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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 + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi363 – 3631Zinc 1By similarity
Metal bindingi367 – 3671Zinc 1By similarity
Metal bindingi380 – 3801Zinc 1By similarity
Metal bindingi385 – 3851Zinc 1By similarity
Metal bindingi394 – 3941Zinc 2By similarity
Metal bindingi398 – 3981Zinc 2By similarity
Metal bindingi404 – 4041Zinc 2By similarity
Metal bindingi409 – 4091Zinc 2By similarity
Metal bindingi418 – 4181Zinc 3By similarity
Metal bindingi422 – 4221Zinc 3By similarity
Metal bindingi427 – 4271Zinc 3By similarity
Metal bindingi430 – 4301Zinc 3By similarity
Binding sitei1493 – 14931Acetyl-CoA; via carbonyl oxygenBy similarity
Binding sitei1498 – 14981Acetyl-CoABy similarity
Binding sitei1502 – 15021Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri347 – 43387TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1701 – 174444ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1765 – 184682TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

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

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • cell-cell adhesion Source: Ensembl
  • cell proliferation Source: Ensembl
  • cellular lipid metabolic process 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 cell adhesion molecule production Source: Ensembl
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • positive regulation of NIK/NF-kappaB signaling Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • 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 smoothened signaling pathway Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • response to hypoxia Source: UniProtKB
  • response to interleukin-1 Source: Ensembl
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: UniProtKB
  • 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...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

Metal-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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
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
  • transcription factor complex Source: Ensembl
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)6 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti650 – 6501Y → F in RSTS1. 1 Publication
VAR_072915
Natural varianti789 – 7891A → T in RSTS1. 1 Publication
Corresponds to variant rs746728741 [ dbSNP | Ensembl ].
VAR_072916
Natural varianti910 – 9101T → A in RSTS1; incomplete. 1 Publication
Corresponds to variant rs143247685 [ dbSNP | Ensembl ].
VAR_072917
Natural varianti1175 – 11751Y → C in RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3. 3 Publications
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].
VAR_037305
Natural varianti1278 – 12781E → A in RSTS1. 1 Publication
VAR_072918
Natural varianti1278 – 12781E → K in RSTS1; abolishes acetyltransferase activity. 2 Publications
Corresponds to variant rs267606752 [ dbSNP | Ensembl ].
VAR_035080
Natural varianti1378 – 13781R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 2 Publications
Corresponds to variant rs121434626 [ dbSNP | Ensembl ].
VAR_015578
Natural varianti1406 – 14061D → Y in RSTS1. 1 Publication
VAR_072919
Natural varianti1415 – 14151Q → P in RSTS1. 1 Publication
VAR_072920
Natural varianti1447 – 14471T → I in RSTS1. 1 Publication
VAR_035081
Natural varianti1450 – 14501Y → H in RSTS1. 1 Publication
VAR_035082
Natural varianti1470 – 14701H → R in RSTS1. 1 Publication
VAR_035083
Natural varianti1475 – 14751P → T in RSTS1. 1 Publication
VAR_072921
Natural varianti1503 – 15031Y → F in RSTS1. 1 Publication
VAR_072922
Natural varianti1507 – 15071L → P in RSTS1. 1 Publication
VAR_072923
Natural varianti1543 – 15431D → N in RSTS1. 1 Publication
VAR_072924
Natural varianti1664 – 16641R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications
VAR_035084

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1116 – 11161D → R: Impairs binding to acetylated histones. 1 Publication
Mutagenesisi1126 – 11261F → A: Impairs binding to acetylated histones. 1 Publication
Mutagenesisi1162 – 11621N → E or R: Abolishes interaction with ASF1A. 1 Publication
Mutagenesisi1165 – 11651W → A: Abolishes interaction with ASF1A. 1 Publication
Mutagenesisi1170 – 11701K → E: Impairs binding to acetylated histones. 1 Publication
Mutagenesisi1179 – 11791S → I: Impairs interaction with ASF1A. 1 Publication
Mutagenesisi1180 – 11801K → E: Abolishes interaction with ASF1A. 1 Publication
Mutagenesisi1183 – 11831E → R: Abolishes interaction with ASF1A. 1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei29 – 302Breakpoint for translocation to form KAT6B-CREBBP
Sitei266 – 2672Breakpoint for translocation to form KAT6A-CREBBP

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiCREBBP.
MIMi180849. phenotype.
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

ChEMBLiCHEMBL3301383.
GuidetoPHARMACOLOGYi2734.

