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Q09472

- EP300_HUMAN

UniProt

Q09472 - EP300_HUMAN

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Protein

Histone acetyltransferase p300

Gene

EP300

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity.17 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei31 – 322Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A
Metal bindingi347 – 3471Zinc 1
Metal bindingi351 – 3511Zinc 1
Metal bindingi364 – 3641Zinc 1
Metal bindingi369 – 3691Zinc 1
Metal bindingi378 – 3781Zinc 2
Metal bindingi382 – 3821Zinc 2
Metal bindingi388 – 3881Zinc 2
Metal bindingi393 – 3931Zinc 2
Metal bindingi402 – 4021Zinc 3
Metal bindingi406 – 4061Zinc 3
Metal bindingi411 – 4111Zinc 3
Metal bindingi414 – 4141Zinc 3
Binding sitei1457 – 14571Acetyl-CoA; via carbonyl oxygen1 Publication
Binding sitei1462 – 14621Acetyl-CoA1 Publication
Binding sitei1466 – 14661Acetyl-CoA1 Publication
Sitei2088 – 20881Interaction with NCOA2
Sitei2142 – 21421Interaction with NCOA2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri331 – 41787TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1664 – 170744ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1728 – 180982TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. activating transcription factor binding Source: UniProtKB
  3. androgen receptor binding Source: BHF-UCL
  4. beta-catenin binding Source: BHF-UCL
  5. chromatin binding Source: UniProtKB
  6. chromatin DNA binding Source: Ensembl
  7. core promoter binding Source: UniProtKB
  8. DNA binding Source: UniProtKB
  9. histone acetyltransferase activity Source: UniProtKB
  10. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  11. nuclear hormone receptor binding Source: UniProtKB
  12. pre-mRNA intronic binding Source: Ensembl
  13. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  14. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  15. transcription coactivator activity Source: UniProtKB
  16. transcription factor binding Source: UniProtKB
  17. transferase activity, transferring acyl groups Source: UniProtKB
  18. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cellular response to hypoxia Source: Reactome
  3. chromatin organization Source: Reactome
  4. circadian rhythm Source: UniProtKB
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. heart development Source: Ensembl
  7. histone H2B acetylation Source: UniProtKB
  8. histone H4 acetylation Source: UniProtKB
  9. innate immune response Source: Reactome
  10. internal peptidyl-lysine acetylation Source: UniProtKB
  11. internal protein amino acid acetylation Source: UniProtKB
  12. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  13. lung development Source: Ensembl
  14. mitotic cell cycle Source: Reactome
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. nervous system development Source: ProtInc
  17. Notch signaling pathway Source: Reactome
  18. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  19. organ morphogenesis Source: Ensembl
  20. positive regulation by host of viral transcription Source: BHF-UCL
  21. positive regulation of protein binding Source: Ensembl
  22. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  24. positive regulation of type I interferon production Source: Reactome
  25. regulation of androgen receptor signaling pathway Source: BHF-UCL
  26. regulation of cell cycle Source: Reactome
  27. regulation of transcription, DNA-templated Source: UniProtKB
  28. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  29. regulation of tubulin deacetylation Source: UniProtKB
  30. response to estrogen Source: UniProtKB
  31. response to hypoxia Source: UniProtKB
  32. skeletal muscle tissue development Source: Ensembl
  33. somitogenesis Source: Ensembl
  34. transcription, DNA-templated Source: UniProtKB-KW
  35. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
REACT_172610. HATs acetylate histones.
REACT_200624. Attenuation phase.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24941. Circadian Clock.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ09472.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase p300 (EC:2.3.1.483 Publications)
Short name:
p300 HAT
Alternative name(s):
E1A-associated protein p300
Gene namesi
Name:EP300
Synonyms:P300
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:3373. EP300.

