Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 242 (17 Jun 2020)
Sequence version 3 (17 Oct 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

CREB-binding protein

Gene

CREBBP

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

Acetylates histones, giving a specific tag for transcriptional activation (PubMed:24616510). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, PubMed:9707565, PubMed:24207024, PubMed:28790157, PubMed:30540930). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers (PubMed:14645221). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:24207024). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (PubMed:28790157). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed:30540930). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493).12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi363Zinc 1By similarity1
Metal bindingi367Zinc 1By similarity1
Metal bindingi380Zinc 1By similarity1
Metal bindingi385Zinc 1By similarity1
Metal bindingi394Zinc 2By similarity1
Metal bindingi398Zinc 2By similarity1
Metal bindingi404Zinc 2By similarity1
Metal bindingi409Zinc 2By similarity1
Metal bindingi418Zinc 3By similarity1
Metal bindingi422Zinc 3By similarity1
Metal bindingi427Zinc 3By similarity1
Metal bindingi430Zinc 3By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1493Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1498Acetyl-CoABy similarity1
Binding sitei1502Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri347 – 433TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1701 – 1744ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1765 – 1846TAZ-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 functionActivator, Acyltransferase, Transferase
Biological processBiological rhythms, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-1368082 RORA activates gene expression
R-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression
R-HSA-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-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
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-350054 Notch-HLH transcription pathway
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-400206 Regulation of lipid metabolism by PPARalpha
R-HSA-400253 Circadian Clock
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-6803204 TP53 Regulates Transcription of Genes Involved in Cytochrome C Release
R-HSA-8866907 Activation of the TFAP2 (AP-2) family of transcription factors
R-HSA-8939246 RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-HSA-8941856 RUNX3 regulates NOTCH signaling
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

More...
SignaLinki
Q92793

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q92793

<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%5Fand%5Ftaxonomy%5Fsection">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:
CREB-binding protein
Alternative name(s):
Histone lysine acetyltransferase CREBBP (EC:2.3.1.481 Publication)
Protein-lysine acetyltransferase CREBBP (EC:2.3.1.-6 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:CREBBP
Synonyms:CBP
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000005339.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2348 CREBBP

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600140 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q92793

