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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O35728 | CP4AE_MOUSE | MGFFLFSPTRYLDGISGFFQWAFLLSLFLVLFKAVQFYLRRQWLLKTLQHFPCMPSHWLWGHHLKDKELQQILIWVEKFPSACLQCLSGSNIRVLLYDPDYVKVVLGRSDPKASGIYQFFAPWIGYGLLLLNGKKWFQHRRMLTPAFHYDILKPYVKIMADSVNIMLDKWEKLDGQDHPLEIFHCVSLMTLDTVMKCAFSYQGSVQLDENSKLYTKAVEDLNNLTFFRLRNAFYKYNIIYNMSSDGRLSHHACQIAHEHTDGVIKMRKSQLQNEEELQKARKKRHLDFLDILLFARMEDRNSLSDEDLRAEVDTFMFEGH... | null | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P20817}; | arachidonic acid metabolic process [GO:0019369]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651] | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid binding [GO:0050544]; arachidonic acid monooxygenase activity [GO:0008391]; fatty acid binding [GO:0005504]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for dodecanoic acid {ECO:0000269|PubMed:17112342}; Vmax=40 nmol/min/nmol enzyme toward dodecanoic acid {ECO:0000269|PubMed:17112342}; | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:17112342}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids (PubMed:17112342). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihem... | Mus musculus (Mouse) |
O35730 | RING1_MOUSE | MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPMPGSDQTATMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGAGAGASSVGTGGGAAGGACGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQETTEPGGPG... | 2.3.2.27 | null | anterior/posterior pattern specification [GO:0009952]; camera-type eye morphogenesis [GO:0048593]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of DNA-templated transcription [GO:0045892]; protein ubiquitination [GO:0016567] | cytosol [GO:0005829]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]; sex chromatin [GO:0001739]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activator activity [GO:0097027] | PF16207;PF13923; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inac... | Mus musculus (Mouse) |
O35732 | CFLAR_MOUSE | MAQSPVSAEVIHQVEECLDEDEKEMMLFLCRDVTENLAAPNVRDLLDSLSERGQLSFATLAELLYRVRRFDLLKRILKTDKATVEDHLRRNPHLVSDYRVLLMEIGESLDQNDVSSLVFLTRDYTGRGKIAKDKSFLDLVIELEKLNLIASDQLNLLEKCLKNIHRIDLNTKIQKYTQSSQGARSNMNTLQASLPKLSIKYNSRLQNGRSKEPRFVEYRDSQRTLVKTSIQESGAFLPPHIREETYRMQSKPLGICLIIDCIGNDTKYLQETFTSLGYHIQLFLFPKSHDITQIVRRYASMAQHQDYDSFACVLVSLGGS... | null | null | apoptotic process [GO:0006915]; cellular response to nitric oxide [GO:0071732]; erythrocyte differentiation [GO:0030218]; execution phase of apoptosis [GO:0097194]; keratinocyte differentiation [GO:0030216]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of ... | CD95 death-inducing signaling complex [GO:0031265]; cytoplasm [GO:0005737]; death-inducing signaling complex [GO:0031264] | cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; death receptor binding [GO:0005123]; enzyme activator activity [GO:0008047]; peptidase activator activity [GO:0016504]; protease binding ... | PF01335;PF00656; | 3.40.50.1460;1.10.533.10; | Peptidase C14A family | PTM: Proteolytically processed by CASP8 generating subunits p43 and p12. {ECO:0000269|PubMed:31511692}. | null | null | null | null | null | null | FUNCTION: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruit... | Mus musculus (Mouse) |
O35734 | TNFA_MARMO | MSTESMIRDVELAEEALPKEAWGPQGSSRCLCLSLFSFLLVAGATTLFCLLHFGVIGPQREEFLNNLPLSPQAQMLTLRSSSQNMNDKPVAHVVAKNEDKEQLVWLSRRANALLANGMELIDNQLVVPANGLYLVYSQVLFKGQGCPSYVLLTHTVSRFAVSYQDKVNLLSAIKSPCPKESLEGAEFKPWYEPIYLGGVFELQKGDRLSAEVNLPSYLDFAESGQVYFGVIAL | null | null | extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; necroptotic signaling pathway [GO:0097527]; negative regulation of protein-containing complex disassembly [GO:0043242]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JUN kinase ac... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secre... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:00... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain c... | Marmota monax (Woodchuck) |
O35738 | KLF12_MOUSE | MNIHMKRKTIKNLSALENRMLMLDGMPAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSSRPASSPTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKAQMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFACSISPFSIESTRRQRRSESPDSRKRRIHRCD... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory re... | PF00096; | 3.30.160.60; | Sp1 C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter. | Mus musculus (Mouse) |
O35739 | KLF9_MOUSE | MSAAAYMDFVAAQCLVSISNRAAVPEHGGAPEAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVCSDSLESPDEDIGSDSDVTTESGSSPSHSPEERQDSGSAPSPLSLLHSGVASKGKHASEKRHKCPYSGCGKVYGKSSHLKAHYRVHTGERPFPCTWPDCLKKFSRSDELTRHYRTHTGEKQFRCPLCEKRFMRSDHLTKHARRHTVFHPSMIKRSKKALACPL | null | null | cellular response to cortisol stimulus [GO:0071387]; embryo implantation [GO:0007566]; negative regulation of keratinocyte proliferation [GO:0010839]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone receptor signaling pathway [GO:0050847]; regulation of DNA-templated transcription [... | 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... | PF00096; | 3.30.160.60; | Sp1 C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13886}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation. {ECO:0000250|UniProtKB:Q13886}... | Mus musculus (Mouse) |
O35740 | CITE2_MOUSE | MADHMMAMNHGRFPDGTNGLHHHPAHRMGMGQFPSPHHHQQQQPQHAFNALMGEHIHYGAGNMNATSGIRHAMGPGTVNGGHPPSALAPAARFNNSQFMGPPVASQGGSLPASMQLQKLNNQYFNHHPYPHNHYMPDLHPTAGHQMNGTNQHFRDCNPKHSGGSSTPGGAGGSGTPGGSGGTSGGAGGSSAGGSGGGSTMPASVAHVPAAMLPPNVIDTDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC | null | null | adrenal cortex formation [GO:0035802]; adrenal gland development [GO:0030325]; blood vessel development [GO:0001568]; bone morphogenesis [GO:0060349]; cardiac neural crest cell development involved in heart development [GO:0061308]; cardiac septum morphogenesis [GO:0060411]; cell population proliferation [GO:0008283]; ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone acetyltransferase binding [GO:0035035]; LBD domain binding [GO:0050693]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]; ... | PF04487; | 6.10.140.2200; | CITED family | null | SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with EP300 in dot-like structures. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its associatio... | Mus musculus (Mouse) |
O35744 | CHIL3_MOUSE | MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDA... | 3.2.1.52 | null | chitin catabolic process [GO:0006032]; inflammatory response [GO:0006954]; polysaccharide catabolic process [GO:0000272] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; rough endoplasmic reticulum lumen [GO:0048237] | beta-N-acetylhexosaminidase activity [GO:0004563]; carbohydrate binding [GO:0030246]; chitin binding [GO:0008061]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00704; | 3.10.50.10;3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class II subfamily | null | SUBCELLULAR LOCATION: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:11733538}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120.8 uM for 4-methylumbelliferone-N-acetylglucosamine (at pH 4-4.5) {ECO:0000269|PubMed:11733538}; Vmax=0.023 umol/min/mg enzyme {ECO:0000269|PubMed:11733538}; Note=4-methylumbelliferone-N-acetylglucosamine (MU-(GlcNAc)1) is a GlcNAc2 analog.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:11733538}; | null | FUNCTION: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymp... | Mus musculus (Mouse) |
O35750 | SHOX2_RAT | RELDMGAAERSREPGSPRLTEVSPELKDRKEDAKGMEDEGQTKIKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQLHKGVLIGAASQFEACRVAPYVNVGALRMPFQQDSHCNVTPLSFQVQAHVQLDSAVRAAHHHLHPHLAAHGPYMMFPAPPFGLPLATLAADSASAASVVAAAAAAKTTSKNSSIADLRLKAKKHAAALGL | null | null | cardiac atrium morphogenesis [GO:0003209]; cardiac pacemaker cell differentiation [GO:0060920]; cardiac right atrium morphogenesis [GO:0003213]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; chondrocyte development [GO:0002063]; chondrocyte differentiation [GO:0002062]; embryonic diges... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation. | Rattus norvegicus (Rat) |
O35757 | VEGFC_RAT | MHLLCFLSLACSLLAAALIPGPREAPATVAAFESGLGFSEAEPDGGEVKGFEGKDLEEQLRSVSSVDELMSVLYPDYWKMYKCQLRKGGWQQPSLNMRTGDTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPANYVWNNYMCQCLAQQDFIFYSNVEDDSSNGFHDVCGPNKELDEDTCQCVCKGGLRPSSCGPHKELDRDSCQCVCKNKLF... | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell population proliferation [GO:0008283]; cellular response to leukemia inhibitory factor [GO:1990830]; glial cell proliferation [GO:0014009]; induction of positive chemotaxis [GO:0050930]; morphogenesis of embryonic epithelium [GO:0016331]; negative... | extracellular space [GO:0005615]; membrane [GO:0016020] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; vascular endothelial growth factor receptor 3 binding [GO:0043185] | PF03128;PF00341; | 2.10.90.10; | PDGF/VEGF growth factor family | PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-2... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentia... | Rattus norvegicus (Rat) |
O35762 | NKX61_RAT | MLAVGAMEGPRQSAFLLSSPPLAALHSMAEMKTPLYPAAYPPLPTGPPSSSSSSSSSSSPSPPLGAHNPGGLKPPAAGGLSSLGSPPQQLSAATPHGINDILSRPSMPVASGAALPSASPSGSSSSSSSSASATSASAAAAAAAAAAAAAASSPAGLLAGLPRFSSLSPPPPPPGLYFSPSAAAVAAVGRYPKPLAELPGRTPIFWPGVMQSPPWRDARLACTPHQGSILLDKDGKRKHTRPTFSGQQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKHAAEMATAKKKQDSETERLKGTSEN... | null | null | cell differentiation [GO:0030154]; cellular response to cytokine stimulus [GO:0071345]; cellular response to peptide hormone stimulus [GO:0071375]; central nervous system neuron differentiation [GO:0021953]; endocrine pancreas development [GO:0031018]; negative regulation of oligodendrocyte differentiation [GO:0048715]... | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA... | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99MA9}. | null | null | null | null | null | FUNCTION: Transcription factor which binds to specific A/T-rich DNA sequences in the promoter regions of a number of genes. Involved in the development of insulin-producing beta cells in the islets of Langerhans at the secondary transition (By similarity). Together with NKX2-2 and IRX3 acts to restrict the generation o... | Rattus norvegicus (Rat) |
O35763 | MOES_RAT | MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMER... | null | null | cellular response to testosterone stimulus [GO:0071394]; establishment of endothelial barrier [GO:0061028]; establishment of epithelial cell apical/basal polarity [GO:0045198]; gland morphogenesis [GO:0022612]; immunological synapse formation [GO:0001771]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration ... | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cell tip [GO:0051286]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; filopodium [GO:0030... | actin binding [GO:0003779]; cell adhesion molecule binding [GO:0050839]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674]; signaling receptor binding [GO:0005102] | PF00769;PF20492;PF09380;PF00373;PF09379; | 1.20.5.450;1.20.80.10;6.10.360.10;2.30.29.30; | null | PTM: Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. Phosphorylation on Thr-558 by STK10 neg... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26038}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P26041}. Apical cell membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0... | null | null | null | null | null | FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions betwee... | Rattus norvegicus (Rat) |
O35764 | NPTXR_RAT | MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGTDNASAASAAGAPGPQRSLSALQGAGGSAGPSVLPGEPAASVFPPPPGPLLSRFLCTPLAAACPSGAEQGDAAGERAELLLLQSTAEQLRQTALQQEARIRADRDTIRELTGKLGRCESGLPRGLQDAGPRRDTMADGAWDSPALLVELENAVRALRDRIERIEQELPARGNLSSSAPAPAVPTALHSKMDELEGQLLAKVLALEKERAALSHGSHQQRQEVEKELDALQGRVAELEHGSSAYSPPDAFKVSIPIRNNYMYARVRKAVPELYAFTACMWLR... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 2 calcium ions per subunit. {ECO:0000250}; | neuron projection development [GO:0031175]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; regulation of postsynaptic specialization assembly [GO:0099150]; response to hydrogen peroxide [GO:0042542] | extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; pentraxin receptor activity [GO:0008029]; protein phosphatase binding [GO:0019903]; protein-containing complex binding [GO:0044877] | PF00354; | 2.60.120.200; | null | PTM: N-glycosylated.; PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing KLHL2. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000269|PubMed:10748068}. | Rattus norvegicus (Rat) |
O35767 | NKX25_RAT | MFPSPALTHTPFSVKDILNLEQQQRSLAAGDLSARLEATLAPASCMLAAFKPDGYSGPEAAAPGLAELRAELGPAPSPPKCSPAFPTAPTFYPRAYGDPDPAKDPRADKKELCALQKAVELDKAETDGAERRRPRRRRKPRVLFSQAQVYELERRFKQQRYLSPAERDQLASVLKLTSTQVKIWFQNRRYKCKRQRQDQTLELLGPPPPPARRIAVPVLVRDGKPCLGDSAAYAPAYGLGLNAYGYNAYPYPGYGGAACSPAYSCAAYPAAPPAAHAPAASANSNFVNFGVGDLNTVQSPGMPQGNSGVSTLHGIRAW | null | null | adult heart development [GO:0007512]; apoptotic process [GO:0006915]; apoptotic process involved in heart morphogenesis [GO:0003278]; atrial cardiac muscle tissue development [GO:0003228]; atrial septum morphogenesis [GO:0060413]; atrioventricular node cell development [GO:0060928]; atrioventricular node cell fate comm... | cytoplasm [GO:0005737]; Nkx-2.5 complex [GO:1990664]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II... | PF00046; | 1.10.10.60; | NK-2 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P42582}. | null | null | null | null | null | FUNCTION: Transcription factor required for the development of the heart and the spleen (By similarity). During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4 (By similarity). May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular cana... | Rattus norvegicus (Rat) |