Polymorphism and mutation databases

BioMutaiCREBBP.
DMDMi116241283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 24422441CREB-binding proteinPRO_0000211190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei601 – 6011Omega-N-methylated arginineBy similarity
Modified residuei625 – 6251Omega-N-methylated arginineBy similarity
Modified residuei657 – 6571N6-acetyllysineBy similarity
Cross-linki998 – 998Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1014 – 10141N6-acetyllysineCombined sources
Modified residuei1030 – 10301PhosphoserineCombined sources
Cross-linki1033 – 1033Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1056 – 1056Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei1076 – 10761PhosphoserineCombined sources
Modified residuei1216 – 12161N6-acetyllysineCombined sources
Modified residuei1382 – 13821Phosphoserine; by IKKA1 Publication
Modified residuei1386 – 13861Phosphoserine; by IKKA1 Publication
Modified residuei1583 – 15831N6-acetyllysineCombined sources
Modified residuei1591 – 15911N6-acetyllysineCombined sources
Modified residuei1592 – 15921N6-acetyllysineCombined sources
Modified residuei1595 – 15951N6-acetyllysineCombined sources
Modified residuei1597 – 15971N6-acetyllysineCombined sources
Modified residuei1741 – 17411N6-acetyllysineCombined sources
Modified residuei1744 – 17441N6-acetyllysineCombined sources
Modified residuei1763 – 17631PhosphoserineCombined sources
Modified residuei2063 – 20631PhosphoserineCombined sources
Modified residuei2076 – 20761PhosphoserineCombined sources
Modified residuei2079 – 20791PhosphoserineCombined sources
Modified residuei2351 – 23511PhosphoserineBy similarity

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.
PhosphoSiteiQ92793.

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

WithEntry#Exp.IntActNotes
P030702EBI-81215,EBI-617698From a different organism.
P032553EBI-81215,EBI-2603114From a different organism.
P032595EBI-81215,EBI-6947456From a different organism.
P03259-23EBI-81215,EBI-7225021From a different organism.
AKT1P317493EBI-81215,EBI-296087
ARP102752EBI-81215,EBI-608057
COPS2P612013EBI-81215,EBI-1050386
CREB1P162202EBI-81215,EBI-711855
CTNNB1P352222EBI-81215,EBI-491549
DAXXQ9UER72EBI-81215,EBI-77321
FOXO1Q127783EBI-81215,EBI-1108782
FOXO3O435243EBI-81215,EBI-1644164
HIF1AQ166652EBI-81215,EBI-447269
HTTP428582EBI-81215,EBI-466029
IFNAR2P485514EBI-81215,EBI-958408
IKBKBO149202EBI-81215,EBI-81266
IRF3Q146534EBI-81215,EBI-2650369
KAT2BQ928314EBI-81215,EBI-477430
MTDHQ86UE42EBI-81215,EBI-1046588
NAP1L1P552093EBI-81215,EBI-356392
NCOA6Q146862EBI-81215,EBI-78670
RELAQ042065EBI-81215,EBI-73886
SNAI1O958639EBI-81215,EBI-1045459
tatP046082EBI-81215,EBI-6164389From a different organism.
TP53P046379EBI-81215,EBI-366083

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

Protein-protein interaction databases

BioGridi107777. 309 interactions.
DIPiDIP-952N.
IntActiQ92793. 69 interactions.
MINTiMINT-104685.
STRINGi9606.ENSP00000262367.

Chemistry

BindingDBiQ92793.

