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Protein

Histone acetyltransferase p300

Gene

Ep300

Organism
Mus musculus (Mouse)
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 (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein (PubMed:18486321, PubMed:24216764). 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 (By similarity). Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac) (By similarity). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2 (PubMed:28883095). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (By similarity). Acetylates HDAC1 leading to its inactivation and modulation of transcription (By similarity). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (By similarity). 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 (By similarity). Promotes cardiac myocyte enlargement (By similarity). Can also mediate transcriptional repression (By similarity). Acetylates FOXO1 and enhances its transcriptional activity (By similarity). Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (By similarity). 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 (By similarity). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:14645221, PubMed:9512516). 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) (By similarity). Acetylates MEF2D (By similarity). 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:27105113). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. 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 (By similarity). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:27105113). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). Acetylates PCK1 and promotes PCK1 anaplerotic activity (By similarity).By similarity1 Publication7 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 bindingi348Zinc 1By similarity1
Metal bindingi352Zinc 1By similarity1
Metal bindingi365Zinc 1By similarity1
Metal bindingi370Zinc 1By similarity1
Metal bindingi379Zinc 2By similarity1
Metal bindingi383Zinc 2By similarity1
Metal bindingi389Zinc 2By similarity1
Metal bindingi394Zinc 2By similarity1
Metal bindingi403Zinc 3By similarity1
Metal bindingi407Zinc 3By similarity1
Metal bindingi412Zinc 3By similarity1
Metal bindingi415Zinc 3By similarity1
<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 sitei1456Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1461Acetyl-CoABy similarity1
Binding sitei1465Acetyl-CoABy similarity1

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 fingeri332 – 418TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1663 – 1706ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1727 – 1808TAZ-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, Differentiation, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-3214847 HATs acetylate histones
R-MMU-3371568 Attenuation phase
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5621575 CD209 (DC-SIGN) signaling
R-MMU-5689901 Metalloprotease DUBs
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-8866907 Activation of the TFAP2 (AP-2) family of transcription factors
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-MMU-8941856 RUNX3 regulates NOTCH signaling
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8951936 RUNX3 regulates p14-ARF
R-MMU-9018519 Estrogen-dependent gene expression
R-MMU-918233 TRAF3-dependent IRF activation pathway
R-MMU-933541 TRAF6 mediated IRF7 activation

<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:2.3.1.48By similarity)
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.-By similarity)
Protein propionyltransferase p300 (EC:2.3.1.-By similarity)
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1276116 Ep300

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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 methionineiRemovedBy similarity
<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_00004093862 – 2412Histone acetyltransferase p300Add BLAST2411

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-acetylalanineBy similarity1
Modified residuei89Phosphoserine; by AMPKBy similarity1
Modified residuei419N6-acetyllysineBy similarity1
Modified residuei424N6-acetyllysineBy similarity1
Modified residuei500PhosphoserineCombined sources1
Modified residuei581Omega-N-methylated arginine; by CARM1By similarity1
Modified residuei605Omega-N-methylated arginine; by CARM1By similarity1
Modified residuei637N6-acetyllysineBy similarity1
Modified residuei976N6-acetyllysineBy similarity1
Modified residuei1019N6-acetyllysine; alternateBy similarity1
<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-linki1019Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei1023N6-acetyllysine; alternateBy similarity1
Cross-linki1023Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei1037PhosphoserineBy similarity1
Modified residuei1179N6-acetyllysineCombined sources1
Modified residuei1335N6-acetyllysineBy similarity1
Modified residuei1472N6-acetyllysineBy similarity1
Modified residuei1498N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei1541N6-acetyllysineBy similarity1
Modified residuei1545N6-acetyllysineBy similarity1
Modified residuei1548N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei1553N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei1554N6-acetyllysineBy similarity1
Modified residuei1557N6-acetyllysineCombined sources1
Modified residuei1559N6-acetyllysineCombined sources1
Modified residuei1582N6-acetyllysineBy similarity1
Modified residuei1698N6-acetyllysineBy similarity1
Modified residuei1703N6-acetyllysineBy similarity1
Modified residuei1706N6-acetyllysineBy similarity1
Modified residuei1725PhosphoserineBy similarity1
Modified residuei2143Asymmetric dimethylarginine; by CARM1; alternateBy similarity1
Modified residuei2143Citrulline; by PADI4; alternateBy similarity1

