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UniProtKB - Q92793 (CBP_HUMAN)

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Protein

CREB-binding protein

Gene

CREBBP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. 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. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902).6 Publications

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Binding sitei1493Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1498Acetyl-CoABy similarity1
Binding sitei1502Acetyl-CoABy similarity1

Regions

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

GO - Molecular functioni

  • acetyltransferase activity Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • damaged DNA binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • MRF binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • peptide N-acetyltransferase activity Source: Reactome
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription coactivator activity Source: BHF-UCL
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • signal transducer activity Source: ProtInc
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL
  • transcriptional repressor activity, RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • cellular response to UV Source: UniProtKB
  • embryonic digit morphogenesis Source: BHF-UCL
  • histone acetylation Source: UniProtKB
  • homeostatic process Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • Notch signaling pathway Source: Reactome
  • N-terminal peptidyl-lysine acetylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  • positive regulation of type I interferon production Source: Reactome
  • protein acetylation Source: UniProtKB
  • protein complex assembly Source: ProtInc
  • regulation of apoptotic process Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of lipid metabolic process Source: Reactome
  • regulation of smoothened signaling pathway Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: HGNC
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • response to hypoxia Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Molecular functionActivator, Acyltransferase, Transferase
Biological processBiological rhythms, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-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-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
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-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (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-8941856. RUNX3 regulates NOTCH signaling.
R-HSA-8951671. RUNX3 regulates YAP1-mediated transcription.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ92793.
SIGNORiQ92793.

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.481 Publication)
Gene namesi
Name:CREBBP
Synonyms:CBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2348. CREBBP.

Subcellular locationi

  • Cytoplasm
  • Nucleus

    • Note: Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • histone acetyltransferase complex Source: InterPro
  • nuclear body Source: UniProtKB
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

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.
See also OMIM:180849
Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 Publication1
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 Publication1
Natural variantiVAR_0729241543D → N in RSTS1. 1 Publication1
Natural variantiVAR_0350841664R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications1
De novo missense mutations in the last part of exon 30 or beginning of exon 31 are associated with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features. No patients have broad thumbs. Patients have intellectual disability of variable severity, a marked speech delay, short stature and microcephaly. Main facial characteristics include short palpebral fissures, telecanthi, depressed nasal ridge, short nose, anteverted nares, short columella and long philtrum.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Sitei29 – 30Breakpoint for translocation to form KAT6B-CREBBP2
Sitei266 – 267Breakpoint for translocation to form KAT6A-CREBBP2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1387.
MalaCardsiCREBBP.
MIMi180849. phenotype.
OpenTargetsiENSG00000005339.
Orphaneti370026. 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.
PharmGKBiPA26866.

Chemistry databases

ChEMBLiCHEMBL5747.
GuidetoPHARMACOLOGYi2734.

Polymorphism and mutation databases

BioMutaiCREBBP.
DMDMi116241283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002111902 – 2442CREB-binding proteinAdd BLAST2441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

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

EPDiQ92793.
MaxQBiQ92793.
PaxDbiQ92793.
PeptideAtlasiQ92793.
PRIDEiQ92793.

PTM databases

iPTMnetiQ92793.
PhosphoSitePlusiQ92793.

Expressioni

Gene expression databases

BgeeiENSG00000005339.
CleanExiHS_CREBBP.
ExpressionAtlasiQ92793. baseline and differential.
GenevisibleiQ92793. HS.

Organism-specific databases

HPAiCAB004212.
HPA055861.

Interactioni

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 HTLV-1 Tax and p30II. Interacts with HIV-1 Tat. 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 (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 human herpes virus 8/HHV-8 protein vIRF-1; this interaction inhibits CREBBP binding to IRF3. 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).By similarity31 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • MRF binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi107777. 314 interactors.
DIPiDIP-952N.
IntActiQ92793. 71 interactors.
MINTiMINT-104685.
STRINGi9606.ENSP00000262367.

Chemistry databases

BindingDBiQ92793.

