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Protein

Histone acetyltransferase p300

Gene

EP300

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

Functioni

Functions as histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:8945521). Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521). 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) (PubMed:23911289). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353). Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (PubMed:12586840). 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. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677). Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (PubMed:12402037). 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 (PubMed:14645221). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:16617102). 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 (PubMed:21030595). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degragation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation or propionylation, respectively (PubMed:25818647, PubMed:17267393). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25818647). Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (E)-but-2-enoyl-CoA (crotonyl-CoA) concentration is low (PubMed:25818647). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393).By similarity1 Publication22 Publications
(Microbial infection) 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. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein.2 Publications

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.3 Publications
(2E)-butenoyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-(2E)-butenoyl-L-lysine.1 Publication
Butanoyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-butanoyl-L-lysine.By similarity
Propanoyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-propanoyl-L-lysine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi347Zinc 11
Metal bindingi351Zinc 11
Metal bindingi364Zinc 11
Metal bindingi369Zinc 11
Metal bindingi378Zinc 21
Metal bindingi382Zinc 21
Metal bindingi388Zinc 21
Metal bindingi393Zinc 21
Metal bindingi402Zinc 31
Metal bindingi406Zinc 31
Metal bindingi411Zinc 31
Metal bindingi414Zinc 31
Binding sitei1457Acetyl-CoA; via carbonyl oxygen1 Publication1
Binding sitei1462Acetyl-CoA1 Publication1
Binding sitei1466Acetyl-CoA1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 417TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1664 – 1707ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1728 – 1809TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

GO - Molecular functioni

  • acetyltransferase activity Source: UniProtKB
  • activating transcription factor binding Source: UniProtKB
  • androgen receptor binding Source: BHF-UCL
  • 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
  • histone butyryltransferase activity Source: Ensembl
  • histone crotonyltransferase activity Source: UniProtKB
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • p53 binding Source: Ensembl
  • peptide butyryltransferase activity Source: UniProtKB
  • peptide-lysine-N-acetyltransferase activity Source: Reactome
  • peptide N-acetyltransferase activity Source: Reactome
  • pre-mRNA intronic binding Source: Ensembl
  • protein C-terminus binding Source: MGI
  • protein propionyltransferase activity Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
  • STAT family protein binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA 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

  • animal organ morphogenesis Source: Ensembl
  • apoptotic process Source: UniProtKB
  • B cell differentiation Source: Ensembl
  • beta-catenin-TCF complex assembly Source: Reactome
  • cellular response to UV Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • fat cell differentiation Source: UniProtKB
  • heart development Source: Ensembl
  • histone acetylation Source: UniProtKB
  • histone H2B acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • internal peptidyl-lysine acetylation Source: UniProtKB
  • internal protein amino acid acetylation Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • lung development Source: Ensembl
  • macrophage derived foam cell differentiation Source: UniProtKB
  • megakaryocyte development Source: Ensembl
  • negative regulation of protein oligomerization Source: ARUK-UCL
  • negative regulation of transcription by RNA polymerase II Source: UniProtKB
  • nervous system development Source: ARUK-UCL
  • Notch signaling pathway Source: Reactome
  • N-terminal peptidyl-lysine acetylation Source: UniProtKB
  • peptidyl-lysine acetylation Source: ARUK-UCL
  • peptidyl-lysine butyrylation Source: UniProtKB
  • peptidyl-lysine crotonylation Source: UniProtKB
  • peptidyl-lysine propionylation Source: UniProtKB
  • platelet formation Source: Ensembl
  • positive regulation by host of viral transcription Source: BHF-UCL
  • positive regulation of DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of gene expression, epigenetic Source: UniProtKB
  • positive regulation of Notch signaling pathway Source: Reactome
  • positive regulation of protein binding Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: ARUK-UCL
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: UniProtKB
  • positive regulation of transcription of Notch receptor target Source: Reactome
  • positive regulation of type I interferon production Source: Reactome
  • protein acetylation Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of androgen receptor signaling pathway Source: BHF-UCL
  • regulation of autophagy Source: ParkinsonsUK-UCL
  • regulation of cell cycle Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of megakaryocyte differentiation Source: Reactome
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • regulation of tubulin deacetylation Source: UniProtKB
  • response to estrogen Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • skeletal muscle tissue development Source: Ensembl
  • somitogenesis Source: Ensembl
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • transcription-coupled nucleotide-excision repair Source: Reactome
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processBiological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-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-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-5689901 Metalloprotease DUBs
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-6811555 PI5P Regulates TP53 Acetylation
R-HSA-8866907 Activation of the TFAP2 (AP-2) family of transcription factors
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8941856 RUNX3 regulates NOTCH signaling
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8951936 RUNX3 regulates p14-ARF
R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription
R-HSA-9018519 Estrogen-dependent gene expression
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
Histone butyryltransferase p300 (EC:2.3.1.-1 Publication)
Histone crotonyltransferase p300 (EC:2.3.1.-1 Publication)
Protein propionyltransferase p300 (EC:2.3.1.-1 Publication)
Gene namesi
Name:EP300
Synonyms:P300
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi

Organism-specific databases

EuPathDBiHostDB:ENSG00000100393.10
HGNCiHGNC:3373 EP300
MIMi602700 gene
neXtProtiNX_Q09472

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, 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)DescriptionActionsGraphical viewLength
Mutagenesisi89S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication1
Mutagenesisi89S → D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. 1 Publication1
Mutagenesisi344L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345. 1 Publication1
Mutagenesisi345L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344. 1 Publication1
Mutagenesisi371 – 376TMKNVL → NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2. 1 Publication6
Mutagenesisi413 – 418VCLPLK → NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. 1 Publication6
Mutagenesisi1020K → A: Abolishes sumoylation and transcriptional repression when associated with A-1024. 2 Publications1
Mutagenesisi1020K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1024. 2 Publications1
Mutagenesisi1024K → A: Abolishes sumoylation and transcriptional repression; when associated with A-1020. 2 Publications1
Mutagenesisi1024K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1020. 2 Publications1
Mutagenesisi1170F → E: Increased acetyltransferase activity. 1 Publication1
Mutagenesisi1204C → R: Increased acetyltransferase activity. 1 Publication1
Mutagenesisi1242E → K: Increased acetyltransferase activity. 1 Publication1
Mutagenesisi1357T → L: 40% decrease in activity. 1 Publication1
Mutagenesisi1357T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. 1 Publication1
Mutagenesisi1396S → R: Loss of activity; when associated with R-1397. 1 Publication1
Mutagenesisi1396S → W: Loss of activity; when associated with W-1396. 1 Publication1
Mutagenesisi1397Y → R: Loss of activity; when associated with R-1396. 1 Publication1
Mutagenesisi1397Y → W: Loss of activity; when associated with W-1397. 1 Publication1
Mutagenesisi1399D → 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 Publications1
Mutagenesisi1467Y → F: Abolishes autoacetylation. Loss of acetyltransferase activity. 1 Publication1
Mutagenesisi1505E → 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 Publication1
Mutagenesisi1625D → 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 Publication1
Mutagenesisi1628D → 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 Publication1
Mutagenesisi1645 – 1646RR → EE: Increased acetyltransferase activity. 1 Publication2
Mutagenesisi2056R → K: No effect on interaction with NCOA2. 1 Publication1
Mutagenesisi2088R → K: Abolishes interaction with NCOA2. 1 Publication1
Mutagenesisi2142R → K: Strongly reduces interaction with NCOA2. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei31 – 32Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2033
GeneReviewsiEP300
MalaCardsiEP300
MIMi613684 phenotype
OpenTargetsiENSG00000100393
Orphaneti353284 Rubinstein-Taybi syndrome due to EP300 haploinsufficiency
PharmGKBiPA27807

Chemistry databases

ChEMBLiCHEMBL3784
GuidetoPHARMACOLOGYi2735

Polymorphism and mutation databases

BioMutaiEP300
DMDMi223590203

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002111932 – 2414Histone acetyltransferase p300Add BLAST2413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei89Phosphoserine; by AMPK2 Publications1
Modified residuei418N6-acetyllysine1 Publication1
Modified residuei423N6-acetyllysine1 Publication1
Modified residuei499PhosphoserineBy similarity1
Modified residuei580Omega-N-methylated arginine; by CARM11 Publication1
Modified residuei604Omega-N-methylated arginine; by CARM11 Publication1
Modified residuei636N6-acetyllysineCombined sources1
Modified residuei977N6-acetyllysineCombined sources1
Modified residuei1020N6-acetyllysine; alternate1 Publication1
Cross-linki1020Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei1024N6-acetyllysine; alternate1 Publication1
Cross-linki1024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei1038PhosphoserineCombined sources1
Modified residuei1180N6-acetyllysineBy similarity1
Modified residuei1336N6-acetyllysine1 Publication1
Modified residuei1473N6-acetyllysine1 Publication1
Modified residuei1499N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei1542N6-acetyllysineCombined sources1 Publication1
Modified residuei1546N6-acetyllysineCombined sources1 Publication1
Modified residuei1549N6-acetyllysine; by autocatalysis2 Publications1
Modified residuei1554N6-acetyllysine; by autocatalysisCombined sources1 Publication1
Modified residuei1555N6-acetyllysineCombined sources1
Modified residuei1558N6-acetyllysineCombined sources1 Publication1
Modified residuei1560N6-acetyllysine; by autocatalysisCombined sources1 Publication1
Modified residuei1583N6-acetyllysineCombined sources1
Modified residuei1699N6-acetyllysine1 Publication1
Modified residuei1704N6-acetyllysine1 Publication1
Modified residuei1707N6-acetyllysine1 Publication1
Modified residuei1726PhosphoserineCombined sources1
Modified residuei2142Asymmetric dimethylarginine; by CARM1; alternate1 Publication1
Modified residuei2142Citrulline; by PADI4; alternate1 Publication1

