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Q92793

- CBP_HUMAN

UniProt

Q92793 - CBP_HUMAN

Protein

CREB-binding protein

Gene

CREBBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    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 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

    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

    1. acetyltransferase activity Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    4. histone acetyltransferase activity Source: UniProtKB
    5. MRF binding Source: UniProtKB
    6. p53 binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    10. RNA polymerase II transcription coactivator activity Source: BHF-UCL
    11. RNA polymerase II transcription factor binding Source: BHF-UCL
    12. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    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

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. cellular response to hypoxia Source: Reactome
    3. chromatin organization Source: Reactome
    4. embryonic digit morphogenesis Source: BHF-UCL
    5. gene expression Source: Reactome
    6. germ-line stem cell maintenance Source: Ensembl
    7. histone acetylation Source: UniProtKB
    8. homeostatic process Source: UniProtKB
    9. innate immune response Source: Reactome
    10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. Notch signaling pathway Source: Reactome
    12. N-terminal peptidyl-lysine acetylation Source: UniProtKB
    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, DNA-templated Source: UniProtKB
    18. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    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

    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.

    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

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 11Removed2 Publications
    Chaini2 – 24422441CREB-binding proteinPRO_0000211190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei121 – 1211Phosphoserine2 Publications
    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 SUMO-1)By similarity
    Modified residuei1014 – 10141N6-acetyllysine2 Publications
    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-acetyllysine2 Publications
    Modified residuei1382 – 13821Phosphoserine; by IKKA1 Publication
    Modified residuei1386 – 13861Phosphoserine; by IKKA1 Publication
    Modified residuei1583 – 15831N6-acetyllysine2 Publications
    Modified residuei1586 – 15861N6-acetyllysine2 Publications
    Modified residuei1591 – 15911N6-acetyllysine2 Publications
    Modified residuei1592 – 15921N6-acetyllysine2 Publications
    Modified residuei1595 – 15951N6-acetyllysine2 Publications
    Modified residuei1597 – 15971N6-acetyllysine2 Publications
    Modified residuei1741 – 17411N6-acetyllysine2 Publications
    Modified residuei1744 – 17441N6-acetyllysine2 Publications
    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.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.5 Publications
    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.By similarity29 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
    IKBKBO149202EBI-81215,EBI-81266
    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. 60 interactions.
    MINTiMINT-104685.
    STRINGi9606.ENSP00000262367.

    Structurei

    Secondary structure

    1
    2442
    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.
    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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni227 – 410184Interaction with SRCAPAdd
    BLAST
    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 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

    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.

    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 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. 1 PublicationVSP_045700Add
    BLAST

    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107777. 265 interactions.
    DIPi DIP-952N.
    IntActi Q92793. 60 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

    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: October 1, 2014
    This is version 182 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