphate ion binding [GO:0042301]; protein tyrosine kinase binding [GO:1990782]; protein-containing complex binding [GO:0044877]; signaling receptor complex adaptor activity [GO:0030159]; stem cell factor receptor binding [GO:0005173]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068] | PF08916;PF00017; | 6.10.140.110;2.30.29.30;3.30.505.10; | SH2B adapter family | PTM: Tyrosine phosphorylated. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}. | Mus musculus (Mouse) |
O09043 | NAPSA_MOUSE | MSPLLLLLLCLLLGNLEPEEAKLIRVPLQRIHLGHRILNPLNGWEQLAELSRTSTSGGNPSFVPLSKFMNTQYFGTIGLGTPPQNFTVVFDTGSSNLWVPSTRCHFFSLACWFHHRFNPKASSSFRPNGTKFAIQYGTGRLSGILSQDNLTIGGIHDAFVTFGEALWEPSLIFALAHFDGILGLGFPTLAVGGVQPPLDAMVEQGLLEKPVFSFYLNRDSEGSDGGELVLGGSDPAHYVPPLTFIPVTIPAYWQVHMESVKVGTGLSLCAQGCSAILDTGTSLITGPSEEIRALNKAIGGYPFLNGQYFIQCSKTPTLPP... | 3.4.23.- | null | membrane protein proteolysis [GO:0033619]; proteolysis [GO:0006508]; surfactant homeostasis [GO:0043129] | alveolar lamellar body [GO:0097208]; extracellular space [GO:0005615]; lysosome [GO:0005764] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in processing of pneumocyte surfactant precursors. {ECO:0000250}. | Mus musculus (Mouse) |
O09044 | SNP23_MOUSE | MDNLSPEEVQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCICPCNRTKNFESGKNYKATWGDGGDNSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS | null | null | exocytic insertion of neurotransmitter receptor to postsynaptic membrane [GO:0098967]; exocytosis [GO:0006887]; membrane fusion [GO:0061025]; protein-containing complex assembly [GO:0065003]; regulation of exocytosis [GO:0017157]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicl... | cytoplasmic vesicle [GO:0031410]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; SNARE complex [GO:0031201]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032] | SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075] | PF00835; | 1.20.5.110; | SNAP-25 family | PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 202-Thr-|-Arg-203 bond; the in vitro reaction is not highly efficient (PubMed:9886085). {ECO:0000269|PubMed:9886085}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type... | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome. Note=Mainly localized to the plasma membrane. | null | null | null | null | null | FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. {ECO:0000250}. | Mus musculus (Mouse) |
O09046 | OXLA_MOUSE | MAGLALRLVLAATLLGLAGSLDWKAASSLNPIEKCMEDHDYEQLLKVVTLGLNRTSKPQKVVVVGAGVAGLVAAKMLSDAGHKVTILEADNRIGGRIFTFRDEKTGWIGELGAMRMPSSHRILHKLCRTLGLNLTQFTQYDENTWTEVHNVKLRNYVVEKMPEKLGYNLNNRERGHSPEDIYQMALNKAFKDLKALGCKKAMNKFNKHTLLEYLLEEGNLSRPAVQLLGDVMSEEGFFYLSFAEALRAHACLSDRLRYSRIVGGWDLLPRALLSSLSGALLLNAPVVSITQGRNDVRVHIATSLHSEKTLTADVVLLTAS... | 1.4.3.2; 1.4.3.25 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15383589}; | adaptive immune response [GO:0002250]; amino acid catabolic process [GO:0009063]; aromatic amino acid metabolic process [GO:0009072]; L-phenylalanine catabolic process [GO:0006559]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell mediated immune response to tumor cell [GO:0002841]; ... | acrosomal vesicle [GO:0001669]; extracellular region [GO:0005576]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; sperm midpiece [GO:0097225] | L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; polyamine oxidase activity [GO:0046592] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96RQ9}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q96RQ9}. Note=Secreted at the immunological synapse. {ECO:0000250|UniProtKB:Q96RQ9}.; SUBCELLULAR LOCATION: [Isoform 1]: Lysosome {ECO:0000269|PubMed:15383589}.; SUBCELLULAR LOCATION: [... | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:15383589}; PhysiologicalDirection=left-to-r... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.5 mM for phenylalanine (at 37 degrees Celsius) {ECO:0000269|PubMed:15383589}; Vmax=0.0099 nmol/min/mg enzyme toward phenylalanine (at 37 degrees Celsius) {ECO:0000269|PubMed:15383589}; | PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway. {ECO:0000250|UniProtKB:Q96RQ9}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:15383589}; | null | FUNCTION: Secreted L-amino-acid oxidase that acts as a key immunoregulator (PubMed:32818467). Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively (PubMed:15... | Mus musculus (Mouse) |
O09047 | C3AR_MOUSE | MESFDADTNSTDLHSRPLFQPQDIASMVILGLTCLLGLLGNGLVLWVAGVKMKTTVNTVWFLHLTLADFLCCLSLPFSLAHLILQGHWPYGLFLCKLIPSIIILNMFASVFLLTAISLDRCLIVHKPIWCQNHRNVRTAFAICGCVWVVAFVMCVPVFVYRDLFIMDNRSICRYNFDSSRSYDYWDYVYKLSLPESNSTDNSTAQLTGHMNDRSAPSSVQARDYFWTVTTALQSQPFLTSPEDSFSLDSANQQPHYGGKPPNVLTAAVPSGFPVEDRKSNTLNADAFLSAHTELFPTASSGHLYPYDFQGDYVDQFTYDN... | null | null | calcium-mediated signaling [GO:0019722]; chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of angiogenesis [GO:0045766]; positive regulation o... | plasma membrane [GO:0005886] | complement component C3a binding [GO:0001850]; complement component C3a receptor activity [GO:0004876]; complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production. | Mus musculus (Mouse) |
O09049 | REG3G_MOUSE | MLPRITITIMSWMLLSCLMLLSQVQGEVAKKDAPSSRSSCPKGSRAYGSYCYALFSVSKNWYDADMACQKRPSGHLVSVLSGAEASFLSSMIKSSGNSGQYVWIGLHDPTLGYEPNRGGWEWSNADVMNYINWETNPSSSSGNHCGTLSRASGFLKWRENYCNLELPYVCKFKA | null | null | acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of cell wall in another organism [GO:0044278]; MyD88-dependent toll-like... | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | hormone activity [GO:0005179]; metal ion binding [GO:0046872]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000269|PubMed:19095652}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28811323, ECO:0000269|PubMed:36240758}. Cytoplasm {ECO:0000250|UniProtKB:P42854}. | null | null | null | null | null | FUNCTION: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune resp... | Mus musculus (Mouse) |
O09051 | GUC2B_MOUSE | MSRSQLWAAVVLLLLLQSAQGVYIKYHGFQVQLESVKKLNELEEKEMSNPQPRRSGLLPAVCHNPALPLDLQPVCASQEAASTFKALRTIATDECELCINVACTGC | null | null | adipose tissue development [GO:0060612]; body fluid secretion [GO:0007589]; cGMP-mediated signaling [GO:0019934]; energy homeostasis [GO:0097009]; glucose homeostasis [GO:0042593]; multicellular organism growth [GO:0035264]; negative regulation of blood pressure [GO:0045776]; reduction of food intake in response to die... | extracellular region [GO:0005576]; photoreceptor outer segment [GO:0001750] | guanylate cyclase activator activity [GO:0030250] | PF02058; | 3.90.1450.10; | Guanylin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water ... | Mus musculus (Mouse) |
O09053 | WRN_MOUSE | METTSLQRKFPEWMSMQSQRCATEEKACVQKSVLEDNLPFLEFPGSIVYSYEASDCSFLSEDISMRLSDGDVVGFDMEWPPIYKPGKRSRVAVIQLCVSESKCYLFHISSMSVFPQGLKMLLENKSIKKAGVGIEGDQWKLLRDFDVKLESFVELTDVANEKLKCAETWSLNGLVKHVLGKQLLKDKSIRCSNWSNFPLTEDQKLYAATDAYAGLIIYQKLGNLGDTAQVFALNKAEENLPLEMKKQLNSISEEMRDLANRFPVTCRNLETLQRVPVILKSISENLCSLRKVICGPTNTETRLKPGSSFNLLSSEDSAAA... | 3.1.-.-; 5.6.2.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17229737}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17229737}; Note=Binds 2 zinc ions in the exonuclease domain. Has high activity with manganese and zinc ions, and no activity with Mg(2+) (in vitro) (PubMed:17229737). ... | base-excision repair [GO:0006284]; cellular response to gamma radiation [GO:0071480]; cellular response to starvation [GO:0009267]; cellular senescence [GO:0090398]; determination of adult lifespan [GO:0008340]; DNA metabolic process [GO:0006259]; DNA replication [GO:0006260]; DNA synthesis involved in DNA repair [GO:0... | centrosome [GO:0005813]; chromosome [GO:0005694]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657] | 3'-5' DNA helicase activity [GO:0043138]; 3'-5' exonuclease activity [GO:0008408]; 3'-flap-structured DNA binding [GO:0070337]; 8-hydroxy-2'-deoxyguanosine DNA binding [GO:1905773]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bubble DNA binding [GO:0000405]; chromatin binding [GO:0003682]; DNA helic... | PF00270;PF01612;PF00271;PF00570;PF14493;PF16124;PF09382; | 1.10.150.80;3.40.50.300;3.30.420.10;1.10.10.10; | Helicase family, RecQ subfamily | PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:Q14191}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14191}. Nucleus {ECO:0000269|PubMed:9618508}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14191}. Chromosome {ECO:0000250|UniProtKB:Q14191}. Note=Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-... | 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:0000250|UniProtKB:Q14191}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:306... | null | null | null | null | FUNCTION: Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity (By similarity). Has 3'->5' exonuclease activity on forked dsDNA (PubMed:17229737). Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing... | Mus musculus (Mouse) |
O09061 | PSB1_MOUSE | MLSTAAYRDVERELGMGPHGSAGPVQLRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD | null | null | proteolysis involved in protein catabolic process [GO:0051603] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774] | null | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus {ECO:0000250|UniProtKB:P20618}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P20618}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteas... | Mus musculus (Mouse) |
O09100 | GATA2_MOUSE | MEVAPEQPRWMAHPAVLNAQHPDSHHPGLAHNYMEPAQLLPPDEVDVFFNHLDSQGNPYYANPAHARARVSYSPAHARLTGGQMCRPHLLHSPGLPWLDGGKAALSAAAAHHHSPWTVSPFSKTPLHPSAAGAPGGPLSVYPGAAGGSGGGSGSSVASLTPTAAHSGSHLFGFPPTPPKEVSPDPSTTGAASPASSSAGGSVARGEDKDGVKYQVSLSESMKMEGGSPLRPGLATMGTQPATHHPIPTYPSYVPAAAHDYGSSLFHPGGFLGGPASSFTPKQRSKARSCSEGRECVNCGATATPLWRRDGTGHYLCNACG... | null | null | angiogenesis [GO:0001525]; brown fat cell differentiation [GO:0050873]; cell differentiation in hindbrain [GO:0021533]; cell fate commitment [GO:0045165]; cell fate determination [GO:0001709]; central nervous system neuron development [GO:0021954]; cochlea development [GO:0090102]; commitment of neuronal cell to specif... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | C2H2 zinc finger domain binding [GO:0070742]; chromatin binding [GO:0003682]; 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]; RNA polymerase II cis-regulatory region seque... | PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'. | Mus musculus (Mouse) |
