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Entry version 240 (10 Apr 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) 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). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097).By similarity1 Publication24 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 ‘Function’ 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 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
<p>This subsection of the ‘Function’ 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 ‘Function’ 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-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-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:2.3.1.483 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)
<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

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100393.10

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.
See also OMIM:613684

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: 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
<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

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

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

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); 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

<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

Encyclopedia of Proteome Dynamics

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EPDi
Q09472

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
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 human 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).By similarity64 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, 523 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, 197 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

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5XZCelectron microscopy10.70A1046-1664[»]
5XZSelectron microscopy9.80A1046-1664[»]
6DS6X-ray1.95A1661-1713[»]
6FGNNMR-A1723-1812[»]
6FGSNMR-A1723-1812[»]
6GYRX-ray3.10A/B/C/D1046-1664[»]
6GYTX-ray2.50A/B1047-1168[»]

Database of protein disorder

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DisProti
DP00633

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q09472

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...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 PublicationAdd BLAST200

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi11 – 17Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi797 – 800Poly-Ser4
Compositional biasi1519 – 1526Poly-Glu8
Compositional biasi2066 – 2069Poly-Gln4
Compositional biasi2190 – 2195Poly-Gln6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1778 Eukaryota
COG5076 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155497

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111353

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000185

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q09472

KEGG Orthology (KO)

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KOi
K04498

Identification of Orthologs from Complete Genome Data

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OMAi
QPGLNQF

Database of Orthologous Groups

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OrthoDBi
135929at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q09472

TreeFam database of animal gene trees

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TreeFami
TF101097

Family and domain databases

Conserved Domains Database

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CDDi
cd15802 RING_CBP-p300, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1630.10, 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

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

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Pfami
View 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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00503 BROMODOMAIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00297 BROMO, 1 hit
SM01250 KAT11, 1 hit
SM00551 ZnF_TAZ, 2 hits
SM00291 ZnF_ZZ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47040 SSF47040, 1 hit
SSF47370 SSF47370, 1 hit
SSF57933 SSF57933, 2 hits
SSF69125 SSF69125, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8E869E1F174A6FEB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0U1RQG3A0A0U1RQG3_HUMAN
Histone acetyltransferase p300
EP300
133Annotation score:

Annotation score:1 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>
A0A0U1RR87A0A0U1RR87_HUMAN
Histone acetyltransferase p300
EP300
187Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<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_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 PublicationCorresponds to variant dbSNP:rs1234168115Ensembl.1
Natural variantiVAR_0740211511N → I1 Publication1
Natural variantiVAR_0144301650S → Y in a pancreatic cancer sample. 1 Publication1
Natural variantiVAR_0807312007Q → R Found in a patient with spinocerebellar ataxia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763892493Ensembl.1
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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS14010.1

Protein sequence database of the Protein Information Resource

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PIRi
A54277

NCBI Reference Sequences

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RefSeqi
NP_001420.2, NM_001429.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.517517
Hs.655211

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000263253; ENSP00000263253; ENSG00000100393

Database of genes from NCBI RefSeq genomes

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GeneIDi
2033

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2033

UCSC genome browser

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UCSCi
uc003azl.5 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi