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E1A binding protein p300, isoform CRA_b (E1A-binding protein p300)

 A0A0G2QC09_RAT          Unreviewed;       728 AA.
A0A0G2QC09;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
23-MAY-2018, entry version 25.
SubName: Full=E1A binding protein p300, isoform CRA_b {ECO:0000313|EMBL:EDM15718.1};
SubName: Full=E1A-binding protein p300 {ECO:0000313|Ensembl:ENSRNOP00000000206};
Name=Ep300 {ECO:0000313|EMBL:EDM15718.1,
ECO:0000313|Ensembl:ENSRNOP00000000206};
ORFNames=rCG_59903 {ECO:0000313|EMBL:EDM15718.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000000206, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000000206, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000206,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDM15718.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM15718.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDM15718.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM15718.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000000206}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000206};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AABR07058539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473950; EDM15718.1; -; Genomic_DNA.
UniGene; Rn.12447; -.
UniGene; Rn.232499; -.
STRING; 10116.ENSRNOP00000000206; -.
Ensembl; ENSRNOT00000000206; ENSRNOP00000000206; ENSRNOG00000000190.
RGD; 620036; Ep300.
GeneTree; ENSGT00760000119206; -.
HOGENOM; HOG000111353; -.
OMA; MRSINAI; -.
TreeFam; TF101097; -.
Reactome; R-RNO-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-RNO-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-RNO-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-RNO-3371568; Attenuation phase.
Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-RNO-5689901; Metalloprotease DUBs.
Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-RNO-6782135; Dual incision in TC-NER.
Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-RNO-6811555; PI5P Regulates TP53 Acetylation.
Reactome; R-RNO-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-RNO-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-RNO-8951936; RUNX3 regulates p14-ARF.
Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
Reactome; R-RNO-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-RNO-933541; TRAF6 mediated IRF7 activation.
Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000000190; -.
GO; GO:0000785; C:chromatin; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IC:RGD.
GO; GO:0003823; F:antigen binding; IDA:RGD.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0031490; F:chromatin DNA binding; IDA:RGD.
GO; GO:0035259; F:glucocorticoid receptor binding; IDA:RGD.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:RGD.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IMP:RGD.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:RGD.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
GO; GO:1990405; F:protein antigen binding; IPI:RGD.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; IDA:RGD.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:RGD.
GO; GO:0003713; F:transcription coactivator activity; IGI:ARUK-UCL.
GO; GO:0008134; F:transcription factor binding; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; IEP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0035984; P:cellular response to trichostatin A; IEP:RGD.
GO; GO:0048565; P:digestive tract development; IEP:RGD.
GO; GO:0043966; P:histone H3 acetylation; IMP:RGD.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0031324; P:negative regulation of cellular metabolic process; IMP:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:2000629; P:negative regulation of miRNA metabolic process; IMP:RGD.
GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
GO; GO:0031325; P:positive regulation of cellular metabolic process; IMP:RGD.
GO; GO:0043388; P:positive regulation of DNA binding; IMP:RGD.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; IMP:RGD.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:RGD.
GO; GO:0014737; P:positive regulation of muscle atrophy; IMP:RGD.
GO; GO:1901985; P:positive regulation of protein acetylation; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
GO; GO:0045862; P:positive regulation of proteolysis; IMP:RGD.
GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:0043491; P:protein kinase B signaling; IDA:RGD.
GO; GO:0065004; P:protein-DNA complex assembly; IDA:RGD.
GO; GO:0060177; P:regulation of angiotensin metabolic process; IDA:RGD.
GO; GO:0051592; P:response to calcium ion; IMP:RGD.
GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
GO; GO:0071548; P:response to dexamethasone; IMP:RGD.
GO; GO:0042493; P:response to drug; IMP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IMP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
Gene3D; 1.20.1020.10; -; 1.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
InterPro; IPR035898; TAZ_dom_sf.
InterPro; IPR000197; Znf_TAZ.
Pfam; PF02172; KIX; 1.
Pfam; PF02135; zf-TAZ; 1.
SMART; SM00551; ZnF_TAZ; 1.
SUPFAM; SSF47040; SSF47040; 1.
SUPFAM; SSF57933; SSF57933; 1.
PROSITE; PS50952; KIX; 1.
PROSITE; PS50134; ZF_TAZ; 1.
4: Predicted;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00203};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Zinc {ECO:0000256|PROSITE-ProRule:PRU00203};
Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00203}.
DOMAIN 332 418 TAZ-type. {ECO:0000259|PROSITE:PS50134}.
DOMAIN 567 646 KIX. {ECO:0000259|PROSITE:PS50952}.
ZN_FING 332 418 TAZ-type. {ECO:0000256|PROSITE-
ProRule:PRU00203}.
SEQUENCE 728 AA; 77345 MW; DEEAC16796C44627 CRC64;
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE 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
PNMGQQPTPS VQQPGLVNPV APGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG
EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN
AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ
IPPQPPVQAK NQQSQPSGQS PQGMRSMNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS
QNPMMNENAS VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP
SAPGMVPVPM NTAPNMGQQP TGMTTNGPLP DPSMIRGSVP NQMMPRMTPQ PGKFWKKKKS
TRLIFKIL


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