O09102 | GCM2_MOUSE | MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSY... | null | null | apoptotic process [GO:0006915]; cellular response to organic substance [GO:0071310]; epithelial cell apoptotic process [GO:1904019]; gene expression [GO:0010467]; glandular epithelial cell differentiation [GO:0002067]; gliogenesis [GO:0042063]; intracellular calcium ion homeostasis [GO:0006874]; intracellular phosphate... | 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]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory re... | PF03615; | 2.20.25.670;3.30.70.3530; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75603}. | null | null | null | null | null | FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. {ECO:0000250|UniProtKB:O75603}. | Mus musculus (Mouse) |
O09105 | NDF4_MOUSE | MAKMYMKSKDMVELVNTQSWMDKGLSSQNEMKEQERRPGSYGMLGTLTEEHDSIEEDEEEEEDGDKPKRRGPKKKKMTKARLERFRARRVKANARERTRMHGLNDALDNLRRVMPCYSKTQKLSKIETLRLARNYIWALSEVLETGQTLEGKGFVEMLCKGLSQPTSNLVAGCLQLGPQSTLLEKHEEKSSICDSTISVHSFNYQSPGLPSPPYGHMETHSLHLKPQPFKSLGDSFGSHPPDCSTPPYEGPLTPPLSISGNFSLKQDGSPDLEKSYNFMPHYTSASLSSGHVHSTPFQTGTPRYDVPVDLSYDSYSHHSI... | null | null | amacrine cell differentiation [GO:0035881]; axon development [GO:0061564]; camera-type eye development [GO:0043010]; cell fate commitment [GO:0045165]; motor neuron migration [GO:0097475]; neuroblast proliferation [GO:0007405]; neuron development [GO:0048666]; Notch signaling pathway [GO:0007219]; oligodendrocyte diffe... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010;PF12533; | 4.10.280.10; | null | PTM: Serine or threonine phosphorylation within the basic region may regulate neurogenic activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina. {ECO:0000269|PubMed:11861467}. | Mus musculus (Mouse) |
O09106 | HDAC1_MOUSE | MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVAL... | 3.5.1.-; 3.5.1.98 | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA methylation-dependent heterochromatin formation [GO:0006346]; embryonic digit morphogenesis [GO:0042733]; endoderm development [GO:0007492]; epidermal cell dif... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterochromatin [GO:0000792]; histone deacetylase complex [GO:0000118]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; perinuclear region of cytoplasm [GO:0048471]; protein-containing compl... | chromatin binding [GO:0003682]; deacetylase activity [GO:0019213]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; Krueppel-assoc... | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.; PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.; PTM: Ubiquiti... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:21454521}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:21960634, EC... | null | null | null | null | FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10615135, PubMed:15542849, PubMed:21960634, PubMed:30279482). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcripti... | Mus musculus (Mouse) |
O09107 | INSL3_MOUSE | MRAPLLLMLLALGSALRSPQPPEARAKLCGHHLVRTLVRVCGGPRWSPEATQPVETRDRELLQWLEQRHLLHALVADVDPALDPQLPRQASQRQRRSAATNAVHRCCLTGCTQQDLLGLCPH | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; in utero embryonic development [GO:0001701]; male gonad development [GO:0008584]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; oocyte maturation [GO:000155... | extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391220, ECO:0000269|PubMed:11342953}. | Mus musculus (Mouse) |
O09110 | MP2K3_MOUSE | MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSNPTPPRNLDSRTFITIGDRNFEVEADDLVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNTQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLEKNMKIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELM... | 2.7.12.2 | null | cardiac muscle contraction [GO:0060048]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to sorbitol [GO:0072709]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; heart development [GO:0007507]; inflammatory response [GO:0006954]; MAPK cascade [GO:0000165]; negativ... | null | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | PTM: Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases positively regulates the kinase activity. Phosphorylated by TAOK2. {ECO:0000250|UniProtKB:P46734}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000250|UniProtKB:P46734}; CATALYTI... | null | null | null | null | FUNCTION: Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation ... | Mus musculus (Mouse) |
O09112 | DUS8_MOUSE | MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSCHVLSSVNICCSKLVKRRLQQGKVTIAELIQPATRSQVDATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPATLPSMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRIPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQTDGPHLGTPEPLM... | 3.1.3.16; 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of MAPK cascade [GO:0043409] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine/threonine phosphatase activity [GO:0008330] | PF00782;PF00581; | 3.90.190.10;3.40.250.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8733137}. Nucleus {ECO:0000269|PubMed:8733137}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation (PubMed:7561881). Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine resi... | Mus musculus (Mouse) |
O09113 | OTP_MOUSE | MLSHADLLDARLGMKDAAELLGHREAVKCRLGVGGSDPGGHPGDLAPNSDPVEGATLLPGEDITTVGSTPASLAVSAKDPDKQPGPQGGPNPSQAGQQQGQQKQKRHRTRFTPAQLNELERSFAKTHYPDIFMREELALRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRAPGTLLPTPGLPQFPSAAAAAAAAMGDSLCSFHANDTRWAAAAMPGVSQLPLPPALGRQQAMAQSLSQCSLAAGPPPNSMGLSNSLAGSNGAGLQSHLYQPAFPGMVPASLPGPSNVSGSPQLCSSPDSSDVWRGTSIASLRRKALEHTV... | null | null | dopaminergic neuron differentiation [GO:0071542]; forebrain neuron differentiation [GO:0021879]; hypothalamus cell differentiation [GO:0021979]; neuroblast proliferation [GO:0007405]; neuroendocrine cell differentiation [GO:0061101]; neurohypophysis development [GO:0021985]; neuron differentiation [GO:0030182]; positiv... | fibrillar center [GO:0001650]; nuclear body [GO:0016604] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. | null | null | null | null | null | FUNCTION: Involved in the specification of hypothalamic neuroendocrine cells. Specifically required for the specification of diencephalic dopaminergic neurons of the A11 group. {ECO:0000269|PubMed:10557207, ECO:0000269|PubMed:11071765, ECO:0000269|PubMed:17481897, ECO:0000269|PubMed:7913821}. | Mus musculus (Mouse) |
O09114 | PTGDS_MOUSE | MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLTSTFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELKEKFTTFSKAQGLTEEDIVFLPQPDKCIQE | 5.3.99.2 | null | gene expression [GO:0010467]; mast cell degranulation [GO:0043303]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; response to glucocorticoid [GO:0051384] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791] | fatty acid binding [GO:0005504]; prostaglandin-D synthase activity [GO:0004667]; retinoid binding [GO:0005501] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic ret... | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for prostaglandin H2 {ECO:0000269|PubMed:19546224}; Vmax=5.9 umol/min/mg enzyme {ECO:0000269|PubMed:19546224}; | null | null | null | FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. B... | Mus musculus (Mouse) |
O09118 | NET1_MOUSE | MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKP... | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; B cell mediated immunity [GO:0019724]; B cell proliferation [GO:0042100]; Cdc42 protein signal transduction [GO:0032488]; cell population prolife... | actin cytoskeleton [GO:0015629]; basement membrane [GO:0005604]; cell periphery [GO:0071944]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654] | cytokine activity [GO:0005125] | PF00053;PF00055;PF01759; | 2.40.50.120;2.60.120.260;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7604039}. Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted. {ECO:0000269|PubMed:7604039}. | null | null | null | null | null | FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased ... | Mus musculus (Mouse) |
O09126 | SEM4D_MOUSE | MRMCAPVRGLFLALVVVLRTAVAFAPVPRLTWEHGEVGLVQFHKPGIFNYSALLMSEDKDTLYVGAREAVFAVNALNISEKQHEVYWKVSEDKKSKCAEKGKSKQTECLNYIRVLQPLSSTSLYVCGTNAFQPTCDHLNLTSFKFLGKSEDGKGRCPFDPAHSYTSVMVGGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIQKSPDGPEGEDDKVYFFFTEVSVEYEFVFKLMIPRVARVCKGDQGGLRTLQKKWTSFLKARLICSKPDSGLVFNILQDVFVLRAPGLKEPVFYAVFTPQLNNV... | null | null | axon guidance [GO:0007411]; axonogenesis [GO:0007409]; bone trabecula morphogenesis [GO:0061430]; leukocyte aggregation [GO:0070486]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of cell adhesion [GO:0007162]; negative regulation of ... | extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | chemorepellent activity [GO:0045499]; receptor ligand activity [GO:0048018]; semaphorin receptor binding [GO:0030215]; signaling receptor binding [GO:0005102]; transmembrane signaling receptor activity [GO:0004888] | PF00047;PF01437;PF01403; | 2.60.40.10;3.30.1680.10;2.130.10.10; | Semaphorin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8969198}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (By similarity). Regulates GABAergic synapse development (PubMed:23699507, PubMed:29981480). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner (PubMed:23699507, PubMed:29981480). Modulate... | Mus musculus (Mouse) |
O09127 | EPHA8_MOUSE | MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPP... | 2.7.10.1 | null | axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; ephrin receptor signaling pathway [GO:0048013]; neuron projection development [GO:0031175]; neuron remodeling [GO:0016322]; positive regulation of MAPK cascade [GO:0043410]; positive regulati... | dendrite [GO:0030425]; early endosome membrane [GO:0031901]; neuron projection [GO:0043005]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; GPI-linked ephrin receptor activity [GO:0005004]; growth factor binding [GO:0019838]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF00041;PF07714;PF00536; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-615 is critical for association with FYN. Autophosphorylation on Tyr-838 modulates tyrosine kinase activity. {ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:9053851}.; PTM: Ubiqui... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9053851}; Single-pass type I membrane protein {ECO:0000255}. Cell projection {ECO:0000269|PubMed:17875921}. Early endosome membrane {ECO:0000269|PubMed:20496116}. Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes (P... | 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 binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... | Mus musculus (Mouse) |
