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Entry version 130 (07 Oct 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Histone lysine acetyltransferase CREBBP

Gene

Crebbp

Organism
Rattus norvegicus (Rat)
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 (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (By similarity). 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 (By similarity). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (By similarity). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (By similarity). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (By similarity). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (By similarity). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity).By similarity

<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 bindingi362Zinc 1By similarity1
Metal bindingi366Zinc 1By similarity1
Metal bindingi379Zinc 1By similarity1
Metal bindingi384Zinc 1By similarity1
Metal bindingi393Zinc 2By similarity1
Metal bindingi397Zinc 2By similarity1
Metal bindingi403Zinc 2By similarity1
Metal bindingi408Zinc 2By similarity1
Metal bindingi417Zinc 3By similarity1
Metal bindingi421Zinc 3By similarity1
Metal bindingi426Zinc 3By similarity1
Metal bindingi429Zinc 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 sitei1494Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1499Acetyl-CoABy similarity1
Binding sitei1503Acetyl-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 fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-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, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-201722, Formation of the beta-catenin:TCF transactivating complex
R-RNO-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-RNO-3371568, Attenuation phase
R-RNO-400206, Regulation of lipid metabolism by PPARalpha
R-RNO-5621575, CD209 (DC-SIGN) signaling
R-RNO-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-RNO-918233, TRAF3-dependent IRF activation pathway
R-RNO-933541, TRAF6 mediated IRF7 activation
R-RNO-9617629, Regulation of FOXO transcriptional activity by acetylation

<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:
Histone lysine acetyltransferase CREBBP (EC:2.3.1.48By similarity)
Alternative name(s):
Protein-lysine acetyltransferase CREBBP (EC:2.3.1.-By similarity)
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2401, Crebbp

<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 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 methionineiRemovedBy similarity
<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_00004093852 – 2442Histone lysine acetyltransferase CREBBPAdd 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-acetylalanineBy similarity1
Modified residuei120PhosphoserineBy similarity1
Modified residuei219Omega-N-methylarginineBy similarity1
Modified residuei600Asymmetric dimethylarginineBy similarity1
Modified residuei624Asymmetric dimethylarginineBy similarity1
Modified residuei656N6-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-linki999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1015N6-acetyllysineBy similarity1
Modified residuei1031PhosphoserineBy similarity1
Cross-linki1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1077PhosphoserineBy similarity1
Modified residuei1217N6-acetyllysineBy similarity1
Modified residuei1383Phosphoserine; by IKKABy similarity1
Modified residuei1387Phosphoserine; by IKKABy similarity1
Modified residuei1584N6-acetyllysineBy similarity1
Modified residuei1592N6-acetyllysineBy similarity1
Modified residuei1593N6-acetyllysineBy similarity1
Modified residuei1596N6-acetyllysineBy similarity1
Modified residuei1598N6-acetyllysineBy similarity1
Modified residuei1742N6-acetyllysineBy similarity1
Modified residuei1745N6-acetyllysineBy similarity1
Modified residuei1764PhosphoserineBy similarity1
Modified residuei2064PhosphoserineCombined sources1
Modified residuei2077PhosphoserineBy similarity1
Modified residuei2080PhosphoserineBy similarity1
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-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B.By similarity
Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q6JHU9

PRoteomics IDEntifications database

More...
PRIDEi
Q6JHU9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6JHU9

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

More...
PhosphoSitePlusi
Q6JHU9

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in hypothalamus and cortex.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by IL-1 treatment.1 Publication

<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 phosphorylated CREB1.

Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A.

Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5, DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12.

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

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

Interacts with MAF.

Interacts with MTDH.

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

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

Interacts with MECOM.

Interacts with CITED1 (via C-terminus)

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

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.

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

Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity).

Forms a complex with KMT2A and CREB1 (By similarity).

Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q6JHU9, 1 interactor

Molecular INTeraction database

More...
MINTi
Q6JHU9

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000007079

<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

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q6JHU9

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

More...
SMRi
Q6JHU9

Database of comparative protein structure models

More...
ModBasei
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%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>Domaini586 – 665KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1104 – 1176BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1324 – 1701CBP/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>Regioni226 – 409Interaction with SRCAPBy similarityAdd BLAST184
Regioni1125 – 1171Interaction with histoneBy similarityAdd BLAST47
Regioni1163 – 1181Interaction with ASF1ABy similarityAdd BLAST19
Regioni1434 – 1436Interaction with histoneBy similarity3
Regioni1435 – 1437Acetyl-CoA bindingBy similarity3
Regioni1447 – 1448Acetyl-CoA bindingBy similarity2

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 coili1548 – 1575Sequence analysisAdd BLAST28

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 biasi682 – 961Pro-richAdd BLAST280
Compositional biasi1556 – 1563Poly-Glu8
Compositional biasi1853 – 2370Gln-richAdd BLAST518
Compositional biasi1879 – 2065Pro-richAdd BLAST187
Compositional biasi1944 – 1949Poly-Pro6
Compositional biasi1968 – 1971Poly-Gln4
Compositional biasi2082 – 2086Poly-Gln5
Compositional biasi2200 – 2217Poly-GlnAdd BLAST18
Compositional biasi2297 – 2300Poly-Gln4