O35776 | HYAS2_RAT | MHCERFLCVLRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSDDDLYMMDIFSEVMGRDKSVTYIWKNNFHERGPGETEESHKESSQHVTQLVLSNKSICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNR... | 2.4.1.212 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | atrioventricular canal development [GO:0036302]; bone morphogenesis [GO:0060349]; cellular response to fluid shear stress [GO:0071498]; cellular response to interleukin-1 [GO:0071347]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to tumor necrosis factor [GO:0071356]; end... | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853] | hyaluronan synthase activity [GO:0050501]; identical protein binding [GO:0042802] | PF03142;PF00535; | null | NodC/HAS family | PTM: Phosphorylation at Thr-328 is essential for hyaluronan synthase activity. {ECO:0000250|UniProtKB:Q92819}.; PTM: O-GlcNAcylation at Ser-221 increases the stability of HAS2 and plasma membrane localization. {ECO:0000250|UniProtKB:Q92819}.; PTM: Ubiquitination at Lys-190; this ubiquitination is essential for hyaluron... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-... | CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.... | null | PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000250|UniProtKB:Q92819}. | null | null | FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By si... | Rattus norvegicus (Rat) |
O35779 | BHE41_RAT | MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSLKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPVQADLDAFHSGFQTCAKEVLQYLARFESWTPREPRCAQLVSHLHAVATQLLTPQVTPGRGPGRAPCSAGAAAASGSERVARCVPVIQRTQPGTEPEHDTDTDSGYGGEAEQGRAAVKQEPPGDPSAAPKRLKLEARGALLGPEPALLGSLVALGGGAPFAQPAAAPFCLPFYLLSPSAAAYVQPWLDKSGLDKYLYP... | null | null | anterior/posterior pattern specification [GO:0009952]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of myotube differentiation [GO:0010832]; negative regulation of transcription by competitive pr... | nucleus [GO:0005634] | bHLH transcription factor binding [GO:0043425]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; histone deacetylase binding [GO:0042826]; MRF binding [GO:0043426]; prote... | PF07527;PF00010; | 6.10.250.980;4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional re... | Rattus norvegicus (Rat) |
O35780 | BHE40_RAT | MERIPSAQPPPTCLPKTPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIMALQSGLQAGDLSGKNIEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGSASRKPLDSAPKPVDFKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFTVGERVSTIKQESEEPPTKKSRMQLSDEEGHFVGSDLMGSPFLGPHPHQPP... | null | null | anterior/posterior pattern specification [GO:0009952]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | bHLH transcription factor binding [GO:0043425]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; MRF binding [GO:0043426]; protein domain specif... | PF07527;PF00010; | 6.10.250.980;4.10.280.10; | null | PTM: Ubiquitinated; which may lead to proteasomal degradation. {ECO:0000250}.; PTM: Sumoylation inhibits its ubiquitination and promotes its negative regulation of the CLOCK-BMAL1 heterodimer transcriptional activator activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}. | null | null | null | null | null | FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional re... | Rattus norvegicus (Rat) |
O35783 | CALU_RAT | MDLRQFLMCLSLCTAFALSKPTEKKDRVHHEPQLSDKVHNDAQNFDYDHDAFLGAEEAKSFGQLTPEESKEKLGMIVDKIDTDKDGFVTEGELKSRIKHAQKKYIYDNVENQWQEFDMNQDGLISWDEYRNVTYGTYLDDPDPDDGFNYKPIMVRDERRFKMADQDGDLIATKEEFTAFLHPEEYDYMKDIVLQETMEDIDQNADGFIDLEEYIGDMYSHDGNADEPQWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQDKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF | null | null | peripheral nervous system axon regeneration [GO:0014012]; response to organic cyclic compound [GO:0014070] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; sarcoplasmic reticulum lumen [GO:0033018] | calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857] | PF13202;PF13499;PF13833; | 1.10.238.10; | CREC family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43852}. Golgi apparatus {ECO:0000250|UniProtKB:O43852}. Secreted {ECO:0000250|UniProtKB:O43852}. Melanosome {ECO:0000250|UniProtKB:O43852}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O43852}. | null | null | null | null | null | FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250, ECO:0000269|PubMed:15075329}. | Rattus norvegicus (Rat) |
O35786 | CML1_RAT | MEYEGYNDSSIYGEEYSDGSDYIVDLEEAGPLEAKVAEVFLVVIYSLVCFLGILGNGLVIVIATFKMKKTVNTVWFVNLAVADFLFNIFLPIHITYAAMDYHWVFGKAMCKISSFLLSHNMYTSVFLLTVISFDRCISVLLPVWSQNHRSVRLAYMTCVVVWVLAFFLSSPSLVFRDTVSTSHGKITCFNNFSLAAPEPFSHSTHPRTDPVGYSRHVAVTVTRFLCGFLIPVFIITACYLTIVFKLQRNRLAKTKKPFKIIITIIITFFLCWCPYHTLYLLELHHTAVPASVFSLGLPLATAVAIANSCMNPILYVFMGH... | null | null | chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of NF-kappaB transcription factor activity [GO:0032088];... | plasma membrane [GO:0005886] | adipokinetic hormone binding [GO:0097004]; adipokinetic hormone receptor activity [GO:0097003]; complement receptor activity [GO:0004875]; G protein-coupled chemoattractant receptor activity [GO:0001637]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | Chemokine-like receptor (CMKLR) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99788}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobi... | Rattus norvegicus (Rat) |
O35787 | KIF1C_RAT | MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSRMFLKASFDYSYWSHTSVEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQLTGLDSEKVSKISLVNLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAM... | null | null | anterograde neuronal dense core vesicle transport [GO:1990048]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; microtubule-based process [GO:0007017]; retrograde neuronal dense core vesicle transport [GO:1990049]; retrograde vesicle-mediated transport, Golgi to end... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF00498;PF00225;PF16183; | 2.60.200.20;6.10.250.2520;3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable motor protein. | Rattus norvegicus (Rat) |
O35789 | B3GA1_RAT | MPKRRDILAIVLIVLPWTLLITVWHQSSLAPLLAVHKDEGSDPRHEAPPGADPREYCMSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSTQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLV... | 2.4.1.135 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9804790}; | carbohydrate metabolic process [GO:0005975]; cellular response to hypoxia [GO:0071456]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; glycosaminoglycan biosynthetic process [GO:0006024]; protein glycosylation [GO:0006486]; visual learning [GO:0008542] | endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139] | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity [GO:0015018]; metal ion binding [GO:0046872] | PF03360; | null | Glycosyltransferase 43 family | PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000269|PubMed:19181664}. | SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:19181664}; Single-pass type II membrane protein. Secreted {ECO:0000269|PubMed:19181664}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:19181664}; Single-pass type II membrane protein. Endoplasmic reticulum... | CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:12573, ChEB... | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the mos... | Rattus norvegicus (Rat) |
O35793 | GREM1_RAT | MNRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fib... | cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | BMP binding [GO:0036122]; cytokine activity [GO:0005125]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043184] | PF03045; | 2.10.90.10; | DAN family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner (By similarity). Antagonist of BMP2;... | Rattus norvegicus (Rat) |
O35795 | ENTP2_RAT | MAGKLVSLVPPLLLAAAGLTGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVQGGGISSYANDPSKAGQSLVRCLEQALRDVPRDRHASTPLYLGATAGMRPFNLTSPEATARVLEAVTQTLTQYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPGNEVHLRLYGQHYRVYTHSFLCYGRDQILLRLLASALQIHRFHPCWPKGYSTQVLLQEVYQSPCTMGQRPRAFNGSAIVSLSGTSNATLCRDLVSRLFNI... | 3.6.1.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cellular response to interferon-alpha [GO:0035457]; cellular response to interleukin-6 [GO:0071354]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; G protein-coupled receptor signaling pathway [GO:0007186]; nucleoside diphosphate catabolic process [GO:0009... | basement membrane [GO:0005604]; cell body [GO:0044297]; cell projection membrane [GO:0031253]; cell surface [GO:0009986]; plasma membrane [GO:0005886] | ADP phosphatase activity [GO:0043262]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GDP phosphatase activity [GO:0004382]; identical protein binding [GO:0042802]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase a... | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent. | Rattus norvegicus (Rat) |
O35796 | C1QBP_RAT | MLPLLRCVPRALGAAATGLRASIPAPPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPELTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQTTGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ | null | null | apoptotic process [GO:0006915]; complement activation, classical pathway [GO:0006958]; cytosolic ribosome assembly [GO:0042256]; immune response [GO:0006955]; innate immune response [GO:0045087]; mRNA processing [GO:0006397]; negative regulation of defense response to virus [GO:0050687]; negative regulation of double-s... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membr... | adrenergic receptor binding [GO:0031690]; complement component C1q complex binding [GO:0001849]; enzyme inhibitor activity [GO:0004857]; hyaluronic acid binding [GO:0005540]; kininogen binding [GO:0030984]; mitochondrial ribosome binding [GO:0097177]; mRNA binding [GO:0003729]; protein kinase C binding [GO:0005080]; tr... | PF02330; | 3.10.280.10; | MAM33 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q07021}. Nucleus {ECO:0000250|UniProtKB:Q07021}. Cell membrane {ECO:0000250|UniProtKB:Q07021}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07021}; Extracellular side {ECO:0000250|UniProtKB:Q07021}. Secreted {ECO:0000250|UniProtKB:Q07021}. Cytopla... | null | null | null | null | null | FUNCTION: Multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma protei... | Rattus norvegicus (Rat) |
O35799 | HFE_RAT | MDRSAGLPVRLLLLLLLLLLWSVAPQALRPGSHSLRYLFMGASKPDLGLPFFEALGYVDDQLFVSYNHESRRAEPRAPWILGQTSSQLWLQLSQSLKGWDYMFIVDFWTIMGNYNHSKVTKLRVVPESHILQVILGCEVHEDNSTSGFWKYGYDGQDHLEFCPKTLNWSAAEPRAWATKMEWEEHRIRARQSRDYLQRDCPQQLKQVLELQRGVLGQQVPTLVKVTRHWASTGTSLRCQALNFFPQNITMRWLKDSQPLDAKDVNPENVLPNGDGTYQGWLTLAVAPGEETRFSCQVEHPGLDQPLTATWEPSRSQDMII... | null | null | acute-phase response [GO:0006953]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; BMP signaling pathway [GO:0030509]; cellular response to iro... | apical part of cell [GO:0045177]; basal part of cell [GO:0045178]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; HFE-transferrin receptor complex [GO:1990712]; perinuclear region of cytoplasm [GO:0048471]; recycling endoso... | beta-2-microglobulin binding [GO:0030881]; co-receptor binding [GO:0039706]; signaling receptor binding [GO:0005102]; transferrin receptor binding [GO:1990459] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q30201}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q30201}. | null | null | null | null | null | FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. {ECO:0000250|UniProtKB:Q30201}. | Rattus norvegicus (Rat) |
O35800 | HIF1A_RAT | MEGAGGENEKKKMSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDEMKAQMNCFYLKAPDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGPVRKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTSSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQ... | null | null | acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axonal transport of mitochondrion [GO:0019896]; B-1 B cell homeostasis [GO:0001922]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; bone mineralization [GO:0030282]; camera-type eye morphogenes... | axon cytoplasm [GO:1904115]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; euchromatin [GO:0000791]; motile cilium [GO:0031514]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription ... | PF11413;PF08778;PF08447;PF13426; | 4.10.280.10;3.30.450.20; | null | PTM: S-nitrosylation of Cys-799 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex. {ECO:0000250|UniProtKB:Q16665}.; PTM: Acetylation of Lys-531 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation. Deacetylated by... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16665}. Nucleus. Nucleus speckle {ECO:0000250|UniProtKB:Q61221}. Note=Colocalizes with HIF3A in the nucleus and speckles (By similarity). Cytoplasmic in normoxia, nuclear translocation in response to hypoxia (By similarity). {ECO:0000250|UniProtKB:Q16665, ECO:0000... | null | null | null | null | null | FUNCTION: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products in... | Rattus norvegicus (Rat) |
O35806 | LTBP2_RAT | MRAPTTVRCSGRIQRARWRGFLPLVLALLMGTSHAQRDSVGRYEPASRDANRLWRPVGNHPAAAAAKVYSLFREPDAPVPGLSPSEWNQPGQGIPGRLAEAEARRPSRAQQLRRVQSPVQTRRSNPRGQQPPAARTAHSVVRLATPQRPAAARRGRLTGRNVCGGQCCPGWTTSNSTNHCIKPVCQPPCQNRGSCSRPQLCICRSGFRGARCEEVIPEEEFDPQNARPVPRRSVEGAPGPHRSSEARGSLVTRIQPLLPPLPPPPSRTLSQTRPLQQHAGLSRTVRRYPATGTNGQLMSNALPSGPGPELRDSSQQAAHM... | null | null | Golgi to vacuole transport [GO:0006896]; protein targeting to vacuole [GO:0006623]; response to alkaloid [GO:0043279]; supramolecular fiber organization [GO:0097435]; transforming growth factor beta receptor signaling pathway [GO:0007179] | endosome [GO:0005768]; extracellular region [GO:0005576]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | calcium ion binding [GO:0005509]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; microfibril binding [GO:0050436] | PF00008;PF07645;PF12661;PF00683; | 2.10.25.10;3.90.290.10; | LTBP family | PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.; PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q14767}. | null | null | null | null | null | FUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly. {ECO:0000250|UniProtKB:Q14767}. | Rattus norvegicus (Rat) |
