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Q92793

- CBP_HUMAN

UniProt

Q92793 - CBP_HUMAN

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Protein
CREB-binding protein
Gene
CREBBP, CBP
Organism
Homo sapiens (Human)
Status
Reviewed - 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 in the presence of EP300. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.5 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei29 – 302Breakpoint for translocation to form KAT6B-CREBBP
Sitei266 – 2672Breakpoint for translocation to form KAT6A-CREBBP
Metal bindingi363 – 3631Zinc 1 By similarity
Metal bindingi367 – 3671Zinc 1 By similarity
Metal bindingi380 – 3801Zinc 1 By similarity
Metal bindingi385 – 3851Zinc 1 By similarity
Metal bindingi394 – 3941Zinc 2 By similarity
Metal bindingi398 – 3981Zinc 2 By similarity
Metal bindingi404 – 4041Zinc 2 By similarity
Metal bindingi409 – 4091Zinc 2 By similarity
Metal bindingi418 – 4181Zinc 3 By similarity
Metal bindingi422 – 4221Zinc 3 By similarity
Metal bindingi427 – 4271Zinc 3 By similarity
Metal bindingi430 – 4301Zinc 3 By similarity

Regions

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

GO - Molecular functioni

  1. MRF binding Source: UniProtKB
  2. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
  4. RNA polymerase II transcription coactivator activity Source: BHF-UCL
  5. RNA polymerase II transcription factor binding Source: BHF-UCL
  6. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
  7. acetyltransferase activity Source: UniProtKB
  8. chromatin binding Source: Ensembl
  9. core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  10. histone acetyltransferase activity Source: UniProtKB
  11. p53 binding Source: UniProtKB
  12. protein binding Source: UniProtKB
  13. sequence-specific DNA binding transcription factor activity Source: ProtInc
  14. signal transducer activity Source: ProtInc
  15. transcription coactivator activity Source: UniProtKB
  16. transcription factor binding Source: UniProtKB
  17. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  2. Notch signaling pathway Source: Reactome
  3. cellular lipid metabolic process Source: Reactome
  4. cellular response to hypoxia Source: Reactome
  5. chromatin organization Source: Reactome
  6. embryonic digit morphogenesis Source: BHF-UCL
  7. gene expression Source: Reactome
  8. germ-line stem cell maintenance Source: Ensembl
  9. histone acetylation Source: UniProtKB
  10. homeostatic process Source: UniProtKB
  11. innate immune response Source: Reactome
  12. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  13. positive regulation of transcription, DNA-templated Source: UniProtKB
  14. positive regulation of type I interferon production Source: Reactome
  15. protein complex assembly Source: ProtInc
  16. regulation of smoothened signaling pathway Source: BHF-UCL
  17. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  18. regulation of transcription, DNA-templated Source: UniProtKB
  19. response to hypoxia Source: UniProtKB
  20. rhythmic process Source: UniProtKB-KW
  21. signal transduction Source: UniProtKB
  22. small molecule metabolic process Source: Reactome
  23. transcription initiation from RNA polymerase II promoter Source: Reactome
  24. 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

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_172610. HATs acetylate histones.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_200624. Attenuation phase.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24941. Circadian Clock.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ92793.

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48)
Gene namesi
Name:CREBBP
Synonyms:CBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: 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.2 Publications

GO - Cellular componenti

  1. condensed chromosome outer kinetochore Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. histone acetyltransferase complex Source: Ensembl
  4. nuclear body Source: UniProtKB
  5. nuclear chromatin Source: BHF-UCL
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
  8. 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) [MIM:180849]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1175 – 11751Y → C in RSTS1; mild form. 1 Publication
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].
VAR_037305
Natural varianti1278 – 12781E → K in RSTS1; abolishes acetyltransferase activity. 2 Publications
VAR_035080
Natural varianti1378 – 13781R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 1 Publication
VAR_015578
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 varianti1664 – 16641R → H in RSTS1; abolishes acetyltransferase activity. 2 Publications
VAR_035084