Structurei

Secondary structure

12442
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 73Combined sources5
Helixi377 – 379Combined sources3
Turni383 – 388Combined sources6
Helixi391 – 395Combined sources5
Turni593 – 596Combined sources4
Helixi598 – 612Combined sources15
Turni618 – 622Combined sources5
Helixi624 – 642Combined sources19
Helixi647 – 669Combined sources23
Turni670 – 672Combined sources3
Helixi1087 – 1102Combined sources16
Turni1105 – 1108Combined sources4
Helixi1109 – 1111Combined sources3
Helixi1117 – 1120Combined sources4
Helixi1125 – 1128Combined sources4
Helixi1135 – 1143Combined sources9
Beta strandi1146 – 1149Combined sources4
Helixi1150 – 1167Combined sources18
Turni1169 – 1171Combined sources3
Helixi1173 – 1195Combined sources23
Beta strandi1214 – 1218Combined sources5
Beta strandi1226 – 1230Combined sources5
Turni1231 – 1233Combined sources3
Beta strandi1234 – 1237Combined sources4
Turni1238 – 1240Combined sources3
Beta strandi1266 – 1272Combined sources7
Beta strandi1280 – 1282Combined sources3
Turni1284 – 1286Combined sources3
Beta strandi1289 – 1291Combined sources3
Helixi1292 – 1295Combined sources4
Turni1309 – 1311Combined sources3
Turni1708 – 1710Combined sources3
Beta strandi1718 – 1721Combined sources4
Beta strandi1725 – 1728Combined sources4
Helixi1730 – 1736Combined sources7
Beta strandi1742 – 1744Combined sources3
Helixi1765 – 1784Combined sources20
Helixi1793 – 1805Combined sources13
Turni1811 – 1815Combined sources5
Helixi1817 – 1832Combined sources16
Helixi1841 – 1853Combined sources13
Helixi2066 – 2072Combined sources7
Helixi2080 – 2091Combined sources12
Helixi2094 – 2103Combined sources10
Turni2104 – 2106Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
4NR6X-ray1.66A1081-1197[»]
4NR7X-ray1.20A1081-1197[»]
4NYVX-ray1.83A/B/C/D1081-1197[»]
4NYWX-ray1.43A1081-1197[»]
4NYXX-ray1.10A1081-1197[»]
4OUFX-ray1.40A/B1082-1197[»]
4TQNX-ray1.70A1081-1197[»]
4TS8X-ray2.00A1081-1197[»]
4WHUX-ray2.11A1081-1197[»]
4YK0X-ray1.65A/B/C/D1083-1196[»]
5CGPX-ray1.96A1081-1197[»]
5DBMX-ray1.86A/B/C1082-1197[»]
5EICX-ray1.50A/B1081-1197[»]
5ENGX-ray1.30A1081-1197[»]
5EP7X-ray1.20A1081-1197[»]
5H85X-ray1.70A1081-1197[»]
5I83X-ray1.35A1082-1197[»]
5I86X-ray1.05A/B1082-1197[»]
5I89X-ray1.07A1082-1197[»]
5I8BX-ray1.52A1081-1312[»]
5I8GX-ray1.41A1081-1312[»]
5J0DX-ray1.05A1081-1197[»]
5JEMX-ray2.50C/D/F/H2065-2111[»]
5KTUX-ray1.38A/B1082-1197[»]
5KTWX-ray1.09A/B/C1085-1194[»]
5KTXX-ray1.27A1085-1194[»]
5MPZX-ray1.40A1081-1197[»]
5MQEX-ray1.65A/B1081-1197[»]
5MQGX-ray1.35A/B1081-1197[»]
5MQKX-ray1.53A/B1081-1197[»]
5TB6X-ray1.79A1081-1197[»]
ProteinModelPortaliQ92793.
SMRiQ92793.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini587 – 666KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1103 – 1175BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1323 – 1700CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST378

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

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

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiQ92793.
KOiK04498.
OMAiSGHSLMN.
OrthoDBiEOG091G0L04.
PhylomeDBiQ92793.
TreeFamiTF101097.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' 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
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

Note: No experimental confirmation available.
Show »
Length:2,404
Mass (Da):260,993
Checksum:iF95ED9F12B5DEDFB
GO

Sequence cautioni

The sequence BAE06125 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 Publication1
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 Publication1
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 Publication1
Natural variantiVAR_0729241543D → N in RSTS1. 1 Publication1
Natural variantiVAR_0350841664R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications1
Natural variantiVAR_0785571710C → R Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785581747L → R Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785591786R → P Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785601819C → F Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785611826C → W Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785621838C → Y Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785631867R → Q Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785641867R → W Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785651868R → W Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 Publication1
Natural variantiVAR_0785661872M → V Probable disease-associated mutation found in patient with growth retardation, craniofacial dysmorphism and additional Rubinstein-Taybi-like features; de novo mutation. 1 PublicationCorresponds to variant dbSNP:rs797045037Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_045700406 – 444VAHCA…RNQQT → A in isoform 2. 1 PublicationAdd BLAST39

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]
UniGeneiHs.459759.

Genome annotation databases

EnsembliENST00000262367; ENSP00000262367; ENSG00000005339. [Q92793-1]
ENST00000382070; ENSP00000371502; ENSG00000005339. [Q92793-2]
GeneIDi1387.
KEGGihsa:1387.
UCSCiuc002cvv.4. human. [Q92793-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCBP_HUMAN
AccessioniPrimary (citable) accession number: Q92793
Secondary accession number(s): D3DUC9
, O00147, Q16376, Q4LE28
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 17, 2006
Last modified: July 5, 2017
This is version 213 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references