O35811 | P2RY4_RAT | MTSAESLLFTSLGPSPSSGDGDCRFNEEFKFILLPMSYAVVFVLGLALNAPTLWLFLFRLRPWDATATYMFHLALSDTLYVLSLPTLVYYYAARNHWPFGTGLCKFVRFLFYWNLYCSVLFLTCISVHRYLGICHPLRAIRWGRPRFASLLCLGVWLVVAGCLVPNLFFVTTNANGTTILCHDTTLPEEFDHYVYFSSAVMVLLFGLPFLITLVCYGLMARRLYRPLPGAGQSSSRLRSLRTIAVVLTVFAVCFVPFHITRTIYYQARLLQADCHVLNIVNVVYKVTRPLASANSCLDPVLYLFTGDKYRNQLQQLCRGS... | null | null | cellular response to prostaglandin E stimulus [GO:0071380]; G protein-coupled receptor signaling pathway [GO:0007186]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; regulation of synaptic vesicle exocytosis [GO:2000300]; transepithelial chloride transport [GO:0030321] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787] | ATP binding [GO:0005524]; G protein-coupled purinergic nucleotide receptor activity [GO:0045028]; G protein-coupled UTP receptor activity [GO:0045030] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Phosphorylation of Ser-329 and Ser-330 is a key step in agonist-dependent desensitization and loss of surface P2RY4. This phosphorylation does not involve PKC, nor other calcium-activated kinases (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ADP or UDP. | Rattus norvegicus (Rat) |
O35814 | STIP1_RAT | MEQVNELKEKGNKALSAGNIDDALQCYSEAIKLDPQNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNLQLKEGLQNMEARLAERKFMNPFNLPNLYQKLENDPRTRTLLSDPTYRELIEQLQNKPSDLGTKLQDPRVMTTLSVLLGVDLGSMDEEEEAATPPPPPPPKKEAKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDKALKHYDKAKELDPTNMTYITNQAAVHFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEERYKDAI... | null | null | cellular response to interleukin-7 [GO:0098761] | dynein axonemal particle [GO:0120293]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; protein-containing complex [GO:0032991] | Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; protein-folding chaperone binding [GO:0051087] | PF17830;PF00515;PF13414;PF13424;PF13181; | 1.10.260.100;1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q7ZWU1}. | null | null | null | null | null | FUNCTION: Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (PubMed:9528774). {ECO:0000250|UniProtKB:P31948, ECO:0000269|PubMed:9528774}. | Rattus norvegicus (Rat) |
O35815 | ATX3_RAT | MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGPGMFDDDEDDLQRALAMSRQEIDMEDEEADLRRAIQLSMQGSSRGMCEDSPQTSSTDLSSEELRKRREAYFEKQQHQQQEADRPGYLSYPCERPTTSSGGLR... | 3.4.19.12 | null | actin cytoskeleton organization [GO:0030036]; cellular response to amino acid starvation [GO:0034198]; cellular response to heat [GO:0034605]; cellular response to misfolded protein [GO:0071218]; chromatin remodeling [GO:0006338]; exploration behavior [GO:0035640]; intermediate filament cytoskeleton organization [GO:00... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosomal membrane [GO:0005765]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; nuclear inclusion body [GO:0042405]; nuclear matrix [GO:0016363]; nucleus [GO:0005634] | ATPase binding [GO:0051117]; cysteine-type deubiquitinase activity [GO:0004843]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; K48-linked deubiquitinase activity [GO:1990380]; K63-linked deubiquitinase activity [GO:0061578]; RNA polymerase II transcription regulatory region sequence-... | PF02099;PF16619;PF02809; | 3.90.70.40;1.10.287.10; | null | PTM: Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity (By similarity). {ECO:0000250|UniProtKB:P54252}. | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:P54252}. Nucleus {ECO:0000250|UniProtKB:P54252}. Lysosome membrane {ECO:0000250|UniProtKB:P54252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54252}. Note=Predominantly nuclear, but not exclusively, inner nuclear matrix. Recruited to lysosomal membran... | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17696782}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:17696782). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (... | Rattus norvegicus (Rat) |
O35819 | KLF6_RAT | MDVLPMCSIFQELQIVHETGYFSALPSLEEYWQQTCLELERYLQSEPCYVSASEIKFDNQEDLWTKIILARERKEESELKISSSPPEDSLISSGFNYNLETNSLNSDVSSESSDSSEELSPTTKFTSDPIGEVLVNSGNLSSSVISTPPSSPEVNRESSQLWGCGPGDLPSPGKVRSGTSGKSGDKGSGDASPDGRRRVHRCHFNGCRKVYTKSSHLKAHQRTHTGEKPYRCSWEGCEWRFARSDELTRHFRKHTGAKPFKCSHCDRCFSRSDHLALHMKRHL | null | null | cellular response to cycloheximide [GO:0071409]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic cyclic compound [GO:0071407]; cellular response to peptide [GO:1901653]; cytokine-mediated signaling pathway [GO:0019221]; positive regulation of connective tissue replacement [GO:1905205];... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; RNA polymerase II c... | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional activator. Binds a GC box motif. Could play a role in B-cell growth and development (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
O35820 | DNPH1_RAT | MAASGEQAPCSVYFCGSIRGGREDQALYARIVSRLRRYGKVLTEHVADAELEPLGEEAAGGDQFIHEQDLNWLQQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEGEVETMLDRYFEAYLPQKTASSSHPSA | 3.2.2.- | null | allantoin metabolic process [GO:0000255]; deoxyribonucleoside monophosphate catabolic process [GO:0009159]; dGMP catabolic process [GO:0046055]; epithelial cell differentiation [GO:0030855]; nucleoside salvage [GO:0043174]; positive regulation of cell growth [GO:0030307] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | deoxyribonucleoside 5'-monophosphate N-glycosidase activity [GO:0070694]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF05014; | 3.40.50.450; | 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43598}. Nucleus {ECO:0000269|PubMed:9271375}. | CATALYTIC ACTIVITY: Reaction=5-hydroxymethyl-dUMP + H2O = 2-deoxy-D-ribose 5-phosphate + 5-hydroxymethyluracil; Xref=Rhea:RHEA:77099, ChEBI:CHEBI:15377, ChEBI:CHEBI:16964, ChEBI:CHEBI:62877, ChEBI:CHEBI:90409; Evidence={ECO:0000250|UniProtKB:O43598}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77100; Evidence=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for dGMP {ECO:0000269|PubMed:17234634}; KM=250 uM for dAMP {ECO:0000269|PubMed:17234634}; KM=450 uM for dIMP {ECO:0000269|PubMed:17234634}; KM=4 mM for dCMP {ECO:0000269|PubMed:17234634}; KM=15.6 mM for dUMP {ECO:0000269|PubMed:17234634}; Vmax=0.09 umol/min/m... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 with dGMP or dCMP as substrate. {ECO:0000269|PubMed:17234634}; | null | FUNCTION: Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate)... | Rattus norvegicus (Rat) |
O35821 | MBB1A_RAT | MAEMKSPTKAEPASPAEAPQGDRRSLLEHSREFLDFFWDIAKPDQETRLRATEKLLEYLRTRPSDSEMKYALKRLITGLGVGREAARPCYSLALAQLLQSFEDIQLCDILGQIQEKYNLQAMNKAMMRPTLFANLFGVLALFQSGRLVKDKEALMKCVRLLKILSHHYNHLQGQPVKALVDILSEVPESMFQEILPKVLKGDMKVILSSPKYLELFLLARQRVPAELESLVGSVDLFSEDNIPSLVNILKVAANSVKKEQKLPDVALNLLRLALQENKFERFWKEVLEEGLLKKPSYTSSYMCFRLLGASLPLLSDEQLQ... | null | null | cellular response to glucose starvation [GO:0042149]; circadian regulation of gene expression [GO:0032922]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of anoikis [GO:2000210]; positive regulation of trans... | B-WICH complex [GO:0110016]; cytoplasm [GO:0005737]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleolus [GO:0005730]; nucleus [GO:0005634] | E-box binding [GO:0070888]; rDNA binding [GO:0000182]; RNA binding [GO:0003723]; sequence-specific DNA binding [GO:0043565]; transcription corepressor activity [GO:0003714] | PF04931; | null | MYBBP1A family | PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q7TPV4}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TPV4}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q7TPV4}. Cytoplasm {ECO:0000250|UniProtKB:Q7TPV4}. Note=Predominantly nucleolar. Also shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on X... | null | null | null | null | null | FUNCTION: May activate or repress transcription via interactions with sequence specific DNA-binding proteins (By similarity). Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) (By similarity). Acts as a corepressor and in concert with CRY1, represses the transcription of the co... | Rattus norvegicus (Rat) |
O35826 | GLCNE_RAT | MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGT... | 2.7.1.60; 3.2.1.183 | null | N-acetylglucosamine biosynthetic process [GO:0006045]; N-acetylneuraminate biosynthetic process [GO:0046380]; UDP-N-acetylglucosamine metabolic process [GO:0006047] | cytosol [GO:0005829] | ATP binding [GO:0005524]; hexokinase activity [GO:0004396]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; metal ion binding [GO:0046872]; N-acylmannosamine kinase activity [GO:0009384]; UDP-N-acetylglucosamine 2-epimerase activity [GO:0008761] | PF02350;PF00480; | 3.30.420.40;3.40.50.2000; | UDP-N-acetylglucosamine 2-epimerase family; ROK (NagC/XylR) family | PTM: Phosphorylated. Phosphorylation by PKC activates the UDP-N-acetylglucosamine 2-epimerase activity. {ECO:0000250|UniProtKB:Q91WG8}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}. | CATALYTIC ACTIVITY: Reaction=H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D-mannosamine + UDP; Xref=Rhea:RHEA:30683, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17122, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=3.2.1.183; Evidence={ECO:0000269|PubMed:10334995, ECO:0000269|PubMed:10497249, ECO:0000269|Pu... | null | PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis. {ECO:0000269|PubMed:10497249, ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}. | null | null | FUNCTION: Bifunctional enzyme that possesses both UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities, and serves as the initiator of the biosynthetic pathway leading to the production of N-acetylneuraminic acid (NeuAc), a critical precursor in the synthesis of sialic acids. By catalyzing this... | Rattus norvegicus (Rat) |
O35831 | CDK17_RAT | MKKFKRRLSLTLRGSQTIDESLSELAEQMTIEESSSKDNEPIVKNGRPPTSHSMHSFLHQYTGSFKKPPLRRPHSVIGGSLGSFMAMPRNGSRLDIVHENLKMGSDGESDQASGTSSDEVQSPTGVCLRNRIHRRISMEDLNKRLSLPADIRIPDGYLEKLQISSPPFDQPMSRRSRRASLSEIGFGKMETYIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGSIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLL... | 2.7.11.22 | null | phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1. | Rattus norvegicus (Rat) |
O35854 | BCAT2_RAT | MSAAILGQVWTRKLLPIPWRLCVPGRCVSSNFKAADLQVQVTREPQKKPAPSQPLLFGKTFTDHMLMVEWNSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGELELATPPLDGIILPGVVRQSLLDLARTWGEFRVAERKVT... | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:O15382}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid catabolic process [GO:0009083]; branched-chain amino acid metabolic process [GO:0009081]; cellular response to leukemia inhibitory factor [GO:1990830]; isoleucine catabolic process [GO:0006550]; isoleucine metabolic process [GO:0006549]; lactation ... | mitochondrion [GO:0005739] | branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9165094}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:9165094}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methy... | null | null | null | null | FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (PubMed:9165094). May also function as a transporter of branched chain alpha-keto acids (PubMed:8428987). {ECO:0000269|PubMed:8428987, ECO:0000269|PubMed:9165094}. | Rattus norvegicus (Rat) |
O35855 | BCAT2_MOUSE | MAAATLGQVWARKLLPVPWLLCGSKRCVSSIFKAADLQIQMTKEPQKKPAPSQALLFGKTFTDHMLMVEWNNKAGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGGDQQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLYVILCPVGSYFPGDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQREAQKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDLARTWGEFRVAERKVT... | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:O15382}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid catabolic process [GO:0009083]; branched-chain amino acid metabolic process [GO:0009081]; cellular response to leukemia inhibitory factor [GO:1990830]; isoleucine catabolic process [GO:0006550]; isoleucine metabolic process [GO:0006549]; leucine bi... | mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O35854}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; Evidence={ECO:0000250|UniProtKB:O15382}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-met... | null | null | null | null | FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine (By similarity). May also function as a transporter of branched chain alpha-keto acids (By similarity). {ECO:0000250|UniProtKB:O15382, ECO:0000250|UniProtKB:O35854}. | Mus musculus (Mouse) |
O35864 | CSN5_MOUSE | MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS... | 3.4.-.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; | exosomal secretion [GO:1990182]; negative regulation of apoptotic process [GO:0043066]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein deneddylation [GO:0000338]; proteolysis [GO:0006508]; regulation of cell ... | chromatin [GO:0000785]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; synaptic vesicle [GO:0008021]; transcription regulator complex [GO:0005667] | deNEDDylase activity [GO:0019784]; enzyme binding [GO:0019899]; macrophage migration inhibitory factor binding [GO:0035718]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; transcription coactivator activity [GO:0003713] | PF18323;PF01398; | 3.40.140.10; | Peptidase M67A family, CSN5 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10721695}. Nucleus {ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}. Note=Nuclear localization is diminished in the presence of... | null | null | null | null | null | FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, l... | Mus musculus (Mouse) |