Subcellular locationi

Cytoplasm. Nucleus
Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. histone acetyltransferase complex Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in EP300 may play a role in epithelial cancer.
Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A.
Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication
Mutagenesisi89 – 891S → D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. 1 Publication
Mutagenesisi344 – 3441L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345. 1 Publication
Mutagenesisi345 – 3451L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344. 1 Publication
Mutagenesisi371 – 3766TMKNVL → NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2. 1 Publication
Mutagenesisi413 – 4186VCLPLK → NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. 1 Publication
Mutagenesisi1020 – 10201K → A: Abolishes sumoylation and transcriptional repression when associated with A-1024. 2 Publications
Mutagenesisi1020 – 10201K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1024. 2 Publications
Mutagenesisi1024 – 10241K → A: Abolishes sumoylation and transcriptional repression; when associated with A-1020. 2 Publications
Mutagenesisi1024 – 10241K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1020. 2 Publications
Mutagenesisi1170 – 11701F → E: Increased acetyltransferase activity. 1 Publication
Mutagenesisi1204 – 12041C → R: Increased acetyltransferase activity. 1 Publication
Mutagenesisi1242 – 12421E → K: Increased acetyltransferase activity. 1 Publication
Mutagenesisi1357 – 13571T → L: 40% decrease in activity. 1 Publication
Mutagenesisi1357 – 13571T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. 1 Publication
Mutagenesisi1396 – 13961S → R: Loss of activity; when associated with R-1397. 1 Publication
Mutagenesisi1396 – 13961S → W: Loss of activity; when associated with W-1396. 1 Publication
Mutagenesisi1397 – 13971Y → R: Loss of activity; when associated with R-1396. 1 Publication
Mutagenesisi1397 – 13971Y → W: Loss of activity; when associated with W-1397. 1 Publication
Mutagenesisi1399 – 13991D → Y: Abolishes autoacetylation. Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. 3 Publications
Mutagenesisi1467 – 14671Y → F: Abolishes autoacetylation. Loss of acetyltransferase activity. 1 Publication
Mutagenesisi1505 – 15051E → R: 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628. 1 Publication
Mutagenesisi1625 – 16251D → R: 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628. 1 Publication
Mutagenesisi1628 – 16281D → R: 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625. 1 Publication
Mutagenesisi1645 – 16462RR → EE: Increased acetyltransferase activity. 1 Publication
Mutagenesisi2056 – 20561R → K: No effect on interaction with NCOA2. 1 Publication
Mutagenesisi2088 – 20881R → K: Abolishes interaction with NCOA2. 1 Publication
Mutagenesisi2142 – 21421R → K: Strongly reduces interaction with NCOA2. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613684. phenotype.
Orphaneti353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
PharmGKBiPA27807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 24142413Histone acetyltransferase p300PRO_0000211193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei89 – 891Phosphoserine; by AMPK2 Publications
Modified residuei285 – 2851Phosphoserine
Modified residuei418 – 4181N6-acetyllysine1 Publication
Modified residuei423 – 4231N6-acetyllysine1 Publication
Modified residuei580 – 5801Omega-N-methylated arginine; by CARM11 Publication
Modified residuei604 – 6041Omega-N-methylated arginine; by CARM11 Publication
Modified residuei636 – 6361N6-acetyllysine1 Publication
Modified residuei885 – 8851Phosphothreonine
Modified residuei887 – 8871Phosphothreonine
Modified residuei977 – 9771N6-acetyllysine1 Publication
Modified residuei1020 – 10201N6-acetyllysine; alternate1 Publication
Cross-linki1020 – 1020Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei1024 – 10241N6-acetyllysine; alternate1 Publication
Cross-linki1024 – 1024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei1038 – 10381Phosphoserine1 Publication
Modified residuei1180 – 11801N6-acetyllysineBy similarity
Modified residuei1336 – 13361N6-acetyllysine1 Publication
Modified residuei1473 – 14731N6-acetyllysine1 Publication
Modified residuei1499 – 14991N6-acetyllysine; by autocatalysis1 Publication
Modified residuei1542 – 15421N6-acetyllysine2 Publications
Modified residuei1546 – 15461N6-acetyllysine2 Publications
Modified residuei1549 – 15491N6-acetyllysine; by autocatalysis2 Publications
Modified residuei1554 – 15541N6-acetyllysine; by autocatalysis2 Publications
Modified residuei1555 – 15551N6-acetyllysine1 Publication
Modified residuei1558 – 15581N6-acetyllysine2 Publications
Modified residuei1560 – 15601N6-acetyllysine; by autocatalysis2 Publications
Modified residuei1583 – 15831N6-acetyllysine1 Publication
Modified residuei1699 – 16991N6-acetyllysine1 Publication
Modified residuei1704 – 17041N6-acetyllysine1 Publication
Modified residuei1707 – 17071N6-acetyllysine1 Publication
Modified residuei1734 – 17341Phosphoserine
Modified residuei1857 – 18571Phosphothreonine
Modified residuei1859 – 18591Phosphothreonine
Modified residuei2142 – 21421Asymmetric dimethylarginine; by CARM1; alternate1 Publication
Modified residuei2142 – 21421Citrulline; by PADI4; alternate1 Publication

Post-translational modificationi

Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-1699, Lys-1704 and Lys-1707.9 Publications
Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.2 Publications
Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1.2 Publications
Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.2 Publications
Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation.
Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG.5 Publications

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ09472.
PaxDbiQ09472.
PRIDEiQ09472.

PTM databases

PhosphoSiteiQ09472.

Expressioni

Gene expression databases

BgeeiQ09472.
CleanExiHS_EP300.
ExpressionAtlasiQ09472. baseline and differential.
GenevestigatoriQ09472.

Organism-specific databases

HPAiCAB000146.
HPA003128.
HPA004112.

Interactioni

Subunit structurei

Interacts with phosphorylated CREB1. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). Binds to HIPK2. Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity. Interacts with FOXO1; the interaction acetylates FOXO1 and enhances its transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and isoform 5. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C.57 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-447295,EBI-617698From a different organism.
P032553EBI-447295,EBI-2603114From a different organism.
P03255-23EBI-447295,EBI-6859460From a different organism.
P032593EBI-447295,EBI-6947456From a different organism.
APEX1P276958EBI-447295,EBI-1048805
ASH2LQ9UBL35EBI-447295,EBI-540797
BRD7Q9NPI13EBI-447295,EBI-711221
CDK2P249415EBI-447295,EBI-375096
CITED2Q999673EBI-447295,EBI-937732
COPS2P612012EBI-447295,EBI-1050386
CREB1P162202EBI-447295,EBI-711855
Creb1Q011472EBI-447295,EBI-2291098From a different organism.
DDX5P178444EBI-447295,EBI-351962
E2P031223EBI-447295,EBI-7028618From a different organism.
E2P064227EBI-447295,EBI-7136851From a different organism.
E2P067906EBI-447295,EBI-7010629From a different organism.
ESR1P033722EBI-447295,EBI-78473
GTF2BQ004032EBI-447295,EBI-389564
HIF1AQ1666515EBI-447295,EBI-447269
Hif1aQ612212EBI-447295,EBI-298954From a different organism.
HIPK2Q9H2X64EBI-447295,EBI-348345
JmyQ9QXM116EBI-447295,EBI-866001From a different organism.
KAT2BQ928312EBI-447295,EBI-477430
NAP1L1P552093EBI-447295,EBI-356392
NBNO609345EBI-447295,EBI-494844
NCOA3Q9Y6Q92EBI-447295,EBI-81196
POU3F2P202653EBI-447295,EBI-1167176
PPP1R13BQ96KQ42EBI-447295,EBI-1105153
PPP1R13LQ8WUF52EBI-447295,EBI-5550163
RUNX3Q137617EBI-447295,EBI-925990
SIRT1Q96EB62EBI-447295,EBI-1802965
SKP2Q133093EBI-447295,EBI-456291
STAT6P422262EBI-447295,EBI-1186478
TFAP2AP055497EBI-447295,EBI-347351
TP53P0463710EBI-447295,EBI-366083
TP53BP2Q136252EBI-447295,EBI-77642
VDRP114733EBI-447295,EBI-286357
YBX1P678092EBI-447295,EBI-354065

Protein-protein interaction databases

BioGridi108347. 393 interactions.
DIPiDIP-257N.
IntActiQ09472. 170 interactions.
MINTiMINT-104535.
STRINGi9606.ENSP00000263253.

Structurei

Secondary structure

1
2414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi332 – 3343
Helixi335 – 35521
Turni356 – 3583
Helixi367 – 37913
Beta strandi386 – 3894
Helixi391 – 40515
Beta strandi408 – 4103
Helixi414 – 4185
Helixi1051 – 106616
Turni1069 – 10724
Helixi1073 – 10753
Helixi1081 – 10844
Helixi1089 – 10924
Helixi1099 – 11079
Helixi1114 – 113118
Helixi1137 – 115923
Beta strandi1178 – 11825
Beta strandi1190 – 11945
Turni1195 – 11973
Beta strandi1198 – 12014
Helixi1202 – 12065
Beta strandi1212 – 12143
Beta strandi1218 – 12214
Beta strandi1225 – 12273
Helixi1228 – 12303
Beta strandi1231 – 12366
Beta strandi1244 – 12463
Turni1248 – 12503
Beta strandi1253 – 12553
Helixi1256 – 12594
Turni1263 – 12653
Helixi1273 – 12775
Turni1278 – 12803
Helixi1297 – 131317
Beta strandi1321 – 133414
Helixi1339 – 13424
Turni1343 – 13475
Beta strandi1351 – 136616
Beta strandi1369 – 138113
Beta strandi1392 – 14009
Helixi1407 – 14093
Helixi1410 – 142819
Beta strandi1432 – 14365
Beta strandi1446 – 14505
Helixi1460 – 147617
Beta strandi1482 – 14854
Helixi1486 – 14938
Helixi1498 – 15003
Helixi1508 – 151710
Helixi1582 – 15909
Helixi1592 – 15943
Beta strandi1595 – 16017
Helixi1603 – 16064
Helixi1622 – 16243
Beta strandi1625 – 16273
Helixi1628 – 16369
Helixi1644 – 166219
Helixi1730 – 174718
Helixi1756 – 177015
Turni1774 – 17785
Helixi1780 – 179314
Helixi1806 – 181813

