Q91XT0 (Q91XT0_RAT) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
E1A-binding protein EMBL BAB62425.1

Submitted name:
Uncharacterized protein Ensembl ENSRNOP00000000206

Gene names

Name:	Ep300 RGD 620036
Synonyms:	p300 EMBL BAB62425.1

Organism

Rattus norvegicus (Rat) [Reference proteome] EMBL BAB62425.1

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal peptidyl-lysine acetylation Inferred from electronic annotation. Source: Compara cellular response to hydrogen peroxide Inferred from expression pattern PubMed 17457521. Source: RGD digestive tract development Inferred from expression pattern PubMed 17916272. Source: RGD heart development Inferred from electronic annotation. Source: Compara histone H4 acetylation Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from electronic annotation. Source: Compara liver development Inferred from expression pattern PubMed 15598887. Source: RGD lung development Inferred from electronic annotation. Source: Compara negative regulation of cellular metabolic process Inferred from mutant phenotype PubMed 18586071. Source: RGD negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from electronic annotation. Source: Compara positive regulation by host of viral transcription Inferred from electronic annotation. Source: Compara positive regulation of DNA binding Inferred from mutant phenotype PubMed 19057620. Source: RGD positive regulation of axon extension Inferred from mutant phenotype PubMed 19339625. Source: RGD positive regulation of cell size Inferred from mutant phenotype PubMed 12724418. Source: RGD positive regulation of collagen biosynthetic process Inferred from mutant phenotype PubMed 18292803. Source: RGD positive regulation of glycoprotein biosynthetic process Inferred from mutant phenotype PubMed 17065349. Source: RGD positive regulation of protein binding Inferred from electronic annotation. Source: Compara positive regulation of protein import into nucleus, translocation Inferred from mutant phenotype PubMed 18292803. Source: RGD positive regulation of protein phosphorylation Inferred from mutant phenotype PubMed 18292803. Source: RGD positive regulation of protein secretion Inferred from mutant phenotype PubMed 12477714. Source: RGD positive regulation of proteolysis Inferred from mutant phenotype PubMed 16973938. Source: RGD positive regulation of sarcomere organization Inferred from mutant phenotype PubMed 12724418. Source: RGD positive regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype PubMed 19057620. Source: RGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 15598887. Source: RGD positive regulation of translation Inferred from mutant phenotype PubMed 12477714. Source: RGD protein kinase B signaling cascade Inferred from direct assay PubMed 18315570. Source: RGD protein-DNA complex assembly Inferred from direct assay PubMed 9215639. Source: RGD regulation of androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of angiotensin metabolic process Inferred from direct assay PubMed 17495236. Source: RGD response to calcium ion Inferred from mutant phenotype PubMed 16000154. Source: RGD response to cobalt ion Inferred from expression pattern PubMed 18586071. Source: RGD response to drug Inferred from mutant phenotype PubMed 15593114. Source: RGD response to estrogen stimulus Inferred from expression pattern PubMed 15722556. Source: RGD response to ethanol Inferred from expression pattern PubMed 17208223. Source: RGD response to fatty acid Inferred from expression pattern PubMed 17916272. Source: RGD response to glucocorticoid stimulus Inferred from mutant phenotype PubMed 16973938. Source: RGD response to glucose stimulus Inferred from mutant phenotype PubMed 18413674. Source: RGD response to hypoxia Inferred from expression pattern PubMed 16000154PubMed 19103185. Source: RGD response to retinoic acid Inferred from expression pattern PubMed 17164434. Source: RGD response to tumor necrosis factor Inferred from expression pattern PubMed 18438857. Source: RGD skeletal muscle tissue development Inferred from electronic annotation. Source: Compara somitogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	chromatin Inferred from direct assay PubMed 20702579. Source: RGD cytoplasm Inferred from direct assay PubMed 19103185. Source: RGD histone acetyltransferase complex Inferred from electronic annotation. Source: Compara protein-DNA complex Inferred from direct assay PubMed 19765194. Source: RGD transcription factor complex Inferred by curator PubMed 15598887. Source: RGD