O35867 | NEB1_RAT | MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKPDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAIIAKTRGKGRPSSPQKRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSGHESGQNNRHSPKKEKAGEAEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSESPGAITPGKAENSNYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSRPSSNKQATDTEEPEKSEAVPVPEVAQKGTSLASLPSEERQLSTEAEDVTAQPDTPDSTDKDS... | null | null | actin filament organization [GO:0007015]; calcium-mediated signaling [GO:0019722]; cellular response to toxic substance [GO:0097237]; excitatory postsynaptic potential [GO:0060079]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative r... | actin cytoskeleton [GO:0015629]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dendritic spine neck [GO:0044326]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; growth cone lamelli... | actin filament binding [GO:0051015]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein phosphatase 1 binding [GO:0008157]; protein-containing complex binding [GO:0044877]; transmembrane transporter binding [GO:... | PF00595;PF17817;PF07647; | 2.30.42.10;1.10.150.50; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse, synaptosome. | null | null | null | null | null | FUNCTION: Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. | Rattus norvegicus (Rat) |
O35874 | SATT_MOUSE | MEKSGETNGYLDGTQAEPAAGPRTPETAMGKSQRCASFFRRHALVLLTVSGVLVGAGMGAALRGLQLTRTQITYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASSLGRLGGIAVAYFGLTTLSASALAVALAFIIKPGAGAQTLQSSSLGLENSGPPPVSKETVDSFLDLLRNLFPSNLVVAAFTTSATDYTVVTHNTSSGNVTKEKIPVVTDVEGMNILGLVLFALVLGVALKKLGPEGEDLIRFFNSFNEATMVLVSWIMWYVPIGIMFLIGSKIVEMKDIVMLVTSLGKYIFASMLGHVIHGGIVLPLVYFAF... | null | null | cognition [GO:0050890]; L-alanine import across plasma membrane [GO:1904273]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamate transmembrane transport [GO:0015813]; L-serine import across plasma membrane [GO:1903812]; L-serine transport [GO:0015825]; proline transport [GO:0015824]; serine import acro... | centrosome [GO:0005813]; dendrite [GO:0030425]; intermediate filament [GO:0005882]; melanosome [GO:0042470]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; L-alanine transmembrane transporter activity [GO:0015180]; L-aspartate transmembrane transporter activity [GO:0015183]; L-cystine transmembrane transporter activity [GO:0015184]; L-hydroxyproline transmembrane transporter activity [GO:0034590]; L-proline transmembrane transporter... | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A4 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43007}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P43007}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P43007}. | CATALYTIC ACTIVITY: Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out); Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926; Evidence={ECO:0000250|UniProtKB:P43007}; CATALYTIC ACTIVITY: Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEB... | null | null | null | null | FUNCTION: Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine. {ECO:0000250|UniProtKB:P43007}. | Mus musculus (Mouse) |
O35876 | SMN_RAT | MAMGSGGGAGSEQEDTVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDMCETSDKPKGTARRKPAKKNKNQKKNATAPLKQWKAGDKCSAVWSEDGCVYPATITSVDLKRETCVVVYTGYGNKEEQNLSDLLSPTCEVANNTEQNTQENESQVSTDDSEHSSRSLRSKAHSKSKAAPWTSFLPPPPPVPGAGLGPGKPGLRFSGPPPPPPPPPPFLPCWMPPFPSGPPIIPPPPPISPDCLDDTDALGSMLISWYMSGYHTGYYMGFRQNKKEGKKCSHTN | null | null | axonogenesis [GO:0007409]; chemical synaptic transmission [GO:0007268]; DNA-templated transcription termination [GO:0006353]; microtubule depolymerization [GO:0007019]; positive regulation of RNA splicing [GO:0033120]; regulation of neuron projection development [GO:0010975]; spliceosomal complex assembly [GO:0000245];... | Cajal body [GO:0015030]; COPI-coated vesicle [GO:0030137]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO... | fibroblast growth factor binding [GO:0017134]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF20636;PF06003;PF20635; | 2.30.30.140;3.40.190.10; | SMN family | null | SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250|UniProtKB:Q16637}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q16637}. Cytoplasm {ECO:0000250|UniProtKB:Q16637}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q16637}. Perikaryon {ECO:0000250|UniProtKB:Q16637}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q16637... | null | null | null | null | null | FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and S... | Rattus norvegicus (Rat) |
O35885 | ASCL2_MOUSE | MEAHLDWYGVPGLQEASDACPRESCSSALPEAREGANVHFPPHPVPREHFSCAAPELVAGAQGLNASLMDGGALPRLMPTSSGVAGACAARRRQASPELLRCSRRRRSGATEASSSSAAVARRNERERNRVKLVNLGFQALRQHVPHGGANKKLSKVETLRSAVEYIRALQRLLAEHDAVRAALAGGLLTPATPPSDECAQPSASPASASLSCASTSPSPDRLGCSEPTSPRSAYSSEESSCEGELSPMEQELLDFSSWLGGY | null | null | axon development [GO:0061564]; cell differentiation [GO:0030154]; chorionic trophoblast cell development [GO:0060719]; forebrain development [GO:0030900]; in utero embryonic development [GO:0001701]; negative regulation of Schwann cell proliferation [GO:0010626]; negative regulation of T-helper 1 cell differentiation [... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | bHLH transcription factor binding [GO:0043425]; 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]; DNA-binding transcription repressor activity,... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19360}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:10611232, PubMed:29500235). Binds to E-box motifs 5'-CANNTG-3' in the regulatory elements of target genes, probably as a heterodimer with another basic helix-loop-helix (bHLH) protein such as the transcription factor TCF3 (PubMed:10611232, PubMed:29500235). May bind both open and ... | Mus musculus (Mouse) |
O35889 | AFAD_RAT | MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPAKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKEERPSQGDDSENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAESLEKYGLEKENPKDYCIARVMLPPGAQHSDERGAKEIILD... | null | null | adherens junction maintenance [GO:0034334]; bicellular tight junction assembly [GO:0070830]; brain morphogenesis [GO:0048854]; cell-cell adhesion mediated by cadherin [GO:0044331]; cerebral cortex development [GO:0021987]; dendrite arborization [GO:0140059]; establishment of endothelial intestinal barrier [GO:0090557];... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical part of cell [GO:0045177]; axon [GO:0030424]; cell junction [GO:0030054]; cell-cell contact zone [GO:0044291]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; pore complex [GO:0046930]; somatodendritic compartmen... | actin filament binding [GO:0051015]; cell adhesion molecule binding [GO:0050839]; LIM domain binding [GO:0030274]; small GTPase binding [GO:0031267] | PF01843;PF00498;PF00595;PF00788; | 2.30.42.10;2.60.200.20; | null | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:9334353}. Note=Not found at cell-matrix AJs. {ECO:0000269|PubMed:9334353}. | null | null | null | null | null | FUNCTION: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (PubMed:9334353). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton... | Rattus norvegicus (Rat) |
O35893 | SP100_MUSCR | MEDSNASPRMSTEHENTEMHPFEYMFKHFKTQKVAISNAIRSTFPFLESLRDREFITGKMYEDLIDSCRSLVPVDKVIYKALDELEKKFDVTVLWELFNEVNMEKYPDLNPIRRSFECVFPNELSFQGIDRGNPNSQLSLEQGPSASYSQGSLNGSSLDLSSSEGWRSNDRRNSNLMQANQTENHQLAESPGHLDSCELQVQLNNGDATPESYSLLPQHEERAVQLNNEFQINPCFVQLIDVKKENSSFSLAGNQQTRARTNQNEDSEVIELSSGDSDDGENFSEATTTIPSQPAPAYSRTPPTLRTDRRGDTSDTESSI... | null | null | negative regulation of endothelial cell migration [GO:0010596]; negative regulation of protein export from nucleus [GO:0046826]; regulation of angiogenesis [GO:0045765]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of Fas signaling pathway [GO:1902044]; regulat... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PML body [GO:0016605] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981] | PF03172;PF01342; | 3.10.390.10; | null | PTM: Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Sumoylation may stabilize the interaction with CBX5 (By similarity). {ECO:0000250}.; PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23497}. Nucleus, PML body {ECO:0000250|UniProtKB:P23497}. Nucleus, nuclear body {ECO:0000250|UniProtKB:P23497}. Cytoplasm {ECO:0000250|UniProtKB:P23497}. Note=Accumulates in the cytoplasm upon FAS activation. {ECO:0000250|UniProtKB:P23497}. | null | null | null | null | null | FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may al... | Mus caroli (Ryukyu mouse) (Ricefield mouse) |
O35899 | SC6A4_CAVPO | METTALNSQKAPSVCKDREDCQENSILQKSGPTSAGGVESGQIFNGYSSVPSTGMGDDAEHSVPTATTTLVAEVHHGERETWGKKVDFLLSVIGYAVDLGNIWRFPYVCYQNGGGAFLLPYIIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYTICIIAFYIASYYNTIIAWALYYLISSFTDRLPWTSCRNSWNTANCTNYFSEDNITWTLHSTSPAEEFYIRHILQIHRSKGLQDVGGVSWQLTLCIMLIFTIIYFSIWKGVKTSGKVVWVTATFPYIVLSVLLVRGATLPGAWKGVLFYLKPNWQKL... | null | null | membrane depolarization [GO:0051899]; platelet aggregation [GO:0070527]; regulation of thalamus size [GO:0090067]; serotonin uptake [GO:0051610] | endomembrane system [GO:0012505]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synapse [GO:0045202] | actin filament binding [GO:0051015]; antiporter activity [GO:0015297]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; monoatomic cation channel activity [GO:0005261]; serotonin binding [GO:0051378]; serotonin:sodium:chloride symporter activity [GO:0005335]; sodium ion binding [GO:0031402] | PF03491;PF00209; | null | Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A4 subfamily | PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required for cGMP-mediated SERT regulation. {ECO:0000250|UniProtKB:P31645}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31645}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|... | CATALYTIC ACTIVITY: Reaction=H(+)(in) + K(+)(in) + Na(+)(out) + serotonin(out) = H(+)(out) + K(+)(out) + Na(+)(in) + serotonin(in); Xref=Rhea:RHEA:75839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:P31645, ECO:0000269|PubMed:8601815}; PhysiologicalDirecti... | null | null | null | null | FUNCTION: Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signal... | Cavia porcellus (Guinea pig) |
O35902 | DSG3_MOUSE | MTCLFPRALGSLALLMVVLLVQGELHVKPGGQHREDGTALQLAKRRYKREWVKFAKPCREREDNSRRNPIAKITSDFQKNQKITYRISGVGIDQPPFGIFVVDPNNGDINITAIVDREETPSFLITCRALNALGQDVERPLILTVKILDVNDNPPIFSQTIFKGEIEENSASNSLVMILNATDADEPNHMNSKIAFKIVSQEPAGMSMFLISRNTGEVRTLTSSLDREQISSYHLVVSGADNDGTGLSTQCECSIKIKDVNDNFPVLRESQYSARIEENTLNAELLRFQVTDWDEEYTDNWLAVYFFTSGNEGNWFEIET... | null | null | cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156] | desmosome [GO:0030057]; plasma membrane [GO:0005886]; spot adherens junction [GO:0005914] | calcium ion binding [GO:0005509] | PF00028; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. | Mus musculus (Mouse) |
O35903 | CCL25_MOUSE | MKLWLFACLVACFVGAWMPVVHAQGAFEDCCLGYQHRIKWNVLRHARNYHQQEVSGSCNLRAVRFYFRQKVVCGNPEDMNVKRAMRILTARKRLVHWKSASDSQTERKKSNHMKSKVENPNSTSVRSATLGHPRMVMMPRKTNN | null | null | cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]; G protein-coupled receptor signaling pathway [GO... | extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of be... | Mus musculus (Mouse) |
O35904 | PK3CD_MOUSE | MPPGVDCPMEFWTKEESQSVVVDFLLPTGVYLNFPVSRNANLSTIKQVLWHRAQYEPLFHMLSDPEAYVFTCVNQTAEQQELEDEQRRLCDIQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLRDPEVNDFRTKMRQFCEEAAAHRQQLGWVEWLQYSFPLQLEPSARGWRAGLLRVSNRALLVNVKFEGSEESFTFQVSTKDMPLALMACALRKKATVFRQPLVEQPEEYALQVNGRHEYLYGNYPLCHFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLE... | 2.7.1.137; 2.7.1.153 | null | adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell homeostasis [GO:0001782]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell surface receptor signaling pathway [GO:0007166]; chemotaxis [GO:0006935]; defense response to fungus [GO:0050832]; homeostasis of number of cells [... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF00454;PF00792;PF02192;PF00794;PF00613; | 3.10.20.770;2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | PTM: Autophosphorylation on Ser-1038 results in the almost complete inactivation of the lipid kinase activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.1... | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000305|PubMed:9235916}. | null | null | FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed... | Mus musculus (Mouse) |
O35906 | SPIB_MOUSE | MLALEAAQLDGPHLSCLYPEGVFYDLDSCKPFSYPDSDGGLDSTWGWTEAPPAPAIAPYEAFDPATAAFSHSQTVQLCYSHGPNPSTYSPMGTLDPAPSLEAPGPGLQVYPPEDFTSQTLGSLAYAPYPSPVLSEEEDIMLDSPALEVSDSESDEALLAGSEGRGSEAGARKKLRLYQFLLGLLLRGDMRECVWWVEPGAGVFQFSSKHKELLARRWGQQKGNRKRMTYQKLARALRNYAKTGEIRKVKRKLTYQFDSALLPASRHV | null | null | immature B cell differentiation [GO:0002327]; macrophage differentiation [GO:0030225]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565] | PF00178; | 1.10.10.10; | ETS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01892}. | null | null | null | null | null | FUNCTION: Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. ... | Mus musculus (Mouse) |
O35910 | MOT4_RAT | MGGAVVDEGPTGIKAPDGGWGWAVLFGCFIITGFSYAFPKAVSVFFKELMHEFGIGYSDTAWISSILLAMLYGTGPLCSMCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQIYLTTGVITGLGLALNFQPSLIMLNRYFNKRRPMANGLAAAGSPVFLCALSPLGQLLQDHYGWRGGFLILGGLLLNCCVCAALMRPLVAPQASGGAEPHGPQRPSPRLLDLSVFRDRGFLIYAVAASIMVLGLFVPPVFVVSYAKDMGVPDTKAAFLLTILGFIDIFARPTAGFITGLKKVRPYSVYLFSFAMFFNGFTDLTGSTAS... | null | null | lactate transmembrane transport [GO:0035873]; monocarboxylic acid transport [GO:0015718]; plasma membrane lactate transport [GO:0035879]; protein catabolic process [GO:0030163]; pyruvate catabolic process [GO:0042867]; pyruvate transmembrane transport [GO:1901475] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; synapse [GO:0045202] | lactate transmembrane transporter activity [GO:0015129]; lactate:proton symporter activity [GO:0015650]; pyruvate transmembrane transporter activity [GO:0050833] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15427}. Basolateral cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is dependent upon the BSG/MCT4 interaction. Basolateral s... | CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:10926847, ECO:0000269|PubMed:9632638}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29416; Evidence={ECO:0000305|PubMed:10926847}; CATA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.1 mM for (S)-lactate {ECO:0000269|PubMed:9632638}; KM=33.7 mM for (S)-lactate {ECO:0000269|PubMed:10926847}; | null | null | null | FUNCTION: Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (By similarity) (PubMed:10926847, PubMed:9632638). Plays a predominant role in the L-lactate efflux from highly glycolytic cells (PubMed:10926847, PubMed:9632638). {ECO:0000250|UniProtKB:O15427, ECO:0000269|PubMed:10926847, ECO:00... | Rattus norvegicus (Rat) |