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L3ENMR-B323-423[»]
1P4QNMR-B323-423[»]
2K8FNMR-A1723-1812[»]
3BIYX-ray1.70A1287-1666[»]
3I3JX-ray2.33A/B/C/D/E/F/G/H/I/J/K/L1040-1161[»]
3IO2X-ray2.50A1723-1836[»]
3P57X-ray2.19P1726-1835[»]
3T92X-ray1.50A1723-1818[»]
4BHWX-ray2.80A/B1043-1519[»]
A/B1581-1666[»]
4PZRX-ray2.10A1287-1664[»]
4PZSX-ray1.94A1287-1664[»]
4PZTX-ray2.80A1287-1664[»]
DisProtiDP00633.
ProteinModelPortaliQ09472.
SMRiQ09472. Positions 323-423, 566-646, 1046-1713, 1726-1834, 2050-2092.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini566 – 64580KIXPROSITE-ProRule annotationAdd
BLAST
Domaini1067 – 113973BromoPROSITE-ProRule annotationAdd
BLAST
Domaini1287 – 1663377CBP/p300-type HATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 149148Interaction with RORAAdd
BLAST
Regioni2 – 139138Interaction with ALX1Add
BLAST
Regioni1017 – 102913CRD1; mediates transcriptional repressionAdd
BLAST
Regioni1397 – 13993Interaction with histone1 Publication
Regioni1398 – 14003Acetyl-CoA binding1 Publication
Regioni1410 – 14112Acetyl-CoA binding1 Publication
Regioni1572 – 1818247Binding region for E1A adenovirusAdd
BLAST
Regioni2003 – 2212210Interaction with HTLV-1 TaxAdd
BLAST
Regioni2041 – 2240200Interaction with NCOA2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 177Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi797 – 8004Poly-Ser
Compositional biasi1519 – 15268Poly-Glu
Compositional biasi2066 – 20694Poly-Gln
Compositional biasi2190 – 21956Poly-Gln

Domaini

The CRD1 domain (cell cycle regulatory domain 1) mediates transcriptional repression of a subset of p300 responsive genes; it can be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It conatins sumoylation and acetylation sites and the same lysine residues may be targeted for the respective modifications. It is proposed that deacetylation by SIRT1 allows sumoylation leading to suppressed activity.

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 CBP/p300-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation
Contains 1 KIX domain.PROSITE-ProRule annotation
Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri331 – 41787TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1664 – 170744ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1728 – 180982TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiQ09472.
KOiK04498.
OMAiPTMIRGS.
OrthoDBiEOG75B84F.
PhylomeDBiQ09472.
TreeFamiTF101097.