O09130 | NF2IP_MOUSE | MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARLIPDTVLVDLVSDSDEEVLEVADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVPVYSGKVQSSLNLIPDNSSLLKLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLSPKQHQSPALQSTDDEVVLVEGPVLPQSSRLFTLKIRCRADLVRLPVRMSEPLQNVVDHMANHLGVSPNRILLLFGESELSPTATPSTLKLGVA... | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF11976; | null | null | PTM: Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production. {ECO:0000269|PubMed:15327772}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus. | null | null | null | null | null | FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation ... | Mus musculus (Mouse) |
O09131 | GSTO1_MOUSE | MSGESSRSLGKGSAPPGPVPEGQIRVYSMRFCPFAQRTLMVLKAKGIRHEVININLKNKPEWFFEKNPLGLVPVLENSQGHLVTESVITCEYLDEAYPEKKLFPDDPYKKARQKMTLESFSKVPPLIASFVRSKRKEDSPNLREALENEFKKLEEGMDNYKSFLGGDSPSMVDYLTWPWFQRLEALELKECLAHTPKLKLWMAAMQQDPVASSHKIDAKTYREYLNLYLQDSPEACDYGL | 1.20.4.2; 1.8.5.1; 2.5.1.18 | null | cellular response to arsenic-containing substance [GO:0071243]; glutathione metabolic process [GO:0006749]; L-ascorbic acid biosynthetic process [GO:0019853]; L-ascorbic acid metabolic process [GO:0019852]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; xenobiotic ... | axon [GO:0030424]; basement membrane [GO:0005604]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965] | glutathione dehydrogenase (ascorbate) activity [GO:0045174]; glutathione transferase activity [GO:0004364]; methylarsonate reductase activity [GO:0050610]; oxidoreductase activity [GO:0016491] | PF00043;PF13409; | 1.20.1050.10;3.40.30.10; | GST superfamily, Omega family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78417}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P78417}; CATALYTIC ACTIVITY: Reaction=2 glutathione + L-... | null | null | null | null | FUNCTION: Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.... | Mus musculus (Mouse) |
O09139 | E2F1_RAT | MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQVPTGPAAPPAGPRDPDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSRTMVGIGQRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDIQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSAETFQISLKSKQGPIDVFLCPEESAEGISPGRTSYQETSGEDRN... | null | null | anoikis [GO:0043276]; cellular response to fatty acid [GO:0071398]; cellular response to hypoxia [GO:0071456]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to xenobiotic stimulus [GO:0071466]; DNA damage checkpoint signaling [GO:0000077]; DNA-templated transcription [GO:0006351]; fo... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; Rb-E2F complex [GO:0035189]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription fac... | PF16421;PF02319; | 6.10.250.540;1.10.10.10; | E2F/DP family | PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis. Phosphorylation at Ser-398 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization. {ECO:0000250|UniProtKB:Q... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle pr... | Rattus norvegicus (Rat) |
O09159 | MA2B1_MOUSE | MGTGPLTSGVRAGGGNTGWLWMSSCNLGSPVLPISFLFWLLLAAPGARAAGYKTCPPTKPGMLNVHLLPHTHDDVGWLKTVDQYYYGILSDVQHASVQYILDSVVSSLLEKPTRRFIYVEMAFFSRWWKQQTSATQDAVRNLVRQGRLEFVNGGWVMNDEAATHYGAIVDQMTLGLRFLQDTFGSDGLPRVAWHIDPFGHSREQASLFAQMGFDGFFLGRIDYQDKLNRKKKLRMEELWRASDSLEPPAADLFTGVLPNNYNPPKYLCWDVLCTDPPVVDNPRSPEFNAKTLVNYFLKLASSQKGFYRTNHTVMTMGSDF... | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | learning or memory [GO:0007611]; mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; oligosaccharide catabolic process [GO:0009313]; protein modification process [GO:0036211] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; nucleoplasm [GO:0005654] | alpha-mannosidase activity [GO:0004559]; mannose binding [GO:0005537]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074;PF21260; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; | null | null | null | null | FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. | Mus musculus (Mouse) |
O09160 | FUT1_MOUSE | MWTPSRRQLCLAFLLVCVLSAGSFFFHLNGGNFFRNGLTLSVLCSDYHLLKSPVAMVCLPHPLQTSNGSPSCPEQSSSLSGTWTITPGGRFGNQMGQYATLLALAQLNGRQAFIQPEMHAALAPVFRISLPVLDPEVDSLTPWQHLVLHDWMSEEYSHLEDPFLKLSGFPCSWTFFHHLREQIRREFTLHNHLREGAQYLLSGLRIGPAGIRPHTFVGVHVRRGDYLEVMPNRWKGVVGDRAYLQQAMDWFRARHKDPIFVVTSNGMKWCLENIDTSHGDVVFAGNGQEGTPGKDFALLTQCNHTIMTIGTFGFWAAYLA... | 2.4.1.344; 2.4.1.69 | null | fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; olfactory bulb development [GO:0021772]; oligosaccharide biosynthetic process [GO:0009312]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-m... | Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580] | alpha-(1,2)-fucosyltransferase activity [GO:0031127]; fucosyltransferase activity [GO:0008417]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107] | PF01531; | null | Glycosyltransferase 11 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305|PubMed:11368156}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.85 mM for phenyl-beta-D-Galactoside {ECO:0000269|PubMed:11368156}; KM=29.09 mM for lactose {ECO:0000269|PubMed:11368156}; KM=0.24 mM for ganglioside GA1 {ECO:0000269|PubMed:11368156}; KM=22.5 uM for ganglioside GA1 {ECO:0000269|PubMed:14967068}; KM=10.8 uM for n... | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P19526}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens (PubMed:11368156, PubMed:14967068, Pu... | Mus musculus (Mouse) |
O09161 | CASQ2_MOUSE | MKRIYLLMVGVYLLSLSGAEEGLNFPTYDGKDRVVSLSEKNLKQMLKRYDLLCLYYHEPVSSDKVSQKQFQLKEIVLELVAQVLEHKNIGFVMVDSRKEAKLAKRLGFSEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIVNNKLEVQAFERIEDQTKLLGFFKNEDSEYYKAFQEAAEHFQPYIKFFATFDKAVAKKLSLKMNEVGFYEPFMDEPNVIPNKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEK... | null | null | negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of potassium ion transport [GO:0043267]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; re... | junctional membrane complex [GO:0030314]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: Phosphorylation in the C-terminus moderately increases calcium buffering capacity. {ECO:0000250|UniProtKB:O14958}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O14958}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}... | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release o... | Mus musculus (Mouse) |
O09164 | SODE_MOUSE | MLAFLFYGLLLAACGSVTMSNPGESSFDLADRLDPVEKIDRLDLVEKIGDTHAKVLEIWMELGRRREVDAAEMHAICRVQPSATLPPDQPQITGLVLFRQLGPGSRLEAYFSLEGFPAEQNASNRAIHVHEFGDLSQGCDSTGPHYNPMEVPHPQHPGDFGNFVVRNGQLWRHRVGLTASLAGPHAILGRSVVVHAGEDDLGKGGNQASLQNGNAGRRLACCVVGTSSSAAWESQTKERKKRRRESECKTT | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | blood vessel diameter maintenance [GO:0097746]; removal of superoxide radicals [GO:0019430]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16371425}. | 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; Evidence={ECO:0000305|PubMed:16371425}; | null | null | null | null | FUNCTION: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. {ECO:0000250}. | Mus musculus (Mouse) |
O09165 | CASQ1_MOUSE | MRATDRMGARAVSELRLALLFVLVLGTPRLGVQGEDGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSVYVFKGDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAYEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPMTIPDKPNSEEEIVSFVEEHRRSTLRKLKPESMYETWEDDLDGIHIVAFAEEADPDGYEFLETLKAVAQDNTENPDLSIIW... | null | null | endoplasmic reticulum organization [GO:0007029]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of store-operated calcium channel activity [GO:1901341]; protein polymerization [GO:0051258]; regulation of muscle contraction [GO:0006937]; regulation of release of ... | I band [GO:0031674]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myofibril [GO:0030016]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; termin... | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P07... | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions (By similarity). Regulates th... | Mus musculus (Mouse) |
O09171 | BHMT1_RAT | MAPIAGKKAKRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSLQTIKLMKEGLEAARLKAYLMSHALAYHTPDCGKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGF... | 2.1.1.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | 'de novo' L-methionine biosynthetic process [GO:0071266]; amino-acid betaine catabolic process [GO:0006579]; amino-acid betaine metabolic process [GO:0006577]; L-methionine salvage [GO:0071267]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; response to organonitrogen compound [GO:0010243] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | betaine-homocysteine S-methyltransferase activity [GO:0047150]; identical protein binding [GO:0042802]; methyltransferase activity [GO:0008168]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270] | PF02574; | 3.20.20.330; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}. Nucleus {ECO:0000269|PubMed:28288879}. Note=Predominantly localized in the cytoplasm with a small fraction detected in the nucleus. Translocates into the nucleus upon oxidative stress. {ECO:0000269|PubMed:28288879}. | CATALYTIC ACTIVITY: Reaction=glycine betaine + L-homocysteine = L-methionine + N,N-dimethylglycine; Xref=Rhea:RHEA:22336, ChEBI:CHEBI:17750, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58251; EC=2.1.1.5; Evidence={ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}; PhysiologicalDirection=left-to-right; Xre... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=106.4 uM for L-homocysteine {ECO:0000269|PubMed:12487625}; KM=333.3 uM for glycine betaine {ECO:0000269|PubMed:12487625}; Vmax=18.67 nmol/min/mg enzyme (L-methionine biosynthesis) {ECO:0000269|PubMed:12487625}; | PATHWAY: Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1. {ECO:0000305|PubMed:12487625}. | null | null | FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline. {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}. | Rattus norvegicus (Rat) |
