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Protein

Histone acetyltransferase p300

Gene

EP300

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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 (PubMed:10733570, PubMed:11430825, PubMed:11701890, PubMed:12402037, PubMed:12586840, PubMed:12929931, PubMed:14645221, PubMed:15186775, PubMed:15890677, PubMed:16617102, PubMed:16762839, PubMed:18722353, PubMed:18995842, PubMed:23415232, PubMed:23911289, PubMed:23934153, PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D.1 Publication19 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

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

  • acetyltransferase activity Source: UniProtKB
  • activating transcription factor binding Source: UniProtKB
  • androgen receptor binding Source: BHF-UCL
  • antigen binding Source: Ensembl
  • beta-catenin binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: Ensembl
  • core promoter binding Source: UniProtKB
  • damaged DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • peptide N-acetyltransferase activity Source: Reactome
  • pre-mRNA intronic binding Source: Ensembl
  • protein C-terminus binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: Ensembl
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transferase activity, transferring acyl groups Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

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

BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2197563. NOTCH2 intracellular domain regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3371568. Attenuation phase.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400253. Circadian Clock.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ09472.
SIGNORiQ09472.

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
Proteomesi
  • UP000005640 Componenti: 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

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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613684

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei31 – 322Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiEP300.
MIMi613684. phenotype.
Orphaneti353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
PharmGKBiPA27807.

Chemistry

ChEMBLiCHEMBL3784.
GuidetoPHARMACOLOGYi2735.

Polymorphism and mutation databases

BioMutaiEP300.
DMDMi223590203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 24142413Histone acetyltransferase p300PRO_0000211193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei89 – 891Phosphoserine; by AMPK2 Publications
Modified residuei418 – 4181N6-acetyllysine1 Publication
Modified residuei423 – 4231N6-acetyllysine1 Publication
Modified residuei499 – 4991PhosphoserineBy similarity
Modified residuei580 – 5801Omega-N-methylated arginine; by CARM11 Publication
Modified residuei604 – 6041Omega-N-methylated arginine; by CARM11 Publication
Modified residuei636 – 6361N6-acetyllysineCombined sources
Modified residuei977 – 9771N6-acetyllysineCombined sources
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 – 10381PhosphoserineCombined sources
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-acetyllysineCombined sources1 Publication
Modified residuei1546 – 15461N6-acetyllysineCombined sources1 Publication
Modified residuei1549 – 15491N6-acetyllysine; by autocatalysis2 Publications
Modified residuei1554 – 15541N6-acetyllysine; by autocatalysisCombined sources1 Publication
Modified residuei1555 – 15551N6-acetyllysineCombined sources
Modified residuei1558 – 15581N6-acetyllysineCombined sources1 Publication
Modified residuei1560 – 15601N6-acetyllysine; by autocatalysisCombined sources1 Publication
Modified residuei1583 – 15831N6-acetyllysineCombined sources
Modified residuei1699 – 16991N6-acetyllysine1 Publication
Modified residuei1704 – 17041N6-acetyllysine1 Publication
Modified residuei1707 – 17071N6-acetyllysine1 Publication
Modified residuei1726 – 17261PhosphoserineCombined sources
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-1707.6 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.4 Publications

Keywords - PTMi

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

Proteomic databases

EPDiQ09472.
MaxQBiQ09472.
PaxDbiQ09472.
PeptideAtlasiQ09472.
PRIDEiQ09472.

PTM databases

iPTMnetiQ09472.
PhosphoSiteiQ09472.

Expressioni

Gene expression databases

BgeeiENSG00000100393.
CleanExiHS_EP300.
GenevisibleiQ09472. HS.