O35913 | SO1A4_RAT | MGKSEKRVATHGVRCFAKIKMFLLALTCAYVSKSLSGTYMNSMLTQIERQFGIPTSIVGLINGSFEIGNLLLIIFVSYFGTKLHRPIMIGVGCAVMGLGCFLISLPHFLMGQYEYETILPTSNVSSNSFFCVENRSQTLNPTQDPSECVKEMKSLMWIYVLVGNIIRGIGETPIMPLGISYIEDFAKSENSPLYIGILETGMTIGPLIGLLLASSCANIYVDIESVNTDDLTITPTDTRWVGAWWIGFLVCAGVNILTSFPFFFFPKTLPKEGLQENVDGTENAKEKKHRKKAKEEKRGITKDFFVFMKSLSCNPIYMLF... | null | null | bile acid and bile salt transport [GO:0015721]; bile acid signaling pathway [GO:0038183]; cellular response to xenobiotic stimulus [GO:0071466]; monoatomic anion transport [GO:0006820]; regulation of bile acid secretion [GO:0120188]; response to estrogen [GO:0043627]; sodium-independent organic anion transport [GO:0043... | basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886] | bile acid transmembrane transporter activity [GO:0015125]; organic anion transmembrane transporter activity [GO:0008514]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; transmembrane transporter activity [GO:0022857] | PF07648;PF03137; | 1.20.1250.20; | Organo anion transporter (TC 2.A.60) family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000305|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:19129463}; CATALYTIC ACTI... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with estrone 3-sulfate, taurocholate, prostaglandin E2 and L-thyroxine (T4) as substrates. {ECO:0000269|PubMed:19129463}; | null | FUNCTION: Mediates the Na(+)-independent transport of organic anions such as taurocholate, cholate, 17-beta-glucuronosyl estradiol, prostaglandin E2, estrone 3-sulfate, L-thyroxine (T4), the cardiac glycosides ouabain and digoxin and thyroid hormones (PubMed:19129463). May play an especially important role in the brain... | Rattus norvegicus (Rat) |
O35914 | BNC1_MOUSE | MAEAIGCTLNCSCQCFKPGKINHRQCEQCRHGWVAHALSKLRIPPVYPTSQVEIVQSNVVFDISSLMLYGTQAIPVRLKILLDRLFSVLKQDEVLQILHALDWTLQDYIRGYVLQDASGKVLDHWSIMTSEEEVATLQQFLRFGETKSIVELMAIQEKEEQSVIVPPTTANVDIRAFIESCGHRSASLPTPVDKGSPGGMHPFENLISNMTFMLPFQFFNPLPPALIGSLPEQYMLEQGQDQSQEPKQELHGPFSDSSFLTSTPFQVEKEQCLNCPETVPQKEDSAHLSDSSSYSIASKLERTQLSPEAKVKPERNSLSA... | null | null | cell differentiation [GO:0030154]; chromosome organization [GO:0051276]; epithelial cell proliferation [GO:0050673]; positive regulation of epithelial cell proliferation [GO:0050679]; regulation of transcription by RNA polymerase I [GO:0006356]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogen... | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF00096;PF12874; | 3.30.160.60; | null | PTM: Phosphorylation on Ser-505 and Ser-509 leads to cytoplasmic localization. {ECO:0000250|UniProtKB:Q01954}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}. Cytoplasm {ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23707421}. Note=Relocates to the midpiece of the flagellum during late spermiogenesis in spermatids. {ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Transcriptional activator (PubMed:23707421, PubMed:9687312). It is likely involved in the regulation of keratinocytes terminal differentiation in squamous epithelia and hair follicles (By similarity). Required for the maintenance of spermatogenesis (PubMed:22266914). It is involved in the positive regulation ... | Mus musculus (Mouse) |
O35921 | EAA4_RAT | MSSHGNSLFLRESGAGGGCLQGLQDSLQQRALRTRLRLQTMTREHVRRFLRRNAFILLTVSAVIIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSRVTGMASLDNKATGRMGMRAAVYYMVTTVIAVFIGILMVTIIHPGKGSKEGLHREGRIETVPTADAFMDLVRNMFPPNLVEACFKQFKTQYSTRVVTRTIVRTDNGSELGASISPPSSAENETSILENVTRALGTLQEVISFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIA... | null | null | establishment of localization in cell [GO:0051649]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamate import across plasma membrane [GO:0098712]; L-glutamate transmembrane transport [GO:0015813]; neurotransmitter uptake [GO:0001504]; regulation of membrane potential [GO:0042391] | glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; membrane protein complex [GO:0098796]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] | glutamate:sodium symporter activity [GO:0015501]; high-affinity L-glutamate transmembrane transporter activity [GO:0005314]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]; metal ion binding [GO:0046872]; monoatomic anion transmembrane transporte... | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A6 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26690923}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:P48664}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=328 uM for L-glutamate {ECO:0000269|PubMed:26690923}; | null | null | null | FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:14506254, PubMed:26690923). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the co... | Rattus norvegicus (Rat) |
O35923 | BRCA2_RAT | MTVEYKRRPTFWEIFKARCSTADLGPISLNWFEELFSEAPPYNTEHPEESEYKPQGHEPQLFKTPQRNPSYHQFASTPIMFKEQSQTLPLDQSPFKELGNVVANSKRKHHSKKKARKDPVVDVASLPLKACPSESPCTPRCTQVAPQRRKPVVSGSLFYTPKLEETPKHISESLGVEVDPDMSWTSSLATPPTLSSTVLIARDEEAHRNAFPADSPASLKSYFSNHNESLKKNDRFIPSVSDSENKSQQEAFSQGLEKMLGDSSSKINRFRDCLRKPIPNVLEDGETAVDTSGEDSFSLCFPKRRTRNLQKTRMGKMKKK... | null | null | brain development [GO:0007420]; cell population proliferation [GO:0008283]; cellular response to ionizing radiation [GO:0071479]; cellular senescence [GO:0090398]; centrosome duplication [GO:0051298]; chordate embryonic development [GO:0043009]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; DN... | BRCA2-MAGE-D1 complex [GO:0033593]; centrosome [GO:0005813]; chromosome [GO:0005694]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; DNA repair complex [GO:1990391]; lateral element [GO:0000800]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]; protein-containing complex [GO:0032... | gamma-tubulin binding [GO:0043015]; histone H3 acetyltransferase activity [GO:0010484]; histone H4 acetyltransferase activity [GO:0010485]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; single-stranded DNA binding [GO:0003697] | PF09169;PF09103;PF09104;PF00634;PF21318;PF09121; | 6.10.70.10;2.40.50.140; | null | PTM: Phosphorylated by ATM upon irradiation-induced DNA damage. Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous reco... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51587}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51587}. | null | null | null | null | null | FUNCTION: Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from... | Rattus norvegicus (Rat) |
O35926 | CD5R2_MOUSE | MGTVLSLSPASSAKGRRPGGLPEEKKKAPPAGDEALGGYGAPPAGKGGKGESRLKRPSVLISALTWKRLVAASAKKKKGSKKVTPKPASTGPDPLVQQRNRENLLRKGRDGPDGGGTAKPLAVPVPTVPTTAATCEPPSGGSAAAPPPGSGGGKPPPPPPPAPQAAPPAPGGSPRRVIVQASTGELLRCLGDFVCRRCYRLKELSPGELVGWFRGVDRSLLLQGWQDQAFITPANLVFVYLLCRESLRGDELASAAELQAAFLTCLYLAYSYMGNEISYPLKPFLVEPDKERFWQRCLRLIQRLSPQMLRLNADPHFFTQ... | null | null | axon guidance [GO:0007411]; brain development [GO:0007420]; cerebellum development [GO:0021549]; hippocampus development [GO:0021766]; layer formation in cerebral cortex [GO:0021819]; neuron migration [GO:0001764]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; superior olivary nucleus maturation... | cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; protein kinase 5 complex [GO:0016533] | actin binding [GO:0003779]; cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cytoskeletal protein binding [GO:0008092]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901] | PF03261; | 1.10.472.10; | Cyclin-dependent kinase 5 activator family | PTM: Myristoylated. The Gly-2-Ala mutant is absent of the cell periphery, suggesting that a proper myristoylation signal is essential for the proper distribution of CDK5R2 (p39) (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: Activator of CDK5/TPKII. | Mus musculus (Mouse) |
O35927 | CTND2_MOUSE | MFARKQSGAAPFGAMPVPDQPPSASEKNSSLSPGLNTSNGDGSETETTSAILASVKEQELQFERLTRELEAERQIVASQLERCKLGSETGSMSSISSAGEQFHWQTQDGQKDIEDELTTGLELVDSCIRSLQESGILDPQDYSTSERPSLLSQSALQLNSKPEGSFQYPASYHSNQTLALGDTAPSQLPARSTQARAAGQSFSQGTTGRAGHLAGSEPAPPPPPPREPFAPSLGSAFHLPDAPPAAAALYYSSSTLPAPPRGGSPLTTTQGGSPTKLQRGGSAPEGAAYAAPRGSSPKQSPSRLAKSYSTSSPINIVVSS... | null | null | cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; dendritic spine morphogenesis [GO:0060997]; learning [GO:0007612]; morphogenesis of a branching structure [GO:0001763]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; regulation of synaptic plasticity [GO:0048... | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | cadherin binding [GO:0045296]; structural constituent of postsynaptic density [GO:0098919] | PF00514; | 1.25.10.10; | Beta-catenin family | PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.; PTM: Phosphorylated by CDK5 (By similarity). Phosphorylated by GSK3B (PubMed:19706605). {ECO:0000250|UniProtKB:O35116, ECO:0000269|PubMed:19706605}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15282317}. Cell junction, adherens junction {ECO:0000269|PubMed:10753311}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon {ECO:0000250|UniProtKB:O35116}. | null | null | null | null | null | FUNCTION: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses (PubMed:17993462, PubMed:25807484). Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interac... | Mus musculus (Mouse) |
O35929 | REM1_MOUSE | MTLNTQQEAKTTLRRRASTPLPLSSRGHQPGRLCTAPSAPSQHPRLGQSVSLNPPVRKPSPAQDGWSSESSDSEGSWEALYRVVLLGDPGVGKTSLASLFAEKQDRDPHEQLGGVYERTLSVDGEDTTLVVMDTWEAEKLDESWCQESCLQAGSAYVIVYSIADRSSFESASELRIQLRRTHQANHVPIILVGNKADLARCREVSVEEGRACAVVFDCKFIETSATLQHNVTELFEGVVRQLRLRRQDNAAPETPSPRRRASLGQRARRFLARLTARSARRRALKARSKSCHNLAVL | null | null | negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; regulation of skeletal muscle contraction by calcium ion signaling [GO:0014722] | I band [GO:0031674]; plasma membrane [GO:0005886]; T-tubule [GO:0030315] | calcium channel regulator activity [GO:0005246]; calmodulin binding [GO:0005516]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; transmembrane transporter binding [GO:0044325] | PF00071; | 3.40.50.300; | Small GTPase superfamily, RGK family | null | null | null | null | null | null | null | FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal reorganization (By similarity). May be involved in angiogenesis. May function in Ca(2+) signaling. {ECO:0000250}. | Mus musculus (Mouse) |
O35930 | GP1BA_MOUSE | MALLILLFLLPSPLHSQHTCSISKVTSLLEVNCENKKLTALPADLPADTGILHLGENQLGTFSTASLVHFTHLTYLYLDRCELTSLQTNGKLIKLENLDLSHNNLKSLPSLGWALPALTTLDVSFNKLGSLSPGVLDGLSQLQELYLQNNDLKSLPPGLLLPTTKLKKLNLANNKLRELPSGLLDGLEDLDTLYLQRNWLRTIPKGFFGTLLLPFVFLHANSWYCDCEILYFRHWLQENANNVYLWKQGVDVKDTTPNVASVRCANLDNAPVYSYPGKGCPTSSGDTDYDDYDDIPDVPATRTEVKFSTNTKVHTTHWSL... | null | null | blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; fibrinolysis [GO:0042730]; hemostasis [GO:0007599]; megakaryocyte development [GO:0035855]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulat... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glycoprotein Ib-IX-V complex [GO:1990779]; membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF13855; | 3.80.10.10; | null | PTM: O-glycosylated. {ECO:0000250}.; PTM: Glycocalicin is the product of a proteolytic cleavage/shedding, catalyzed by ADAM17, which releases most of the extracellular domain. Binding sites for vWF and thrombin are in this part of the protein. {ECO:0000269|PubMed:12907434}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. {ECO:0000250}. | Mus musculus (Mouse) |
O35936 | ALOX8_MOUSE | MAKCRVRVSTGEACGAGTWDKVSVSIVGTHGESPLVPLDHLGKEFSAGAEEDFEVTLPQDVGTVLMLRVHKAPPEVSLPLMSFRSDAWFCRWFELEWLPGAALHFPCYQWLEGAGELVLREGAAKVSWQDHHPTLQDQRQKELESRQKMYSWKTYIEGWPRCLDHETVKDLDLNIKYSAMKNAKLFFKAHSAYTELKVKGLLDRTGLWRSLREMRRLFNFRKTPAAEYVFAHWQEDAFFASQFLNGINPVLIRRCHSLPNNFPVTDEMVAPVLGPGTSLQAELEKGSLFLVDHGILSGVHTNILNGKPQFSAAPMTLLHQ... | 1.13.11.-; 1.13.11.58 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O15296, ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:O15296, ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; cannabinoid biosynthetic process [GO:1901696]; endocannabinoid signaling pathway [GO:0071926]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxin A4 biosynthetic process [GO:2001303]; lipoxygen... | adherens junction [GO:0005912]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886] | arachidonate 15-lipoxygenase activity [GO:0050473]; arachidonate 8(S)-lipoxygenase activity [GO:0036403]; calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; linoleate 9S-lipoxygenase activity [GO:1990136]; lipid binding [GO:0008289] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15296}. Membrane {ECO:0000250|UniProtKB:O15296}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15296}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. {ECO:0000250|UniProtKB:O15296}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; Evidence={ECO:0000269|PubMed:15558016, ECO:0000269|PubMed:9305900, ECO:0000305|PubMed:27435673}; PhysiologicalDirection... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for arachidonate (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=2.1 uM for (8S)-HPETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=5.7 uM for (8S)-HETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:9305900}. | null | null | FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:10625675, PubMed:10965849, PubMed:15558016, PubMed:16112079, PubMed:16143298, PubMed:27435673, PubMed:9305900). Cat... | Mus musculus (Mouse) |
