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Q92793 (CBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CREB-binding protein

EC=2.3.1.48
Gene names
Name:CREBBP
Synonyms:CBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2442 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.17 Ref.28 Ref.30

Catalytic activity

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

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.38

Subcellular location

Cytoplasm. Nucleus. Note: Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Ref.30 Ref.33

Domain

The KIX domain mediates binding to HIV-1 Tat.

Post-translational modification

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. Ref.36

Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX By similarity.

Involvement in disease

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. Ref.50 Ref.51 Ref.52 Ref.53

Sequence similarities

Contains 1 bromo domain.

Contains 1 KIX domain.

Contains 2 TAZ-type zinc fingers.

Contains 1 ZZ-type zinc finger.

Sequence caution

The sequence BAE06125.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseDisease mutation
   DomainBromodomain
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Transferase
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal peptidyl-lysine acetylation

Inferred from direct assay PubMed 12435739. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to hypoxia

Traceable author statement. Source: Reactome

chromatin organization

Traceable author statement. Source: Reactome

embryonic digit morphogenesis

Traceable author statement PubMed 11001584. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

germ-line stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

histone acetylation

Inferred from direct assay Ref.47. Source: UniProtKB

homeostatic process

Non-traceable author statement PubMed 15261140. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21539536. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.47. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

protein complex assembly

Traceable author statement PubMed 7913207. Source: ProtInc

regulation of smoothened signaling pathway

Traceable author statement PubMed 11001584. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Traceable author statement PubMed 15261140. Source: UniProtKB

response to hypoxia

Traceable author statement PubMed 15261140. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 15261140. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed chromosome outer kinetochore

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.30. Source: UniProtKB

histone acetyltransferase complex

Inferred from electronic annotation. Source: Ensembl

nuclear body

Inferred from direct assay Ref.33. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 21539536. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.30. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionMRF binding

Inferred from direct assay PubMed 8621548. Source: UniProtKB

RNA polymerase II activating transcription factor binding

Traceable author statement PubMed 11001584. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 21539536. Source: BHF-UCL

RNA polymerase II transcription coactivator activity

Traceable author statement PubMed 11001584. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 21539536. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 21539536. Source: BHF-UCL

acetyltransferase activity

Inferred from direct assay Ref.47. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 21539536. Source: BHF-UCL

histone acetyltransferase activity

Inferred from direct assay Ref.47. Source: UniProtKB

p53 binding

Inferred from physical interaction PubMed 9194565. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 7913207. Source: ProtInc

signal transducer activity

Traceable author statement PubMed 7913207PubMed 8028671. Source: ProtInc

transcription coactivator activity

Inferred from direct assay PubMed 12435739PubMed 12586840. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15509593. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92793-1)

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.
Isoform 2 (identifier: Q92793-2)

The sequence of this isoform differs from the canonical sequence as follows:
     406-444: VAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQT → A
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.40
Chain2 – 24422441CREB-binding protein
PRO_0000211190

Regions

Domain587 – 66680KIX
Domain1103 – 117573Bromo
Zinc finger347 – 43387TAZ-type 1
Zinc finger1701 – 174444ZZ-type
Zinc finger1765 – 184682TAZ-type 2
Region227 – 410184Interaction with SRCAP
Region1460 – 1891432Interaction with TRERF1
Compositional bias1061 – 10644Poly-Glu
Compositional bias1199 – 1487289Cys/His-rich
Compositional bias1555 – 15628Poly-Glu
Compositional bias1943 – 19486Poly-Pro
Compositional bias1967 – 19704Poly-Gln
Compositional bias2081 – 20855Poly-Gln
Compositional bias2199 – 221618Poly-Gln
Compositional bias2245 – 22484Poly-Gln
Compositional bias2297 – 23004Poly-Gln

Sites

Metal binding3631Zinc 1 By similarity
Metal binding3671Zinc 1 By similarity
Metal binding3801Zinc 1 By similarity
Metal binding3851Zinc 1 By similarity
Metal binding3941Zinc 2 By similarity
Metal binding3981Zinc 2 By similarity
Metal binding4041Zinc 2 By similarity
Metal binding4091Zinc 2 By similarity
Metal binding4181Zinc 3 By similarity
Metal binding4221Zinc 3 By similarity
Metal binding4271Zinc 3 By similarity
Metal binding4301Zinc 3 By similarity
Site29 – 302Breakpoint for translocation to form KAT6B-CREBBP
Site266 – 2672Breakpoint for translocation to form KAT6A-CREBBP