O09172 | GSH0_MOUSE | MGTDSRAAGALLARASTLHLQTGNLLNWGRLRKKCPSTHSEELRDCIQKTLNEWSSQISPDLVREFPDVLECTMSHAVEKINPDEREEMKVSAKLFIVGSNSSSSTRSAVDMACSVLGVAQLDSVIMASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIEAQDWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS | null | null | apoptotic mitochondrial changes [GO:0008637]; blood vessel diameter maintenance [GO:0097746]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to glucose stimulus [GO:0071333]; cellular response to hepatocyte ... | glutamate-cysteine ligase complex [GO:0017109] | enzyme regulator activity [GO:0030234]; glutamate-cysteine ligase activity [GO:0004357]; glutamate-cysteine ligase catalytic subunit binding [GO:0035226]; protein-containing complex binding [GO:0044877] | PF00248; | 3.20.20.100; | Aldo/keto reductase family, Glutamate--cysteine ligase light chain subfamily | null | null | null | null | PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. | null | null | null | Mus musculus (Mouse) |
O09173 | HGD_MOUSE | MAELKYISGFGNECASEDPRCPGSLPKGQNNPQVCPYNLYAEQLSGSAFTCPRNTNKRSWLYRILPSVSHKPFESIDQGHVTHNWDEVGPDPNQLRWKPFEIPKASEKKVDFVSGLYTLCGAGDIKSNNGLAVHIFLCNSSMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICVIQRGMRFSVDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQGKLFACKQDVSPFNVVAWHGNYTPYKYNLENFMVINAVAFDHADPSIFTVLTAKSLRPGVAIADFVIFPP... | 1.13.11.5 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:7705358}; | amino acid metabolic process [GO:0006520]; L-phenylalanine catabolic process [GO:0006559]; tyrosine catabolic process [GO:0006572] | cytoplasm [GO:0005737] | homogentisate 1,2-dioxygenase activity [GO:0004411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF04209;PF20510; | 2.60.120.10; | Homogentisate dioxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+); Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5; Evidence={ECO:0000269|PubMed:7705358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15450; Evidence={ECO:0000269|PubMed:7... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=188 uM for homogentisate {ECO:0000269|PubMed:7705358}; | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.1. {ECO:0000269|PubMed:7705358}; | null | FUNCTION: Catalyzes the conversion of homogentisate to maleylacetoacetate. {ECO:0000269|PubMed:7705358}. | Mus musculus (Mouse) |
O09174 | AMACR_MOUSE | MVLRGVRVVELAGLAPGPFCGMVLADFGAEVVRVNRLGSTGENFLARGKRSLALDLKRSQGVTVLRRMCARADVLLEPFRCGVMEKLQLGPETLLQDNPKLIYARLSGFGQSGIFSKVAGHDINYLALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGIVLALFERTRSGRGQVIDSSMVEGTAYLSSFLWKTQPMGLWKQPRGQNILDGGAPFYTTYKTADGEFMAVGAIEPQFYALLLKGLGLESEELPSQMSSADWPEMKKKFADVFAKKTKAEWCQIFDGTDACVTPVLTFEEALHHQHNRERASFITDGEQ... | 5.1.99.4 | null | bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; fatty acid metabolic process [GO:0006631]; isoprenoid catabolic process [GO:0008300] | mitochondrion [GO:0005739]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | alpha-methylacyl-CoA racemase activity [GO:0008111] | PF02515; | 3.30.1540.10; | CoA-transferase III family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10770938}. Mitochondrion {ECO:0000269|PubMed:10770938}. | CATALYTIC ACTIVITY: Reaction=a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA; Xref=Rhea:RHEA:12657, ChEBI:CHEBI:57313, ChEBI:CHEBI:57314; EC=5.1.99.4; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12658; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=ri... | null | PATHWAY: Lipid metabolism; bile acid biosynthesis.; PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (... | Mus musculus (Mouse) |
O09175 | AMPB_RAT | MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLA... | 3.4.11.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | negative regulation of blood pressure [GO:0045776]; protein processing [GO:0016485]; proteolysis [GO:0006508]; retina development in camera-type eye [GO:0060041] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; secretory granule [GO:0030141] | aminopeptidase activity [GO:0004177]; cobalt ion binding [GO:0050897]; copper ion binding [GO:0005507]; metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF09127;PF01433;PF17900; | 3.30.2010.30;1.10.390.10;1.25.40.320;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; | null | null | null | null | FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4). | Rattus norvegicus (Rat) |
O09185 | P53_CRIGR | MEEPQSDLSIELPLSQETFSDLWKLLPPNNVLSTLPSSDSIEELFLSENVTGWLEDSGGALQGVAAAAASTAEDPVTETPAPVASAPATPWPLSSSVPSYKTYQGDYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVNSTPPPGTRVRAMAIYKKLQYMTEVVRRCPHHERSSEGDSLAPPQHLIRVEGNLHAEYLDDKQTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDPSGNLLGRNSFEVRICACPGRDRRTEEKNFQKKGEPCPELPPKSAKRALPTNTSSSPPPKK... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | cell cycle [GO:0007049]; cellular senescence [GO:0090398]; circadian behavior [GO:0048512]; DNA damage response [GO:0006974]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; nucleotide-excision ... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP-dependent DNA/DNA annealing activity [GO:0036310]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [G... | PF00870;PF08563;PF07710; | 2.60.40.720;6.10.50.20;4.10.170.10; | P53 family | PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which p... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, cen... | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of t... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
O09198 | MAL_MOUSE | MAPAAASGGSTLPSGFSVFTTFPDLLFVCEFVFGGLVWILIASSLVPLPLAQGWVMFVSVFCFVATTSLMILYIIGTHGGETSWITLDAAYHCVAALFYLSASVLEALATISMFDGFTYKHYHENIAAVVFAYVVTLIYVVHAVFSLIRWKSS | null | null | central nervous system myelination [GO:0022010]; myelination [GO:0042552]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; protein insertion into plasma membrane [GO:0098737]; protein localization to paranode region of axon [GO:0002175] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; hinge region between urothelial plaques of apical plasma membrane [GO:0120003]; membrane raft [GO:0045121]; plasma membrane raft [GO:0044853]; Schmidt-Lanterman incisure [GO:0043220] | structural constituent of myelin sheath [GO:0019911] | PF01284; | null | MAL family | PTM: Lipoprotein. {ECO:0000250}. | SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note=Found in lipid raft. | null | null | null | null | null | FUNCTION: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Plays a role in the maintenance of the myelin sheath and in axon-glia and glia-glia interactions. {ECO:0000269|PubMed:15337780}. | Mus musculus (Mouse) |
O09232 | HBB_MELAE | MVEWTDDERAIINGIFSNLDYEEIGRKSLCRCLIVYPWTQRYFGGFGNLYNAETILCNPLIAAHGTKILHGLDRALKNMDDIKNTYAELSLLHSDKLHVDPDNFRLLADCLTVVIAAKMGAAFTVDTQVAWQKFLAVVVSALGRQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Melanogrammus aeglefinus (Haddock) (Gadus aeglefinus) |
O09460 | PCKA_ANASU | MSLSESLAKYGITGATNIVHNPSHEELFAAETQASLEGFEKGTVTEMGAVNVMTGVYTGRSPKDKFIVKNEASKEIWWTSDEFKNDNKPVTEEAWAQLKALAGKELSNKPLYVVDLFCGANENTRLKIRFVMEVAWQAHFVTNMFIRPTEEELKGFEPDFVVLNASKAKVENFKELGLNSETAVVFNLAEKMQIILNTWYGGEMKKGMFSMMNFYLPLQGIAAMHCSANTDLEGKNTAIFFGLSGTGKTTLSTDPKRLLIGDDEHGWDDDGVFNFEGGCYAKVINLSKENEPDIWGAIKRNALLENVTVDANGKVDFADK... | 4.1.1.49 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945}; | gluconeogenesis [GO:0006094] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoenolpyruvate carboxykinase (ATP) activity [GO:0004612] | PF01293; | 3.90.228.20;3.40.449.10;2.170.8.10; | Phosphoenolpyruvate carboxykinase (ATP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}. | CATALYTIC ACTIVITY: Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate; Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=4.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 mM for ADP (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=0.54 mM for PEP (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=1.2 mM for OAA (at 37 degrees Celsi... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_00453}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.7 and 7.1. The enzyme is stable from pH 5.0 to 9.0. It completely losing activity at pH values lower than 4.5 and retaining some activity in the pH range 9-12. {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; | null | FUNCTION: Involved in gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA (By similarity). {ECO:0000250, ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}. | Anaerobiospirillum succiniciproducens |
O11436 | POLG_RGMVD | MMNFGSLNVGLKQVDGTWVPRVFEEKEMARLLAEKQHARVMRATQEMMKAPNPFAEFDEMHQRGNPFAGRVRKCETREPKSAQKPIVTVDTVPVAIYTDVIWPENGKVHALSRRRAPRKHARRSKILACDLLTQVLNISRRAGKSVEVIGKRRCCLKPRRRDGKSCFGVITKHHKGVLSSRDMVKDLFVDSIIEHIAYTGHTPLIDAADIKPGDSGLIYREKKDGYVTRVVRGRHDGDIIDARDYVRAGIHTIKHYSDDGKSLVKYAPYCQPSHHTFGHMCRVTWSDTEILQFREMLSQAIMPQRDPRCDICAEVAGQRT... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviru... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle membrane. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles a... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyz... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Ryegrass mosaic virus (isolate Denmark/Danish) (RGMV) |
O11457 | VGP_EBOG4 | MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETRYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTAVSNRAKNISG... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF01611; | 1.10.287.210; | Filoviruses glycoprotein family | PTM: The signal peptide region modulates GP's high mannose glycosylation, thereby determining the efficiency of the interactions with DC-SIGN(R). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.; PTM: Palmitoylation of GP2 is not required for its function... | SUBCELLULAR LOCATION: [GP2]: Virion membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent t... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein]: Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that... | Zaire ebolavirus (strain Gabon-94) (ZEBOV) (Zaire Ebola virus) |
