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Protein
Submitted name:

E1A-binding protein

Gene

Ep300

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • activating transcription factor binding Source: RGD
  • antigen binding Source: RGD
  • bHLH transcription factor binding Source: RGD
  • chromatin binding Source: RGD
  • chromatin DNA binding Source: RGD
  • core promoter binding Source: RGD
  • core promoter proximal region DNA binding Source: RGD
  • glucocorticoid receptor binding Source: RGD
  • histone acetyltransferase activity Source: RGD
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: RGD
  • mitogen-activated protein kinase binding Source: RGD
  • NF-kappaB binding Source: RGD
  • p53 binding Source: RGD
  • peroxisome proliferator activated receptor binding Source: RGD
  • protein antigen binding Source: RGD
  • protein complex binding Source: RGD
  • protein kinase binding Source: RGD
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: RGD
  • SMAD binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • cellular response to antibiotic Source: RGD
  • cellular response to cAMP Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to drug Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to mineralocorticoid stimulus Source: RGD
  • cellular response to nerve growth factor stimulus Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to retinoic acid Source: RGD
  • cellular response to trichostatin A Source: RGD
  • digestive tract development Source: RGD
  • histone acetylation Source: RGD
  • histone H3 acetylation Source: RGD
  • internal peptidyl-lysine acetylation Source: RGD
  • liver development Source: RGD
  • memory Source: RGD
  • negative regulation of cell death Source: RGD
  • negative regulation of cellular metabolic process Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • negative regulation of miRNA metabolic process Source: RGD
  • positive regulation of axon extension Source: RGD
  • positive regulation of cell death Source: RGD
  • positive regulation of cell growth Source: RGD
  • positive regulation of cell size Source: RGD
  • positive regulation of cellular metabolic process Source: RGD
  • positive regulation of collagen biosynthetic process Source: RGD
  • positive regulation of DNA binding Source: RGD
  • positive regulation of gene expression Source: RGD
  • positive regulation of glycoprotein biosynthetic process Source: RGD
  • positive regulation of histone acetylation Source: RGD
  • positive regulation of muscle atrophy Source: RGD
  • positive regulation of protein acetylation Source: RGD
  • positive regulation of protein import into nucleus, translocation Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of protein secretion Source: RGD
  • positive regulation of proteolysis Source: RGD
  • positive regulation of sarcomere organization Source: RGD
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • positive regulation of translation Source: RGD
  • protein-DNA complex assembly Source: RGD
  • protein kinase B signaling Source: RGD
  • regulation of angiotensin metabolic process Source: RGD
  • response to calcium ion Source: RGD
  • response to cobalt ion Source: RGD
  • response to dexamethasone Source: RGD
  • response to drug Source: RGD
  • response to estrogen Source: RGD
  • response to ethanol Source: RGD
  • response to fatty acid Source: RGD
  • response to glucose Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to hypoxia Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to retinoic acid Source: RGD
  • response to tumor necrosis factor Source: RGD
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_274139. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_274349. formation of the beta-catenin:TCF transactivating complex.
REACT_275282. TRAF3-dependent IRF activation pathway.
REACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_301576. TRAF6 mediated IRF7 activation.
REACT_316815. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_327685. Attenuation phase.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_351396. Transcriptional regulation of white adipocyte differentiation.
REACT_359478. CD209 (DC-SIGN) signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
E1A-binding proteinImported
Submitted name:
Protein Ep300Imported
Gene namesi
Name:Ep300Imported
Synonyms:p300Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi620036. Ep300.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: RGD
  • cytoplasm Source: RGD
  • nucleus Source: RGD
  • protein-DNA complex Source: RGD
  • transcription factor complex Source: RGD
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000206.

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG074064.
OMAiEHRASSM.
TreeFamiTF101097.

Sequencei

Sequence statusi: Complete.

Q91XT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS
60 70 80 90 100
TELGLTNGGD ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP
110 120 130 140 150
GQVMASQAQQ NSPGLSLINS MVKSPMAQTG LTSPNMGMGS SGPNQGPTQS
160 170 180 190 200
TAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN QVMNGSIGAG
210 220 230 240 250
RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QSHKMGMMSN
260 270 280 290 300
PTPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVTGGGM
310 320 330 340 350
PNMGQQPTPS VQQPGLVNPV APGMGSGAHT ADPEKRKLIQ QQLVLLLHAH

KCQ
Length:353
Mass (Da):36,049
Last modified:December 1, 2001 - v1
Checksum:iF12C37E246848407
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06052095 Genomic DNA. No translation available.
AB066220 mRNA. Translation: BAB62425.1.
UniGeneiRn.12447.
Rn.232499.

Genome annotation databases

EnsembliENSRNOT00000000206; ENSRNOP00000000206; ENSRNOG00000000190.
UCSCiRGD:620036. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06052095 Genomic DNA. No translation available.
AB066220 mRNA. Translation: BAB62425.1.
UniGeneiRn.12447.
Rn.232499.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000206; ENSRNOP00000000206; ENSRNOG00000000190.
UCSCiRGD:620036. rat.

Organism-specific databases

RGDi620036. Ep300.

Phylogenomic databases

GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG074064.
OMAiEHRASSM.
TreeFamiTF101097.

Enzyme and pathway databases

ReactomeiREACT_274139. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_274349. formation of the beta-catenin:TCF transactivating complex.
REACT_275282. TRAF3-dependent IRF activation pathway.
REACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_301576. TRAF6 mediated IRF7 activation.
REACT_316815. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_327685. Attenuation phase.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_351396. Transcriptional regulation of white adipocyte differentiation.
REACT_359478. CD209 (DC-SIGN) signaling.

Miscellaneous databases

NextBioi35576275.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 intestineImported.
  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 NorwayImported.
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ91XT0_RAT
AccessioniPrimary (citable) accession number: Q91XT0
Secondary accession number(s): F1LPY5
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.