<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-1019. Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.By similarity
Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.By similarity
Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 (By similarity).By similarity
Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 (By similarity).By similarity
Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation.By similarity
Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG (By similarity). 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 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
B2RWS6

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

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PaxDbi
B2RWS6

PeptideAtlas

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PeptideAtlasi
B2RWS6

PRoteomics IDEntifications database

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PRIDEi
B2RWS6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
B2RWS6

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

More...
PhosphoSitePlusi
B2RWS6

<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
ENSMUSG00000055024 Expressed in 237 organ(s), highest expression level in embryonic stem cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
B2RWS6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
B2RWS6 MM

<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 HIPK2, 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 with PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with CITED1 and CITED2. Interacts with ROCK2. Interacts with NEUROD1. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). 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 (PubMed:18486321, PubMed:24216764). Interacts with ARNTL/BMAL1 and CLOCK (By similarity). Interacts with SIRT2. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C (By similarity). Interacts with TRIP4 (By similarity). Interacts with NPAS2. Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A (By similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764). Interacts with ZNF451 (By similarity). Interacts with HSF1 (By similarity). Interacts with ZBTB48/TZAP (By similarity). Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation (By similarity). Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements (By similarity). Interacts with BCL11B (By similarity). Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity).By similarity10 Publications

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>Sitei2089Interaction with NCOA2By similarity1
Sitei2143Interaction with NCOA2By similarity1

<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

WithEntry#Exp.IntActNotes
Tp53P023403EBI-3953360,EBI-474016

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
236625, 52 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
B2RWS6

Database of interacting proteins

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DIPi
DIP-60610N

Protein interaction database and analysis system

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IntActi
B2RWS6, 8 interactors

Molecular INTeraction database

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MINTi
B2RWS6

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000066789

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
B2RWS6

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

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SMRi
B2RWS6

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...

<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>Domaini567 – 646KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1066 – 1138BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1286 – 1662CBP/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 RORAAdd BLAST148
Regioni2 – 139Interaction with ALX1By similarityAdd BLAST138
Regioni1016 – 1028CRD1; mediates transcriptional repressionBy similarityAdd BLAST13
Regioni1396 – 1398Interaction with histoneBy similarity3
Regioni1397 – 1399Acetyl-CoA bindingBy similarity3
Regioni1409 – 1410Acetyl-CoA bindingBy similarity2
Regioni2042 – 2237Interaction with NCOA2By similarityAdd BLAST196

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1510 – 1539Sequence analysisAdd BLAST30

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 biasi660 – 942Pro-richAdd BLAST283
Compositional biasi798 – 801Poly-Ser4
Compositional biasi1518 – 1525Poly-Glu8

<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 (By similarity).By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri332 – 418TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1663 – 1706ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1727 – 1808TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1778 Eukaryota
COG5076 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155497

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000111353

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000185

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
B2RWS6

KEGG Orthology (KO)

More...
KOi
K04498

Identification of Orthologs from Complete Genome Data

More...
OMAi
QPGLNQF

Database of Orthologous Groups

More...
OrthoDBi
236283at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
B2RWS6

TreeFam database of animal gene trees

More...
TreeFami
TF101097

Family and domain databases

Conserved Domains Database

More...
CDDi
cd15802 RING_CBP-p300, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
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

More...
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

More...
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

More...
PRINTSi
PR00503 BROMODOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
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

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

PROSITE; a protein domain and family database

More...
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 3 potential isoforms that are computationally mapped.Show allAlign All

B2RWS6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS
60 70 80 90 100
TELGLTNGGD ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP
110 120 130 140 150
GQAMASQAQQ NSPGLSLINS MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS
160 170 180 190 200
PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN QVMNGSIGAG
210 220 230 240 250
RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QPLKMGMMNN
260 270 280 290 300
PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM
310 320 330 340 350
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH
360 370 380 390 400
KCQRREQANG EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI
410 420 430 440 450
ISHWKNCTRH DCPVCLPLKN AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS
460 470 480 490 500
TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ IPPQPQVQAK NQQSQPSGQS
510 520 530 540 550
PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS QNPMMSENAG
560 570 580 590 600
VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
610 620 630 640 650
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR
660 670 680 690 700
TRLQKQNMLP NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP
710 720 730 740 750
NHMMPRMTPQ PGLNQFGQMN MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM
760 770 780 790 800
GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN MPLAPSSGQA PVSQAQMSSS
810 820 830 840 850
SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP TPHHTPPSIG
860 870 880 890 900
NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL
910 920 930 940 950
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV
960 970 980 990 1000
SNPPSTSSTE VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK
1010 1020 1030 1040 1050
GEDVKVEPTE MEERGPELKT DGKEEEEQPS TSATQSSPAP GQSKKKIFKP
1060 1070 1080 1090 1100
EELRQALMPT LEALYRQDPE SLPFRQPVDP QLLGIPDYFD IVKSPMDLST
1110 1120 1130 1140 1150
IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY CSKLSEVFEQ
1160 1170 1180 1190 1200
EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC
1210 1220 1230 1240 1250
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG
1260 1270 1280 1290 1300
RKMHQICVLH HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF
1310 1320 1330 1340 1350
LENRVNDFLR RQNHPESGEV TVRVVHASDK TVEVKPGMKA RFVDSGEMAE
1360 1370 1380 1390 1400
SFPYRTKALF AFEEIDGVDL CFFGMHVQEY GSDCPPPNQR RVYISYLDSV
1410 1420 1430 1440 1450
HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS EGDDYIFHCH
1460 1470 1480 1490 1500
PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL
1510 1520 1530 1540 1550
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK
1560 1570 1580 1590 1600
NNKKTSKNKS SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI
1610 1620 1630 1640 1650
ACPAPNSLPP IVDPDPLIPC DLMDGRDAFL TLARDKHLEF SSLRRAQWST
1660 1670 1680 1690 1700
MCMLVELHTQ SQDRFVYTCN ECKHHVETRW HCTVCEDYDL CITCYNTKNH
1710 1720 1730 1740 1750
DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS LVHACQCRNA
1760 1770 1780 1790 1800
NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC
1810 1820 1830 1840 1850
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT
1860 1870 1880 1890 1900
PATPTTPTGQ QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG
1910 1920 1930 1940 1950
KAPGQVTPPT PPQTAQAPLP GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ
1960 1970 1980 1990 2000
RPIQHQMPQM SPMAPMGMNP PPMARGPGGH LDPGIGPAGM QQQPPWAQGG
2010 2020 2030 2040 2050
MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS PLKPGTVSQQ
2060 2070 2080 2090 2100
ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP
2110 2120 2130 2140 2150
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ
2160 2170 2180 2190 2200
PQQQLQPPMG AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP
2210 2220 2230 2240 2250
GMANQFQQPQ GIGYPPQQQQ QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA
2260 2270 2280 2290 2300
GASLQAYQQR LLQQQMGSPA QPNPMSPQQH MLPNQAQSPH LQGQQIPNSL
2310 2320 2330 2340 2350
SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ TSSPHPGLVA
2360 2370 2380 2390 2400
AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL
2410
NSNLSQSTLD IH
Length:2,412
Mass (Da):263,305
Last modified:April 16, 2014 - 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:i0E9B2D9508237671
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0U1RNN6A0A0U1RNN6_MOUSE
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>
A0A087WPR8A0A087WPR8_MOUSE
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>
A0A0U1RQ52A0A0U1RQ52_MOUSE
Histone acetyltransferase p300
Ep300
46Annotation 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 conflicti677G → E in AAI44977 (PubMed:15489334).Curated1
Sequence conflicti677G → E in AAI50682 (PubMed:15489334).Curated1
Sequence conflicti2217Q → QQQQ in AAI44977 (PubMed:15489334).Curated1
Sequence conflicti2217Q → QQQQ in AAI50682 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC102262 Genomic DNA No translation available.
AC160528 Genomic DNA No translation available.
BC144976 mRNA Translation: AAI44977.1
BC150681 mRNA Translation: AAI50682.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS37149.1

NCBI Reference Sequences

More...
RefSeqi
NP_808489.4, NM_177821.6

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.258397

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
328572

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:328572

UCSC genome browser

More...
UCSCi
uc007wws.1 mouse

<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

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC102262 Genomic DNA No translation available.
AC160528 Genomic DNA No translation available.
BC144976 mRNA Translation: AAI44977.1
BC150681 mRNA Translation: AAI50682.1
CCDSiCCDS37149.1
RefSeqiNP_808489.4, NM_177821.6
UniGeneiMm.258397