Family and domain databases

Gene3Di1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProiIPR001487. 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]
PfamiPF00439. 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]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51727. CBP_P300_HAT. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q09472-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS
60 70 80 90 100
TELGLTNGGD INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP
110 120 130 140 150
GQVMASQAQQ SSPGLGLINS MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS
160 170 180 190 200
TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA GNGQGIMPNQ VMNGSIGAGR
210 220 230 240 250
GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ PLKMGMMNNP
260 270 280 290 300
NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP
310 320 330 340 350
NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK
360 370 380 390 400
CQRREQANGE VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII
410 420 430 440 450
SHWKNCTRHD CPVCLPLKNA GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA
460 470 480 490 500
PNLSTVSQID PSSIERAYAA LGLPYQVNQM PTQPQVQAKN QQNQQPGQSP
510 520 530 540 550
QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ NPMMSENASV
560 570 580 590 600
PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL
610 620 630 640 650
KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT
660 670 680 690 700
RLQKQNMLPN AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN
710 720 730 740 750
QMMPRITPQS GLNQFGQMSM AQPPIVPRQT PPLQHHGQLA QPGALNPPMG
760 770 780 790 800
YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI PLAPSSGQAP VSQAQMSSSS
810 820 830 840 850
CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP TPHHTPPSIG
860 870 880 890 900
AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS
910 920 930 940 950
LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ
960 970 980 990 1000
VSNPPSTSST EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES
1010 1020 1030 1040 1050
KVEDCKMEST ETEERSTELK TEIKEEEDQP STSATQSSPA PGQSKKKIFK
1060 1070 1080 1090 1100
PEELRQALMP TLEALYRQDP ESLPFRQPVD PQLLGIPDYF DIVKSPMDLS
1110 1120 1130 1140 1150
TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK YCSKLSEVFE
1160 1170 1180 1190 1200
QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF
1210 1220 1230 1240 1250
CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC
1260 1270 1280 1290 1300
GRKMHQICVL HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT
1310 1320 1330 1340 1350
FLENRVNDFL RRQNHPESGE VTVRVVHASD KTVEVKPGMK ARFVDSGEMA
1360 1370 1380 1390 1400
ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE YGSDCPPPNQ RRVYISYLDS
1410 1420 1430 1440 1450
VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP SEGDDYIFHC
1460 1470 1480 1490 1500
HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE
1510 1520 1530 1540 1550
LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK
1560 1570 1580 1590 1600
KNNKKTSKNK SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL
1610 1620 1630 1640 1650
IAGPAANSLP PIVDPDPLIP CDLMDGRDAF LTLARDKHLE FSSLRRAQWS
1660 1670 1680 1690 1700
TMCMLVELHT QSQDRFVYTC NECKHHVETR WHCTVCEDYD LCITCYNTKN
1710 1720 1730 1740 1750
HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ SLVHACQCRN
1760 1770 1780 1790 1800
ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK
1810 1820 1830 1840 1850
CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP
1860 1870 1880 1890 1900
TPATPTTPTG QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK
1910 1920 1930 1940 1950
AAGQVTPPTP PQTAQPPLPG PPPAAVEMAM QIQRAAETQR QMAHVQIFQR
1960 1970 1980 1990 2000
PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL EPGMGPTGMQ QQPPWSQGGL
2010 2020 2030 2040 2050
PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP LKPGTVSQQA
2060 2070 2080 2090 2100
LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI
2110 2120 2130 2140 2150
PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP
2160 2170 2180 2190 2200
QQQLQPPMGG MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG
2210 2220 2230 2240 2250
IGPGMANHNQ FQQPQGVGYP PQQQQRMQHH MQQMQQGNMG QIGQLPQALG
2260 2270 2280 2290 2300
AEAGASLQAY QQRLLQQQMG SPVQPNPMSP QQHMLPNQAQ SPHLQGQQIP
2310 2320 2330 2340 2350
NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV SPQTSSPHPG
2360 2370 2380 2390 2400
LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS
2410
DLNSNLSQST LDIH
Length:2,414
Mass (Da):264,161
Last modified:February 10, 2009 - v2
Checksum:i8E869E1F174A6FEB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691M → T in AAA18639. (PubMed:7523245)Curated
Sequence conflicti204 – 2041N → D in AAA18639. (PubMed:7523245)Curated
Sequence conflicti928 – 9281T → N in AAA18639. (PubMed:7523245)Curated
Sequence conflicti1924 – 19241A → T in AAA18639. (PubMed:7523245)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti289 – 2891M → V.
Corresponds to variant rs2230111 [ dbSNP | Ensembl ].
VAR_055554
Natural varianti827 – 8271L → P in a breast cancer sample. 1 Publication
VAR_014428
Natural varianti997 – 9971I → V.
Corresponds to variant rs20551 [ dbSNP | Ensembl ].
VAR_020425
Natural varianti1013 – 10131E → G in a breast cancer sample. 1 Publication
VAR_014429
Natural varianti1650 – 16501S → Y in a pancreatic cancer sample. 1 Publication
VAR_014430
Natural varianti2174 – 21741T → S.
Corresponds to variant rs5758252 [ dbSNP | Ensembl ].
VAR_038376
Natural varianti2221 – 22211P → Q in a colorectal cancer sample. 1 Publication
Corresponds to variant rs28937578 [ dbSNP | Ensembl ].
VAR_014431
Natural varianti2223 – 22231Q → P.1 Publication
Corresponds to variant rs1046088 [ dbSNP | Ensembl ].
VAR_038377

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01877 mRNA. Translation: AAA18639.1.
AL080243, AL035658, AL096765 Genomic DNA. Translation: CAH70384.1.
AL096765, AL035658, AL080243 Genomic DNA. Translation: CAH73688.1.
AL035658, AL080243, AL096765 Genomic DNA. Translation: CAI23037.1.
CH471095 Genomic DNA. Translation: EAW60408.1.
CCDSiCCDS14010.1.
PIRiA54277.
RefSeqiNP_001420.2. NM_001429.3.
UniGeneiHs.517517.
Hs.655211.

Genome annotation databases

EnsembliENST00000263253; ENSP00000263253; ENSG00000100393.
GeneIDi2033.
KEGGihsa:2033.
UCSCiuc003azl.4. human.