Structurei

Secondary structure

1
2442
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 735Combined sources
Helixi377 – 3793Combined sources
Turni383 – 3886Combined sources
Helixi391 – 3955Combined sources
Turni593 – 5964Combined sources
Helixi598 – 61215Combined sources
Turni618 – 6225Combined sources
Helixi624 – 64219Combined sources
Helixi647 – 66923Combined sources
Turni670 – 6723Combined sources
Helixi1087 – 110216Combined sources
Turni1105 – 11084Combined sources
Helixi1109 – 11113Combined sources
Helixi1117 – 11204Combined sources
Helixi1125 – 11284Combined sources
Helixi1135 – 11439Combined sources
Beta strandi1146 – 11494Combined sources
Helixi1150 – 116718Combined sources
Turni1169 – 11713Combined sources
Helixi1173 – 119523Combined sources
Beta strandi1214 – 12185Combined sources
Beta strandi1226 – 12305Combined sources
Turni1231 – 12333Combined sources
Beta strandi1234 – 12374Combined sources
Turni1238 – 12403Combined sources
Beta strandi1266 – 12727Combined sources
Beta strandi1280 – 12823Combined sources
Turni1284 – 12863Combined sources
Beta strandi1289 – 12913Combined sources
Helixi1292 – 12954Combined sources
Turni1309 – 13113Combined sources
Helixi1765 – 178420Combined sources
Helixi1793 – 180513Combined sources
Turni1811 – 18155Combined sources
Helixi1817 – 183216Combined sources
Helixi1841 – 185313Combined sources
Helixi2066 – 20727Combined sources
Helixi2080 – 209112Combined sources
Helixi2094 – 210310Combined sources
Turni2104 – 21063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5I83X-ray1.35A1082-1197[»]
5I86X-ray1.05A/B1082-1197[»]
5I89X-ray1.07A1082-1197[»]
5I8BX-ray1.52A1081-1312[»]
5I8GX-ray1.41A1081-1312[»]
5JEMX-ray2.50C/D/F/H2065-2111[»]
ProteinModelPortaliQ92793.
SMRiQ92793. Positions 341-440, 587-673, 1049-1750, 1763-1854, 2065-2111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini587 – 66680KIXPROSITE-ProRule annotationAdd
BLAST
Domaini1103 – 117573BromoPROSITE-ProRule annotationAdd
BLAST
Domaini1323 – 1700378CBP/p300-type HATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 410184Interaction with SRCAPAdd
BLAST
Regioni1124 – 117047Interaction with histone1 PublicationAdd
BLAST
Regioni1162 – 118019Interaction with ASF1A1 PublicationAdd
BLAST
Regioni1433 – 14353Interaction with histoneBy similarity
Regioni1434 – 14363Acetyl-CoA bindingBy similarity
Regioni1446 – 14472Acetyl-CoA bindingBy similarity
Regioni1460 – 1891432Interaction with TRERF1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1061 – 10644Poly-Glu
Compositional biasi1199 – 1487289Cys/His-richAdd
BLAST
Compositional biasi1555 – 15628Poly-Glu
Compositional biasi1943 – 19486Poly-Pro
Compositional biasi1967 – 19704Poly-Gln
Compositional biasi2081 – 20855Poly-Gln
Compositional biasi2199 – 221618Poly-GlnAdd
BLAST
Compositional biasi2245 – 22484Poly-Gln
Compositional biasi2297 – 23004Poly-Gln

Domaini

The KIX domain mediates binding to HIV-1 Tat.

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 CBP/p300-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation
Contains 1 KIX domain.PROSITE-ProRule annotation
Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri347 – 43387TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1701 – 174444ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1765 – 184682TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

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

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.
InterProiIPR001487. 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.
[Graphical view]
PfamiPF00439. 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.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. 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.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1511 – 15133FAE → NSG in AAC51340 (PubMed:9177780).Curated
Sequence conflicti1724 – 17252ED → VV in AAC51340 (PubMed:9177780).Curated
Sequence conflicti1770 – 17701L → V in AAC51770 (PubMed:9238046).Curated
Sequence conflicti1789 – 17891N → F in AAC51340 (PubMed:9177780).Curated
Sequence conflicti1812 – 18121T → P in AAC51340 (PubMed:9177780).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti503 – 5031Q → H.1 Publication
Corresponds to variant rs748447855 [ dbSNP | Ensembl ].
VAR_072912
Natural varianti532 – 5321P → T.1 Publication
VAR_072913
Natural varianti546 – 5461I → N.1 Publication
VAR_072914
Natural varianti650 – 6501Y → F in RSTS1. 1 Publication
VAR_072915
Natural varianti789 – 7891A → T in RSTS1. 1 Publication
Corresponds to variant rs746728741 [ dbSNP | Ensembl ].
VAR_072916
Natural varianti910 – 9101T → A in RSTS1; incomplete. 1 Publication
Corresponds to variant rs143247685 [ dbSNP | Ensembl ].
VAR_072917
Natural varianti1175 – 11751Y → C in RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3. 3 Publications
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].
VAR_037305
Natural varianti1278 – 12781E → A in RSTS1. 1 Publication
VAR_072918
Natural varianti1278 – 12781E → K in RSTS1; abolishes acetyltransferase activity. 2 Publications
Corresponds to variant rs267606752 [ dbSNP | Ensembl ].
VAR_035080
Natural varianti1378 – 13781R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 2 Publications
Corresponds to variant rs121434626 [ dbSNP | Ensembl ].
VAR_015578
Natural varianti1406 – 14061D → Y in RSTS1. 1 Publication
VAR_072919
Natural varianti1414 – 14141V → I.
Corresponds to variant rs130015 [ dbSNP | Ensembl ].
VAR_027953
Natural varianti1415 – 14151Q → P in RSTS1. 1 Publication
VAR_072920
Natural varianti1447 – 14471T → I in RSTS1. 1 Publication
VAR_035081
Natural varianti1450 – 14501Y → H in RSTS1. 1 Publication
VAR_035082
Natural varianti1470 – 14701H → R in RSTS1. 1 Publication
VAR_035083
Natural varianti1475 – 14751P → T in RSTS1. 1 Publication
VAR_072921
Natural varianti1503 – 15031Y → F in RSTS1. 1 Publication
VAR_072922
Natural varianti1507 – 15071L → P in RSTS1. 1 Publication
VAR_072923
Natural varianti1543 – 15431D → N in RSTS1. 1 Publication
VAR_072924
Natural varianti1664 – 16641R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications
VAR_035084