Amino acid modifications

Modified residue21N-acetylalanine Ref.40 Ref.45
Modified residue1211Phosphoserine Ref.39 Ref.43
Modified residue6011Omega-N-methylated arginine By similarity
Modified residue6251Omega-N-methylated arginine By similarity
Modified residue6571N6-acetyllysine By similarity
Modified residue10141N6-acetyllysine Ref.42
Modified residue10301Phosphoserine Ref.37
Modified residue12161N6-acetyllysine Ref.42
Modified residue13821Phosphoserine; by IKKA Ref.36
Modified residue13861Phosphoserine; by IKKA Ref.36
Modified residue15831N6-acetyllysine Ref.42
Modified residue15861N6-acetyllysine Ref.42
Modified residue15911N6-acetyllysine Ref.42
Modified residue15921N6-acetyllysine Ref.42
Modified residue15951N6-acetyllysine Ref.42
Modified residue15971N6-acetyllysine Ref.42
Modified residue17411N6-acetyllysine Ref.42
Modified residue17441N6-acetyllysine Ref.42
Modified residue20631Phosphoserine Ref.39 Ref.41
Modified residue20761Phosphoserine Ref.39
Modified residue20791Phosphoserine Ref.39
Cross-link998Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link1033Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link1056Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Natural variations

Alternative sequence406 – 44439VAHCA…RNQQT → A in isoform 2.
VSP_045700
Natural variant11751Y → C in RSTS1; mild form. Ref.51
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].
VAR_037305
Natural variant12781E → K in RSTS1; abolishes acetyltransferase activity. Ref.52 Ref.53
VAR_035080
Natural variant13781R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. Ref.50
VAR_015578
Natural variant14141V → I.
Corresponds to variant rs130015 [ dbSNP | Ensembl ].
VAR_027953
Natural variant14471T → I in RSTS1. Ref.53
VAR_035081
Natural variant14501Y → H in RSTS1. Ref.53
VAR_035082
Natural variant14701H → R in RSTS1. Ref.53
VAR_035083
Natural variant16641R → H in RSTS1; abolishes acetyltransferase activity. Ref.52 Ref.53
VAR_035084

Experimental info

Sequence conflict1511 – 15133FAE → NSG in AAC51340. Ref.2
Sequence conflict1724 – 17252ED → VV in AAC51340. Ref.2
Sequence conflict17701L → V in AAC51770. Ref.1
Sequence conflict17891N → F in AAC51340. Ref.2
Sequence conflict18121T → P in AAC51340. Ref.2

Secondary structure

......................................................... 2442
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 3BEA9B8558BA1A5E

FASTA2,442265,351
        10         20         30         40         50         60 
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE LGLLNSGNLV 

        70         80         90        100        110        120 
PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG GQAQGQPNSA NMASLSAMGK 

       130        140        150        160        170        180 
SPLSQGDSSA PSLPKQAAST SGPTPAASQA LNPQAQKQVG LATSSPATSQ TGPGICMNAN 

       190        200        210        220        230        240 
FNQTHPGLLN SNSGHSLINQ ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA 

       250        260        270        280        290        300 
ETLTQVSPQM TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK 

       310        320        330        340        350        360 
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK RKLIQQQLVL 

       370        380        390        400        410        420 
LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA GKACQVAHCA SSRQIISHWK 

       430        440        450        460        470        480 
NCTRHDCPVC LPLKNASDKR NQQTILGSPA SGIQNTIGSV GTGQQNATSL SNPNPIDPSS 

       490        500        510        520        530        540 
MQRAYAALGL PYMNQPQTQL QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ 

       550        560        570        580        590        600 
QPPNLISESA LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL 

       610        620        630        640        650        660 
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY YHLLAEKIYK 

       670        680        690        700        710        720 
IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP VRPPNGPLSL PVNRMQVSQG 