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 (PubMed:10545121, PubMed:10722728, PubMed:10823961, PubMed:11073989, PubMed:11073990, PubMed:11080476, PubMed:11349124, PubMed:11430825, PubMed:11463834, PubMed:11481323, PubMed:11518699, PubMed:11559821, PubMed:11564735, PubMed:11581164, PubMed:11581372, PubMed:11701890, PubMed:11744733, PubMed:11864910, PubMed:11959990, PubMed:11997499, PubMed:12446687, PubMed:12527917, PubMed:12586840, PubMed:12750254, PubMed:12778114, PubMed:12837748, PubMed:12929931, PubMed:14605447, PubMed:14645221, PubMed:14716005, PubMed:14752053, PubMed:15075319, PubMed:15186775, PubMed:15297880, PubMed:15509808, PubMed:15731352, PubMed:15890677, PubMed:16478997, PubMed:16574662, PubMed:16617102, PubMed:16864582, PubMed:17226766, PubMed:17872950, PubMed:18273021, PubMed:19217391, PubMed:19680224, PubMed:20081228, PubMed:23145062, PubMed:23999430, PubMed:24177535, PubMed:24413532, PubMed:8684459, PubMed:8917528, PubMed:9528808, PubMed:9590696, PubMed:9862959, PubMed:9887100). Interacts with TRIP4 (PubMed:25219498). Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A (PubMed:25245946). Interacts with NR4A3 (By similarity). Interacts with ZNF451 (PubMed:24324267). Interacts with human adenovirus 5 E1A protein; this interaction stimulates the acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-protein complex (PubMed:11433299). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity).By similarity60 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2088 – 20881Interaction with NCOA2
Sitei2142 – 21421Interaction with NCOA2

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
HIF1AQ1666516EBI-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
SNAI1O958633EBI-447295,EBI-1045459
STAT6P422262EBI-447295,EBI-1186478
tatP046083EBI-447295,EBI-6164389From a different organism.
TFAP2AP055497EBI-447295,EBI-347351
TP53P0463710EBI-447295,EBI-366083
TP53BP2Q136252EBI-447295,EBI-77642
VDRP114733EBI-447295,EBI-286357
YBX1P678092EBI-447295,EBI-354065

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • androgen receptor binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • nuclear hormone receptor binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108347. 484 interactions.
DIPiDIP-257N.
IntActiQ09472. 186 interactions.
MINTiMINT-104535.
STRINGi9606.ENSP00000263253.

Chemistry

BindingDBiQ09472.

Structurei

Secondary structure

1
2414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi332 – 3343Combined sources
Helixi335 – 35521Combined sources
Turni356 – 3583Combined sources
Helixi367 – 37913Combined sources
Beta strandi386 – 3894Combined sources
Helixi391 – 40515Combined sources
Beta strandi408 – 4103Combined sources
Helixi414 – 4185Combined sources
Helixi1051 – 106616Combined sources
Turni1069 – 10724Combined sources
Helixi1073 – 10753Combined sources
Helixi1081 – 10844Combined sources
Helixi1089 – 10924Combined sources
Helixi1099 – 11079Combined sources
Helixi1114 – 113118Combined sources
Helixi1137 – 116024Combined sources
Beta strandi1178 – 11825Combined sources
Beta strandi1190 – 11945Combined sources
Turni1195 – 11973Combined sources
Beta strandi1198 – 12014Combined sources
Helixi1202 – 12065Combined sources
Beta strandi1212 – 12143Combined sources
Beta strandi1218 – 12214Combined sources
Beta strandi1225 – 12273Combined sources
Helixi1228 – 12303Combined sources
Beta strandi1231 – 12366Combined sources
Beta strandi1244 – 12463Combined sources
Turni1248 – 12503Combined sources
Beta strandi1253 – 12553Combined sources
Helixi1256 – 12594Combined sources
Turni1263 – 12653Combined sources
Helixi1273 – 12775Combined sources
Turni1278 – 12803Combined sources
Helixi1297 – 131317Combined sources
Beta strandi1321 – 133414Combined sources
Helixi1339 – 13424Combined sources
Turni1343 – 13475Combined sources
Beta strandi1351 – 136616Combined sources
Beta strandi1369 – 138113Combined sources
Beta strandi1392 – 14009Combined sources
Helixi1407 – 14093Combined sources
Helixi1410 – 142819Combined sources
Beta strandi1432 – 14365Combined sources
Beta strandi1446 – 14505Combined sources
Helixi1460 – 147617Combined sources
Beta strandi1482 – 14854Combined sources
Helixi1486 – 14938Combined sources
Helixi1498 – 15003Combined sources
Helixi1508 – 151710Combined sources
Helixi1582 – 15909Combined sources
Helixi1592 – 15943Combined sources
Beta strandi1595 – 16017Combined sources
Helixi1603 – 16064Combined sources
Helixi1622 – 16243Combined sources
Beta strandi1625 – 16273Combined sources
Helixi1628 – 16369Combined sources
Helixi1644 – 166219Combined sources
Turni1726 – 17283Combined sources
Helixi1730 – 174718Combined sources
Helixi1756 – 177015Combined sources
Turni1774 – 17785Combined sources
Helixi1780 – 179314Combined sources
Beta strandi1799 – 18024Combined sources
Helixi1806 – 181813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L3ENMR-B323-423[»]
1P4QNMR-B323-423[»]
2K8FNMR-A1723-1812[»]
2MH0NMR-B1723-1812[»]
2MZDNMR-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[»]
5BT3X-ray1.05A1048-1161[»]
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 ALX11 PublicationAdd
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