O35942 | NEK2_MOUSE | MPSRVEDYEVLHSIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEVEKQMLVSEVNLLRELKHPNIVSYYDRIIDRTNTTLYIVMEYCEGGDLASVISKGTKDRQYLEEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDSKHNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMSCLSYNEKSDIWSLGCLLYELCALMPPFTAFNQKELAGKIREGRFRRIPYRYSDGLNDLITRMLNLKDYHRPSVEEILESPLIADLVAEEQRRNLERRGRRSGEPSKLPDSSPVLSELKLKERQLQDREQAL... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | blastocyst development [GO:0001824]; cell division [GO:0051301]; centrosome separation [GO:0051299]; chromosome segregation [GO:0007059]; meiotic cell cycle [GO:0051321]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly [GO:0090307]; negative regulation of centriole-centriole cohesion [GO:190... | centrosome [GO:0005813]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein phosphatase binding [GO:0019903]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | PTM: Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome. {ECO:0000250|UniProtKB:P51955}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9187143}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P51955}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51955}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome, centromere, kinetoch... | 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: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating cent... | Mus musculus (Mouse) |
O35943 | FRDA_MOUSE | MWAFGGRAAVGLLPRTASRASAWVGNPRWREPIVTCGRRGLHVTVNAGATRHAHLNLHYLQILNIKKQSVCVVHLRNLGTLDNPSSLDETAYERLAEETLDSLAEFFEDLADKPYTLEDYDVSFGDGVLTIKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLARELTKALNTKLDLSSLAYSGKGT | 1.16.3.1 | null | [2Fe-2S] cluster assembly [GO:0044571]; [4Fe-4S] cluster assembly [GO:0044572]; adult walking behavior [GO:0007628]; aerobic respiration [GO:0009060]; cellular response to hydrogen peroxide [GO:0070301]; embryo development ending in birth or egg hatching [GO:0009792]; heme biosynthetic process [GO:0006783]; intracellul... | iron-sulfur cluster assembly complex [GO:1990229]; L-cysteine desulfurase complex [GO:1990221]; mitochondrial iron-sulfur cluster assembly complex [GO:0099128]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; iron chaperone activity [GO:0034986] | PF01491; | 3.30.920.10; | Frataxin family | PTM: [Frataxin mature form]: Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (frataxin(81-210)) which is the predominant form. The additional forms, frataxin(56-210) and frat... | SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion {ECO:0000269|PubMed:17597094, ECO:0000269|PubMed:9241270}.; SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}. | CATALYTIC ACTIVITY: [Frataxin mature form]: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:Q16595}; | null | null | null | null | FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly (PubMed:19805308, PubMed:25597503). Accelerates sulfur transfer from NFS1 persulfide int... | Mus musculus (Mouse) |
O35945 | AL1A7_MOUSE | MSSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFV... | 1.2.1.3 | null | ethanol catabolic process [GO:0006068]; fructose catabolic process [GO:0006001] | cytoplasm [GO:0005737] | 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; identical protein binding [GO:0042802] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13601}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. | null | null | FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde (By similarity). No detectable activity with retinal. {ECO:0000250, ECO:0000269|PubMed:10191271}. | Mus musculus (Mouse) |
O35949 | ELOV3_MOUSE | MDTSMNFSRGLKMDLMQPYDFETFQDLRPFLEEYWVSSFLIVVVYLLLIVVGQTYMRTRKSFSLQRPLILWSFFLAIFSILGTLRMWKFMATVMFTVGLKQTVCFAIYTDDAVVRFWSFLFLLSKVVELGDTAFIILRKRPLIFVHWYHHSTVLLFTSFGYKNKVPSGGWFMTMNFGVHSVMYTYYTMKAAKLKHPNLLPMVITSLQILQMVLGTIFGILNYIWRQEKGCHTTTEHFFWSFMLYGTYFILFAHFFHRAYLRPKGKVASKSQ | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cold-induced thermogenesis [GO:0120162]; sphingoli... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL3 subfamily | PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03203}; Ph... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03203}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that... | Mus musculus (Mouse) |
O35952 | GLO2_RAT | MVLGRGSLCLRSLSVLGAACARRGLGQALLGLSLCHTDFRKNLTVQQDMMKIELLPALTDNYMYLIIDEDTQEAAVVDPVQPQKVIETVKKHRVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGDDRIGALTHKVTHLSTLEVGSLSVKCLSTPCHTSGHICYFVSKPGSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGRLPPDTKVICGHEYTVNNLKFARHVEPGNTAVQEKLAWAKEKNAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKDQFKVPRD | 3.1.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q16775}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775}; | glutathione biosynthetic process [GO:0006750]; glutathione metabolic process [GO:0006749]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; spermatogenesis [GO:0007283] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | hydroxyacylglutathione hydrolase activity [GO:0004416]; metal ion binding [GO:0046872] | PF16123;PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Glyoxalase II family | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16775}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q16775}. | CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6; Evidence={ECO:0000269|PubMed:8719777}; PhysiologicalDirection=left-to-right;... | null | PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. | null | null | FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. {ECO:0000269|PubMed:8719777}. | Rattus norvegicus (Rat) |
O35954 | PITM1_MOUSE | MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGNGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRIVDTIDIVRDAVAPGEYKAEEDPRLYRSAKTGRGPLADDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWIELSMADIRALEEETARMLAQRMAKCNTGSEGPEAQTPGKSSTEARPGTSTAGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQ... | null | null | protein transport [GO:0015031] | cell body [GO:0044297]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; lipid droplet [GO:0005811]; midbody [GO:0030496] | calcium ion binding [GO:0005509]; phosphatidic acid binding [GO:0070300]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine transporter activity [GO:0008525]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol transfer activity [GO:0008526]; phospholipid binding [GO:0005543]; receptor tyrosine ... | PF02862;PF02121; | 3.30.530.20;3.40.50.1000; | PtdIns transfer protein family, PI transfer class IIA subfamily | PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid. {ECO:0000250}.; PTM: Phosphorylated ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00562}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Lip... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; Evidence={ECO:0000250|UniProtKB:O00562}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; Evidence={ECO:0000250|UniProtKB:O... | null | null | null | null | FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between membranes (By similarity). Binds PI (PubMed:10400687). Also binds phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (By similarity). Regulates RHOA activity, and plays a role in cytoskeleton remodelin... | Mus musculus (Mouse) |
O35955 | PSB10_MOUSE | MLKQAVEPTGGFSFENCQRNASLEHVLPGLRVPHARKTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAITAGILSDLGSGGNVDACVITAGGAKLQRALSTPTEPVQRAGRYRFAPGTTPVLTREVRPLTLELLEETVQAMEVE | 3.4.25.1 | null | cell morphogenesis [GO:0000902]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; T cell proliferation [GO:0042098] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774]; spermatoproteasome complex [GO:1990111] | endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298] | PF12465;PF00227; | 3.60.20.10; | Peptidase T1B family | PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000305|PubMed:10413086}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; | null | null | null | null | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... | Mus musculus (Mouse) |
O35956 | S22A6_RAT | MAFNDLLKQVGGVGRFQLIQVTMVVAPLLLMASHNTLQNFTAAIPPHHCRPPANANLSKDGGLEAWLPLDKQGQPESCLRFTSPQWGPPFYNGTEANGTRVTEPCIDGWVYDNSTFPSTIVTEWNLVCSHRAFRQLAQSLYMVGVLLGAMVFGYLADRLGRRKVLILNYLQTAVSGTCAAYAPNYTVYCVFRLLSGMSLASIAINCMTLNVEWMPIHTRAYVGTLIGYVYSLGQFLLAGIAYAVPHWRHLQLVVSVPFFIAFIYSWFFIESARWYSSSGRLDLTLRALQRVARINGKQEEGAKLSIEVLRTSLQKELTLS... | null | null | alpha-ketoglutarate transport [GO:0015742]; metanephric proximal tubule development [GO:0072237]; monoatomic anion transport [GO:0006820]; organic anion transport [GO:0015711]; prostaglandin transport [GO:0015732]; renal tubular secretion [GO:0097254]; response to organic cyclic compound [GO:0014070]; sodium-independen... | basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | alpha-ketoglutarate transmembrane transporter activity [GO:0015139]; antiporter activity [GO:0015297]; chloride ion binding [GO:0031404]; identical protein binding [GO:0042802]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; sodium-independe... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Glycosylated. Glycosylation is necessary for proper targeting of the transporter to the plasma membrane. {ECO:0000250|UniProtKB:Q4U2R8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VC69}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VC69}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:000030... | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(out) + a dicarboxylate(in) = (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76071, ChEBI:CHEBI:28965, ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:Q4U2R8}; CATALYTIC ACTIVITY: Reaction=a dicarboxylate(in... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27.5 uM for hippurate/N-benzoylglycine {ECO:0000269|PubMed:14675047}; KM=47.1 uM for indole acetate {ECO:0000269|PubMed:14675047}; KM=17.7 uM for indoxyl sulfate {ECO:0000269|PubMed:14675047}; KM=154 uM for 3-carboxy-4- methyl-5-propyl-2-furanpropionate {ECO:000026... | null | null | null | FUNCTION: Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as alpha-ketoglutarate or glutarate (PubMed:14675047, PubMed:2383237... | Rattus norvegicus (Rat) |
O35963 | RB33B_MOUSE | MTSEMESSLEVSFSSSCAVSGASGCLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVDIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPAWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQLPDNRISLKPETKPAVTCWC | null | null | autophagosome assembly [GO:0000045]; intra-Golgi vesicle-mediated transport [GO:0006891]; negative regulation of constitutive secretory pathway [GO:1903434]; protein localization to Golgi apparatus [GO:0034067]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0... | endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; presynapse [GO:0098793] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:9512502}; Lipid-anchor {ECO:0000305}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18448665}. Note=Under starvation conditions punctate RAB33B-positive structures are often observed in the cytoplasm (PubMed:1844866... | null | null | null | null | null | FUNCTION: Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). It is involved in autophagy, acting as a modulator of autophagosome formation. {ECO:0000250, ECO:0000269|PubMed:18448665}. | Mus musculus (Mouse) |
O35964 | SH3G1_RAT | MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFREMEKKVDITSKAVAEVLVRTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMVRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILEELADKLKRRVREASSRPRREFKPRPQEPFELGELEQPNGGFPCASAPKITASSSFRSGDKPTRTPSKSMPPLDQPSCKALYDFEPE... | null | null | modulation of excitatory postsynaptic potential [GO:0098815]; positive regulation of synaptic vesicle endocytosis [GO:1900244]; regulation of synaptic vesicle endocytosis [GO:1900242]; synaptic vesicle uncoating [GO:0016191] | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; podosome [GO:0002102]; postsynaptic density, intracellular component [GO:0099092]; presynapse [GO:0098793]... | beta-1 adrenergic receptor binding [GO:0031697]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phosphatase binding [GO:0019902]; SH3 domain binding [GO:0017124]; transmembrane transporter binding [GO:0044325] | PF03114;PF00018; | 1.20.1270.60;2.30.30.40; | Endophilin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088211}. Early endosome membrane {ECO:0000269|PubMed:17088211}; Peripheral membrane protein {ECO:0000269|PubMed:17088211}. Cell projection, podosome {ECO:0000250}. Note=Associated with postsynaptic endosomes in hippocampal neurons. | null | null | null | null | null | FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
O35969 | GAMT_MOUSE | MSSSAASPLFAPGEDCGPAWRAAPAAYDASDTHLQILGKPVMERWETPYMHALAAAAASRGGRVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQDWALRQPHKVVPLKGLWEEVAPTLPDGHFDGILYDTYPLSEEAWHTHQFNFIKNHAFRLLKTGGVLTYCNLTSWGELMKSKYTDITTMFEETQVPALQEAGFLKENICTEVMALVPPADCRYYAFPQMITPLVTKH | 2.1.1.2 | null | animal organ morphogenesis [GO:0009887]; creatine biosynthetic process [GO:0006601]; methylation [GO:0032259]; regulation of multicellular organism growth [GO:0040014]; S-adenosylhomocysteine metabolic process [GO:0046498]; S-adenosylmethionine metabolic process [GO:0046500]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; microvillus [GO:0005902]; nucleus [GO:0005634] | guanidinoacetate N-methyltransferase activity [GO:0030731]; identical protein binding [GO:0042802]; protein arginine N5-methyltransferase activity [GO:0019702]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | null | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, RMT2 methyltransferase family | null | SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000269|PubMed:8312439}. Note=Detected in microvilli of the epithelial cells lining the caput epididymis. | CATALYTIC ACTIVITY: Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947, ChEBI:CHEBI:59789; EC=2.1.1.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00892}; | null | PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis; creatine from L-arginine and glycine: step 2/2. | null | null | FUNCTION: Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development. {ECO:0000250|UniProtKB:Q14353}. | Mus musculus (Mouse) |