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
PhosphoSitePlusiQ09472

Expressioni

Gene expression databases

BgeeiENSG00000100393
CleanExiHS_EP300
ExpressionAtlasiQ09472 baseline and differential
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 ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity). Interacts with HSF1 (PubMed:27189267). Interacts with ZBTB48/TZAP (PubMed:24382891). Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation (PubMed:26479788). Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954). Interacts with BCL11B (PubMed:27959755, PubMed:16809611).By similarity65 Publications
(Microbial infection) Interacts with human adenovirus 5 E1A protein; this interaction stimulates the acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-protein complex.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2088Interaction with NCOA21
Sitei2142Interaction with NCOA21

Binary interactionsi

Show more details

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
  • p53 binding Source: Ensembl
  • protein C-terminus binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • STAT family protein binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108347, 502 interactors
CORUMiQ09472
DIPiDIP-257N
IntActiQ09472, 197 interactors
MINTiQ09472
STRINGi9606.ENSP00000263253

Chemistry databases

BindingDBiQ09472

Structurei

Secondary structure

12414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi332 – 334Combined sources3
Helixi335 – 355Combined sources21
Turni356 – 358Combined sources3
Helixi367 – 379Combined sources13
Beta strandi386 – 389Combined sources4
Helixi391 – 405Combined sources15
Beta strandi408 – 410Combined sources3
Helixi414 – 418Combined sources5
Helixi1051 – 1066Combined sources16
Turni1069 – 1072Combined sources4
Helixi1073 – 1075Combined sources3
Helixi1081 – 1084Combined sources4
Helixi1089 – 1092Combined sources4
Helixi1099 – 1107Combined sources9
Helixi1114 – 1131Combined sources18
Helixi1137 – 1160Combined sources24
Helixi1165 – 1168Combined sources4
Helixi1182 – 1190Combined sources9
Turni1195 – 1197Combined sources3
Helixi1199 – 1205Combined sources7
Helixi1208 – 1216Combined sources9
Beta strandi1218 – 1221Combined sources4
Helixi1225 – 1245Combined sources21
Turni1248 – 1250Combined sources3
Beta strandi1255 – 1257Combined sources3
Beta strandi1264 – 1272Combined sources9
Helixi1273 – 1278Combined sources6
Helixi1290 – 1292Combined sources3
Helixi1297 – 1313Combined sources17
Beta strandi1321 – 1334Combined sources14
Turni1336 – 1338Combined sources3
Helixi1339 – 1342Combined sources4
Turni1343 – 1347Combined sources5
Beta strandi1351 – 1366Combined sources16
Beta strandi1369 – 1381Combined sources13
Beta strandi1392 – 1400Combined sources9
Helixi1407 – 1409Combined sources3
Helixi1410 – 1428Combined sources19
Beta strandi1432 – 1436Combined sources5
Beta strandi1446 – 1450Combined sources5
Turni1453 – 1455Combined sources3
Helixi1460 – 1476Combined sources17
Beta strandi1478 – 1480Combined sources3
Beta strandi1482 – 1485Combined sources4
Helixi1486 – 1493Combined sources8
Helixi1498 – 1500Combined sources3
Helixi1508 – 1517Combined sources10
Helixi1582 – 1590Combined sources9
Helixi1592 – 1594Combined sources3
Beta strandi1595 – 1601Combined sources7
Helixi1603 – 1606Combined sources4
Helixi1622 – 1624Combined sources3
Beta strandi1625 – 1627Combined sources3
Helixi1628 – 1636Combined sources9
Helixi1644 – 1662Combined sources19
Turni1726 – 1728Combined sources3
Helixi1730 – 1747Combined sources18
Helixi1756 – 1770Combined sources15
Turni1774 – 1778Combined sources5
Helixi1780 – 1793Combined sources14
Beta strandi1799 – 1802Combined sources4
Helixi1806 – 1818Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KJ2X-ray1.95A1287-1522[»]
A1555-1666[»]
5LKTX-ray2.04A1043-1519[»]
A1581-1666[»]
5LKUX-ray3.50A1043-1519[»]
A1581-1666[»]
5LKXX-ray2.52A1043-1519[»]
A1581-1666[»]
5LKZX-ray2.50A1043-1519[»]
A1581-1666[»]
5LPKX-ray2.10A/B/C/D/E/F/G1040-1161[»]
5LPMX-ray1.50A/B1048-1161[»]
5NU5X-ray1.60A/B1048-1161[»]
DisProtiDP00633
ProteinModelPortaliQ09472
SMRiQ09472
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09472

