Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91XT0 (Q91XT0_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names

Uncharacterized protein Ensembl ENSRNOP00000000206
Gene names
Name:Ep300 RGD 620036
Synonyms:p300 EMBL BAB62425.1
OrganismRattus norvegicus (Rat) [Reference proteome] EMBL BAB62425.1
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

Ontologies

Keywords
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal peptidyl-lysine acetylation

Inferred from electronic annotation. Source: Ensembl

cellular response to antibiotic

Inferred from expression pattern PubMed 22562121. Source: RGD

cellular response to cAMP

Inferred from expression pattern PubMed 20352046. Source: RGD

cellular response to dexamethasone stimulus

Inferred from expression pattern PubMed 22465009. Source: RGD

cellular response to drug

Inferred from expression pattern PubMed 20888352. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 23211718. Source: RGD

cellular response to hydrogen peroxide

Inferred from expression pattern PubMed 17457521. Source: RGD

cellular response to mineralocorticoid stimulus

Inferred from expression pattern PubMed 22465009. Source: RGD

cellular response to nerve growth factor stimulus

Inferred from expression pattern PubMed 20399742. Source: RGD

cellular response to organic cyclic compound

Inferred from expression pattern PubMed 23632743. Source: RGD

cellular response to retinoic acid

Inferred from expression pattern PubMed 20711222. Source: RGD

cellular response to trichostatin A

Inferred from expression pattern PubMed 20094059. Source: RGD

digestive tract development

Inferred from expression pattern PubMed 17916272. Source: RGD

heart development

Inferred from electronic annotation. Source: Ensembl

histone H2B acetylation

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from mutant phenotype PubMed 22648458. Source: RGD

histone H4 acetylation

Inferred from electronic annotation. Source: Ensembl

internal peptidyl-lysine acetylation

Inferred from mutant phenotype PubMed 22292478. Source: RGD

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from expression pattern PubMed 15598887. Source: RGD

lung development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell death

Inferred from mutant phenotype PubMed 22562121. Source: RGD

negative regulation of cellular metabolic process

Inferred from mutant phenotype PubMed 18586071. Source: RGD

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 22562121. Source: RGD

negative regulation of miRNA metabolic process

Inferred from mutant phenotype PubMed 22367739. Source: RGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

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 death

Inferred from mutant phenotype PubMed 23585551. Source: RGD

positive regulation of cell growth

Inferred from mutant phenotype PubMed 15593114. Source: RGD

positive regulation of cell size

Inferred from mutant phenotype PubMed 12724418PubMed 23211718. Source: RGD

positive regulation of cellular metabolic process

Inferred from mutant phenotype PubMed 19103185. Source: RGD

positive regulation of collagen biosynthetic process

Inferred from mutant phenotype PubMed 18292803. Source: RGD

positive regulation of gene expression

Inferred from direct assay PubMed 18438857. Source: RGD

positive regulation of glycoprotein biosynthetic process

Inferred from mutant phenotype PubMed 17065349. Source: RGD

positive regulation of muscle atrophy

Inferred from mutant phenotype PubMed 22292478. Source: RGD

positive regulation of protein acetylation

Inferred from mutant phenotype PubMed 22566696. Source: RGD

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

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 18292803PubMed 22566696. 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

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: Ensembl

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 dexamethasone

Inferred from mutant phenotype PubMed 16973938. Source: RGD

response to drug

Inferred from mutant phenotype PubMed 15593114. Source: RGD

response to estrogen

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 glucose

Inferred from mutant phenotype PubMed 18413674. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 17457521. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16000154PubMed 19103185. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18292809. 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: Ensembl

somitogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

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: Ensembl

nucleus

Inferred from direct assay PubMed 17544441. Source: RGD

protein-DNA complex

Inferred from direct assay PubMed 19765194. Source: RGD

transcription factor complex

Inferred by curator PubMed 15598887. Source: RGD

   Molecular_functionNF-kappaB binding

Inferred from physical interaction PubMed 17252537. Source: RGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 20702579. Source: RGD

SMAD binding

Inferred from physical interaction PubMed 18486259. Source: RGD

activating transcription factor binding

Inferred from physical interaction PubMed 15598887PubMed 21252119. Source: RGD

antigen binding

Inferred from direct assay PubMed 8985331PubMed 9252373. Source: RGD

bHLH transcription factor binding

Inferred from physical interaction PubMed 11466227. Source: RGD

chromatin DNA binding

Inferred from direct assay PubMed 20702579. Source: RGD

chromatin binding

Inferred from direct assay PubMed 23652932. Source: RGD

core promoter binding

Inferred from direct assay PubMed 21307242. Source: RGD

core promoter proximal region DNA binding

Inferred from direct assay PubMed 19057620. Source: RGD

glucocorticoid receptor binding

Inferred from direct assay PubMed 17884810. Source: RGD

histone acetyltransferase activity

Inferred from direct assay PubMed 21307242. Source: RGD

lysine N-acetyltransferase activity

Inferred from mutant phenotype PubMed 12724418. Source: RGD

mitogen-activated protein kinase binding

Inferred from physical interaction PubMed 10363932. Source: RGD

p53 binding

Inferred from physical interaction PubMed 21792911. 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

protein kinase binding

Inferred from physical interaction PubMed 19088076. Source: RGD

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from direct assay PubMed 15117818. Source: RGD

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q91XT0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F12C37E246848407

FASTA35336,049
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
UniGeneRn.12447.
Rn.232499.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000206; ENSRNOP00000000206; ENSRNOG00000000190.
UCSCRGD:620036. rat.

Organism-specific databases

RGD620036. Ep300.

Phylogenomic databases

GeneTreeENSGT00730000110623.
HOGENOMHOG000111353.
HOVERGENHBG074064.
InParanoidQ91XT0.
OMAEHRASSM.
TreeFamTF101097.

Gene expression databases

GenevestigatorQ91XT0.

Family and domain databases

ProtoNetSearch...

Other

NextBio35576275.

Entry information

Entry nameQ91XT0_RAT
AccessionPrimary (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: April 16, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)