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiQ09472.
KOiK04498.
OMAiPTMIRGS.
OrthoDBiEOG091G0L04.
PhylomeDBiQ09472.
TreeFamiTF101097.

Family and domain databases

CDDicd15802. RING_CBP-p300. 1 hit.
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.
IPR031162. CBP_P300_HAT.
IPR013178. Histone_AcTrfase_Rtt109/CBP.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR010303. RING_CBP-p300.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. HAT_KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 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 varianti1511 – 15111N → I.1 Publication
VAR_074021
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:
EMBLi
GenBanki
DDBJi
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.5. human.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L3ENMR-B323-423[»]
1P4QNMR-B323-423[»]
2K8FNMR-A1723-1812[»]
2MH0NMR-B1723-1812[»]
2MZDNMR-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[»]
5BT3X-ray1.05A1048-1161[»]
DisProtiDP00633.
ProteinModelPortaliQ09472.
SMRiQ09472. Positions 323-423, 566-646, 1046-1713, 1726-1834, 2050-2092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108347. 484 interactions.
DIPiDIP-257N.
IntActiQ09472. 186 interactions.
MINTiMINT-104535.
STRINGi9606.ENSP00000263253.

Chemistry

BindingDBiQ09472.
ChEMBLiCHEMBL3784.
GuidetoPHARMACOLOGYi2735.

PTM databases

iPTMnetiQ09472.
PhosphoSiteiQ09472.

Polymorphism and mutation databases

BioMutaiEP300.
DMDMi223590203.

Proteomic databases

EPDiQ09472.
MaxQBiQ09472.
PaxDbiQ09472.
PeptideAtlasiQ09472.
PRIDEiQ09472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263253; ENSP00000263253; ENSG00000100393.
GeneIDi2033.
KEGGihsa:2033.
UCSCiuc003azl.5. human.

Organism-specific databases

CTDi2033.
GeneCardsiEP300.
GeneReviewsiEP300.
H-InvDBHIX0203186.
HGNCiHGNC:3373. EP300.
HPAiCAB000146.
HPA003128.
HPA004112.
MalaCardsiEP300.
MIMi602700. gene.
613684. phenotype.
neXtProtiNX_Q09472.
Orphaneti353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
PharmGKBiPA27807.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiQ09472.
KOiK04498.
OMAiPTMIRGS.
OrthoDBiEOG091G0L04.
PhylomeDBiQ09472.
TreeFamiTF101097.

Enzyme and pathway databases

BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2197563. NOTCH2 intracellular domain regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3371568. Attenuation phase.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400253. Circadian Clock.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ09472.
SIGNORiQ09472.

Miscellaneous databases

ChiTaRSiEP300. human.
EvolutionaryTraceiQ09472.
GeneWikiiEP300.
GenomeRNAii2033.
PROiQ09472.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100393.
CleanExiHS_EP300.
GenevisibleiQ09472. HS.

Family and domain databases

CDDicd15802. RING_CBP-p300. 1 hit.
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.
IPR031162. CBP_P300_HAT.
IPR013178. Histone_AcTrfase_Rtt109/CBP.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR010303. RING_CBP-p300.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. HAT_KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 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]
ProtoNetiSearch...

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: September 7, 2016
This is version 212 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

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 one 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.