Polymorphism databases

DMDMi223590203.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

P300/CBP entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01877 mRNA. Translation: AAA18639.1 .
AL080243 , AL035658 , AL096765 Genomic DNA. Translation: CAH70384.1 .
AL096765 , AL035658 , AL080243 Genomic DNA. Translation: CAH73688.1 .
AL035658 , AL080243 , AL096765 Genomic DNA. Translation: CAI23037.1 .
CH471095 Genomic DNA. Translation: EAW60408.1 .
CCDSi CCDS14010.1.
PIRi A54277.
RefSeqi NP_001420.2. NM_001429.3.
UniGenei Hs.517517.
Hs.655211.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L3E NMR - B 323-423 [» ]
1P4Q NMR - B 323-423 [» ]
2K8F NMR - A 1723-1812 [» ]
3BIY X-ray 1.70 A 1287-1666 [» ]
3I3J X-ray 2.33 A/B/C/D/E/F/G/H/I/J/K/L 1040-1161 [» ]
3IO2 X-ray 2.50 A 1723-1836 [» ]
3P57 X-ray 2.19 P 1726-1835 [» ]
3T92 X-ray 1.50 A 1723-1818 [» ]
4BHW X-ray 2.80 A/B 1043-1519 [» ]
A/B 1581-1666 [» ]
4PZR X-ray 2.10 A 1287-1664 [» ]
4PZS X-ray 1.94 A 1287-1664 [» ]
4PZT X-ray 2.80 A 1287-1664 [» ]
DisProti DP00633.
ProteinModelPortali Q09472.
SMRi Q09472. Positions 323-423, 566-646, 1046-1713, 1726-1834, 2050-2092.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108347. 393 interactions.
DIPi DIP-257N.
IntActi Q09472. 170 interactions.
MINTi MINT-104535.
STRINGi 9606.ENSP00000263253.

Chemistry

BindingDBi Q09472.
ChEMBLi CHEMBL3784.
GuidetoPHARMACOLOGYi 2735.

PTM databases

PhosphoSitei Q09472.

Polymorphism databases

DMDMi 223590203.

Proteomic databases

MaxQBi Q09472.
PaxDbi Q09472.
PRIDEi Q09472.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263253 ; ENSP00000263253 ; ENSG00000100393 .
GeneIDi 2033.
KEGGi hsa:2033.
UCSCi uc003azl.4. human.

Organism-specific databases

CTDi 2033.
GeneCardsi GC22P041487.
GeneReviewsi EP300.
H-InvDB HIX0203186.
HGNCi HGNC:3373. EP300.
HPAi CAB000146.
HPA003128.
HPA004112.
MIMi 602700. gene.
613684. phenotype.
neXtProti NX_Q09472.
Orphaneti 353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
PharmGKBi PA27807.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119206.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.
InParanoidi Q09472.
KOi K04498.
OMAi PTMIRGS.
OrthoDBi EOG75B84F.
PhylomeDBi Q09472.
TreeFami TF101097.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
REACT_172610. HATs acetylate histones.
REACT_200624. Attenuation phase.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24941. Circadian Clock.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q09472.

Miscellaneous databases

ChiTaRSi EP300. human.
EvolutionaryTracei Q09472.
GeneWikii EP300.
GenomeRNAii 2033.
NextBioi 8251.
PROi Q09472.
SOURCEi Search...

Gene expression databases

Bgeei Q09472.
CleanExi HS_EP300.
ExpressionAtlasi Q09472. baseline and differential.
Genevestigatori Q09472.