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 20702579. Source: RGD antigen binding Inferred from direct assay PubMed 8985331PubMed 9252373. Source: RGD chromatin DNA binding Inferred from direct assay PubMed 20702579. Source: RGD core promoter binding Inferred from electronic annotation. Source: Compara glucocorticoid receptor binding Inferred from direct assay PubMed 17884810. Source: RGD histone acetyltransferase activity Inferred from mutant phenotype PubMed 18292803. Source: RGD lysine N-acetyltransferase activity Inferred from mutant phenotype PubMed 12724418. Source: RGD peroxisome proliferator activated receptor binding Inferred from direct assay Ref.1. Source: RGD protein complex binding Inferred from direct assay PubMed 11755530. Source: RGD transcription coactivator activity Inferred from electronic annotation. Source: Compara transcription factor binding Inferred from direct assay PubMed 15117818. Source: RGD
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q91XT0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F12C37E246848407	FASTA	353	36,049
	10 20 30 40 50 60 MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 70 80 90 100 110 120 ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ NSPGLSLINS 130 140 150 160 170 180 MVKSPMAQTG LTSPNMGMGS SGPNQGPTQS TAGMMNSPVN QPAMGMNTGM NAGMNPGMLA 190 200 210 220 230 240 AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP 250 260 270 280 290 300 QSHKMGMMSN PTPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVTGGGM 310 320 330 340 350 PNMGQQPTPS VQQPGLVNPV APGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Major intestinal coactivator p300 strongly activates peroxisome proliferator-activated receptor in intestinal cell line, Caco-2." Mochizuki K., Suruga K., Sakaguchi N., Takase S., Goda T. Gene 291:271-277(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Small intestine EMBL BAB62425.1.
[2]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." 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. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway Ensembl ENSRNOP00000000206.
[3]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION. Strain: Brown Norway Ensembl ENSRNOP00000000206.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR06052095 Genomic DNA. No translation available. AB066220 mRNA. Translation: BAB62425.1.
IPI	IPI00765110.
UniGene	Rn.12447. Rn.232499.
3D structure databases
HSSP	HSSP built from PDB template 1L3E based on UniProtKB Q09472.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000000206; ENSRNOP00000000206; ENSRNOG00000000190.
UCSC	RGD:620036. rat.
Organism-specific databases
RGD	620036. Ep300.
Phylogenomic databases
GeneTree	ENSGT00700000104285.
HOGENOM	HOG000111353.
HOVERGEN	HBG074064.
InParanoid	Q91XT0.
Gene expression databases
Genevestigator	Q91XT0.
Family and domain databases
Gene3D	1.10.1630.10. 1 hit. 1.10.246.20. 1 hit. 1.20.1020.10. 2 hits. 1.20.920.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR010303. DUF902_CREBbp. IPR013178. Histone_H3-K56_AcTrfase_RTT109. IPR003101. KIX_dom. IPR009110. Nuc_rcpt_coact. IPR014744. Nuc_rcpt_coact_CREBbp. IPR000197. Znf_TAZ. IPR000433. Znf_ZZ. [Graphical view]
Pfam	PF00439. Bromodomain. 1 hit. PF09030. Creb_binding. 1 hit. PF06001. DUF902. 1 hit. PF08214. KAT11. 1 hit. PF02172. KIX. 1 hit. PF02135. zf-TAZ. 2 hits. PF00569. ZZ. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00551. ZnF_TAZ. 2 hits. SM00291. ZnF_ZZ. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF47040. KIX. 1 hit. SSF69125. Nuc_recept_coact. 1 hit. SSF57933. TAZ_finger. 2 hits.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS50952. KIX. 1 hit. PS50134. ZF_TAZ. 2 hits. PS01357. ZF_ZZ_1. 1 hit. PS50135. ZF_ZZ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35576275.

Entry information

Entry name

Q91XT0_RAT

Accession

Primary (citable) accession number: Q91XT0
Secondary accession number(s): F1LPY5

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)