O12157 | GAG_HV192 | MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLL... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12158 | POL_HV192 | MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLL... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12161 | TAT_HV192 | MEPVDPNLEPWNHPGSQPKTACNNCYCKRCSYHCLVCFQTKGLGISYGRKKRRQRRSAPPSSEDHQNPIPKQPLPQTRGDQTGSEESKKKVESKTETDPFD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12164 | ENV_HV192 | MRVEGIQRNWKQWWIWGILGFWMVMIYNVRGNLWVTVYYGVPVWKEAKTTLFCASDAKAYDAEVHNVWATHACVPTDPNPQEMVLENVTENFNMWENDMVEQMHQDIISLWDQSLKPCVKLTPLCVTLHCSNRTIDYNNRTDNMGGEIKNCSFNMTTEVRDKREKVHALFYRLDIVPLKNESSNTSGDYRLINCNTSAITQACPKVSFDPIPIHYCAPAGYAILKCNNKTFNGTGPCNNVSTIQCTHGTKPVVSTQLLLNGSLAEEEIIIRSKNLTDNVKTIIVHLNESVEINCTRPNNNTRKSIRIGPGQAFYATGEII... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12165 | NEF_HV192 | MGNKWSKCSTVGRPAIRERMRRAPAAEGVGPASQDSDKYGALTSSSTPANNADCAWLEAQQEEEEVGFPVRPQVPLRPMTYKAVVDLSFFLEEKGGLEGLIYSKKRQDILDLWVYNTQGYFPDWQNYTPGPGVRFPLTFGWCFKLVPVDPREVEEANTGENNSLLHPMSLHGMEDSHREVLQWKFDSLLARRHMARELHPEYYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12940 | TOM1_CHICK | MDFLLGNPFSSPVGQRIERATDGSLRGEDWSLNMEICDIINETEEGPKDAFRAIKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHILVASQDFVESVLVRTILPKNNPPAIVHDKVLTLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPRRSVYSSNSQSGQNSPAVNSPQQMESILHPVTLPSGRDTSSNVPITPTQEQIKKLRSELEVVNGNVKVMSEMLTELVPSQAETSDLELLQELNRTCRAMQQRVLELIPRVQHEQLTEELLLINDNLNNVFLRHERFERVRTGQPVKAPSEAENNL... | null | null | autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; positive regulation of autophagosome maturation [GO:1901098]; protein transport [GO:0015031]; regulation of endosome organization [GO:1904978]; signal transduction [GO:0007165]; substrate localization to autophagosome [GO:0061753] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; membrane [GO:0016020] | clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; myosin VI binding [GO:0070853]; phosphatidylinositol-5-phosphate binding [GO:0010314]; polyubiquitin modification-dependent protein binding [GO:0031593]; ubiquitin binding [GO:0043130] | PF03127;PF00790; | 1.20.58.160;1.25.40.90; | TOM1 family | PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O60784}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60784}. Endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By ... | Gallus gallus (Chicken) |
O12971 | LFNG_CHICK | MLKSCGRKLLLSLVGSMFTCLLVLMVEPPGRPGLARGEAGGAQRALQSLGAARAAGQGAPGLRSFADYFGRLSRARRELPAAPPSPPRPPAEDITPRDVFIAVKTTKKFHKARLELLLDTWISRNRDMTFIFTDGEDEELKKQARNVINTNCSAAHSRQALSCKMAVEYDKFIESGRKWFCHVDDDNYVNVRTLVKLLSSYPHTQDIYIGKPSLDRPIQATERISENKMHPVHFWFATGGAGFCISRGLALKMSPWASGGHFMSTAEKIRLPDDCTIGYIIESVLGVKLIRSNLFHSHLENLHQVPKTEIHKQVTLSYGM... | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O09010}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:O09010}; Note=Manganese is the most effective. Can also use cobalt with lower efficiency. Has some activity with magnesium and calcium, but not zinc. {ECO:0000250|... | compartment pattern specification [GO:0007386]; marginal zone B cell differentiation [GO:0002315]; negative regulation of Notch signaling pathway involved in somitogenesis [GO:1902367]; ovarian follicle development [GO:0001541]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of Notch signal... | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | PTM: A soluble form may be derived from the membrane form by proteolytic processing. {ECO:0000305}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, C... | null | null | null | null | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Essential mediator of somite segmentation and patterning. {ECO:0000250|UniProtKB:O09010}. | Gallus gallus (Chicken) |
O12976 | PSN1_XENLA | MNDTSERRSNENSESQSNGQTQSSSQQVLEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRFDGQLIYTPFTEDTESVGQRALNSILNATIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSYIYLGEVFKTYNVAVDYITLALLIWNFGVVGMICIHWKGPLLLQQAYLIMISALMALVFIKYLPEWTTWLILAVISVYDLVAVLSPKGPLRMLVETAQERNETLFPALIYSSTMIWLVNMADGDPGLKQSASTKTYNTQAPTAHPRSDSAASDDNGGFDTTWEDHRNAQIGPINST... | 3.4.23.- | null | amyloid precursor protein metabolic process [GO:0042982]; amyloid-beta formation [GO:0034205]; membrane protein ectodomain proteolysis [GO:0006509]; Notch signaling pathway [GO:0007219]; positive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]; regulation of canonical Wnt signaling pathwa... | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296] | PF01080; | 1.10.472.100; | Peptidase A22A family | PTM: Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by a caspase. {ECO:0000250|UniProtKB:P49768}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule {ECO:0000250|UniProtKB:P49768}. Cell m... | null | null | null | null | null | FUNCTION: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. P... | Xenopus laevis (African clawed frog) |
O12977 | PSN2_XENLA | MIKLSDSEDEECNERTSLITSESPPLPSYQDGVQASEGLETSYHRERQPDSTQNNEDVPNGRTSGADAYNSETTVENEEEELTLKYGARHVIMLFVPVTLCMVVVVATIKSVSFYTEKDGQLIYTPFSEDTTSVGERLLNSVLNTLIMISVILVMTIFLVLLYKYRCYKFIHGWLILSSLMLLFMFTYIYLSEVFKTYNIAMDYPTLFMVIWNFGAVGMICIHWKGPLQLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLLAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMMWTVGMADSATADGRMNQQ... | 3.4.23.- | null | amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta metabolic process [GO:0050435]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007... | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochond... | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500] | PF01080; | 1.10.472.100; | Peptidase A22A family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (By similarity). May play a role in negative regulation of apoptotic cascades during oogenesis and embryogenesis, and in developmen... | Xenopus laevis (African clawed frog) |
O12990 | JAK1_DANRE | MPELAVMDLGRQLCVKMKKQRKAEMTIPTAMKGLEIHFYLADTHQLEFFKACYTAEDLCVEAAKRCRISPLCHNLFALYEESQDLWYAPNHVFKVTDETSIKLHYRMRFYFTNWHGTSEIESPVWRHTLSKQKSVLNSQKTTEGTPLLDAASLDYLFAQGQYDFLRGLSPVRPTQTDEEHHEIENECLGMAVLAITHHAKSNNLPLSGAGAETSYKRFIPDSLNRTIKQRNFLTRIRISNVFKNFLNEFNSKTIQDSNIGLYDLKVKYLSTLETLTQGVGREIFKPKNLKVTGESEGSPAQMLPLGDNGMGYEVQVYGTT... | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P23458}; Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000250|UniProtKB:P23458}; | cell differentiation [GO:0030154]; cytokine-mediated signaling pathway [GO:0019221]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]; receptor signaling pathway via JAK-STAT [GO:0007259]; T cell differentiation in ... | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020] | ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715] | PF18379;PF18377;PF17887;PF07714; | 3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, JAK subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Wholly intracellular, possibly membrane associated. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (By similarity). Appears to be required in early development for specific cell migrations (epiboly), expression of homeobox protein goosecoid and formation of anterior structures (PubMed:9096349). {ECO:0000250|UniPro... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13010 | PI42A_PIG | MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSXARSGARFHTSYDRRYVIKTITSEDVAEMHNILKNYHQHIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNXKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDGTHPVGTPPDSPGNT... | 2.7.1.149 | null | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; autophagosome-lysosome fusion [GO:0061909]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of autophagy [... | cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803] | PF01504; | 3.30.810.10;3.30.800.10; | null | PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light and increases kinase activity. {ECO:0000250|UniProtKB:Q9R0I8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O70172}. Nucleus {ECO:0000250|UniProtKB:P48426}. Lysosome {ECO:0000250|UniProtKB:O70172}. Cytoplasm {ECO:0000250|UniProtKB:P48426}. Photoreceptor inner segment {ECO:0000250|UniProtKB:O70172}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|Uni... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evid... | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which fun... | Sus scrofa (Pig) |
O13012 | ESR2_ANGJA | MAGSPGNELPLLQLQEVDSSKVGESGGSSGLLPTMYNGALPALSMESHAVCIPSPYTDSSHDYAALTFYSPPILSHGGPAVPESPAARQSLSPSLFWPAHGHHGHVSPLALHFQQPLVYREPAHSPWAEPKPLEHGQAQTSKLAGKRMAESEEGTSSVGGCFAGKGDMHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNGYICPATNQCTIDKNRRKSCQACRLRKCYEVGMMKCGVRRERCTYRGARHRRMPHIRELAGTGGGARTQRRGEGVVPQTQEAQSSALTPEQLINRIIEAEPPEIYLMKELKKPFTED... | null | null | cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; intracellular estrogen receptor signaling pathway [GO:0030520] | nucleus [GO:0005634] | estrogen response element binding [GO:0034056]; hormone binding [GO:0042562]; nuclear estrogen receptor activity [GO:0030284]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270] | PF12497;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. | Anguilla japonica (Japanese eel) |
O13016 | PTN1_CHICK | MEIEKEFHRLDQAASWAAIYQDIRHEASDFPCKVAKHPRNKNRNRYRDVSPFDHSRIKLNQGDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSIKCAQYWPRKEEKEMFFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPEYGPVVVHCSAGIGRSGTFCLVDTCLLLMDKRKDPSSVDVKQVLLEMRKYRMGLIQTADQLRFSYLAVIEGAKFIMGDASVQEQWKELSNEDLDPPPEHTPPPPRPPKRTSEMH... | 3.1.3.48 | null | actin cytoskeleton organization [GO:0030036]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; peptidyl-tyrosine dephosphorylation [GO:0035335]; regulation of endocytosis ... | cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class 1 subfamily | PTM: Phosphorylated on serine and threonine residues near the N-terminus by casein kinase II (CK2). | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By simi... | Gallus gallus (Chicken) |
O13023 | HHEX_XENLA | MQYQHPSSSALGLSVPLFAPTPLQHPTPFYIDDILGRNSASNGTPALPTPTLPSPNSSFTSLVATYRTPIYEPTPIHPAFTHPGAALAASYGASTYASPLYPFSRPVSDYTHALIRHDSLGKPLLWSPFIQRPLHKRKGGQVRFSNDQTIELEKKFETQKYLSPPERKRLAKMLQLSERQVKTWFQNRRAKWRRLKQENPQGNKKDETESLENICEESQERCLSAEQKSRESSLDDPTSSPTSQGNLDSEVSDDSDQEVDIEGDKGYYNCAH | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic hemopoiesis [GO:0035162]; heart development [GO:0007507]; liver development [GO:0001889]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of Wnt s... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}. | null | null | null | null | null | FUNCTION: Recognizes the DNA sequence 5'-ATTAA-3'. Transcriptional repressor. Regulates the differentiation of both endothelial and blood cells (By similarity). Probably plays a role in the proliferation of vascular endothelial cells during blood vessel development. Establishes anterior identity at two levels; acts ear... | Xenopus laevis (African clawed frog) |