<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

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

Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with KAT6A; translocation t(11;16)(q23;p13.3) with KMT2A/MLL1; translocation t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription.
Rubinstein-Taybi syndrome 1 (RSTS1)7 Publications
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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072915650Y → F in RSTS1. 1 Publication1
Natural variantiVAR_072916789A → T in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs746728741Ensembl.1
Natural variantiVAR_072917910T → A in RSTS1; incomplete. 1 PublicationCorresponds to variant dbSNP:rs143247685Ensembl.1
Natural variantiVAR_0373051175Y → C in RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3. 3 PublicationsCorresponds to variant dbSNP:rs28937315Ensembl.1
Natural variantiVAR_0729181278E → A in RSTS1. 1 Publication1
Natural variantiVAR_0350801278E → K in RSTS1; abolishes acetyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs267606752Ensembl.1
Natural variantiVAR_0155781378R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 2 PublicationsCorresponds to variant dbSNP:rs121434626Ensembl.1
Natural variantiVAR_0729191406D → Y in RSTS1. 1 Publication1
Natural variantiVAR_0729201415Q → P in RSTS1. 1 Publication1
Natural variantiVAR_0350811447T → I in RSTS1. 1 Publication1
Natural variantiVAR_0350821450Y → H in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs1555473499Ensembl.1
Natural variantiVAR_0350831470H → R in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs797044860Ensembl.1
Natural variantiVAR_0729211475P → T in RSTS1. 1 Publication1
Natural variantiVAR_0729221503Y → F in RSTS1. 1 Publication1
Natural variantiVAR_0729231507L → P in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs1057520191Ensembl.1
Natural variantiVAR_0729241543D → N in RSTS1. 1 Publication1
Natural variantiVAR_0350841664R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications1
Menke-Hennekam syndrome 1 (MKHK1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Menke-Hennekam syndrome, a congenital autosomal dominant disease characterized by developmental delay, growth retardation, and craniofacial dysmorphism. Patients have intellectual disability of variable severity, speech delay, autistic behavior, short stature and microcephaly. Main facial characteristics include short palpebral fissures, telecanthi, depressed nasal ridge, short nose, anteverted nares, short columella and long philtrum.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0785571710C → R in MKHK1. 1 Publication1
Natural variantiVAR_0819791719H → D in MKHK1. 1 Publication1
Natural variantiVAR_0819801724E → K in MKHK1. 1 Publication1
Natural variantiVAR_0785581747L → R in MKHK1. 1 Publication1
Natural variantiVAR_0819811782A → V in MKHK1. 1 Publication1
Natural variantiVAR_0785591786R → P in MKHK1. 1 Publication1
Natural variantiVAR_0785601819C → F in MKHK1. 1 Publication1
Natural variantiVAR_0785611826C → W in MKHK1. 1 Publication1
Natural variantiVAR_0819821829H → D in MKHK1. 1 Publication1
Natural variantiVAR_0785621838C → Y in MKHK1. 1 Publication1
Natural variantiVAR_0819831865 – 1866MR → I in MKHK1. 1 Publication2
Natural variantiVAR_0785631867R → Q in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs1131691326Ensembl.1
Natural variantiVAR_0785641867R → W in MKHK1. 1 Publication1
Natural variantiVAR_0819841868R → Q in MKHK1. 1 Publication1
Natural variantiVAR_0785651868R → W in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs886039491Ensembl.1
Natural variantiVAR_0819851870A → P in MKHK1. 1 Publication1
Natural variantiVAR_0785661872M → V in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs797045037Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1116D → R: Impairs binding to acetylated histones. 1 Publication1
Mutagenesisi1126F → A: Impairs binding to acetylated histones. 1 Publication1
Mutagenesisi1162N → E or R: Abolishes interaction with ASF1A. 1 Publication1
Mutagenesisi1165W → A: Abolishes interaction with ASF1A. 1 Publication1
Mutagenesisi1170K → E: Impairs binding to acetylated histones. 1 Publication1
Mutagenesisi1179S → I: Impairs interaction with ASF1A. 1 Publication1
Mutagenesisi1180K → E: Abolishes interaction with ASF1A. 1 Publication1
Mutagenesisi1183E → R: Abolishes interaction with ASF1A. 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>Sitei29 – 30Breakpoint for translocation to form KAT6B-CREBBP2
Sitei266 – 267Breakpoint for translocation to form KAT6A-CREBBP2

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1387

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

More...
GeneReviewsi
CREBBP

MalaCards human disease database

More...
MalaCardsi
CREBBP
MIMi180849 phenotype
618332 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000005339

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

More...
Orphaneti
370026 Acute myeloid leukemia with t(8;16)(p11;p13) translocation
353281 Rubinstein-Taybi syndrome due to 16p13.3 microdeletion
353277 Rubinstein-Taybi syndrome due to CREBBP mutations

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26866

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q92793 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5747

Drug and drug target database

More...
DrugBanki
DB08655 9-ACETYL-2,3,4,9-TETRAHYDRO-1H-CARBAZOL-1-ONE

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2734

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CREBBP

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116241283

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002111902 – 2442CREB-binding proteinAdd BLAST2441

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 residuei121PhosphoserineCombined sources1
Modified residuei220Omega-N-methylarginineCombined sources1
Modified residuei601Omega-N-methylated arginineBy similarity1
Modified residuei625Omega-N-methylated arginineBy similarity1
Modified residuei657N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki998Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1014N6-acetyllysineCombined sources1
Modified residuei1030PhosphoserineCombined sources1
Cross-linki1033Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1056Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1076PhosphoserineCombined sources1
Modified residuei1216N6-acetyllysineCombined sources1
Modified residuei1382Phosphoserine; by IKKA1 Publication1
Modified residuei1386Phosphoserine; by IKKA1 Publication1
Modified residuei1583N6-acetyllysineCombined sources1
Modified residuei1591N6-acetyllysineCombined sources1
Modified residuei1592N6-acetyllysineCombined sources1
Modified residuei1595N6-acetyllysineCombined sources1
Modified residuei1597N6-acetyllysineCombined sources1
Modified residuei1741N6-acetyllysineCombined sources1
Modified residuei1744N6-acetyllysineCombined sources1
Modified residuei1763PhosphoserineCombined sources1
Modified residuei2063PhosphoserineCombined sources1
Modified residuei2076PhosphoserineCombined sources1
Modified residuei2079PhosphoserineCombined sources1
Modified residuei2351PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity).By similarity
Phosphorylated by CHUK/IKKA at Ser-1382 and Ser-1386; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B.1 Publication
Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.By similarity
Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q92793

