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Entry version 247 (13 Nov 2019)
Sequence version 2 (10 Feb 2009)
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Protein

Histone acetyltransferase p300

Gene

EP300

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2 (PubMed:12929931, PubMed:16762839, PubMed:18722353). 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), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation or propionylation, respectively (PubMed:17267393, PubMed:25818647, PubMed:29775581). 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 (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (PubMed:25818647). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes (PubMed:29775581). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097). Acetylates RXRA and RXRG (PubMed:17761950).1 Publication26 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi347Zinc 12 Publications1
Metal bindingi351Zinc 12 Publications1
Metal bindingi364Zinc 12 Publications1
Metal bindingi369Zinc 12 Publications1
Metal bindingi378Zinc 22 Publications1
Metal bindingi382Zinc 22 Publications1
Metal bindingi388Zinc 22 Publications1
Metal bindingi393Zinc 22 Publications1
Metal bindingi402Zinc 32 Publications1
Metal bindingi406Zinc 32 Publications1
Metal bindingi411Zinc 32 Publications1
Metal bindingi414Zinc 32 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1457Acetyl-CoA; via carbonyl oxygen1 Publication1
Binding sitei1462Acetyl-CoA1 Publication1
Binding sitei1466Acetyl-CoA1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri331 – 417TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1664 – 1707ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1728 – 1809TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processBiological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.1.48 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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-210744 Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells
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-3899300 SUMOylation of transcription cofactors
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-9013695 NOTCH4 Intracellular Domain Regulates Transcription
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-9029569 NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
R-HSA-918233 TRAF3-dependent IRF activation pathway
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-9614657 FOXO-mediated transcription of cell death genes
R-HSA-9616222 Transcriptional regulation of granulopoiesis
R-HSA-9617629 Regulation of FOXO transcriptional activity by acetylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q09472

SIGNOR Signaling Network Open Resource

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SIGNORi
Q09472

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
Q09472 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone acetyltransferase p300 (EC:2.3.1.484 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 2-hydroxyisobutyryltransferase p300 (EC:2.3.1.-1 Publication)
Protein propionyltransferase p300 (EC:2.3.1.-1 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EP300
Synonyms:P300
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3373 EP300

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602700 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q09472

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM
Menke-Hennekam syndrome 2 (MKHK2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Menke-Hennekam syndrome, a congenital autosomal dominant disease characterized by developmental delay, growth retardation, and craniofacial dysmorphism. Patients have intellectual disability of variable severity, speech delay, autistic behavior, short stature and microcephaly. Main facial characteristics include short palpebral fissures, telecanthi, depressed nasal ridge, short nose, anteverted nares, short columella and long philtrum.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0819861824Q → P in MKHK2. 1 Publication1
Natural variantiVAR_0819871831Missing in MKHK2. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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: Abolished acetyltransferase and acyltransferase activities. 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. No acetylation of RXRA. 5 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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei31 – 32Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A2

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
2033

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
EP300

MalaCards human disease database

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MalaCardsi
EP300
MIMi613684 phenotype
618333 phenotype

Open Targets

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OpenTargetsi
ENSG00000100393

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
353284 Rubinstein-Taybi syndrome due to EP300 haploinsufficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27807

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q09472

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3784

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2735

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EP300

Domain mapping of disease mutations (DMDM)

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DMDMi
223590203

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002111932 – 2414Histone acetyltransferase p300Add BLAST2413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1020Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei1024N6-acetyllysine; alternate1 Publication1
Cross-linki1024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

The CPTAC Assay portal

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CPTACi
CPTAC-1240

Encyclopedia of Proteome Dynamics

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EPDi
Q09472

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q09472

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q09472

MaxQB - The MaxQuant DataBase

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MaxQBi
Q09472

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q09472

PeptideAtlas

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PeptideAtlasi
Q09472

PRoteomics IDEntifications database

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PRIDEi
Q09472

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58723

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q09472

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q09472

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000100393 Expressed in 233 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q09472 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q09472 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000146
HPA003128
HPA004112

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 p30II.

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:10722728, PubMed:10823961, PubMed:11073989, PubMed:11073990, PubMed:11349124, PubMed:11430825, 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).

Interacts with SMAD4; negatively regulated by ZBTB7A (PubMed:25514493).

Interacts with DUX4 (via C-terminus) (PubMed:26951377).

Interacts with NUPR1; this interaction enhances the effect of EP300 on PAX2 transcription factor activity (PubMed:11940591).

Interacts with RXRA; the interaction is decreased by 9-cis retinoic acid (PubMed:17761950). NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA (PubMed:17761950).

Interacts with RB1 (By similarity).

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

(Microbial infection) Interacts with and acetylates HIV-1 Tat.

3 Publications

(Microbial infection) Interacts with HTLV-1 proteins Tax, p30II and HBZ.

3 Publications

Sites

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108347, 569 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q09472

Database of interacting proteins

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DIPi
DIP-257N

Protein interaction database and analysis system

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IntActi
Q09472, 205 interactors

Molecular INTeraction database

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MINTi
Q09472

STRING: functional protein association networks

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STRINGi
9606.ENSP00000263253

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q09472

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q09472

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q09472

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini566 – 645KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1067 – 1139BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1287 – 1663CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST377

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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 Publication