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini566 – 645KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1067 – 1139BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1287 – 1663CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST377

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 149Interaction with RORA1 PublicationAdd BLAST148
Regioni2 – 139Interaction with ALX11 PublicationAdd BLAST138
Regioni1017 – 1029CRD1; mediates transcriptional repressionAdd BLAST13
Regioni1397 – 1399Interaction with histone1 Publication3
Regioni1398 – 1400Acetyl-CoA binding1 Publication3
Regioni1410 – 1411Acetyl-CoA binding1 Publication2
Regioni1572 – 1818Binding region for E1A adenovirusAdd BLAST247
Regioni2003 – 2212Interaction with HTLV-1 TaxAdd BLAST210
Regioni2041 – 2240Interaction with NCOA21 PublicationAdd BLAST200

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi11 – 17Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi797 – 800Poly-Ser4
Compositional biasi1519 – 1526Poly-Glu8
Compositional biasi2066 – 2069Poly-Gln4
Compositional biasi2190 – 2195Poly-Gln6

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.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 417TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1664 – 1707ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1728 – 1809TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

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

Family and domain databases

CDDicd15802 RING_CBP-p300, 1 hit
Gene3Di1.10.1630.10, 1 hit
1.20.1020.10, 2 hits
1.20.920.10, 1 hit
2.10.110.40, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR031162 CBP_P300_HAT
IPR013178 Histone_AcTrfase_Rtt109/CBP
IPR003101 KIX_dom
IPR036529 KIX_dom_sf
IPR009110 Nuc_rcpt_coact
IPR014744 Nuc_rcpt_coact_CREBbp
IPR037073 Nuc_rcpt_coact_CREBbp_sf
IPR010303 RING_CBP-p300
IPR038547 RING_CBP-p300_sf
IPR035898 TAZ_dom_sf
IPR013083 Znf_RING/FYVE/PHD
IPR000197 Znf_TAZ
IPR000433 Znf_ZZ
PfamiView protein in Pfam
PF00439 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
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00297 BROMO, 1 hit
SM01250 KAT11, 1 hit
SM00551 ZnF_TAZ, 2 hits
SM00291 ZnF_ZZ, 1 hit
SUPFAMiSSF47040 SSF47040, 1 hit
SSF47370 SSF47370, 1 hit
SSF57933 SSF57933, 2 hits
SSF69125 SSF69125, 1 hit
PROSITEiView protein in PROSITE
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

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)DescriptionActionsGraphical viewLength
Sequence conflicti169M → T in AAA18639 (PubMed:7523245).Curated1
Sequence conflicti204N → D in AAA18639 (PubMed:7523245).Curated1
Sequence conflicti928T → N in AAA18639 (PubMed:7523245).Curated1
Sequence conflicti1924A → T in AAA18639 (PubMed:7523245).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055554289M → V. Corresponds to variant dbSNP:rs2230111EnsemblClinVar.1
Natural variantiVAR_014428827L → P in a breast cancer sample. 1 Publication1
Natural variantiVAR_020425997I → V. Corresponds to variant dbSNP:rs20551EnsemblClinVar.1
Natural variantiVAR_0144291013E → G in a breast cancer sample. 1 Publication1
Natural variantiVAR_0740211511N → I1 Publication1
Natural variantiVAR_0144301650S → Y in a pancreatic cancer sample. 1 Publication1
Natural variantiVAR_0383762174T → S. Corresponds to variant dbSNP:rs5758252Ensembl.1
Natural variantiVAR_0144312221P → Q in a colorectal cancer sample. 1 PublicationCorresponds to variant dbSNP:rs28937578EnsemblClinVar.1
Natural variantiVAR_0383772223Q → P1 PublicationCorresponds to variant dbSNP:rs1046088EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01877 mRNA Translation: AAA18639.1
AL080243 Genomic DNA No translation available.
AL096765 Genomic DNA No translation available.
AL035658 Genomic DNA No translation available.
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

Entry informationi

Entry nameiEP300_HUMAN
AccessioniPrimary (citable) accession number: Q09472
Secondary accession number(s): B1AKC2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 10, 2009
Last modified: May 23, 2018
This is version 231 of the entry and version 2 of the sequence. See 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

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