O13024 | INCEA_XENLA | MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRQSNASWSSSVRRLSVRNQNKANDDSIQEEPAQLKRMTRARAQASIKSTPVLETALPESPSQICQKNAQVKISEQERRSAEQKLIESDFELKTVPEITKDNVSETVNSAVPAVPVTPENKSRAAGKLKIAASSTPEQKAEMVDLTCESPRPANEQQLNLSNQSATPTGSKSDRRSVRRSLVVRKSSSRRASLASQFSLASKRESMTREAVRKSIRQSISQKKAAMEISSTSSQR... | null | null | chromosome segregation [GO:0007059]; meiotic spindle midzone assembly [GO:0051257]; metaphase chromosome alignment [GO:0051310]; mitotic cytokinesis [GO:0000281]; spindle assembly [GO:0051225] | chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle midzone [GO:1990385]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; spindle... | protein kinase binding [GO:0019901] | PF03941;PF12178; | 1.20.5.3600;6.10.250.2990; | INCENP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome {ECO:0000269|PubMed:12464631}. Chromosome, centromere {ECO:0000269|PubMed:10996078}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10996078}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB... | null | null | null | null | null | FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts... | Xenopus laevis (African clawed frog) |
O13033 | RAG1_DANRE | MEKGRWSSEDAPRASMPDELSHPKFSEWKFKLFRVRSMEKAPVQNETPVEKENQPELAMEKTSSQGSVMRLCFGGKSKENVESARGRVDLKLQEIDTHMNLLKNMCRLCGIAIQKAKGPSHEVQGVLEESSRCALRRMGCKLVTWPEVILKVFKVDVTTDMETVHPSLFCHRCWTAAIRGGGFCSFTNTRIPDWKPHTSQCNLCFPKKSSFQRVGRKRTKPLKSAHILPKRFRRDSSESSRVWRQTTENPDGKEWLKLSVQRGQWVKNITRCQRDHLSTKLIPTEVPADLIRAVTCQVCDHLLSDPVQSPCRHLFCRLCI... | 2.3.2.27; 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). {ECO:0000250}; | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; pre-B cell allelic exclusion [GO:0002331]; protein-DNA complex assembly [GO:0065004]; somatic diversification of immune receptors via germline recombination within a single locus [GO:0002562]; T cell differe... | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleus [GO:0005634] | double-stranded DNA endonuclease activity [GO:1990238]; endonuclease activity [GO:0004519]; histone binding [GO:0042393]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; ubiquitin protein ligase activity [GO:... | PF12940;PF12560;PF00097; | 6.10.140.510;3.30.40.10; | RAG1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in s... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13034 | RAG2_DANRE | MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGG... | null | null | B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; hematopoietic or lymphoid organ development [GO:0048534]; immunoglobulin V(D)J recombination [GO:0033152]; lymphocyte differentiation [GO:0030098]; protein-DNA complex assembly [GO:0065004]; T cell differentiation [GO:0030217]; T cell differentia... | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-... | PF03089;PF13341; | 2.120.10.80;3.30.160.290; | RAG2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some c... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13065 | MMP18_XENLA | MNSLLLKLLLCVAITAAFPADKQDEPPATKEEMAENYLKRFYSLGTDGGPVGRKKHIQPFTEKLEQMQKFFGLKVTGTLDPKTVEVMEKPRCGVYDVGQYSTVAKSSAWQKKDLTYRILNFTPDLPQADVETAIQRAFKVWSDVTPLTFTRIYNEVSDIEISFTAGDHKDNSPFDGSGGILAHAFQPGNGIGGDAHFDEDETWTKTSEIYNLFLVAAHEFGHSLGLSHSTDQGALMYPTYSNTDPKTFQLPQDDINAIQYLYGKSSNPVQPTGPSTPSRCDPNVVFNAVTTMRGELIFFVKRFLWRKHPQASEAELMFVQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cleaves collagen type I. May play a role in larval tissue degeneration and adult organogenesis during amphibian metamorphosis. May be involved in tail resorption. | Xenopus laevis (African clawed frog) |
O13076 | AA2BR_CHICK | MNTMKTTYIVLELIIAVLSIAGNVLVCWAVAINSTLKNATNYFLVSLAVADIAVGLLAIPFAITISIGFQVDFHSCLFFACFVLVLTQSSIFSLLAVAIDRYLAIKIPLRYNSLVTGKRARGLIAVLWLLSFVIGLTPLMGWNKAMSGCPNSTNETGADHGAGHHGCFISCLFENVVTMSYMVYFNFFGCVLLPLIIMLGIYIKIFMVACKQLHQIELMGNSRTTLQKEVHAAKSLAIIVGLFAFCWLPLHILNCITHFHEEFSKSKPEWVMYVAIILSHANSVINPIIYAYRIRDFRYTFHKIISKILCKTDDFPKCTT... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to extracellular stimulus [GO:0031668]; cGMP-mediated signaling [GO:0019934]; mast cell degranulation [GO:0043303]; positive regulation of cGMP-mediated signaling [GO:0010753]; positive regulation of chemokine prod... | glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685] | G protein-coupled adenosine receptor activity [GO:0001609]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. | Gallus gallus (Chicken) |
O13078 | HBB_MERMR | MVEWTDDERAIINSIFSTLDYEEIGRKSLCRCLIVYPWTQRYFGGFGNLYNAETILCNPLIAAHGTKILHGLDRALKNMDDIKNTYAELSQLHSDKLHVDPDNFRLLADCLTVVIAAKMGTAFTVETQVAWQKFLAVVVSALGRQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Merlangius merlangus (Whiting) (Gadus merlangus) |
O13097 | EFNB1_XENLA | MEGLRRLLGLLLVLYRLCSALGKNLEPVTWNSQNPRFISGKGLVLYPEIGDRLDIICPKGDSSQPYEYYKLYMVRRDQLEACSTVIDPNVLVTCNQPGKEYRFTIKFQEFSPNYMGLEFRRNQDYYITSTSNSTLQGLENREGGVCQTRSMKIIMKVGQDPNAVPPEQLTTTRPSKEADNTGKIATFGPWNGPVENPGKSDTNLSDKPTAGGGVDGFFNSKIAVFAAIGAGCVIFILIIIFLVVLLIKIRKRHRKHTQQRAAALSLSTLASPKCSGNAGSEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQ... | null | null | axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013] | plasma membrane [GO:0005886] | ephrin receptor binding [GO:0046875] | PF00812; | 2.60.40.420; | Ephrin family | PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. Tyrosine phosphorylation inhibits TLE4-binding. {ECO:0000269|PubMed:21429299}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional sign... | Xenopus laevis (African clawed frog) |
O13146 | EPHA3_DANRE | MALFRIYSFLAPFHILVLCQALRNYPDNEVTLLDSMSAPGDLGWEAYPSEGWEEISVMDERNIPMRTYQVCNVMEANQNNWLRTGLIQREGAQRVYVEIKFTLRDCNSLPGVPGTCKETFNVYYHESNNAVAAPLRHIRESQYIKIDTIAADESFTQTDVGDRVMKLNTEVRDISGLSKRGLYLAFQDLGACIALVSVRVFYKRCPLAVLNLARFPDTVTGGDSALVEVRGTCVEDAEELEGPRMFCSADGGWLVPIGRCVCRPGFEEVDGHCQPCRSGFYKASAMDAYCVKCPPHSYSHQDKASECVCERGFYRAESDP... | 2.7.10.1 | null | axon guidance [GO:0007411]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]; fasciculation of sensory neuron axon [GO:0097155]; phosphorylation [GO:0016310]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of epithelial ... | dendrite [GO:0030425]; early endosome [GO:0005769]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; GPI-linked ephrin receptor activity [GO:0005004]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF00041;PF07714;PF00536; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Autophosphorylates upon activation by efna5. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein {ECO:0000255}. | 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 binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13147 | EPHB3_DANRE | PLLVLDLIIQERGESFSHTVTAQHTSAKVEGLKAGTVYSVQVRARTVAGYGRYSNPVDFSTSLYVCPVSSSSTSMHLRRREELTTTTTGLKSREERFQKSDDPERSVQDLLPLIVGSASAGFVVILAMIVIAVVCLRRQRTGSELEYTEKLQQYVSPGVKVYIDPFTYEDPNEAVHEFAREIDISCVKIEEVIGAGEFGEVCRGRLKQAGRKETTVAIKTLKAGYTEHQRRDFLSEASIMGQFDHPNVIHLEGVLTRSCPVLIVTEFMENGALDSFLRLNDGRFTVTQLVGMLRGIAAGMKYLSDMNYVHRDLAARNVLV... | 2.7.10.1 | null | angiogenesis [GO:0001525]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; positive regulation of synapse assembly [GO:0051965]; protein autop... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF00041;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-168 is required for interaction with SH2 domain-containing proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. | 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 binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway dow... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13148 | EPA4A_DANRE | IGIGEFGEVCSGRLKMPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIRLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGILRGIASGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEEDPDAAYTTREITGTYQSQGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPVSLHQLMLDCWQKERAERPKFSQIVNMLDKLIRNPNSLKRTGGEIARPNTTLLEPSSPE | 2.7.10.1 | null | anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; cell-cell recognition [GO:0009988]; forebrain development [GO:0030900]; negative regulation of axon extension [GO:0030517]; negative regulation of collateral sprouting of intact axon in response to injury [GO:0048685]; optic vesicle morp... | dendrite [GO:0030425]; early endosome [GO:0005769]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03137}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q03137}. Early endosome {ECO:0000250|UniProtKB:Q03137}. Note=Clustered upon activation and targeted to early endosome. {ECO:0000250|UniProtKB:Q03137}. | 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 binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13154 | PACN2_CHICK | MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKK... | null | null | actin cytoskeleton organization [GO:0030036]; caveola assembly [GO:0070836]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; negative regulation of endocytosis [GO:0045806]; plasma membrane tubulation [GO:0097320]; regulation of endocytosis [GO:0030100] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; ruffle membrane [GO:0032587] | cytoskeletal protein binding [GO:0008092]; phosphatidic acid binding [GO:0070300]; phospholipid binding [GO:0005543] | PF00611;PF14604; | 1.20.1270.60;2.30.30.40; | PACSIN family | PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9287337}. | SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:9287337}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome membra... | null | null | null | null | null | FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface rec... | Gallus gallus (Chicken) |
O13163 | HBB_SILAS | MVXWTDXERHVIADVWGKINPDEIGPHALARLLIVYPWTQRYFSSFGNLSNAAAILGNPKVAAHGKVVVGGLDKAVKHLDNVKGTYAKLSELHSEKLHVDPSNFTLLADCLTITLAAKFGPSVFTPEVHEVWQKFLNVAVAALGKQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Silurus asotus (Amur catfish) (Parasilurus asotus) |
O13186 | GCR_SAIBB | MDSKESLTPGKEENPSSVLTQERGNVMDFCKILRGGATLKVSVSSTSLAAASQSDSKQQRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLQLLEESIANLNRSTSVPENPKSSASSSVSAAPKEKEFPKTHSDVSSEQQNLKGQTGSNGGNVKLYTADQSTFDILQDLEFSSGSPGKETNQSPWKSDLLIDENCLLSPLAGEEDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSSSNVTLPQVKTEKEDFIELCTPGVIKQEKLSTVYCQASFPGANIIGNKMSAIS... | null | null | cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle [GO:0005819] | DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270] | PF02155;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000250|UniProtKB:P04150}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated i... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=A... | null | null | null | null | null | FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in... | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
