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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 transcript leveli

Functioni

GO - Molecular functioni

  1. activating transcription factor binding Source: RGD
  2. antigen binding Source: RGD
  3. bHLH transcription factor binding Source: RGD
  4. chromatin binding Source: RGD
  5. chromatin DNA binding Source: RGD
  6. core promoter binding Source: RGD
  7. core promoter proximal region DNA binding Source: RGD
  8. glucocorticoid receptor binding Source: RGD
  9. histone acetyltransferase activity Source: RGD
  10. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: RGD
  11. mitogen-activated protein kinase binding Source: RGD
  12. NF-kappaB binding Source: RGD
  13. p53 binding Source: RGD
  14. peroxisome proliferator activated receptor binding Source: RGD
  15. protein antigen binding Source: RGD
  16. protein complex binding Source: RGD
  17. protein kinase binding Source: RGD
  18. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: RGD
  19. SMAD binding Source: RGD
  20. transcription factor binding Source: RGD

GO - Biological processi

  1. cellular response to antibiotic Source: RGD
  2. cellular response to cAMP Source: RGD
  3. cellular response to dexamethasone stimulus Source: RGD
  4. cellular response to drug Source: RGD
  5. cellular response to glucose stimulus Source: RGD
  6. cellular response to hydrogen peroxide Source: RGD
  7. cellular response to mineralocorticoid stimulus Source: RGD
  8. cellular response to nerve growth factor stimulus Source: RGD
  9. cellular response to organic cyclic compound Source: RGD
  10. cellular response to retinoic acid Source: RGD
  11. cellular response to trichostatin A Source: RGD
  12. digestive tract development Source: RGD
  13. histone acetylation Source: RGD
  14. histone H3 acetylation Source: RGD
  15. internal peptidyl-lysine acetylation Source: RGD
  16. liver development Source: RGD
  17. memory Source: RGD
  18. negative regulation of cell death Source: RGD
  19. negative regulation of cellular metabolic process Source: RGD
  20. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  21. negative regulation of miRNA metabolic process Source: RGD
  22. positive regulation of axon extension Source: RGD
  23. positive regulation of cell death Source: RGD
  24. positive regulation of cell growth Source: RGD
  25. positive regulation of cell size Source: RGD
  26. positive regulation of cellular metabolic process Source: RGD
  27. positive regulation of collagen biosynthetic process Source: RGD
  28. positive regulation of DNA binding Source: RGD
  29. positive regulation of gene expression Source: RGD
  30. positive regulation of glycoprotein biosynthetic process Source: RGD
  31. positive regulation of histone acetylation Source: RGD
  32. positive regulation of muscle atrophy Source: RGD
  33. positive regulation of protein acetylation Source: RGD
  34. positive regulation of protein import into nucleus, translocation Source: RGD
  35. positive regulation of protein phosphorylation Source: RGD
  36. positive regulation of protein secretion Source: RGD
  37. positive regulation of proteolysis Source: RGD
  38. positive regulation of sarcomere organization Source: RGD
  39. positive regulation of sequence-specific DNA binding transcription factor activity Source: RGD
  40. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  41. positive regulation of translation Source: RGD
  42. protein-DNA complex assembly Source: RGD
  43. protein kinase B signaling Source: RGD
  44. regulation of angiotensin metabolic process Source: RGD
  45. response to calcium ion Source: RGD
  46. response to cobalt ion Source: RGD
  47. response to dexamethasone Source: RGD
  48. response to drug Source: RGD
  49. response to estrogen Source: RGD
  50. response to ethanol Source: RGD
  51. response to fatty acid Source: RGD
  52. response to glucose Source: RGD
  53. response to hydrogen peroxide Source: RGD
  54. response to hypoxia Source: RGD
  55. response to organic cyclic compound Source: RGD
  56. response to retinoic acid Source: RGD
  57. response to tumor necrosis factor Source: RGD
Complete GO annotation...

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

  1. chromatin Source: RGD
  2. cytoplasm Source: RGD
  3. nucleus Source: RGD
  4. protein-DNA complex Source: RGD
  5. transcription factor complex Source: RGD
Complete GO annotation...

Expressioni

Gene expression databases

GenevestigatoriQ91XT0.

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...

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.

Miscellaneous databases

NextBioi35576275.

Gene expression databases

GenevestigatoriQ91XT0.

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: April 29, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.