Keywords - Diseasei

Disease mutation

Organism-specific databases

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 24422441CREB-binding protein
PRO_0000211190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei121 – 1211Phosphoserine2 Publications
Modified residuei601 – 6011Omega-N-methylated arginine By similarity
Modified residuei625 – 6251Omega-N-methylated arginine By similarity
Modified residuei657 – 6571N6-acetyllysine By similarity
Cross-linki998 – 998Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Modified residuei1014 – 10141N6-acetyllysine1 Publication
Modified residuei1030 – 10301Phosphoserine1 Publication
Cross-linki1033 – 1033Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-linki1056 – 1056Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Modified residuei1216 – 12161N6-acetyllysine1 Publication
Modified residuei1382 – 13821Phosphoserine; by IKKA1 Publication
Modified residuei1386 – 13861Phosphoserine; by IKKA1 Publication
Modified residuei1583 – 15831N6-acetyllysine1 Publication
Modified residuei1586 – 15861N6-acetyllysine1 Publication
Modified residuei1591 – 15911N6-acetyllysine1 Publication
Modified residuei1592 – 15921N6-acetyllysine1 Publication
Modified residuei1595 – 15951N6-acetyllysine1 Publication
Modified residuei1597 – 15971N6-acetyllysine1 Publication
Modified residuei1741 – 17411N6-acetyllysine1 Publication
Modified residuei1744 – 17441N6-acetyllysine1 Publication
Modified residuei2063 – 20631Phosphoserine2 Publications
Modified residuei2076 – 20761Phosphoserine1 Publication
Modified residuei2079 – 20791Phosphoserine1 Publication

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.
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92793.
PaxDbiQ92793.
PRIDEiQ92793.

PTM databases

PhosphoSiteiQ92793.

Expressioni

Gene expression databases

ArrayExpressiQ92793.
BgeeiQ92793.
CleanExiHS_CREBBP.
GenevestigatoriQ92793.

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/BMAL1.27 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
FOXO1Q127782EBI-81215,EBI-1108782
HIF1AQ166652EBI-81215,EBI-447269
HTTP428582EBI-81215,EBI-466029
IFNAR2P485514EBI-81215,EBI-958408
IRF3Q146534EBI-81215,EBI-2650369
KAT2BQ928314EBI-81215,EBI-477430
MTDHQ86UE42EBI-81215,EBI-1046588
NAP1L1P552093EBI-81215,EBI-356392
NCOA6Q146862EBI-81215,EBI-78670
RELAQ042063EBI-81215,EBI-73886
TP53P046378EBI-81215,EBI-366083

Protein-protein interaction databases

BioGridi107777. 265 interactions.
DIPiDIP-952N.
IntActiQ92793. 56 interactions.
MINTiMINT-104685.
STRINGi9606.ENSP00000262367.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 735
Helixi377 – 3793
Turni383 – 3886
Helixi391 – 3955
Turni593 – 5964
Helixi598 – 61215
Turni618 – 6225
Helixi624 – 64219
Helixi647 – 66923
Turni670 – 6723
Helixi1087 – 110216
Turni1105 – 11084
Helixi1109 – 11113
Helixi1117 – 11204
Helixi1125 – 11284
Helixi1135 – 11439
Beta strandi1146 – 11494
Helixi1150 – 116718
Turni1169 – 11713
Helixi1173 – 119624
Beta strandi1280 – 12823
Turni1284 – 12863
Beta strandi1289 – 12913
Helixi1292 – 12954
Turni1309 – 13113
Helixi1765 – 178420
Helixi1793 – 180513
Turni1811 – 18155
Helixi1817 – 183216
Helixi1841 – 185313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliQ92793.
SMRiQ92793. Positions 341-440, 587-673, 1049-1750, 1763-1854, 2065-2111.