O13282 | TAF5_SCHPO | MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTF... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; transcription initiation at RNA polymerase II promoter [GO:0006367]; transcription initiation-coupled chromatin remodeling [GO:0045815] | cytosol [GO:0005829]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFIID complex [GO:0005669] | RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF08513;PF04494;PF00400; | 1.25.40.500;2.130.10.10; | WD repeat TAF5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis. {ECO:0000269|PubMed:11279037}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13286 | SRW1_SCHPO | MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDA... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; mitotic G1 cell size control checkpoint signaling [GO:0031568]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; positive regulation of anaphase-promoting complex-dependent catabolic process [GO:1905786] | anaphase-promoting complex [GO:0005680]; nucleus [GO:0005634] | anaphase-promoting complex binding [GO:0010997]; ubiquitin ligase activator activity [GO:1990757] | PF12894;PF00400; | 2.130.10.10; | WD repeat CDC20/Fizzy family | PTM: Phosphorylated by cdc2-cdc13-CDK complex. This targets srw1 for proteolysis which in turn promotes cdc13 turnover. Dephosphorylated during G1 arrest. {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:18257517}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Has a role in cell differentiation and cell cycling by negatively regulating cig2 and cdc12-associated cdc2. Down-regulates the level of cdc13, particularly in a nitrogen deprived environment. Regulator of cell cycle G1 phase progression. Prevents onset of mitosis during the pre-Start G1 period. Required for ... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13289 | CATA_CANAL | MAPTFTNSNGQPIPEPFATQRVGQHGPLLLQDFNLIDSLAHFDRERIPERVVHAKGSGAYGVFEVTDDITDICAAKFLDTVGKKTRIFTRFSTVGGELGSADTARDPRGFATKFYTEEGNLDLVYNNTPVFFIRDPSKFPHFIHTQKRNPETHLKDANMFWDYLTSNEESIHQVMVLFSDRGTPASYREMNGYSGHTYKWSNKKGEWFYVQVHFISDQGIKTLTNEEAGALAGSNPDYAQEDLFKNIAAGNYPSWTAYIQTMTEAEAKEAEFSVFDLTKVWPHKKYPLRRFGKFTLNENPKNYFAEVEQAAFSPAHTVPY... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P15202}; | biological process involved in interaction with host [GO:0051701]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; filamentous gr... | cytoplasm [GO:0005737]; fungal-type cell wall [GO:0009277]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P15202}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. {ECO:0000269|PubMed:18352908}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13290 | DYHC_SCHPO | MDKNDNSQCQLSTVSDEILIFLKKLLSLSVSDNLDDICETIALQSTFVDTFRSFINDEYYTVIYLYGSPCLTSSPTSPDSCTFGNMTFQWTSLLQDVFSGTSAFAIFKRFPLTDTPLTLQNMLYINQLPILKGGHKSNEIPERPINAIFLYTKYVMSCYFTAYLAMESVDDRSTIDLNSPSKGKELELTCQKFADFERSFTFFCREYQNSDTILQHHPLILSTIKHAEENNLDLSVRLLPSKVLSDSEFYKSLSNLVNVWLKTTRSLIKLFHDQISKTALEEFNFWQFYYRSLSRLNDQLHSRPVLFVLDILAFGKRFHT... | null | null | attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cytoplasmic microtubule organization [GO:0031122]; dynein-driven meiotic oscillatory nuclear movement [GO:0030989]; homologous chromosome pairing at meiosis [GO:0007129]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; mitotic ... | cell cortex [GO:0005938]; cortical microtubule cytoskeleton [GO:0030981]; cytoplasmic dynein complex [GO:0005868]; cytoplasmic microtubule [GO:0005881]; meiotic spindle astral microtubule [GO:1990574]; meiotic spindle pole body [GO:0035974]; spindle pole body [GO:0005816] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; dynein intermediate chain binding [GO:0045505]; dynein light intermediate chain binding [GO:0051959]; minus-end-directed microtubule motor activity [GO:0008569] | PF12774;PF12775;PF12780;PF12781;PF18198;PF08385;PF08393;PF17852;PF03028;PF12777; | 1.10.287.2620;1.10.472.130;1.10.8.710;1.20.58.1120;1.20.920.20;1.20.920.30;6.10.140.1060;1.20.140.100;3.20.180.20;3.40.50.300;1.10.8.720; | Dynein heavy chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10366596}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10366596}. Note=Localized at the astral microtubules and the spindle pole body (SPB) during nuclear movements associated with meiotic prophase. | null | null | null | null | null | FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for nuclear movement during meiotic prophase. {ECO:0000269|PubMed:10366596}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13297 | CET1_YEAST | MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPD... | 3.6.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:6094533}; | 7-methylguanosine mRNA capping [GO:0006370]; polynucleotide 5' dephosphorylation [GO:0098507]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968] | mRNA capping enzyme complex [GO:0031533] | mRNA 5'-phosphatase activity [GO:0140818]; polynucleotide 5'-phosphatase activity [GO:0004651] | PF02940; | 3.20.100.10; | Fungal TPase family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for pppA-poly(A) {ECO:0000269|PubMed:6094533}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:6094533}; | null | FUNCTION: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. {ECO:0000269|PubMed:12788946, ECO:0000269|PubMed:3029058, ECO:0000269|PubMed:6094533}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13298 | PHD1_SCHPO | MDTPETSTPYEQVEKGSFFSFRPQKKRVTYHLDEQVGNYHYGDKHPMKPHRITITNHLVMGYGLHNKMSVFSPRMATFGEMSEFHREDYLDFLKRVTPDNAEQFADKFQQFNIGDDCPVFDGTYEFSQRSAGASLDASRKLVQGQTDIAINWSGGLHHAKRGEASGFCYVNDIVLAILNMLRFFPRVLYIDIDIHHGDGVQQAFYESDRVLTVSFHKYNGDFFPATGNFDENGVKGGKYFALNVPLEDGIGDEQYTSLFKSIIEPTINTFQPSAIVLQCGADSLGYDRLGVFNLSIHAHGECVRFTRSFNIPMLVVGGGG... | 3.5.1.98 | null | epigenetic regulation of gene expression [GO:0040029]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; Rpd3L-Expanded complex [GO:0070210]; Set3 complex [GO:0034967] | histone deacetylase activity [GO:0004407]; histone H4K16 deacetylase activity [GO:0034739] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9781677}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:9781677}; PhysiologicalDirection=left-to-... | null | null | null | null | FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:9781677). Histone deacetylases act via the formation of l... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13310 | ORB6_SCHPO | MDKNDYLHFERNPSLFPKSTLDKVQKTKKYIEHYYKVAVDHAVERNQRRINLEQRLATERGSEERKNRQLRASGEKESQFLRFRRTRLSLEDFSTIKVIGKGAFGEVRLVQKLDTGKIYAMKSLLKTEMFKRDQLAHVKAERDLLVESDSPWVVSLYYAFQDSLYLYLIMEFLPGGDLMTMLINYDTFSEDVTRFYMAECVLAIADVHRMGYIHRDIKPDNILIDRDGHIKLSDFGLSTGFYKQDQSASYMKPRTGNTVKRGQMVDAIWLTMSSKDKMATWKKNRRVMAYSTVGTPDYIAPEIFLQQGYGQDCDWWSLGA... | 2.7.11.1 | null | cellular response to salt stress [GO:0071472]; cortical actin cytoskeleton organization [GO:0030866]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; intracellular signal transduction [GO:0035556]; maintenance of protein location in cell cortex of cell tip [GO:0097248]; phosphorylation [GO:001... | cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cytosol [GO:0005829]; growing cell tip [GO:0035838]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Interacts with pak1/shk1 and coordinates cell morphogenesis with the cell cycle. It is essential for maintenance of cell polarity and is involved in mitotic control. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13318 | PHR2_CANAL | MLLKSLFPSILAATSFVSSVAAEDLPAIEIVGNKFFYSNNGSQFYIKGIAYQQNNLDSNESFVDPLANPEHCKRDIPYLEAVDTNVIRVYALDTSQDHTECMQMLQDAGIYVIADLSQPDESINRDDPSWDLDLFERYTSVVDLFHNYTNILGFFAGNEVTNKKSNTDASAFVKAAIRDTKAYIKSKGYRSIPVGYSANDDSAIRVSLADYFACGDEDEAADFFGINMYEWCGDSSYKASGYESATNDYKNLGIPIFFSEYGCNEVRPRKFTEVATLFGDQMTPVWSGGIVYMYFEEENNYGLVSIKDNTVSTLKDYSYY... | null | null | fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall organization [GO:0031505] | cell surface [GO:0009986]; extracellular vesicle [GO:1903561]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; yeast-form cell wall [GO:0030445] | 1,3-beta-glucanosyltransferase activity [GO:0042124]; glucanosyltransferase activity [GO:0042123] | PF03198;PF07983; | 1.20.58.1040;3.20.20.80; | Glycosyl hydrolase 72 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism (By similarity). {ECO:0000250}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13326 | CYSD_SCHPO | MPVESEHFETLQLHAGQEPDAATSSRAVPIYATTSYVFRDCDHGGRLFGLQEPGYIYSRMMNPTADVFEKRIAALEHGAAAIATSSGTSALFMALTTLAKAGDNIVSTSYLYGGTYNLFKVTLPRLGITTKFVNGDDPNDLAAQIDENTKAVYVESIGNPMYNVPDFERIAEVAHAAGVPLMVDNTFGGGGYLVRPIDHGADIVTHSATKWIGGHGTTIGGVIVDSGKFDWKKNSKRFPEFNEPHPGYHGMVFTETFGNLAYAFACRTQTLRDVGGNANPFGVFLLLQGLETLSLRMERHVQNAFALAKYLEKHPKVNWV... | 2.5.1.49 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6526818}; | cysteine biosynthetic process from serine [GO:0006535]; L-homocysteine biosynthetic process [GO:0071269]; methionine metabolic process [GO:0006555]; transsulfuration [GO:0019346] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine synthase activity [GO:0004124]; O-acetylhomoserine aminocarboxypropyltransferase activity [GO:0003961]; O-acetylhomoserine sulfhydrylase activity [GO:0051009]; pyridoxal phosphate binding [GO:0030170] | PF01053; | 3.90.1150.10;3.40.640.10; | Trans-sulfuration enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818}; CATALYTIC ACTIVITY: Rea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=11.1 mM for O-succinyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=10.4 mM for L-homoserine {ECO:0000269|PubMed:6526818}; KM=0.053 mM for H(2)S {ECO:0000269|PubMed:6526818}; Vmax=15.5 umol/min/mg ... | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine. {ECO:0000305|PubMed:11754480}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:6526818}; | null | FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:11754480, PubMed:6526818). Can also use O-succinyl-L-homoserine and L-homoserine as substrates (PubMed:6526818). Has also cysteine synthase (O-acetylserine sulfhydrylase) activity in vitro,... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13329 | FOB1_YEAST | MTKPRYNDVLFDDDDSVPSESVTRKSQRRKATSPGESRESSKDRLLILPSMGESYTEYVDSYLNLELLERGERETPIFLESLTRQLTQKIYELIKTKSLTADTLQQISDKYDGVVAENKLLFLQRQYYVDDEGNVRDGRNNDKIYCEPKHVYDMVMATHLMNKHLRGKTLHSFLFSHFANISHAIIDWVQQFCSKCNKKGKIKPLKEYKRPDMYDKLLPMERIHIEVFEPFNGEAIEGKYSYVLLCRDYRSSFMWLLPLKSTKFKHLIPVVSSLFLTFARVPIFVTSSTLDKDDLYDICEEIASKYGLRIGLGLKSSARF... | null | null | chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA recombination [GO:0006310]; maintenance of DNA repeat elements [GO:0043570]; maintenance of rDNA [GO:0043007]; negative regulation of DNA replication [GO:0008156]; positive regulation of DNA recombination [GO:0045911]; protein localization to... | nucleolus [GO:0005730]; rDNA heterochromatin [GO:0033553] | metal ion binding [GO:0046872]; rDNA spacer replication fork barrier binding [GO:0043110] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10230397, ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB. {ECO:0000269|PubMed:14645529, ECO:0000269|Pu... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13339 | TERT_SCHPO | MTEHHTPKSRILRFLENQYVYLCTLNDYVQLVLRGSPASSYSNICERLRSDVQTSFSIFLHSTVVGFDSKPDEGVQFSSPKCSQSELIANVVKQMFDESFERRRNLLMKGFSMNHEDFRAMHVNGVQNDLVSTFPNYLISILESKNWQLLLEIIGSDAMHYLLSKGSIFEALPNDNYLQISGIPLFKNNVFEETVSKKRKRTIETSITQNKSARKEVSWNSISISRFSIFYRSSYKKFKQDLYFNLHSICDRNTVHMWLQWIFPRQFGLINAFQVKQLHKVIPLVSQSTVVPKRLLKVYPLIEQTAKRLHRISLSKVYNH... | 2.7.7.49 | null | DNA strand elongation [GO:0022616]; telomerase catalytic core complex assembly [GO:1904868]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric repeat region [GO:0140445]; nucleus [GO:0005634]; telomerase catalytic core complex [GO:0000333]; telomere cap complex [GO:0000782] | enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activity [GO:0003721]; telomeric DNA binding [GO:0042162] | PF00078;PF12009; | 1.10.132.70;3.30.70.2630; | Reverse transcriptase family, Telomerase subfamily | null | SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:24793650}; | null | null | null | null | FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. {ECO:0000269|PubMed... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13345 | AFLQ_ASPPU | MIYSIIICAGALLGFLILQKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHHERYGPMSSLEVMGQTIIMINDAHLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNKQAWKTIRANMKQEIGTRRAIATFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCTRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALY... | 1.14.14.117 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | aflatoxin biosynthetic process [GO:0045122] | null | aflatoxin B synthase activity [GO:0140399]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=8-O-methylsterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B1 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:35759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:2504, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ... | null | PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis. {ECO:0000305|PubMed:15006741}. | null | null | FUNCTION: O-methylsterigmatocystin oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:11996570, PubMed:15006741). The four major aflatoxins produced... | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) |
O13351 | PMT3_SCHPO | MSESPSANISDADKSAITPTTGDTSQQDVKPSTEHINLKVVGQDNNEVFFKIKKTTEFSKLMKIYCARQGKSMNSLRFLVDGERIRPDQTPAELDMEDGDQIEAVLEQLGGCTHLCL | null | null | mitotic recombination-dependent replication fork processing [GO:1990426]; protein sumoylation [GO:0016925]; stalled replication fork localization to nuclear periphery [GO:0120290]; telomere maintenance [GO:0000723] | linear element [GO:0030998]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; PML body [GO:0016605]; septin ring [GO:0005940] | protein tag activity [GO:0031386]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567589}. | null | null | null | null | null | FUNCTION: Required for chromosome segregation where it may be involved in microtubule assembly. Loss of smt3 leads to an increase in telomere length. {ECO:0000269|PubMed:10567589}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13370 | DED1_SCHPO | MSDNVQQQVDSVGSVTEKLQKTNISRPRKYIPPFARDKPSAGAAPAVGDDESVSSRGSSRSQTPSEFSSNYGGRREYNRGGHYGGGEGRQNNYRGGREGGYSNGGGYRNNRGFGQWRDGQHVIGARNTLLERQLFGAVADGTKVSTGINFEKYDDIPVEVSGGDIEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLI... | 3.6.4.13 | null | cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cytoplasmic translational initiation [GO:0002183]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; regulatory ncRNA-mediated gene silencing [GO:0031047] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; translation initiation factor activity [GO:0003743] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Inactivation of ded1 blocks mitotic cell cycle progression at G1 and G2/M. Induces sexual development and ascus fo... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13397 | ATN1_SCHOC | MTPSIGYVDEDENGQKSKFLRSSDDPYRLSIEEVIEKFETHLENGLSDEQAKSKLAKVGLNNLGADEKISISKILAHQIFNAMVLVLIISLIIALAIKDWISGGVIGFVVFINIFVGFIQELKAEKTMGSLRSLSSPMARALRNGVDSNINAEEVVPGDIIHIKVGDTIPADLRLVDCMNLETDEALLTGESLPVAKDHEEIYDYGAPIPVGDRLNMAFSSSIVAKGRGTGIVVATGLDTEIGKIAKSLKNNDDAVVVKVDKSLNPSTKDYLIAVIKTTKNIIFNVLGTNVGTPLQRKLSWLAILLFWVAVLFAIVVMAS... | 7.2.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | intracellular calcium ion homeostasis [GO:0006874]; intracellular sodium ion homeostasis [GO:0006883]; sodium ion export across plasma membrane [GO:0036376] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type potassium transmembrane transporter activity [GO:0008556]; P-type sodium transporter activity [GO:0008554]; salt transmembrane transporter activity [GO:1901702] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IID subfamily | PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH. Not phosphorylated in presence of calcium ions. {ECO:0000250|UniProtKB:P13587}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9430707}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000305|PubMed:9430707}; PhysiologicalDirection=left-to-right; Xref... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell (PubMed:9430707). May be an inefficient potassium exporter (PubMed:9430707). May transport other cations such as lithium (By similarity). Sodium/potassium efflux ATPases are involved in salt tolerance and maintaining... | Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
O13398 | ATN2_SCHOC | MSSINTNVAEKHSYKERVNTDASSLSADGSVEAHRLTIEQVAKIFNTDIINGLSTSQANQTLKDFGANTLGDGDKISLTKIIAHQVCNAMILVLIISMVIALAIKDWISGGVIGFVVLINISVGFVQEYKAEKTMGSLRSLSSPTARVTRNGDDTTIPAEEVVPGDIVHIKVGDTVPADLRLIDLMNLETDEALLTGESLPITKNHLDVYDDYSVPIPVGDRLNLAYSSSVVSKGRGTGIVIATALDTQIGQIAKSLRNNNSVIRKVDKSNGKPKKREYSKAFCGTIKDIFYNILGINVGTPLQRKLSWLAIFLFWGCRY... | 7.2.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | intracellular calcium ion homeostasis [GO:0006874]; intracellular pH reduction [GO:0051452]; potassium ion export across plasma membrane [GO:0097623] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type potassium:proton transporter activity [GO:0008900]; P-type sodium transporter activity [GO:0008554]; salt transmembrane transporter activity [GO:1901702] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IID subfamily | PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH. Not phosphorylated in presence of calcium ions. {ECO:0000250|UniProtKB:P13587}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9430707}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000250|UniProtKB:P13587}; PhysiologicalDirection=left-to-right; Xr... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell (PubMed:9430707). May be an inefficient sodium exporter (PubMed:9430707). May transport other cations such as lithium (By similarity). Sodium/potassium efflux ATPases are involved in salt tolerance and maintaining th... | Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
O13426 | GLYC_CANAL | MSAYALSQSHRQLTEGHLKDTDPEVDQIIKDEIDRQQHSIVLIASENFTTTAVFDALGTPMCNKYSEGYPGARYYGGNEHIDRMELLCQERALKAFGLTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLDLPHGGHLSHGYQTDSRKISAVSTYFETMPYRVDLETGLIDYDMLEKTAVLYRPKVLVAGTSAYCRLIDYKRMREIADKVGAYLVVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSVNPKTGQEILYDLENPINFSVFPGHQGGPHNHTIAALATALKQANTPEFKEYQ... | 2.1.2.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. | null | null | FUNCTION: Interconversion of serine and glycine. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13437 | FDH_CANBO | MKIVLVLYDAGKHAADEEKLYGCTENKLGIANWLKDQGHELITTSDKEGETSELDKHIPDADIIITTPFHPAYITKERLDKAKNLKLVVVAGVGSDHIDLDYINQTGKKISVLEVTGSNVVSVAEHVVMTMLVLVRNFVPAHEQIINHDWEVAAIAKDAYDIEGKTIATIGAGRIGYRVLERLLPFNPKELLYYDYQALPKEAEEKVGARRVENIEELVAQADIVTVNAPLHAGTKGLINKELLSKFKKGAWLVNTARGAICVAEDVAAALESGQLRGYGGDVWFPQPAPKDHPWRDMRNKYGAGNAMTPHYSGTTLDAQ... | 1.17.1.9 | null | choline catabolic process [GO:0042426]; formate catabolic process [GO:0042183]; methanol oxidation [GO:0015946]; methylamine metabolic process [GO:0030416]; NADH metabolic process [GO:0006734]; NADH regeneration [GO:0006735] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; formate dehydrogenase (NAD+) activity [GO:0008863]; NAD+ binding [GO:0070403]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; protein homodimerization activity [GO:0042803] | PF00389;PF02826; | 3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family, FDH subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}. | CATALYTIC ACTIVITY: Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 mM for formate (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:1248477}; KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:1248477}; KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:10691964}; K... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11054119, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Broad temperature optima between 45 and 55 degrees Celsius. Reaction rate increases steeply up to 55 degrees Celsius. 50% of activity lost after incubation for 20 minutes at 57 degrees Celsius. Thermal stability increases in the presence of glycerol. {ECO:0000269|... | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms. {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|Pu... | Candida boidinii (Yeast) |
O13516 | RS9A_YEAST | MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE | null | null | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]; translation [GO:0006412] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00163;PF01479; | 3.10.290.10; | Universal ribosomal protein uS4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13527 | YA11B_YEAST | METFTGYLKSTCFHQISPYPPSIMSIQVKVHANILILSFIECLRMPMHRQIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKLRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKK... | 2.7.7.49; 2.7.7.7; 3.1.26.4 | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665;PF07727; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
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