Family and domain databases

Gene3Di 1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProi 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 ]
Pfami 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 ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51727. CBP_P300_HAT. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor."
    Eckner R., Ewen M.E., Newsome D., Gerdes M., Decaprio J.A., Lawrence J.B., Livingston D.M.
    Genes Dev. 8:869-884(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-2223.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, CHROMOSOMAL TRANSLOCATION WITH KAT6A.
  5. "Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP."
    Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H.
    Nature 374:85-88(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
  6. "A transcriptional switch mediated by cofactor methylation."
    Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
    Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT ARG-580 AND ARG-604, FUNCTION.
  7. "The transcriptional coactivators p300 and CBP are histone acetyltransferases."
    Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.
    Cell 87:953-959(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  8. "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A."
    Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.
    Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCAF.
  9. Cited for: INTERACTION WITH HIF1A AND CREBBP.
  10. "Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300."
    Bex F., Yin M.-J., Burny A., Gaynor R.B.
    Mol. Cell. Biol. 18:2392-2405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  11. "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
    Fryer C.J., Archer T.K.
    Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1.
  12. Cited for: INTERACTION WITH HIV-1 TAT.
  13. "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1."
    Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L., Livingston D.M.
    Genes Dev. 13:64-75(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED2 AND HIF1A, MUTAGENESIS OF 371-THR--LEU-376 AND 413-VAL--LYS-418.
  14. "Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD."
    Lau P., Bailey P., Dowhan D.H., Muscat G.E.
    Nucleic Acids Res. 27:411-420(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RORA.
  15. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
    Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
    J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED1.
  16. "A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation."
    Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.
    Mol. Cell. Biol. 20:2676-2686(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION.
  17. Erratum
    Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.
    Mol. Cell. Biol. 20:5360-5360(2000)
  18. "Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle."
    Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.
    Mol. Cell. Biol. 20:8889-8902(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EID1.
  19. "A novel Rb- and p300-binding protein inhibits transactivation by MyoD."
    MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.
    Mol. Cell. Biol. 20:8903-8915(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EID1.
  20. "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator."
    Ko L., Cardona G.R., Chin W.W.
    Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  21. "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones."
    Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D., Lambert P., Li H., Lee C.-G., Kashanchi F.
    Virology 277:278-295(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  22. "Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein."
    Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., Isselbacher K.J., Brown M., Shioda T.
    Genes Dev. 15:2598-2612(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ESR1.
  23. "Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors."
    Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.
    J. Biol. Chem. 276:38341-38344(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-89, MUTAGENESIS OF SER-89, INTERACTION WITH PPARG.
  24. "Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription."
    Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E., Chrivia J., Yaciuk P.
    J. Virol. 75:10033-10040(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRCAP.
  25. "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation."
    Scoggin K.E.S., Ulloa A., Nyborg J.K.
    Mol. Cell. Biol. 21:5520-5530(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  26. "Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300."
    Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T., Lairmore M.D.
    J. Virol. 75:9885-9895(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
  27. "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression."
    Gizard F., Lavallee B., DeWitte F., Hum D.W.
    J. Biol. Chem. 276:33881-33892(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRERF1.
  28. "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha."
    Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R.
    J. Biol. Chem. 276:38272-38279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  29. Cited for: INTERACTION WITH DTX1.
  30. "Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300."
    Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O.
    Mol. Cell 7:1221-1231(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FEN1.
  31. "Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb."
    Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.
    Cell Growth Differ. 13:69-75(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIB.
  32. "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
    Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
    J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED4.
  33. "Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities."
    Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.
    Mol. Cell. Biol. 22:3621-3632(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
  34. "Acetylation inactivates the transcriptional repressor BCL6."
    Bereshchenko O.R., Gu W., Dalla-Favera R.
    Nat. Genet. 32:606-613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BCL6 ACETYLATION.
  35. "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."
    Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.
    Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ING4 AND ING5.
  36. "Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4."
    Hecht A., Stemmler M.P.
    J. Biol. Chem. 278:3776-3785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH TCF7L2 AND LEF1.
  37. "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
    Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
    J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CITED2 AND TFAP2A, MUTAGENESIS OF ASP-1399.
  38. Cited for: INTERACTION WITH SP3.
  39. "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain."
    Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.
    J. Bone Miner. Res. 18:1419-1429(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALX1.
  40. "SATB1 makes a complex with p300 and represses gp91(phox) promoter activity."
    Fujii Y., Kumatori A., Nakamura M.
    Microbiol. Immunol. 47:803-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SATB1.
  41. Cited for: SUMOYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
  42. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
    Rossow K.L., Janknecht R.
    Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5.
  43. "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53."
    An W., Kim J., Roeder R.G.
    Cell 117:735-748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53, FUNCTION.
  44. "Regulation of human SRY subcellular distribution by its acetylation/deacetylation."
    Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.
    EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  45. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
    Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
    J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
  46. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
    Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
    J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELF3.
  47. "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53."
    Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R., Ball K.L.
    Mol. Cell. Biol. 24:10083-10098(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRF1.