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q92793

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q92793

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q92793

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

More...
PaxDbi
Q92793

PeptideAtlas

More...
PeptideAtlasi
Q92793

PRoteomics IDEntifications database

More...
PRIDEi
Q92793

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
62237
75472 [Q92793-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q92793

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

More...
PhosphoSitePlusi
Q92793

<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

More...
Bgeei
ENSG00000005339 Expressed in testis and 240 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q92793 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q92793 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000005339 Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300.

Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1.

Interacts with MAF AND ZCCHC12.

Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX (By similarity).

Interacts with phosphorylated CREB1.

Interacts with CITED4 (C-terminal region).

Interacts (via the TAZ-type 1 domain) with HIF1A.

Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5, DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1.

Interacts with KLF1; the interaction results in acetylation of KLF1 and enhancement of its transcriptional activity.

Interacts with MTDH.

Interacts with NFATC4.

Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity.

Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter.

Interacts with IRF3 (when phosphorylated); forming the dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I interferon genes (PubMed:27302953).

Interacts (via N-terminus) with SS18L1/CREST (via C-terminus).

Interacts with MECOM.

Interacts with CITED1 (via C-terminus).

Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity.

Interacts with NPAS2, CLOCK and ARNTL/BMAL1.

Interacts with ASF1A and ASF1B; this promotes histone acetylation.

Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4.

Interacts (via transactivation domain and C-terminus) with PCNA; the interaction occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902).

Interacts with DHX9 (via N-terminus); this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (PubMed:9323138).

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

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

Forms a complex with KMT2A and CREB1 (PubMed:23651431).

Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (PubMed:28128295).

By similarity32 Publications

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

3 Publications

(Microbial infection) Interacts with human herpes virus 8/HHV-8 protein vIRF-1; this interaction inhibits CREBBP binding to IRF3.

1 Publication

(Microbial infection) Interacts with HIV-1 Tat.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
107777, 382 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q92793

Database of interacting proteins

More...
DIPi
DIP-952N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q92793

Protein interaction database and analysis system

More...
IntActi
Q92793, 91 interactors

Molecular INTeraction database

More...
MINTi
Q92793

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000262367

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q92793

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q92793 protein

<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

12442
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q92793

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q92793

<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%5Fand%5Fdomains%5Fsection">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>Domaini587 – 666KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1103 – 1175BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1323 – 1700CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST378

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>Regioni227 – 410Interaction with SRCAP1 PublicationAdd BLAST184
Regioni1124 – 1170Interaction with histone1 PublicationAdd BLAST47
Regioni1162 – 1180Interaction with ASF1A1 PublicationAdd BLAST19
Regioni1433 – 1435Interaction with histoneBy similarity3
Regioni1434 – 1436Acetyl-CoA bindingBy similarity3
Regioni1446 – 1447Acetyl-CoA bindingBy similarity2
Regioni1460 – 1891Interaction with TRERF11 PublicationAdd BLAST432

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 biasi1061 – 1064Poly-Glu4
Compositional biasi1199 – 1487Cys/His-richAdd BLAST289
Compositional biasi1555 – 1562Poly-Glu8
Compositional biasi1943 – 1948Poly-Pro6
Compositional biasi1967 – 1970Poly-Gln4
Compositional biasi2081 – 2085Poly-Gln5
Compositional biasi2199 – 2216Poly-GlnAdd BLAST18
Compositional biasi2245 – 2248Poly-Gln4
Compositional biasi2297 – 2300Poly-Gln4

<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 KIX domain mediates binding to HIV-1 Tat.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri347 – 433TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1701 – 1744ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1765 – 1846TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1778 Eukaryota
COG5076 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155364