O35973 | PER1_MOUSE | MSGPLEGADGGGDPRPGEPFCPGGVPSPGAPQHRPCPGPSLADDTDANSNGSSGNESNGPESRGASQRSSHSSSSGNGKDSALLETTESSKSTNSQSPSPPSSSIAYSLLSASSEQDNPSTSGCSSEQSARARTQKELMTALRELKLRLPPERRGKGRSGTLATLQYALACVKQVQANQEYYQQWSLEEGEPCAMDMSTYTLEELEHITSEYTLRNQDTFSVAVSFLTGRIVYISEQAGVLLRCKRDVFRGARFSELLAPQDVGVFYGSTTPSRLPTWGTGTSAGSGLKDFTQEKSVFCRIRGGPDRDPGPRYQPFRLTP... | null | null | chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regu... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; kinase binding [GO:0019900]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor binding [GO:0001222]; ubiquitin protein ligase binding [GO:0031625] | PF08447;PF21353;PF12114; | 3.30.450.20; | null | PTM: Phosphorylated on serine residues by CSNK1D, CSNK1E and probably also by CSNK1G2. Phosphorylation by CSNK1D or CSNK1E promotes nuclear location of PER proteins as well as ubiquitination and subsequent degradation. May be dephosphorylated by PP1. {ECO:0000269|PubMed:11865049}.; PTM: Ubiquitinated; requires phosphor... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation. Translocate to the nucleus after phosphorylation by CSNK1D or ... | null | null | null | null | null | FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a... | Mus musculus (Mouse) |
O35975 | NAR2B_MOUSE | MTSKIFKFFLTWWLTQQVTGLAVPFMLDMAPNAFDDQYESCVEDMEKKAPQLLQEDFNMNEELKLEWEKAEINWKEIKNSTSYPAGFHDFHGTALVAYTGNLAIDFNRAVRDFKKSPDNFHYKAFHYYLTRAVQLLNDQGCSLVYRGTKVMFEYTGKGSVRFGQFSSSSLTKRVALSSNFFSNHGTLFIIRTCLGVNIKEFSSFPREEEVLIPGYEVYHKVTAQNDNGYNEIFLDSPERKKSNFNCFYNGSAQTVNIDFSISGSRESCVSLFLVVLLGLLVQQLTLAEL | 2.4.2.31; 3.2.2.5 | null | NAD catabolic process [GO:0019677] | external side of plasma membrane [GO:0009897]; extrinsic component of plasma membrane [GO:0019897]; membrane [GO:0016020] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; nucleotidyltransferase activity [GO:001... | PF01129; | null | Arg-specific ADP-ribosyltransferase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:000... | null | null | null | null | FUNCTION: Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity. {ECO:0000269|PubMed:17928361, ECO:0000269|PubMed:9300695}. | Mus musculus (Mouse) |
O35980 | NTH_MOUSE | MNSGVRMVTRSRSRATRIASEGCREELAPREAAAEGRKSHRPVRHPRRTQKTHVAYEAANGEEGEDAEPLKVPVWEPQNWQQQLANIRIMRSKKDAPVDQLGAEHCYDASASPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVESILQTDDDTLGRLIYPVGFWRNKVKYIKQTTAILQQRYEGDIPASVAELVALPGVGPKMAHLAMAVAWGTISGIAVDTHVHRIANRLRWTKKMTKTPEETRKNLEEWLPRVLWSEVNGLLVGFGQQICLPVHPRCQACLNKALCPAAQDL | 3.2.2.-; 4.2.99.18 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03183}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000255|HAMAP-Rule:MF_03183}; | base-excision repair, AP site formation [GO:0006285]; DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA binding [GO:0003690]; meta... | PF00633;PF00730; | 1.10.1670.10; | Nth/MutY family | PTM: Ubiquitinated by TRIM26; leading to proteasomal degradation. {ECO:0000250|UniProtKB:P78549}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:12531031}. | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH... | null | null | null | null | FUNCTION: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glyco... | Mus musculus (Mouse) |
O35984 | PBX2_MOUSE | MDERLLGPPPPGGGRGGLGLVGAEPGGPGEPPGGGDPGGGSGGVPGGRGKQDIGDILQQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRSSQEEEPVDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGGVSPDNSIEHSDYRSKLAQIRHIYHSELEKYEQACNEFTTHVMNLLREQSRTRPVAPKEMERMVSIIHRKFSAIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEVLNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAVKT... | null | null | animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; embryonic limb morphogenesis [GO:0030326]; embryonic organ development [GO:0048568]; eye development [GO:0001654]; neuron development [GO:0048666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern for... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; RNA polymerase II cis-regulatory region sequence-specific DNA ... | PF05920;PF03792; | 1.10.10.60; | TALE/PBX homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1 (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O35987 | NSF1C_RAT | MAEERQDALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISD... | null | null | autophagosome assembly [GO:0000045]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; negative regulation of protein localization to centrosome [GO:1904780]; nuclear membrane reassembly [GO:0031468]; positive regulation of mitotic centrosome separ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi stack [GO:0005795]; nucleus [GO:0005634]; spindle pole centrosome [GO:0031616]; VCP-NSFL1C complex [GO:1990730] | ATPase binding [GO:0051117]; lipid binding [GO:0008289]; ubiquitin binding [GO:0043130] | PF08059;PF14555;PF00789; | 1.10.8.10;3.30.420.210; | NSFL1C family | PTM: Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis. {ECO:0000269|PubMed:12810701}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12810701}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:12810701, ECO:0000269|PubMed:9214505}. Chromosome {ECO:0000269|PubMed:1495983}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23649807}. Note=Predominantly nuclear in in... | null | null | null | null | null | FUNCTION: Reduces the ATPase activity of VCP (PubMed:9214505, PubMed:9824302). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (PubMed:12411482). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (PubMed:109... | Rattus norvegicus (Rat) |
O35988 | SDC4_MOUSE | MAPACLLAPLLLLLLGGFPLVPGESIRETEVIDPQDLLEGRYFSGALPDDEDAGGSDDFELSGSGDLDDTEEPRPFPEVIEPLVPLDNHIPENAQPGIRVPSEPKELEENEVIPKRAPSDVGDDMSNKVSMSSTAQGSNIFERTEVLAALIVGGVVGILFAVFLILLLVYRMKKKDEGSYDLGKKPIYKKAPTNEFYA | null | null | cell migration [GO:0016477]; inner ear receptor cell stereocilium organization [GO:0060122]; negative regulation of T cell proliferation [GO:0042130]; neural tube closure [GO:0001843]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; positive re... | cell surface [GO:0009986]; costamere [GO:0043034]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; Golgi lumen [GO:0005796]; membrane [GO:0016020] | fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; protein kinase C binding [GO:0005080]; thrombospondin receptor activity [GO:0070053] | PF01034; | null | Syndecan proteoglycan family | PTM: Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3. {ECO:0000269|PubMed:10684261}.; PTM: O-glycosylated; contains both chondroitin sulfate and heparan sulfate. Ser-44, Ser-62 and Ser-64 can all be modified b... | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:10684261}. | null | null | null | null | null | FUNCTION: Cell surface proteoglycan which regulates exosome biogenesis in concert with SDCBP and PDCD6IP. {ECO:0000250|UniProtKB:P31431}. | Mus musculus (Mouse) |
O36006 | P53_MARMO | MEEAQSDLSIEPPLSQETFSDLWNLLPENNVLSPVLSPPMDDLLLSSEDVENWFDKGPDEALQMSAAPAPKAPTPAASTLAAPSPATSWPLSSSVPSQNTYPGVYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPYEPPEVGSECTTIHYNYMCNSSCMGGMNRRPILTIITLEGSSGNLLGRNSFEVRVCACPGRDRRTEEENFRKRGEPCPEPPPRSTKRALPNGTSSSPQPKKKP... | 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}. Note=Interaction with BANP promotes nuclear localization. R... | 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... | Marmota monax (Woodchuck) |
O36015 | TRM7_SCHPO | MGRSSKDKRDAYYRLAKEQGWRARSAFKLLQLNEQFNLFEGAKRVVDLCAAPGSWSQVLSRELLKNIDTSIAADEKPMIVAVDLQPMAPIDGVCTLQLDITHPNTLSIILSHFGNEPADLVVSDGAPDVTGLHDLDEYIQAQILLAAFNLAVCVLKPGGKFVAKIFRGRDVSLLYSQLRLMFRKVSCAKPRSSRASSIESFVVCEDFNPPSNFQPDLTKPLCVIDPTNAHEIAPFIACGDLDGYDADATYPVEINMKKATLDVIQPPTAPPYKRAIELKHSKMMS | 2.1.1.205 | null | cytoplasmic translation [GO:0002181]; tRNA methylation [GO:0030488]; wobble position ribose methylation [GO:0002130] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | S-adenosyl-L-methionine binding [GO:1904047]; tRNA (cytidine(32)-2'-O)-methyltransferase activity [GO:0106339]; tRNA (guanine(34)-2'-O)-methyltransferase activity [GO:0106340]; tRNA (guanine) methyltransferase activity [GO:0016423]; tRNA 2'-O-methyltransferase activity [GO:0106050]; tRNA methyltransferase activity [GO:... | PF01728; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, RNA methyltransferase RlmE family, TRM7 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}. | CATALYTIC ACTIVITY: Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:... | null | null | null | null | FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs (PubMed:25404562). Requires trm732 for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs (PubMed:25404562). Requires trm734 for methylation of the nucleotide at posi... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O36019 | ATG13_SCHPO | MPRLNTQLPRMYSAPPGHSKAVSTELNKDLSSVGGRSAKLGQVIHHCFYKTGLIILESRLNVFGTSRPRESSKNNKWFNLEIVETELYAEQFKIWKNIELSPSRKIPPMVLHTYLDISDLSKNQTLSVSDGTHSHAINFNNMSTMKIVLERWIVNLDGEALSTPLELAVLYKKLVVLFRSLYTYTHLMPLWKLKSKIHKLRAHGTSLKVGCALSTDDVLSNDFLPISAPISSSLGSSIATFSFSPVGTPAGDFRISVQYRKNCHFEVHDSDALLSNQLLSADKHQLAASNNSQDFEDGKQYDQPPPSFATRLAKQSDPNS... | null | null | autophagosome assembly [GO:0000045]; macroautophagy [GO:0016236]; meiotic cell cycle [GO:0051321]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein localization to phagophore assembly site [GO:0034497]; protein transport [GO:0015031]; sporulation resulting in formation of a cellular... | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phagophore assembly site [GO:0000407] | protein kinase regulator activity [GO:0019887] | PF10033; | 3.30.900.10; | ATG13 family, Fungi subfamily | PTM: Phosphorylated (PubMed:17295836). Dephosphorylated under depletion of nitrogen (PubMed:17295836). {ECO:0000269|PubMed:17295836}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Preautophagosomal structure {ECO:0000269|PubMed:23950735}. | null | null | null | null | null | FUNCTION: Component of the atg1 kinase complex that activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (PubMed:23950735, PubMed:26030876). Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring t... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O36023 | SPN1_SCHPO | MASMVLADGMPTVKDDSTRSRGSDVDSFTSTDNVTQINVEAAISENKNEEKPIQDNSEQEFNPHVSIIQRQLNGYVGFASLPNQWHRRCVRQGFNFNVLVLGESGSGKSTLVNTLLNRDVYPPTQKSLTGDFGVNPEPTVMINSSAVEIVENGISLQLNVIDTPGFGDFIDNTDCWQPVLTDIEGRYDQYLELEKHNPRSTIQDPRVHACIFFIQPTGHAISAMELRVMLALHEKVNIIPIIAKADTLTDDELNFTKEMILRDIQYHNIRIFFPPTYETDDPESVAENADIMSRIPFAIIASNTFVVNNEGKRVRGRRYP... | null | null | cytoskeleton-dependent cytokinesis [GO:0061640]; mitotic cytokinesis [GO:0000281] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; medial cortex [GO:0031097]; medial cortex septin ring [GO:0036391]; microtubule cytoskeleton [GO:0015630]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; mitotic septin complex [GO:0032151]; nucleus [GO:0005634]; septin co... | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:15385632}. Note=Localizes to the medial ring at the cell cortex of dividing cells. | null | null | null | null | null | FUNCTION: Plays a role in the cell cycle. Involved in a late stage of septum formation leading to the separation of the daughter cells. {ECO:0000269|PubMed:15385632}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O36027 | WSP1_SCHPO | MPPSSSITQEDKATIRKYIPKSTNKIIAAAVVKLYVAYPDPNKWNYTGLCGALVLSYDTTAKCCWFKLVDVVNNSGIIWDQELYQNMDYRQDRTFFHSFELDKCLAGFSFANETDAQKFYKKVLDKGCHPESIENPVLSFITRKGSSRHAPNNSNIQPPSAAPPVPGKENYNAVGSKSPNEPELLNSLDPSLIDSLMKMGISQDQIAENADFVKAYLNESAGTPTSTSAPPIPPSIPSSRPPERVPSLSAPAPPPIPPPSNGTVSSPPNSPPRPIAPVSMNPAINSTSKPPLPPPSSRVSAAALAANKKRPPPPPPPSRR... | null | null | actin cortical patch assembly [GO:0000147]; actin filament branching [GO:0090135]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; endocytosis [GO:0006897]; establishment or maintenance of cell polarity [GO:0007163]; mitotic actomyosin contractile ring assembly [GO:1903475]; mitotic cytokinesis [GO:0000281] | actin cortical patch [GO:0030479]; mating projection tip [GO:0043332]; medial cortex [GO:0031097] | actin monomer binding [GO:0003785]; Arp2/3 complex binding [GO:0071933] | PF00568; | 2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Has a role in regulating actin assembly, so regulating polarized growth. {ECO:0000269|PubMed:11076964}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O36028 | ATCZ_SCHPO | MPSLINFDAISSLKSSLHGLSICAFNHLHHVPQHNGSLAHEGPTNQTDYSSRHHESQFSQEAHAEQRSRDDEEANSFEGSCNNSDQSWTSRVTSKKNEAGTESGDASVRRIYVTSIPEEHRHLPSQWFPSNKIRTTKYTPVSFIPKNLWNQFKNIANAFFLFVTLLQCIPLFCPEHLGLSFIPLSVILLTTAIKDGIEDYRRCVLDKKFNNTLTWKLVGFNNANALGEHIGLWRKLKKFISHTVADMSYCLKNSGISSGLATLTVDNISHRHSLESDSAFTLSSVSQDSLEIHEIGNSGPSNSFSVIQEQSTGSSNAKFE... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; | phospholipid translocation [GO:0045332] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554... | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phospha... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide, phosphatidylcholine, phosphatidylethanolamine, and small amounts of phosphatidylserine from the lumenal to the cytosolic leaflet of the cell membrane and ensures the maintena... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O36307 | NCAP_ANDV | MSTLQELQENITAHEQQLVTARQKLKDAEKAVEVDPDDVNKSTLQSRRAAVSTLETKLGELKRQLADLVAAQKLATKPVDPTGLEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGAYILGFAIPIILKALYMLSTRGRQTVKDNKGTRIRFKDDSSFEEVNGIRKPKHLYVSMPTAQSTMKAEEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFGFFVKDWMDRIEEFLAAECPFLPKPKVASEAFMSTNKMYFLNRQRQVNESKVQDIIDLIDHAETESATLFTEIATPHSVWVFACAPDRCPPTALY... | 3.1.-.- | null | virus-mediated perturbation of host defense response [GO:0019049] | host cell Golgi apparatus [GO:0044177]; host cell perinuclear region of cytoplasm [GO:0044220]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | PF00846; | 1.20.58.90; | Hantavirus nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}. | null | null | null | null | null | FUNCTION: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a... | Andes orthohantavirus (ANDV) (Andes virus) |
