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UniProtKB - P45481 (CBP_MOUSE)

Entry version 220 (10 Feb 2021)
Sequence version 3 (27 Jul 2011)
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Protein

Histone lysine acetyltransferase CREBBP

Gene

Crebbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (PubMed:10207073, PubMed:11701890, PubMed:16287980, PubMed:15220471). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes (By similarity). Acts as a coactivator of ALX1 (By similarity). 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) (PubMed:24737000). 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 similarity5 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 bindingi362Zinc 11
Metal bindingi366Zinc 11
Metal bindingi379Zinc 11
Metal bindingi384Zinc 11
Metal bindingi393Zinc 21
Metal bindingi397Zinc 21
Metal bindingi403Zinc 21
Metal bindingi408Zinc 21
Metal bindingi417Zinc 31
Metal bindingi421Zinc 31
Metal bindingi426Zinc 31
Metal bindingi429Zinc 31
<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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-MMU-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-201722, Formation of the beta-catenin:TCF transactivating complex
R-MMU-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-MMU-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-3371568, Attenuation phase
R-MMU-350054, Notch-HLH transcription pathway
R-MMU-400206, Regulation of lipid metabolism by PPARalpha
R-MMU-5621575, CD209 (DC-SIGN) signaling
R-MMU-8866907, Activation of the TFAP2 (AP-2) family of transcription factors
R-MMU-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-MMU-8941856, RUNX3 regulates NOTCH signaling
R-MMU-9018519, Estrogen-dependent gene expression
R-MMU-918233, TRAF3-dependent IRF activation pathway
R-MMU-933541, TRAF6 mediated IRF7 activation
R-MMU-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.-1 Publication)
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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

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

More...MGIi		MGI:1098280, 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 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

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>Mutagenesisi600R → N: Abolishes binding to CREB. 1 Publication1
Mutagenesisi999K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-1034 and R-1057. 1 Publication1
Mutagenesisi1015K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1034K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1057. 1 Publication1
Mutagenesisi1043K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1053K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1057K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1034. 1 Publication1
Mutagenesisi1061K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1087K → R: No change in sumoylation. 1
Mutagenesisi1690 – 1691LC → KL: Abolishes histone acetyltransferase activity. 1 Publication2

<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_00002111912 – 2441Histone lysine acetyltransferase CREBBPAdd BLAST2440

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 residuei120PhosphoserineCombined sources1
Modified residuei219Omega-N-methylarginineBy similarity1
Modified residuei600Asymmetric dimethylarginine1 Publication1
Modified residuei624Asymmetric dimethylarginine1 Publication1
Modified residuei656N6-acetyllysineCombined sources1
<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)1 Publication
Modified residuei1015N6-acetyllysineBy similarity1
Modified residuei1031PhosphoserineBy similarity1
Cross-linki1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei1077PhosphoserineBy similarity1
Modified residuei1217N6-acetyllysineCombined sources1
Modified residuei1383Phosphoserine; by IKKABy similarity1
Modified residuei1387Phosphoserine; by IKKABy similarity1
Modified residuei1584N6-acetyllysineBy similarity1
Modified residuei1592N6-acetyllysineBy similarity1
Modified residuei1593N6-acetyllysineBy similarity1
Modified residuei1596N6-acetyllysineCombined sources1
Modified residuei1598N6-acetyllysineCombined sources1
Modified residuei1742N6-acetyllysineBy similarity1
Modified residuei1745N6-acetyllysineCombined sources1
Modified residuei1764PhosphoserineBy similarity1
Modified residuei2064PhosphoserineCombined sources1
Modified residuei2077PhosphoserineBy similarity1
Modified residuei2080PhosphoserineBy similarity1
Modified residuei2350PhosphoserineCombined sources1

<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.1 Publication
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.1 Publication
Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P45481

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P45481

MaxQB - The MaxQuant DataBase

More...MaxQBi		P45481

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

More...PaxDbi		P45481

PRoteomics IDEntifications database

More...PRIDEi		P45481

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P45481

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

More...PhosphoSitePlusi		P45481

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P45481

<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

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

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

Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A.