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000162_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q92793

KEGG Orthology (KO)

More...
KOi
K04498

Identification of Orthologs from Complete Genome Data

More...
OMAi
NACTRDI

Database of Orthologous Groups

More...
OrthoDBi
236283at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q92793

TreeFam database of animal gene trees

More...
TreeFami
TF101097

Family and domain databases

Conserved Domains Database

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

Database of protein disorder

More...
DisProti
DP02004

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1630.10, 1 hit
1.10.246.20, 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
3.30.60.90, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID00092

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
IPR043145 Znf_ZZ_sf

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q92793-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE
60 70 80 90 100
LGLLNSGNLV PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG
110 120 130 140 150
GQAQGQPNSA NMASLSAMGK SPLSQGDSSA PSLPKQAAST SGPTPAASQA
160 170 180 190 200
LNPQAQKQVG LATSSPATSQ TGPGICMNAN FNQTHPGLLN SNSGHSLINQ
210 220 230 240 250
ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA ETLTQVSPQM
260 270 280 290 300
TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK
310 320 330 340 350
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK
360 370 380 390 400
RKLIQQQLVL LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA
410 420 430 440 450
GKACQVAHCA SSRQIISHWK NCTRHDCPVC LPLKNASDKR NQQTILGSPA
460 470 480 490 500
SGIQNTIGSV GTGQQNATSL SNPNPIDPSS MQRAYAALGL PYMNQPQTQL
510 520 530 540 550
QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ QPPNLISESA
560 570 580 590 600
LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL
610 620 630 640 650
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY
660 670 680 690 700
YHLLAEKIYK IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP
710 720 730 740 750
VRPPNGPLSL PVNRMQVSQG MNSFNPMSLG NVQLPQAPMG PRAASPMNHS
760 770 780 790 800
VQMNSMGSVP GMAISPSRMP QPPNMMGAHT NNMMAQAPAQ SQFLPQNQFP
810 820 830 840 850
SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA SQLPCPPVTQ
860 870 880 890 900
SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT
910 920 930 940 950
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT
960 970 980 990 1000
PVHAQPPGTP LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE
1010 1020 1030 1040 1050
TQAEDTEPDP GESKGEPRSE MMEEDLQGAS QVKEETDIAE QKSEPMEVDE
1060 1070 1080 1090 1100
KKPEVKVEVK EEEESSSNGT ASQSTSPSQP RKKIFKPEEL RQALMPTLEA
1110 1120 1130 1140 1150
LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR KLDTGQYQEP
1160 1170 1180 1190 1200
WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC
1210 1220 1230 1240 1250
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT
1260 1270 1280 1290 1300
LGDDPSQPQT TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI
1310 1320 1330 1340 1350
IWPSGFVCDN CLKKTGRPRK ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN
1360 1370 1380 1390 1400
HPEAGEVFVR VVASSDKTVE VKPGMKSRFV DSGEMSESFP YRTKALFAFE
1410 1420 1430 1440 1450
EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF RPRCLRTAVY
1460 1470 1480 1490 1500
HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ
1510 1520 1530 1540 1550
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE
1560 1570 1580 1590 1600
ESIKELEQEE EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI
1610 1620 1630 1640 1650
SRANKKKPSM PNVSNDLSQK LYATMEKHKE VFFVIHLHAG PVINTLPPIV
1660 1670 1680 1690 1700
DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS LRRSKWSTLC MLVELHTQGQ
1710 1720 1730 1740 1750
DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH KMVKWGLGLD
1760 1770 1780 1790 1800
DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR
1810 1820 1830 1840 1850
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL
1860 1870 1880 1890 1900
RQQQIQHRLQ QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP
1910 1920 1930 1940 1950
QTPQPPAQPQ PSPVSMSPAG FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ
1960 1970 1980 1990 2000
PPPAAVEAAR QIEREAQQQQ HLYRVNINNS MPPGRTGMGT PGSQMAPVSL
2010 2020 2030 2040 2050
NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI SMQAQAAVAG
2060 2070 2080 2090 2100
PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF
2110 2120 2130 2140 2150
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP
2160 2170 2180 2190 2200
RPGVPPQQQA MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ
2210 2220 2230 2240 2250
QQQQQQQQQQ QQQQQQGSAG MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM
2260 2270 2280 2290 2300
QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ
2310 2320 2330 2340 2350
MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ
2360 2370 2380 2390 2400
SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL
2410 2420 2430 2440
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL
Length:2,442
Mass (Da):265,351
Last modified:October 17, 2006 - v3
<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:i3BEA9B8558BA1A5E
GO
Isoform 2 (identifier: Q92793-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     406-444: VAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQT → A