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6JHU9

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
1.10.246.20, 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

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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q6JHU9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL
60 70 80 90 100
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG
110 120 130 140 150
QAQGQPNSTS MASLGAMGKS PLNPGDSSTP SLPKQAASTS GPTPPASQAL
160 170 180 190 200
NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA
210 220 230 240 250
QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA
260 270 280 290 300
GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ
310 320 330 340 350
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA TGPTADPEKR
360 370 380 390 400
KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG
410 420 430 440 450
KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS
460 470 480 490 500
GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ
510 520 530 540 550
PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL
560 570 580 590 600
PTSLGATNPL MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
610 620 630 640 650
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY
660 670 680 690 700
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV
710 720 730 740 750
RPPNGPLSLP VNRVQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV
760 770 780 790 800
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS
810 820 830 840 850
SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP QTSQLPCPPV
860 870 880 890 900
TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP
910 920 930 940 950
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP
960 970 980 990 1000
TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT
1010 1020 1030 1040 1050
EVQTDDAEPD PAESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE
1060 1070 1080 1090 1100
EKKPEVKVEA KEEEENSANG TASQSTSPSQ PRKKIFKPEE LRQALMPTLE
1110 1120 1130 1140 1150
ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE
1160 1170 1180 1190 1200
PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
1210 1220 1230 1240 1250
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV
1260 1270 1280 1290 1300
TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD
1310 1320 1330 1340 1350
IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ
1360 1370 1380 1390 1400
NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF
1410 1420 1430 1440 1450
EEIDGVDVCF FGMHVQEYGS DCPPPNTRRV YISYLDSIHF FRPRCLRTAV
1460 1470 1480 1490 1500
YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
1510 1520 1530 1540 1550
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL
1560 1570 1580 1590 1600
EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS
1610 1620 1630 1640 1650
ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI
1660 1670 1680 1690 1700
VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG
1710 1720 1730 1740 1750
QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL
1760 1770 1780 1790 1800
DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
1810 1820 1830 1840 1850
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK
1860 1870 1880 1890 1900
LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST
1910 1920 1930 1940 1950
PQTPQPPAQP QPSPVNMSPA GFPSVARTQP PTIVSAGKPT NQVPAPPPPA
1960 1970 1980 1990 2000
QPPPAAVEAA RQIEREGQQQ QHLYRANINN GMPPGRAGMG TPGSQMAPVG
2010 2020 2030 2040 2050
LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA
2060 2070 2080 2090 2100
GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
2110 2120 2130 2140 2150
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV
2160 2170 2180 2190 2200
PRPGVPPPQQ AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ
2210 2220 2230 2240 2250
HQQQQQQQQQ QQQQQQQSSA SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM
2260 2270 2280 2290 2300
QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ
2310 2320 2330 2340 2350
MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ
2360 2370 2380 2390 2400
SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL
2410 2420 2430 2440
GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL
Length:2,442
Mass (Da):265,424
Last modified:July 5, 2004 - v1
<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:i2E77EF213C72C024
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1M9G7F1M9G7_RAT
Histone acetyltransferase
Crebbp
2,444Annotation score:

Annotation score:4 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>

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
AY462245 mRNA Translation: AAR23149.1

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:2401, rat

<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
AY462245 mRNA Translation: AAR23149.1

3D structure databases

BMRBiQ6JHU9
SMRiQ6JHU9
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ6JHU9, 1 interactor
MINTiQ6JHU9
STRINGi10116.ENSRNOP00000007079

PTM databases

iPTMnetiQ6JHU9
PhosphoSitePlusiQ6JHU9

Proteomic databases

PaxDbiQ6JHU9
PRIDEiQ6JHU9

Genome annotation databases

UCSCiRGD:2401, rat

Organism-specific databases

RGDi2401, Crebbp

Phylogenomic databases

eggNOGiKOG1778, Eukaryota
InParanoidiQ6JHU9

Enzyme and pathway databases

ReactomeiR-RNO-201722, Formation of the beta-catenin:TCF transactivating complex
R-RNO-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-RNO-3371568, Attenuation phase
R-RNO-400206, Regulation of lipid metabolism by PPARalpha
R-RNO-5621575, CD209 (DC-SIGN) signaling
R-RNO-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-RNO-918233, TRAF3-dependent IRF activation pathway
R-RNO-933541, TRAF6 mediated IRF7 activation
R-RNO-9617629, Regulation of FOXO transcriptional activity by acetylation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6JHU9

Family and domain databases

CDDicd15802, RING_CBP-p300, 1 hit
Gene3Di1.10.1630.10, 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
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
IPR043145, Znf_ZZ_sf
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiCBP_RAT
<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: Q6JHU9
<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%5Fand%5Fisoforms">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: July 5, 2004
Last modified: October 7, 2020
This is version 130 of the entry and version 1 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

Reference proteome
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