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

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

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 (By similarity).

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

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

Interacts with MECOM and MTDH.

Interacts with ASF1A and ASF1B; this promotes histone acetylation.

Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4 (By similarity).

Interacts with CITED1 (via C-terminus).

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

Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region).

Interacts with phosphorylated CREB1.

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 NPAS2, CLOCK and ARNTL/BMAL1.

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 similarity14 Publications

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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P45481

Database of interacting proteins

More...DIPi		DIP-5974N

Protein interaction database and analysis system

More...IntActi		P45481, 39 interactors

Molecular INTeraction database

More...MINTi		P45481

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000023165

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P45481, 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

12441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P45481

Small Angle Scattering Biological Data Bank

More...SASBDBi		P45481

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

More...SMRi		P45481

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		P45481

<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

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 biasi1062 – 1065Poly-Glu4
Compositional biasi1556 – 1563Poly-Glu8
Compositional biasi1944 – 1949Poly-Pro6
Compositional biasi1968 – 1971Poly-Gln4
Compositional biasi2082 – 2086Poly-Gln5
Compositional biasi2200 – 2216Poly-GlnAdd BLAST17
Compositional biasi2296 – 2299Poly-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, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1778, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P45481

Family and domain databases

Conserved Domains Database

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

Database of protein disorder

More...DisProti		DP00348

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		IID50008

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 6 potential isoforms that are computationally mapped.Show allAlign All

P45481-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL 
        60         70         80         90        100
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG 
       110        120        130        140        150
QAQGQPNSTN MASLGAMGKS PLNQGDSSTP NLPKQAASTS 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 TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ 
       310        320        330        340        350
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA 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 MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 
       610        620        630        640        650
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY 
       660        670        680        690        700
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV 
       710        720        730        740        750
RPPNGPLPLP VNRMQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV 
       760        770        780        790        800
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS 
       810        820        830        840        850
SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP QASQLPCPPV 
       860        870        880        890        900
TQSPLHPTPP PASTAAGMPS LQHPTAPGMT 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
EVQTDDAEPE PTESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE 
      1060       1070       1080       1090       1100
EKKPEVKVEA KEEEENSSND 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 FGMHVQNTAL IAPHQIQGRV 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 GFPNVARTQP PTIVSAGKPT NQVPAPPPPA 
      1960       1970       1980       1990       2000
QPPPAAVEAA RQIEREAQQQ QHLYRANINN GMPPGRAGMG TPGSQMTPVG 
      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
PRPGVPPPQP AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ 
      2210       2220       2230       2240       2250
HQQQQQQQQQ QQQQQQNSAS LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ 
      2260       2270       2280       2290       2300
QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA DSTPNIQQAL QQRILQQQQM 
      2310       2320       2330       2340       2350
KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN QVRSPAPVQS 
      2360       2370       2380       2390       2400
PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG 
      2410       2420       2430       2440 
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
Length:2,441
Mass (Da):265,494
Last modified:July 27, 2011 - 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:iD89AF52B7BD33347
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VPR5F8VPR5_MOUSE
Histone acetyltransferase
Crebbp
2,441Annotation 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>
A0A0U1RQB6A0A0U1RQB6_MOUSE
Histone acetyltransferase
Crebbp
2,403Annotation 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>
A0A0U1RPL2A0A0U1RPL2_MOUSE
Histone acetyltransferase
Crebbp
1,107Annotation 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>
A0A0U1RP23A0A0U1RP23_MOUSE
Histone acetyltransferase
Crebbp
172Annotation 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>
A0A0U1RP46A0A0U1RP46_MOUSE
Histone acetyltransferase
Crebbp
127Annotation 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>
A0A0U1RPQ3A0A0U1RPQ3_MOUSE
Histone lysine acetyltransferase CR...
Crebbp
247Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti400G → P in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti530I → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti670S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti826V → E in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti978S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1159W → R in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1239E → G in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1417N → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1429R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1466G → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1470G → A in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1850 – 1851KL → NV in AAB28651 (PubMed:8413673).Curated2
Sequence conflicti1859R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1987A → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2060P → N in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2381S → T in AAB28651 (PubMed:8413673).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
S66385 mRNA Translation: AAB28651.1
AC132380 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS27915.1