Miscellaneous databases

EvolutionaryTraceiQ92793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini587 – 66680KIX
Add
BLAST
Domaini1103 – 117573Bromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 410184Interaction with SRCAP
Add
BLAST
Regioni1460 – 1891432Interaction with TRERF1
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1061 – 10644Poly-Glu
Compositional biasi1199 – 1487289Cys/His-rich
Add
BLAST
Compositional biasi1555 – 15628Poly-Glu
Compositional biasi1943 – 19486Poly-Pro
Compositional biasi1967 – 19704Poly-Gln
Compositional biasi2081 – 20855Poly-Gln
Compositional biasi2199 – 221618Poly-Gln
Add
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.
Contains 1 KIX domain.

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
KOiK04498.
OMAiLPNPLNM.
OrthoDBiEOG75B84F.
PhylomeDBiQ92793.
TreeFamiTF101097.

Family and domain databases

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.
IPR010303. DUF902_CREBbp.
IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 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.
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. Align

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

MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE     50
LGLLNSGNLV PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG 100
GQAQGQPNSA NMASLSAMGK SPLSQGDSSA PSLPKQAAST SGPTPAASQA 150
LNPQAQKQVG LATSSPATSQ TGPGICMNAN FNQTHPGLLN SNSGHSLINQ 200
ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA ETLTQVSPQM 250
TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK 300
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK 350
RKLIQQQLVL LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA 400
GKACQVAHCA SSRQIISHWK NCTRHDCPVC LPLKNASDKR NQQTILGSPA 450
SGIQNTIGSV GTGQQNATSL SNPNPIDPSS MQRAYAALGL PYMNQPQTQL 500
QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ QPPNLISESA 550
LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL 600
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY 650
YHLLAEKIYK IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP 700
VRPPNGPLSL PVNRMQVSQG MNSFNPMSLG NVQLPQAPMG PRAASPMNHS 750
VQMNSMGSVP GMAISPSRMP QPPNMMGAHT NNMMAQAPAQ SQFLPQNQFP 800
SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA SQLPCPPVTQ 850
SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT 900
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT 950
PVHAQPPGTP LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE 1000
TQAEDTEPDP GESKGEPRSE MMEEDLQGAS QVKEETDIAE QKSEPMEVDE 1050
KKPEVKVEVK EEEESSSNGT ASQSTSPSQP RKKIFKPEEL RQALMPTLEA 1100
LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR KLDTGQYQEP 1150
WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC 1200
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT 1250
LGDDPSQPQT TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI 1300
IWPSGFVCDN CLKKTGRPRK ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN 1350
HPEAGEVFVR VVASSDKTVE VKPGMKSRFV DSGEMSESFP YRTKALFAFE 1400
EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF RPRCLRTAVY 1450
HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ 1500
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE 1550
ESIKELEQEE EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI 1600
SRANKKKPSM PNVSNDLSQK LYATMEKHKE VFFVIHLHAG PVINTLPPIV 1650
DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS LRRSKWSTLC MLVELHTQGQ 1700
DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH KMVKWGLGLD 1750
DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR 1800
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL 1850
RQQQIQHRLQ QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP 1900
QTPQPPAQPQ PSPVSMSPAG FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ 1950
PPPAAVEAAR QIEREAQQQQ HLYRVNINNS MPPGRTGMGT PGSQMAPVSL 2000
NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI SMQAQAAVAG 2050
PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF 2100
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP 2150
RPGVPPQQQA MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ 2200
QQQQQQQQQQ QQQQQQGSAG MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM 2250
QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ 2300
MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ 2350
SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL 2400
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL 2442
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 BAE06125.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1175 – 11751Y → C in RSTS1; mild form. 1 Publication
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].
VAR_037305
Natural varianti1278 – 12781E → K in RSTS1; abolishes acetyltransferase activity. 2 Publications
VAR_035080
Natural varianti1378 – 13781R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. 1 Publication
VAR_015578
Natural varianti1414 – 14141V → I.
Corresponds to variant rs130015 [ dbSNP | Ensembl ].
VAR_027953
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 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.
VSP_045700Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1511 – 15133FAE → NSG in AAC51340. 1 Publication
Sequence conflicti1724 – 17252ED → VV in AAC51340. 1 Publication
Sequence conflicti1770 – 17701L → V in AAC51770. 1 Publication
Sequence conflicti1789 – 17891N → F in AAC51340. 1 Publication
Sequence conflicti1812 – 18121T → P in AAC51340. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q92793-1]