Show »
Length:2,404
Mass (Da):260,993
Checksum:iF95ED9F12B5DEDFB
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L466I3L466_HUMAN
CREB-binding protein
CREBBP
1,105Annotation score:

Annotation score:2 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>
I3L0Q1I3L0Q1_HUMAN
CREB-binding protein
CREBBP
254Annotation 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>
I3L293I3L293_HUMAN
CREB-binding protein
CREBBP
181Annotation 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>
I3L3I5I3L3I5_HUMAN
CREB-binding protein
CREBBP
196Annotation 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>
A0A1B0GUU0A0A1B0GUU0_HUMAN
CREB-binding protein
CREBBP
33Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAE06125 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti1511 – 1513FAE → NSG in AAC51340 (PubMed:9177780).Curated3
Sequence conflicti1724 – 1725ED → VV in AAC51340 (PubMed:9177780).Curated2
Sequence conflicti1770L → V in AAC51770 (PubMed:9238046).Curated1
Sequence conflicti1789N → F in AAC51340 (PubMed:9177780).Curated1
Sequence conflicti1812T → P in AAC51340 (PubMed:9177780).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072912503Q → H1 PublicationCorresponds to variant dbSNP:rs748447855Ensembl.1
Natural variantiVAR_072913532P → T1 PublicationCorresponds to variant dbSNP:rs902901184Ensembl.1
Natural variantiVAR_072914546I → N1 Publication1
Natural variantiVAR_072915650Y → F in RSTS1. 1 Publication1
Natural variantiVAR_072916789A → T in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs746728741Ensembl.1
Natural variantiVAR_072917910T → A in RSTS1; incomplete. 1 PublicationCorresponds to variant dbSNP:rs143247685Ensembl.1
Natural variantiVAR_0373051175Y → C in RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3. 3 PublicationsCorresponds to variant dbSNP:rs28937315Ensembl.1
Natural variantiVAR_0729181278E → A in RSTS1. 1 Publication1
Natural variantiVAR_0350801278E → K in RSTS1; abolishes acetyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs267606752Ensembl.1
Natural variantiVAR_0155781378R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 2 PublicationsCorresponds to variant dbSNP:rs121434626Ensembl.1
Natural variantiVAR_0729191406D → Y in RSTS1. 1 Publication1
Natural variantiVAR_0279531414V → I. Corresponds to variant dbSNP:rs130015Ensembl.1
Natural variantiVAR_0729201415Q → P in RSTS1. 1 Publication1
Natural variantiVAR_0350811447T → I in RSTS1. 1 Publication1
Natural variantiVAR_0350821450Y → H in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs1555473499Ensembl.1
Natural variantiVAR_0350831470H → R in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs797044860Ensembl.1
Natural variantiVAR_0729211475P → T in RSTS1. 1 Publication1
Natural variantiVAR_0729221503Y → F in RSTS1. 1 Publication1
Natural variantiVAR_0729231507L → P in RSTS1. 1 PublicationCorresponds to variant dbSNP:rs1057520191Ensembl.1
Natural variantiVAR_0729241543D → N in RSTS1. 1 Publication1
Natural variantiVAR_0350841664R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications1
Natural variantiVAR_0785571710C → R in MKHK1. 1 Publication1
Natural variantiVAR_0819791719H → D in MKHK1. 1 Publication1
Natural variantiVAR_0819801724E → K in MKHK1. 1 Publication1
Natural variantiVAR_0785581747L → R in MKHK1. 1 Publication1
Natural variantiVAR_0819811782A → V in MKHK1. 1 Publication1
Natural variantiVAR_0785591786R → P in MKHK1. 1 Publication1
Natural variantiVAR_0785601819C → F in MKHK1. 1 Publication1
Natural variantiVAR_0785611826C → W in MKHK1. 1 Publication1
Natural variantiVAR_0819821829H → D in MKHK1. 1 Publication1
Natural variantiVAR_0785621838C → Y in MKHK1. 1 Publication1
Natural variantiVAR_0819831865 – 1866MR → I in MKHK1. 1 Publication2
Natural variantiVAR_0785631867R → Q in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs1131691326Ensembl.1
Natural variantiVAR_0785641867R → W in MKHK1. 1 Publication1
Natural variantiVAR_0819841868R → Q in MKHK1. 1 Publication1
Natural variantiVAR_0785651868R → W in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs886039491Ensembl.1
Natural variantiVAR_0819851870A → P in MKHK1. 1 Publication1
Natural variantiVAR_0785661872M → V in MKHK1. 2 PublicationsCorresponds to variant dbSNP:rs797045037Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045700406 – 444VAHCA…RNQQT → A in isoform 2. 1 PublicationAdd BLAST39

