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Database: UniProt
Entry: A0A0G2QC09_RAT
LinkDB: A0A0G2QC09_RAT
Original site: A0A0G2QC09_RAT 
ID   A0A0G2QC09_RAT          Unreviewed;       365 AA.
AC   A0A0G2QC09;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=Ep300 {ECO:0000313|Ensembl:ENSRNOP00000000206.8,
GN   ECO:0000313|RGD:620036};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000000206.8, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000000206.8, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000206.8,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000000206.8}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000206.8};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A0G2QC09; -.
DR   STRING; 10116.ENSRNOP00000000206; -.
DR   PaxDb; 10116-ENSRNOP00000000206; -.
DR   Ensembl; ENSRNOT00000000206.8; ENSRNOP00000000206.8; ENSRNOG00000000190.8.
DR   AGR; RGD:620036; -.
DR   RGD; 620036; Ep300.
DR   VEuPathDB; HostDB:ENSRNOG00000000190; -.
DR   eggNOG; KOG1778; Eukaryota.
DR   GeneTree; ENSGT00940000155497; -.
DR   InParanoid; A0A0G2QC09; -.
DR   TreeFam; TF101097; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000000190; Expressed in spleen and 18 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0000123; C:histone acetyltransferase complex; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0016407; F:acetyltransferase activity; ISO:RGD.
DR   GO; GO:0016746; F:acyltransferase activity; ISO:RGD.
DR   GO; GO:0003823; F:antigen binding; IDA:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IPI:RGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:RGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003684; F:damaged DNA binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:RGD.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:RGD.
DR   GO; GO:0140069; F:histone butyryltransferase activity; ISO:RGD.
DR   GO; GO:0140068; F:histone crotonyltransferase activity; ISO:RGD.
DR   GO; GO:0044013; F:histone H2B acetyltransferase activity; ISO:RGD.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0140908; F:histone H3K122 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0120301; F:histone lactyltransferase activity; ISO:RGD.
DR   GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:RGD.
DR   GO; GO:0051059; F:NF-kappaB binding; IPI:RGD.
DR   GO; GO:0050681; F:nuclear androgen receptor binding; ISO:RGD.
DR   GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IDA:RGD.
DR   GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR   GO; GO:0002039; F:p53 binding; IPI:RGD.
DR   GO; GO:0140065; F:peptide butyryltransferase activity; ISO:RGD.
DR   GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:RGD.
DR   GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:RGD.
DR   GO; GO:0097157; F:pre-mRNA intronic binding; ISO:RGD.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
DR   GO; GO:1990405; F:protein antigen binding; IPI:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:0061920; F:protein propionyltransferase activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR   GO; GO:0046332; F:SMAD binding; IPI:RGD.
DR   GO; GO:0097677; F:STAT family protein binding; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IGI:ARUK-UCL.
DR   GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:RGD.
DR   GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR   GO; GO:0002209; P:behavioral defense response; ISO:RGD.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IMP:RGD.
DR   GO; GO:0071233; P:cellular response to leucine; ISO:RGD.
DR   GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; IEP:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0031669; P:cellular response to nutrient levels; ISO:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR   GO; GO:0035984; P:cellular response to trichostatin A; IEP:RGD.
DR   GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR   GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR   GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR   GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR   GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR   GO; GO:0007611; P:learning or memory; ISO:RGD.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0010742; P:macrophage derived foam cell differentiation; ISO:RGD.
DR   GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR   GO; GO:0007613; P:memory; IEP:RGD.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:RGD.
DR   GO; GO:2000629; P:negative regulation of miRNA metabolic process; IMP:RGD.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0030220; P:platelet formation; ISO:RGD.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR   GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR   GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
DR   GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IMP:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
DR   GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; IMP:RGD.
DR   GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IMP:RGD.
DR   GO; GO:0014737; P:positive regulation of muscle atrophy; IMP:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR   GO; GO:1901985; P:positive regulation of protein acetylation; IMP:RGD.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IMP:RGD.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:RGD.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR   GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR   GO; GO:0036211; P:protein modification process; IMP:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0065004; P:protein-DNA complex assembly; IDA:RGD.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:RGD.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; IDA:RGD.
DR   GO; GO:0006110; P:regulation of glycolytic process; ISO:RGD.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD.
DR   GO; GO:0051592; P:response to calcium ion; IMP:RGD.
DR   GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IMP:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IMP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR   GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR   GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR   GO; GO:0036268; P:swimming; ISO:RGD.
DR   GO; GO:0001966; P:thigmotaxis; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISO:RGD.
DR   Gene3D; 1.20.1020.10; TAZ domain; 1.
DR   InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR   InterPro; IPR035898; TAZ_dom_sf.
DR   InterPro; IPR000197; Znf_TAZ.
DR   PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR   PANTHER; PTHR13808:SF29; HISTONE ACETYLTRANSFERASE P300; 1.
DR   Pfam; PF02135; zf-TAZ; 1.
DR   SMART; SM00551; ZnF_TAZ; 1.
DR   SUPFAM; SSF57933; TAZ domain; 1.
DR   PROSITE; PS50134; ZF_TAZ; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00203}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00203}.
FT   DOMAIN          306..365
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   ZN_FING         306..365
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT   REGION          125..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  38324 MW;  A5767D2CA1590852 CRC64;
     SSSPSHGGLQ PSVMRPKALF WYFGSLFDLE HDLPDELINS TELGLTNGGD ISQLQTSLGI
     VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ NSPGLSLINS MVKSPMAQTG
     LTSPNMGMGS SGPNQGPTQS TAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN
     QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QSHKMGMMSN
     PTPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVTGGGM ANSLPPSVQQ
     PAHTADPEKR KLIQQQLVLL LHAHKCQRRE QANGEVRQCN LPHCRTMKNV LNHYDTLSVR
     QILSR
//
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