Polymorphism databases

DMDMi116241283.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

P300/CBP entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10509.1. [Q92793-1 ]
CCDS45399.1. [Q92793-2 ]
PIRi S39162.
RefSeqi NP_001073315.1. NM_001079846.1. [Q92793-2 ]
NP_004371.2. NM_004380.2. [Q92793-1 ]
UniGenei Hs.459759.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JSP NMR - B 1081-1197 [» ]
1LIQ NMR - A 376-402 [» ]
1RDT X-ray 2.40 E 58-80 [» ]
1WO3 NMR - A 387-398 [» ]
1WO4 NMR - A 387-398 [» ]
1WO5 NMR - A 387-398 [» ]
1WO6 NMR - A 376-400 [» ]
1WO7 NMR - A 376-400 [» ]
1ZOQ X-ray 2.37 C/D 2065-2111 [» ]
2D82 NMR - A 1081-1197 [» ]
2KJE NMR - A 1763-1854 [» ]
2KWF NMR - A 587-673 [» ]
2L84 NMR - A 1081-1197 [» ]
2L85 NMR - A 1081-1197 [» ]
2LXS NMR - A 587-673 [» ]
2LXT NMR - A 587-673 [» ]
2RNY NMR - A 1081-1197 [» ]
3DWY X-ray 1.98 A/B 1081-1197 [» ]
3P1C X-ray 1.82 A/B 1081-1197 [» ]
3P1D X-ray 1.86 A/B 1081-1197 [» ]
3P1E X-ray 1.80 A/B 1081-1197 [» ]
3P1F X-ray 1.63 A/B 1081-1197 [» ]
3SVH X-ray 1.80 A/B 1081-1197 [» ]
4A9K X-ray 1.81 A/B 1081-1197 [» ]
4N3W X-ray 1.90 A 1080-1316 [» ]
4N4F X-ray 1.83 A 1080-1316 [» ]
4NR4 X-ray 1.69 A/B 1081-1197 [» ]
4NR5 X-ray 1.66 A 1081-1197 [» ]
4NR6 X-ray 1.66 A 1081-1197 [» ]
4NR7 X-ray 1.20 A 1081-1197 [» ]
4NYV X-ray 1.83 A/B/C/D 1081-1197 [» ]
4NYW X-ray 1.43 A 1081-1197 [» ]
4NYX X-ray 1.10 A 1081-1197 [» ]
4OUF X-ray 1.40 A/B 1082-1197 [» ]
ProteinModelPortali Q92793.
SMRi Q92793. Positions 341-440, 587-673, 1049-1750, 1763-1854, 2065-2111.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107777. 265 interactions.
DIPi DIP-952N.
IntActi Q92793. 56 interactions.
MINTi MINT-104685.
STRINGi 9606.ENSP00000262367.

Chemistry

BindingDBi Q92793.
ChEMBLi CHEMBL5747.
GuidetoPHARMACOLOGYi 2734.

PTM databases

PhosphoSitei Q92793.

Polymorphism databases

DMDMi 116241283.

Proteomic databases

MaxQBi Q92793.
PaxDbi Q92793.
PRIDEi Q92793.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262367 ; ENSP00000262367 ; ENSG00000005339 . [Q92793-1 ]
ENST00000382070 ; ENSP00000371502 ; ENSG00000005339 . [Q92793-2 ]
GeneIDi 1387.
KEGGi hsa:1387.
UCSCi uc002cvv.3. human. [Q92793-1 ]

Organism-specific databases

CTDi 1387.
GeneCardsi GC16M003775.
GeneReviewsi CREBBP.
HGNCi HGNC:2348. CREBBP.
HPAi CAB004212.
HPA055861.
MIMi 180849. phenotype.
600140. gene.
neXtProti NX_Q92793.
Orphaneti 370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
353281. Rubinstein-Taybi syndrome due to 16p13.3 microdeletion.
353277. Rubinstein-Taybi syndrome due to CREBBP mutations.
PharmGKBi PA26866.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.
KOi K04498.
OMAi LPNPLNM.
OrthoDBi EOG75B84F.
PhylomeDBi Q92793.
TreeFami TF101097.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_172610. HATs acetylate histones.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_200624. Attenuation phase.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24941. Circadian Clock.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q92793.