O36634 | FUS_HRSVB | MELLIHRLSAIFLTLAINALYLTSSQNITEEFYQSTCSAVSRGYFSALRTGWYTSVITIELSNIKETKCNGTDTKVKLIKQELDKYKNAVTELQLLMQNTPAANNRARREAPQYMNYTINTTKNLNVSISKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYINNQLLPIVNQQSCRISNIETVIEFQQKNSRLLEINREFSVNAGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYVVQLPIYGVIDTPCWKLHTSP... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of syncytium formation by virus [GO:0060141]; symbiont entry into host cell [GO:0046718] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00523; | 1.10.287.2480;6.10.250.1160;6.20.370.50; | Paramyxoviruses fusion glycoprotein family | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavag... | SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 c... | Human respiratory syncytial virus B (strain B1) |
O36635 | L_HRSVB | MDPIINGNSANVYLTDSYLKGVISFSECNALGSYLFNGPYLKNDYTNLISRQSPLLEHMNLKKLTITQSLISRYHKGELKLEEPTYFQSLLMTYKSMSSSEQIATTNLLKKIIRRAIEISDVKVYAILNKLGLKEKDRVKPNNNSGDENSVLTTIIKDDILSAVESNQSYTNSDKNHSVNQNITIKTTLLKKLMCSMQHPPSWLIHWFNLYTKLNNILTQYRSNEVKSHGFILIDNQTLSGFQFILNQYGCIVYHKGLKKITTTTYNQFLTWKDISLSRLNVCLITWISNCLNTLNKSLGLRCGFNNVVLSQLFLYGDCI... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P28887}; Note=For RNA-directed RNA polymerase activity. Mn(2+) can stimulate de novo initiation but it is inefficient at supporting elongation of de novo initiated RNA. {ECO:0000250|UniProtKB:P28887}; | null | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF14314;PF14318;PF00946; | null | Paramyxovirus L protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P28887}. Host cytoplasm {ECO:0000250|UniProtKB:P28887}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000250|UniProtKB:P28887}. | 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=GTP + H2... | null | null | null | null | FUNCTION: Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation. Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes. The template is composed of the viral RNA tightly encapsidated by the nucleo... | Human respiratory syncytial virus B (strain B1) |
O36966 | POLN_DCVEB | MESDKSMACLNRILMNKMMFVEDKISTLKMVADYYQKEVKYDFDAVESPREAPVFRCTCRFLGYTIMTQGIGKKNPKQEAARQMLLLLSGDVETNPGPVQSRPVYYRYNDPRYTRLEKAIERRDDKIKTLIKELRRQIKNRKIYSQGMFDKLTKQISDGIKDGVGSEQMNGNLTRICDFLENTLPGLQANIQATVIDTTDKYVSLKEDIMKIVLVILLVRLLMVWKKYRASLCVILIFIFKFYGFDQKLIDLIMDLKNKIFSQGALEDTVEEVVYHPWFHTCGKIIFAVMAFLTIKKIPGKQDWDSYITRLDRIPKSIEG... | 2.7.7.48; 3.4.22.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | null | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF12381;PF00680;PF00910; | 3.30.160.20;3.30.70.270;2.40.10.10; | null | PTM: Protein 1A might be expressed through a ribosomal skip from one codon to the next without formation of a peptide bond. | null | 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}; | null | null | null | null | FUNCTION: Protein 1A functions as a suppressor of RNA-mediated gene silencing, an antiviral defense mechanism of insect cells. Binds to long dsRNA and to a lesser extent, to siRNA.; FUNCTION: RNA-directed RNA polymerase replicates genomic and antigenomic RNA. | Drosophila C virus (strain EB) (DCV) |
O36979 | POLG_ZYMVS | MAAIMIGSISVPIIGSAQCATAPIGNRVNIVAPGHMAICKPQMRSHAYYKHASQKLSEQSSRGIEVLNSFFNNDPEDAFRLTRNGMSKVKKGPNGRIILRKPKARHVFERINLEKSEKEQKGKFFNGEYDTTVTSIKGVTTSKENDLGAFSLRSPFYKRTCKKEKRRITRENIVCVDDVNNLCERILKITRDKNIPVEIIGKRRNHHTLTFKKFKGSFVGKVSLAPERSQMKHVEMSYGQFDYILQAICRITSTKHVRDEDIKPGCSGWVFSTDHALTQKYSRLPYLVIRGRDDDGIVNALEPVLFYSDVEHYSFQNEVQ... | 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 [GO:0044161]; host cell nucleus [GO:0042025] | 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]; structural molecule activity [GO:000... | 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]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. 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 associate ... | 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... | Zucchini yellow mosaic virus (strain Singapore) (ZYMV) |
O39521 | REPA_BEYDV | MPSASKNFRLQSKYVFLTYPKCSSQRDDLFQFLWEKLTPFLIFFLGVASELHQDGTTHYHALIQLDKKPCIRDPSFFDFEGNHPNIQPARNSKQVLDYISKDGDIKTRGDFRDHKVSPRKSDARWRTIIQTATSKEEYLDMIKEEFPHEWATKLQWLEYSANKLFPPQPEQYVSPFTESDLRCHEDLHNWRETHLYHVSIDAYTFIHPVSYDQAQSDLEWMADLTRMREGLGSDTPASTSADQLVPERPPGLEVSGDTTTGTGPSTSPTTMNTPPIISSTTSPSSSSHCGSN | 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000255|PROSITE-ProRule:PRU01364}; | DNA replication [GO:0006260]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; nucleotidyltransferase activity [GO:0016779]; structural molecule activity [GO:0005198] | PF00799;PF08283; | 3.40.1310.20; | Geminiviridae Rep protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16972938}. Host cytoplasm {ECO:0000269|PubMed:16972938}. Note=distributed equally throughout both the nucleus and the cytoplasm. | null | null | null | null | null | FUNCTION: Implicated in enhancement of V-sense gene expression. Acts a an inhibitor of C-sense gene transcription. {ECO:0000269|PubMed:14645928, ECO:0000269|PubMed:16972938}. | Bean yellow dwarf virus (BeYDV) |
O39522 | REP_BEYDV | MPSASKNFRLQSKYVFLTYPKCSSQRDDLFQFLWEKLTPFLIFFLGVASELHQDGTTHYHALIQLDKKPCIRDPSFFDFEGNHPNIQPARNSKQVLDYISKDGDIKTRGDFRDHKVSPRKSDARWRTIIQTATSKEEYLDMIKEEFPHEWATKLQWLEYSANKLFPPQPEQYVSPFTESDLRCHEDLHNWRETHLYHDEGRTGVRHPSLYICGPTRTGKTTWARSLGRHNYWNGTIDFTNYDEHATYNIIDDIPFKFVPLWKQLIGCQSDFTVNPKYGKKKKIKGGIPSIILCNPDEDWMLSMTSQQKDYFEDNCVTHYM... | 2.7.7.-; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000255|PROSITE-ProRule:PRU01364}; | DNA replication [GO:0006260] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; structural molecule activity [GO:0005198] | PF00799;PF08283; | 3.40.1310.20; | Geminiviridae Rep protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16972938}. | null | null | null | null | null | FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome... | Bean yellow dwarf virus (BeYDV) |
O39828 | MREP_FBNY2 | MARQVICWCFTLNNPLSPLSLHDSMKYLVYQTEQGEAGNIHFQGYIEMKKRTSLAGMKKLIPGAHFEKRRGTQGEARAYSMKEDTRLEGPWEYGEFVPTIEDKLREVMNDMKITGKRPIEYIEECCNTYDKSASTLREFRGELKKKKAISSWELQRKPWMGEVDALLQERDGRRIIWVYGPQGGEGKTSYAKHLVKTRDAFYSTGGKTADIAFAWDHQELVLFDFPRSFEEYVNYGVIEQLKNGIIQSGKYQSVIKYSDYVEVIVFANFTPRSGMFSEDRIVYVYA | 2.7.7.-; 3.1.21.-; 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:17472345}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:17472345}; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000305|PubMed:17472345}; | DNA replication [GO:0006260] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00910;PF02407; | 3.40.1310.20; | Nanoviridea/circoviridae replication-associated protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. | 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; | null | null | null | null | FUNCTION: Essential for the replication of all genomic viral ssDNA (trans-replication). The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-A[GT]TATTAC-3' in the... | Faba bean necrotic yellows virus (isolate SV292-88) (FBNYV) |
O39927 | POLG_HCVEU | MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRKGPRLGVRATRKTSERSQPRGRRQPIPKARQPQGRHWAQPGYPWPLYGSEGCGWAGWLLSPRGSRPHWGPNDPRRRSRNLGKVIDTLTCGFADLMWYIPVVGAPLGGVAAALAHGVRAIEDGINYATGNLPGCSFSIFLLALLSCLTTPASALTYGNSSGLYHLTNDCSNSSIVLEADAMILHLPGCLPCVRVGNQSTCWHAVSPTLATPNASTPATGFRRHVDLLAGAAVVCSSLYIGDLCGSLFLAGQLFAFQPRRHWTVQDCNCSIYTGHVTGHKMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF07652;PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 6a (isolate EUHK2) (HCV) |
O39928 | POLG_HCVEV | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPKLGVRATRKNSERSQPRGRRQPIPKARRPTGRSWGQPGYPWPLYANEGLGWAGWLLSPRSSRPNWGPNDPRRKSPNLGRVIHTLTCGFPHLMGYIPLVGGPVGGVSRALAHGVKVLEDGINYATGNLPGCPFSIFVLALLWCLTVPASAVPYRNASGVYHVTNDCPNSSIVYEADNLILHAPGCVPCVLEDNVSRCWVQITPTLSAPSFGAVTALLRRAVDYLAGGAAFCSALYVGDACGALSLVGQMFTYKPRQHTTVQDCNCSIYSGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 5a (isolate EUH1480) (HCV) |
O39929 | POLG_HCVED | MSTNPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRSWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPNDPRGRSRNLGKVIDTLTCGFADLMGYIPLVGAPVGSVARALAHGVRALEDGINYATGNLPGCSFSIFLLALLSCLTVPASAVNYRNVSGIYHVTNDCPNSSIVYEADHHIMHLPGCVPCVREGNQSRCWVALTPTVAAPYIGAPLESLRSHVDLMVGAATVCSGLYIGDLCGGLFLVGQMFSFRPRRHWTTQDCNCSIYTGHITGHRMAW... | 2.7.7.48; 3.4.21.98; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: [Protease NS2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P26663}; Note=Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host cell cycle G1/S transiti... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell lipid droplet [GO:0044186]; host cell mitochondrial membrane [GO:0044191]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; ribonucleoprotein complex [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:000425... | PF01543;PF01542;PF01539;PF01560;PF01538;PF01006;PF01001;PF01506;PF08300;PF08301;PF12941;PF02907;PF00998; | 2.40.10.120;3.30.70.270;6.10.250.1610;6.10.250.1750;6.10.250.2920;2.20.25.210;3.30.160.890;2.30.30.710;1.20.1280.150;2.20.25.220;3.40.50.300;1.10.820.10;2.40.10.10; | Hepacivirus polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membran... | SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the c... | CATALYTIC ACTIVITY: [Serine protease/helicase NS3]: Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; Evidence={ECO:0000250|UniProtKB:P27958}; CATALYTIC ACTIVITY: [Serine protease/helicase NS3... | null | null | null | null | FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA struc... | Hepatitis C virus genotype 4a (isolate ED43) (HCV) |
O40955 | POLN_RUBVR | MERLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRPCTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE... | 2.7.7.48; 3.4.22.-; 3.6.1.15; 3.6.4.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01237}; Note=Zn(2+) is necessary for the protease activity. The protease can also function efficiently with Cd(2+) and Co(2+). {ECO:0000255|PROSITE-ProRule:PRU01237}; | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694] | host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; mRNA methyltransferase activity [GO:0008174]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-depend... | PF01661;PF05407;PF00978;PF12601;PF01443; | 3.40.220.10;3.40.50.300; | null | PTM: [Non-structural polyprotein p200]: Specific enzymatic cleavage by its own cysteine protease yield mature proteins p150 and p90. {ECO:0000250|UniProtKB:Q86500}. | SUBCELLULAR LOCATION: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}.; SUBCELLULAR LOCATIO... | 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:0000250|UniProtKB:Q86500, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}.; FUNCTION: [Protease/methyltrans... | Rubella virus (strain RA27/3 vaccine) (RUBV) |
O41174 | POLG_PEV9U | MGMQMSKNTAGSHTTVTQASGGSHINYTNINYYSHSASASQNKQDITQDPSKFTQPMVDIMKESAVPLKSPSAEACGYSDRVAQLTLGNSTITTQEAANITVAYGEWPSYLSDLDATAVDKTTKPGVSCDRFYTLPGKKWEATTKGWEWKLPDALTELGVFGQNCQFHFLYRCGWSIHVQCNATKFHQGTLLVVAVPDHQLGTTYQPEFDNVMPGKAGREVKYPYNFEDGTSLANSLIYPHQWINLRTNNSATLVLPYANAIPMDSPIRHSSWSLLVIPVVPLACATGTTPFVGITITLAPMFSEFSGLRRAIAQGIPTT... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Porcine enterovirus 9 (strain UKG/410/73) |
O41515 | MLP3B_BOVIN | MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPICEVYESEKDEDGFLYMVYASQETFGMKLSV | null | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; cellular response to nitrogen starvation [GO:0006995]; cellular response to starvation [GO:0009267]; mitophagy [GO:0000423] | autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; microtubule [GO:0005874]; mitochondrial membrane [GO:0031966]; organelle membrane [GO:0031090] | microtubule binding [GO:0008017]; phosphatidylethanolamine binding [GO:0008429]; ubiquitin protein ligase binding [GO:0031625] | PF02991; | null | ATG8 family | PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, LC3-I. The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, ... | SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CQV6}; Lipid-anchor {ECO:0000250|UniProtKB:Q9GZQ8}. Endomembrane system {ECO:0000250|UniProtKB:Q9CQV6}; Lipid-anchor {ECO:0000250|UniProtKB:Q9GZQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor {ECO:0000250... | null | null | null | null | null | FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. I... | Bos taurus (Bovine) |
O41798 | POL_HV19N | MGARASVLSGGKLDSWEKIRLRPGGRKKYKLKHIVWASRELGRFALNRDLLETAEGCVQIMKQLQPALTGTEELRSLFNTVATLYCVHQKIEVKDTKEAPEEVEKIQKNSQQEIQQAAKNEGNSNPVSQNYPIVQNAQGQMIHQAISPWTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINDEAAEWDRIHPQQAGPIPPGQIREPSGSDIAGTTSTLQEQIRWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTL... | 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 G (isolate 92NG083) (HIV-1) |
O41801 | TAT_HV19N | MDPVDPKLEPWNHPGSQPTTPCNKCYCKVCCWHCQVCFLNKGLGISYGRKKRRPRRGTPQGSKDHQNPVPKQPLPITSGNPTGSEKPKKEVASKTETDPLD | 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 G (isolate 92NG083) (HIV-1) |
O41803 | ENV_HV19N | MRVKGIQRNWQHLWKWGTLILGLVIICSASDNLWVTVYYGVPVWEDADTPLFCASDAKSYSSEKHNVWATHACVPTDPNPQEIAIENVTENFNMWKNNMVEQMQEDIISLWEESLKPCVKLTPLCITLNCTNVNSANHTEANNTVENKEEIKNCSFKITTERGGKKKEEYALFYKLDVVPISNGNKTSYRLIHCNVSTIKQACPKVNFDPIPIHYCAPAGFAILKCRDKEYNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIRIRSENFTDNTKVIIVQLNNSIEINCIRPNNNTRKSIPIGPGQAFYATGDII... | 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 G (isolate 92NG083) (HIV-1) |
O41804 | NEF_HV19N | MGGKWSKSSIVGWPQIRERIRQTPVAAEGVGAVSQDLARHGAITSSNTATNNPDCAWLEAQEEDSDVGFPVRPQVPLRPMTYKAAFDLSFFLKEKGGLDGLIYSKRRQDILDLWVYNTQGFFPDWQNYTPGPGTRLPLTFGWCFKLVPMDPAEIEEANKGENISLLHPICQHGMEDEDREVLVWRFNSSLARRHLARELHPEYYKDC | 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 G (isolate 92NG083) (HIV-1) |
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