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei406 – 44439VAHCA…RNQQT → A in isoform 2. 1 PublicationVSP_045700Add
BLAST

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

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

P300/CBP entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85962 mRNA. Translation: AAC51331.2.
U89354 mRNA. Translation: AAC51339.1.
U89355 mRNA. Translation: AAC51340.1.
U47741 mRNA. Translation: AAC51770.1.
AB210043 mRNA. Translation: BAE06125.1. Different initiation.
CH471112 Genomic DNA. Translation: EAW85335.1.
CH471112 Genomic DNA. Translation: EAW85336.1.
CH471112 Genomic DNA. Translation: EAW85337.1.
CCDSiCCDS10509.1. [Q92793-1]
CCDS45399.1. [Q92793-2]
PIRiS39162.
RefSeqiNP_001073315.1. NM_001079846.1. [Q92793-2]
NP_004371.2. NM_004380.2. [Q92793-1]
UniGeneiHs.459759.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5I83X-ray1.35A1082-1197[»]
5I86X-ray1.05A/B1082-1197[»]
5I89X-ray1.07A1082-1197[»]
5I8BX-ray1.52A1081-1312[»]
5I8GX-ray1.41A1081-1312[»]
5JEMX-ray2.50C/D/F/H2065-2111[»]
ProteinModelPortaliQ92793.
SMRiQ92793. Positions 341-440, 587-673, 1049-1750, 1763-1854, 2065-2111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107777. 309 interactions.
DIPiDIP-952N.
IntActiQ92793. 69 interactions.
MINTiMINT-104685.
STRINGi9606.ENSP00000262367.

Chemistry

BindingDBiQ92793.
ChEMBLiCHEMBL3301383.
GuidetoPHARMACOLOGYi2734.

PTM databases

iPTMnetiQ92793.
PhosphoSiteiQ92793.

Polymorphism and mutation databases

BioMutaiCREBBP.
DMDMi116241283.

Proteomic databases

EPDiQ92793.
MaxQBiQ92793.
PaxDbiQ92793.
PeptideAtlasiQ92793.
PRIDEiQ92793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1387.
GeneCardsiCREBBP.
GeneReviewsiCREBBP.
HGNCiHGNC:2348. CREBBP.
HPAiCAB004212.
HPA055861.
MalaCardsiCREBBP.
MIMi180849. phenotype.
600140. gene.
neXtProtiNX_Q92793.
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.
GenAtlasiSearch...

Phylogenomic databases

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

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-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.

Miscellaneous databases

ChiTaRSiCREBBP. human.
EvolutionaryTraceiQ92793.
GeneWikiiCREB-binding_protein.
GenomeRNAii1387.
PROiQ92793.
SOURCEiSearch...

Gene expression databases

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

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.
InterProiIPR001487. 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.
[Graphical view]
PfamiPF00439. 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.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBP_HUMAN
AccessioniPrimary (citable) accession number: Q92793
Secondary accession number(s): D3DUC9
, O00147, Q16376, Q4LE28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 17, 2006
Last modified: September 7, 2016
This is version 204 of the entry and version 3 of the sequence. [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
  6. SIMILARITY comments
    Index of protein domains and families

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.