Protein sequence database of the Protein Information Resource

More...PIRi		S39161

<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
S66385 mRNA Translation: AAB28651.1
AC132380 Genomic DNA No translation available.
CCDSiCCDS27915.1
PIRiS39161

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
1F81NMR-A1764-1850[»]
1JJSNMR-A2067-2112[»]
1KBHNMR-B2059-2117[»]
1KDXNMR-A586-666[»]
1L8CNMR-A345-439[»]
1R8UNMR-B340-439[»]
1SB0NMR-A586-672[»]
1TOTNMR-A1700-1751[»]
1U2NNMR-A340-439[»]
2AGHNMR-B586-672[»]
2C52NMR-A2059-2117[»]
2KA4NMR-A340-439[»]
2KA6NMR-A1764-1855[»]
2KKJNMR-A2059-2117[»]
2L14NMR-A2059-2117[»]
2LQHNMR-A586-672[»]
2LQINMR-A586-672[»]
2LWWNMR-A340-439[»]
4I9OX-ray2.00A586-672[»]
5HOUNMR-A340-439[»]
5HP0NMR-A1764-1857[»]
5HPDNMR-A1764-1855[»]
5U4KNMR-A586-672[»]
5U7GX-ray2.40A/B1079-1556[»]
5W0IX-ray1.43A1083-1198[»]
6DMXX-ray2.80B/D/G/I586-672[»]
6DNQX-ray2.35B/D586-672[»]
BMRBiP45481
SASBDBiP45481
SMRiP45481
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

CORUMiP45481
DIPiDIP-5974N
IntActiP45481, 39 interactors
MINTiP45481
STRINGi10090.ENSMUSP00000023165

PTM databases

iPTMnetiP45481
PhosphoSitePlusiP45481
SwissPalmiP45481

Proteomic databases

EPDiP45481
jPOSTiP45481
MaxQBiP45481
PaxDbiP45481
PRIDEiP45481

Organism-specific databases

MGIiMGI:1098280, Crebbp

Phylogenomic databases

eggNOGiKOG1778, Eukaryota
InParanoidiP45481

Enzyme and pathway databases

ReactomeiR-MMU-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-MMU-201722, Formation of the beta-catenin:TCF transactivating complex
R-MMU-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-MMU-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-MMU-3371568, Attenuation phase
R-MMU-350054, Notch-HLH transcription pathway
R-MMU-400206, Regulation of lipid metabolism by PPARalpha
R-MMU-5621575, CD209 (DC-SIGN) signaling
R-MMU-8866907, Activation of the TFAP2 (AP-2) family of transcription factors
R-MMU-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-MMU-8941856, RUNX3 regulates NOTCH signaling
R-MMU-9018519, Estrogen-dependent gene expression
R-MMU-918233, TRAF3-dependent IRF activation pathway
R-MMU-933541, TRAF6 mediated IRF7 activation
R-MMU-9617629, Regulation of FOXO transcriptional activity by acetylation

Miscellaneous databases

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

More...ChiTaRSi		Crebbp, mouse
EvolutionaryTraceiP45481

Protein Ontology

More...PROi		PR:P45481
RNActiP45481, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

CDDicd15802, RING_CBP-p300, 1 hit
DisProtiDP00348
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
IDEALiIID50008
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_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P45481
Secondary accession number(s): E9QPH4
<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: November 1, 1995
Last sequence update: July 27, 2011
Last modified: February 10, 2021
This is version 220 of the entry and version 3 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

3D-structure, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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