3D structure databases

ProteinModelPortaliB2RWS6
SMRiB2RWS6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi236625, 52 interactors
CORUMiB2RWS6
DIPiDIP-60610N
IntActiB2RWS6, 8 interactors
MINTiB2RWS6
STRINGi10090.ENSMUSP00000066789

PTM databases

iPTMnetiB2RWS6
PhosphoSitePlusiB2RWS6

Proteomic databases

EPDiB2RWS6
PaxDbiB2RWS6
PeptideAtlasiB2RWS6
PRIDEiB2RWS6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024
GeneIDi328572
KEGGimmu:328572
UCSCiuc007wws.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2033
MGIiMGI:1276116 Ep300

Phylogenomic databases

eggNOGiKOG1778 Eukaryota
COG5076 LUCA
GeneTreeiENSGT00940000155497
HOGENOMiHOG000111353
HOVERGENiHBG000185
InParanoidiB2RWS6
KOiK04498
OMAiQPGLNQF
OrthoDBi236283at2759
PhylomeDBiB2RWS6
TreeFamiTF101097

Enzyme and pathway databases

ReactomeiR-MMU-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-MMU-3134973 LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-3214847 HATs acetylate histones
R-MMU-3371568 Attenuation phase
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5621575 CD209 (DC-SIGN) signaling
R-MMU-5689901 Metalloprotease DUBs
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-8866907 Activation of the TFAP2 (AP-2) family of transcription factors
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-MMU-8941856 RUNX3 regulates NOTCH signaling
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8951936 RUNX3 regulates p14-ARF
R-MMU-9018519 Estrogen-dependent gene expression
R-MMU-918233 TRAF3-dependent IRF activation pathway
R-MMU-933541 TRAF6 mediated IRF7 activation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Ep300 mouse

Protein Ontology

More...
PROi
PR:B2RWS6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000055024 Expressed in 237 organ(s), highest expression level in embryonic stem cell
ExpressionAtlasiB2RWS6 baseline and differential
GenevisibleiB2RWS6 MM

Family and domain databases

CDDicd15802 RING_CBP-p300, 1 hit
Gene3Di1.10.1630.10, 1 hit
1.20.1020.10, 2 hits
1.20.920.10, 1 hit
2.10.110.40, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR031162 CBP_P300_HAT
IPR013178 Histone_AcTrfase_Rtt109/CBP
IPR003101 KIX_dom
IPR036529 KIX_dom_sf
IPR009110 Nuc_rcpt_coact
IPR014744 Nuc_rcpt_coact_CREBbp
IPR037073 Nuc_rcpt_coact_CREBbp_sf
IPR010303 RING_CBP-p300
IPR038547 RING_CBP-p300_sf
IPR035898 TAZ_dom_sf
IPR013083 Znf_RING/FYVE/PHD
IPR000197 Znf_TAZ
IPR000433 Znf_ZZ
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF09030 Creb_binding, 1 hit
PF06001 DUF902, 1 hit
PF08214 HAT_KAT11, 1 hit
PF02172 KIX, 1 hit
PF02135 zf-TAZ, 2 hits
PF00569 ZZ, 1 hit
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00297 BROMO, 1 hit
SM01250 KAT11, 1 hit
SM00551 ZnF_TAZ, 2 hits
SM00291 ZnF_ZZ, 1 hit
SUPFAMiSSF47040 SSF47040, 1 hit
SSF47370 SSF47370, 1 hit
SSF57933 SSF57933, 2 hits
SSF69125 SSF69125, 1 hit
PROSITEiView protein in PROSITE
PS00633 BROMODOMAIN_1, 1 hit
PS50014 BROMODOMAIN_2, 1 hit
PS51727 CBP_P300_HAT, 1 hit
PS50952 KIX, 1 hit
PS50134 ZF_TAZ, 2 hits
PS01357 ZF_ZZ_1, 1 hit
PS50135 ZF_ZZ_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEP300_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B2RWS6
Secondary accession number(s): E9PYJ8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 16, 2014
Last modified: January 16, 2019
This is version 111 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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