  48. Cited for: ACETYLATION AT LYS-1499; LYS-1549; LYS-1554; LYS-1558 AND LYS-1560.
  49. "Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD."
    Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S.
    Mol. Endocrinol. 18:776-790(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEUROD1 AND TCF3.
  50. "Dendrite development regulated by CREST, a calcium-regulated transcriptional activator."
    Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I., Cowan M., Ghosh A.
    Science 303:197-202(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SS18L1/CREST.
  51. "Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease."
    Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D., Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H., Hennekam R.C., Peters D.J.M.
    Am. J. Hum. Genet. 76:572-580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RSTS2.
  52. "SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1."
    Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T., Gu W., Pestell R.G.
    J. Biol. Chem. 280:10264-10276(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEACETYLATION BY SIRT1, ACETYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
  53. "The coactivator p300 directly acetylates the forkhead transcription factor Foxo1 and stimulates Foxo1-induced transcription."
    Perrot V., Rechler M.M.
    Mol. Endocrinol. 19:2283-2298(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXO1, FUNCTION, MUTAGENESIS OF ASP-1399.
  54. "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination."
    Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.
    Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH NCOA2, MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
  55. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ROCK2, PHOSPHORYLATION AT SER-89.
  56. "The transcriptional activity of CITED1 is regulated by phosphorylation in a cell cycle-dependent manner."
    Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T., de Caestecker M.P.
    J. Biol. Chem. 281:27426-27435(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED1.
  57. "Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation."
    Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A.
    J. Biol. Chem. 281:40292-40301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-1336 AND LYS-1473, IDENTIFICATION BY MASS SPECTROMETRY.
  58. "HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription."
    Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., Hendarwanto A., Martinez E.D., Chen Y., Lu H., Adkins N.L., Stavreva D.A., Wiench M., Georgel P.T., Schiltz R.L., Hager G.L.
    Mol. Cell 22:669-679(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLATION OF HDAC1.
  59. "Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
    Hung J.J., Wang Y.T., Chang W.C.
    Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP1.
  60. Cited for: FUNCTION, INTERACTION WITH MTA1.
  61. Erratum
    Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.
    Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013)
  62. "Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
    Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
    J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDIT3.
  63. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
    Shin S., Janknecht R.
    J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX17.
  64. Cited for: FUNCTION IN ACETYLATION OF SIRT2.
  65. "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis."
    Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.
    Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY HIPK2.
  66. "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation."
    Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.
    Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FBXO3-MEDIATED DEGRADATION.
  67. "The SIRT2 deacetylase regulates autoacetylation of p300."
    Black J.C., Mosley A., Kitada T., Washburn M., Carey M.
    Mol. Cell 32:449-455(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-418; LYS-423; LYS-1542; LYS-1546; LYS-1549; LYS-1699; LYS-1704 AND LYS-1707, DEACETYLATION BY SIRT2, FUNCTION IN TRANSCRIPTIONAL REGULATION.
  68. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  69. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  70. "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation."
    Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.
    EMBO J. 28:2748-2762(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SENP3, SUMOYLATION.
  71. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  72. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-1542; LYS-1546; LYS-1554; LYS-1555; LYS-1558; LYS-1560 AND LYS-1583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  73. "Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex required for phenylephrine-induced hypertrophy in cardiomyocytes."
    Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T., Fujita M., Shimatsu A., Kita T., Hasegawa K.
    J. Biol. Chem. 285:9556-9568(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH CCNT1; CDK9 AND GATA4.
  74. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  75. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  76. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  77. "Human ALKBH4 interacts with proteins associated with transcription."
    Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
    PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALKBH4.
  78. "Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
    Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
    Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  79. Cited for: FUNCTION AS ACETYLTRANSFERASE OF H3K27.
  80. Cited for: INTERACTION WITH KLF15.
  81. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
    Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
    Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC4 AND HDAC5.
  82. "Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform."
    Rack J.G., Vanlinden M.R., Lutter T., Aasland R., Ziegler M.
    J. Mol. Biol. 426:1677-1691(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH EP300.
  83. "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha."
    Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M., Wagner G., Eck M.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH HIF1A PEPTIDE AND ZINC IONS.
  84. "Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2."
    Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.
    Nat. Struct. Biol. 10:504-512(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 323-423 IN COMPLEX WITH 216-259 OF CITED2 AND ZINC IONS, INTERACTION WITH CITED2, MUTAGENESIS OF LEU-344 AND LEU-345.
  85. "The structural basis of protein acetylation by the p300/CBP transcriptional coactivator."
    Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R., Cole P.A.
    Nature 451:846-850(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH LYS-COA, MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505; ASP-1625 AND ASP-1628.
  86. "Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation."
    Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J., Cherry S., Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y.
    Structure 17:202-210(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1723-1812, INTERACTION WITH TP53.
  87. Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1040-1161.
  88. "Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation."
    Delvecchio M., Gaucher J., Aguilar-Gurrieri C., Ortega E., Panne D.
    Nat. Struct. Mol. Biol. 20:1040-1046(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1043-1519 AND 1581-1666 OF MUTANT PHE-1467 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION, AUTOACETYLATION, MUTAGENESIS OF PHE-1170; CYS-1204; GLU-1242; ASP-1399; TYR-1467 AND 1645-ARG-ARG-1646.
  89. "Structure of the p300 histone acetyltransferase bound to acetyl-coenzyme A and its analogues."
    Maksimoska J., Segura-Pena D., Cole P.A., Marmorstein R.
    Biochemistry 53:3415-3422(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1287-1664 OF MUTANT PHE-1467 IN COMPLEX WITH ACETYL-COA AND COENZYME A.
  90. Cited for: VARIANTS PRO-827; GLY-1013; TYR-1650 AND GLN-2221, POSSIBLE INVOLVEMENT IN CANCER.

Entry informationi

Entry nameiEP300_HUMAN
AccessioniPrimary (citable) accession number: Q09472
Secondary accession number(s): B1AKC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 10, 2009
Last modified: October 29, 2014
This is version 191 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3