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
U85962 mRNA Translation: AAC51331.2
U89354 mRNA Translation: AAC51339.1
U89355 mRNA Translation: AAC51340.1
U47741 mRNA Translation: AAC51770.1
AB210043 mRNA Translation: BAE06125.1 Different initiation.
CH471112 Genomic DNA Translation: EAW85335.1
CH471112 Genomic DNA Translation: EAW85336.1
CH471112 Genomic DNA Translation: EAW85337.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10509.1 [Q92793-1]
CCDS45399.1 [Q92793-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S39162

NCBI Reference Sequences

More...
RefSeqi
NP_001073315.1, NM_001079846.1 [Q92793-2]
NP_004371.2, NM_004380.2 [Q92793-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262367; ENSP00000262367; ENSG00000005339 [Q92793-1]
ENST00000382070; ENSP00000371502; ENSG00000005339 [Q92793-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1387

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1387

UCSC genome browser

More...
UCSCi
uc002cvv.4 human [Q92793-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

P300/CBP entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85962 mRNA Translation: AAC51331.2
U89354 mRNA Translation: AAC51339.1
U89355 mRNA Translation: AAC51340.1
U47741 mRNA Translation: AAC51770.1
AB210043 mRNA Translation: BAE06125.1 Different initiation.
CH471112 Genomic DNA Translation: EAW85335.1
CH471112 Genomic DNA Translation: EAW85336.1
CH471112 Genomic DNA Translation: EAW85337.1
CCDSiCCDS10509.1 [Q92793-1]
CCDS45399.1 [Q92793-2]
PIRiS39162
RefSeqiNP_001073315.1, NM_001079846.1 [Q92793-2]
NP_004371.2, NM_004380.2 [Q92793-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JSPNMR-B1081-1197[»]
1LIQNMR-A376-402[»]
1RDTX-ray2.40E58-80[»]
1WO3NMR-A387-398[»]
1WO4NMR-A387-398[»]
1WO5NMR-A387-398[»]
1WO6NMR-A376-400[»]
1WO7NMR-A376-400[»]
1ZOQX-ray2.37C/D2065-2111[»]
2D82NMR-A1081-1197[»]
2KJENMR-A1763-1854[»]
2KWFNMR-A587-673[»]
2L84NMR-A1081-1197[»]
2L85NMR-A1081-1197[»]
2LXSNMR-A587-673[»]
2LXTNMR-A587-673[»]
2N1ANMR-B1699-1751[»]
2RNYNMR-A1081-1197[»]
3DWYX-ray1.98A/B1081-1197[»]
3P1CX-ray1.82A/B1081-1197[»]
3P1DX-ray1.86A/B1081-1197[»]
3P1EX-ray1.80A/B1081-1197[»]
3P1FX-ray1.63A/B1081-1197[»]
3SVHX-ray1.80A/B1081-1197[»]
4A9KX-ray1.81A/B1081-1197[»]
4N3WX-ray1.90A1080-1316[»]
4N4FX-ray1.83A1080-1316[»]
4NR4X-ray1.69A/B1081-1197[»]
4NR5X-ray1.66A1081-1197[»]