Miscellaneous databases

ChiTaRSi CREBBP. human.
EvolutionaryTracei Q92793.
GeneWikii CREB-binding_protein.
GenomeRNAii 1387.
NextBioi 5635.
PROi Q92793.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92793.
Bgeei Q92793.
CleanExi HS_CREBBP.
Genevestigatori Q92793.

Family and domain databases

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.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3)."
    Sobulo O.M., Borrow J., Tomek R., Reshimi S., Harden A., Schlegelberger B., Housman D., Doggett N.A., Rowley J.D., Zeleznik-Le N.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:8732-8737(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3."
    Giles R.H., Petrij F., Dauwerse H.G., den Hollander A.I., Lushnikova T., van Ommen G.J.B., Goodman R.H., Deaven L.L., Doggett N.A., Peters D.J.M., Breuning M.H.
    Genomics 42:96-114(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Petrij F., den Hollander A.I., Chrivia J.C.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 1724-1725; 1789 AND 1812.
  4. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein."
    Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G., Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M., Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.
    Nat. Genet. 14:33-41(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-405, CHROMOSOMAL TRANSLOCATION WITH KAT6A.
  7. "Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)."
    Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R., Stroembeck B., Mitelman F., Johansson B.
    Hum. Mol. Genet. 10:395-404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-83, CHROMOSOMAL TRANSLOCATION WITH KAT6B.
  8. "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A."
    Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.
    Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCAF.
  9. Cited for: INTERACTION WITH HIF1A AND EP300.
  10. "Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300."
    Bex F., Yin M.-J., Burny A., Gaynor R.B.
    Mol. Cell. Biol. 18:2392-2405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  11. "Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases."
    Zhang W., Bieker J.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLF1, FUNCTION.
  12. "Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein."
    Johnston H., Kneer J., Chackalaparampil I., Yaciuk P., Chrivia J.
    J. Biol. Chem. 274:16370-16376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRCAP.
  13. "Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling."
    Doucas V., Tini M., Egan D.A., Evans R.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:2627-2632(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML.
  14. "Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase."
    Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.
    Cell 98:675-686(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION OF NCOA3.
  15. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
    Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
    J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED1.
  16. "A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
    Mahajan M.A., Samuels H.H.
    Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  17. "Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation."
    Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A.
    J. Biol. Chem. 276:10715-10721(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAFG, FUNCTION IN ACETYLATION OF MAFG.
  18. "Requirement of two NFATc4 transactivation domains for CBP potentiation."
    Yang T.T.C., Davis R.J., Chow C.-W.
    J. Biol. Chem. 276:39569-39576(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFATC4.
  19. "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
    Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
    J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MECOM.
  20. "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation."
    Scoggin K.E.S., Ulloa A., Nyborg J.K.
    Mol. Cell. Biol. 21:5520-5530(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  21. "Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300."
    Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T., Lairmore M.D.
    J. Virol. 75:9885-9895(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
  22. "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression."
    Gizard F., Lavallee B., DeWitte F., Hum D.W.
    J. Biol. Chem. 276:33881-33892(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRERF1.
  23. "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha."
    Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R.
    J. Biol. Chem. 276:38272-38279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  24. "HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators."
    Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A., Harrington W.J. Jr., Barber G.N., Hiscott J.
    Oncogene 20:800-811(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-8 PROTEIN VIRF1.
  25. "Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb."
    Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.
    Cell Growth Differ. 13:69-75(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIB.
  26. "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
    Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
    J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED4.
  27. "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
    Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
    Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NCOA2; NCOA3; IKKA; IKKB AND IKBKG.
  28. "Interferon regulatory factor-2 regulates cell growth through its acetylation."
    Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.
    J. Biol. Chem. 278:25401-25407(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRF2, FUNCTION IN ACETYLATION OF IRF2.
  29. "Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination."
    Watanabe N., Wachi S., Fujita T.
    J. Biol. Chem. 278:26102-26110(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH N4BP2.
  30. "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain."
    Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.
    J. Bone Miner. Res. 18:1419-1429(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  31. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
    Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
    J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPAS2 AND CLOCK.
  32. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
    Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
    J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELF3.
  33. "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)."
    van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A., Medema R.H., Burgering B.M.T.
    J. Biol. Chem. 279:28873-28879(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLLT7.
  34. "The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies."
    Pradhan A., Liu Y.
    Neurosci. Lett. 370:191-195(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  35. "Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity."
    Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T., Miyagishi M., Nakajima T., Fukamizu A.
    Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXO1.
  36. "Dendrite development regulated by CREST, a calcium-regulated transcriptional activator."
    Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I., Cowan M., Ghosh A.
    Science 303:197-202(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SS18L1/CREST.
  37. "Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB."
    Huang W.C., Ju T.K., Hung M.C., Chen C.C.
    Mol. Cell 26:75-87(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1382 AND SER-1386 BY CHUK/IKKA.
  38. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  39. "Molecular basis of nuclear factor-kappaB activation by astrocyte elevated gene-1."
    Sarkar D., Park E.S., Emdad L., Lee S.-G., Su Z.-Z., Fisher P.B.
    Cancer Res. 68:1478-1484(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTDH.
  40. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-2063; SER-2076 AND SER-2079, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  41. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  42. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2063, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  43. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1014; LYS-1216; LYS-1583; LYS-1586; LYS-1591; LYS-1592; LYS-1595; LYS-1597; LYS-1741 AND LYS-1744, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  47. "Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response."
    Dames S.A., Martinez-Yamout M., De Guzman R.N., Dyson H.J., Wright P.E.
    Proc. Natl. Acad. Sci. U.S.A. 99:5271-5276(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 345-439 IN COMPLEX WITH 776-826 OF HIF1A.
  48. "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
    Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
    EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH KAT6A.
  49. "NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP."
    Vendel A.C., Lumb K.J.
    Biochemistry 43:904-908(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 589-679 IN COMPLEX WITH HIV-1 TAT.
  50. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1081-1197.
  51. "Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome."
    Murata T., Kurokawa R., Krones A., Tatsumi K., Ishii M., Taki T., Masuno M., Ohashi H., Yanagisawa M., Rosenfeld M.G., Glass C.K., Hayashi Y.
    Hum. Mol. Genet. 10:1071-1076(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RSTS1 PRO-1378.
  52. "Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including a mild variant showing a missense mutation in codon 1175 of CREBBP."
    Bartsch O., Locher K., Meinecke P., Kress W., Seemanova E., Wagner A., Ostermann K., Roedel G.
    J. Med. Genet. 39:496-501(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RSTS1 CYS-1175.
  53. "Loss of CBP acetyltransferase activity by PHD finger mutations in Rubinstein-Taybi syndrome."
    Kalkhoven E., Roelfsema J.H., Teunissen H., den Boer A., Ariyuerek Y., Zantema A., Breuning M.H., Hennekam R.C.M., Peters D.J.M.
    Hum. Mol. Genet. 12:441-450(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RSTS1 LYS-1278 AND HIS-1664, CHARACTERIZATION OF VARIANTS RSTS1 LYS-1278 AND HIS-1664.
  54. "Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease."
    Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D., Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H., Hennekam R.C., Peters D.J.M.
    Am. J. Hum. Genet. 76:572-580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RSTS1 LYS-1278; ILE-1447; HIS-1450; ARG-1470 AND HIS-1664.

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 3, 2014
This is version 181 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

External Data

Dasty 3

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