       730        740        750        760        770        780 
MNSFNPMSLG NVQLPQAPMG PRAASPMNHS VQMNSMGSVP GMAISPSRMP QPPNMMGAHT 

       790        800        810        820        830        840 
NNMMAQAPAQ SQFLPQNQFP SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA 

       850        860        870        880        890        900 
SQLPCPPVTQ SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT 

       910        920        930        940        950        960 
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT PVHAQPPGTP 

       970        980        990       1000       1010       1020 
LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE TQAEDTEPDP GESKGEPRSE 

      1030       1040       1050       1060       1070       1080 
MMEEDLQGAS QVKEETDIAE QKSEPMEVDE KKPEVKVEVK EEEESSSNGT ASQSTSPSQP 

      1090       1100       1110       1120       1130       1140 
RKKIFKPEEL RQALMPTLEA LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR 

      1150       1160       1170       1180       1190       1200 
KLDTGQYQEP WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC 

      1210       1220       1230       1240       1250       1260 
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT LGDDPSQPQT 

      1270       1280       1290       1300       1310       1320 
TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI IWPSGFVCDN CLKKTGRPRK 

      1330       1340       1350       1360       1370       1380 
ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN HPEAGEVFVR VVASSDKTVE VKPGMKSRFV 

      1390       1400       1410       1420       1430       1440 
DSGEMSESFP YRTKALFAFE EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF 

      1450       1460       1470       1480       1490       1500 
RPRCLRTAVY HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ 

      1510       1520       1530       1540       1550       1560 
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE ESIKELEQEE 

      1570       1580       1590       1600       1610       1620 
EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI SRANKKKPSM PNVSNDLSQK 

      1630       1640       1650       1660       1670       1680 
LYATMEKHKE VFFVIHLHAG PVINTLPPIV DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS 

      1690       1700       1710       1720       1730       1740 
LRRSKWSTLC MLVELHTQGQ DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH 

      1750       1760       1770       1780       1790       1800 
KMVKWGLGLD DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR 

      1810       1820       1830       1840       1850       1860 
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL RQQQIQHRLQ 

      1870       1880       1890       1900       1910       1920 
QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP QTPQPPAQPQ PSPVSMSPAG 

      1930       1940       1950       1960       1970       1980 
FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ PPPAAVEAAR QIEREAQQQQ HLYRVNINNS 

      1990       2000       2010       2020       2030       2040 
MPPGRTGMGT PGSQMAPVSL NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI 

      2050       2060       2070       2080       2090       2100 
SMQAQAAVAG PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF 

      2110       2120       2130       2140       2150       2160 
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP RPGVPPQQQA 

      2170       2180       2190       2200       2210       2220 
MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ QQQQQQQQQQ QQQQQQGSAG 

      2230       2240       2250       2260       2270       2280 
MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG 

      2290       2300       2310       2320       2330       2340 
ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS 

      2350       2360       2370       2380       2390       2400 
NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL 

      2410       2420       2430       2440 
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL 

« Hide

Isoform 2 [UniParc].

Checksum: F95ED9F12B5DEDFB
Show »

FASTA2,404260,993

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"An essential role for p300/CBP in the cellular response to hypoxia."
Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C., Goldberg M.A., Bunn H.F., Livingston D.M.
Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996) [PubMed] [Europe PMC] [Abstract]
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]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[38]"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.
[39]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
[40]"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].
[41]"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.
[42]"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].
[43]"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.
[44]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[45]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"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.
[47]"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.
[48]"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.
[49]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1081-1197.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS39162.
RefSeqNP_001073315.1. NM_001079846.1.
NP_004371.2. NM_004380.2.
UniGeneHs.459759.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JSPNMR-B1081-1197[»]
1LIQNMR-A376-402[»]
1RDTX-ray2.40E58-80[»]
1WO3NMR-A394-398[»]
1WO4NMR-A394-398[»]
1WO5NMR-A394-398[»]
1WO6NMR-A133-138[»]
1WO7NMR-A133-138[»]
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[»]
ProteinModelPortalQ92793.
SMRQ92793. Positions 341-440, 587-673, 1049-1750, 1763-1854, 2065-2111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107777. 264 interactions.
DIPDIP-952N.
IntActQ92793. 56 interactions.
MINTMINT-104685.
STRING9606.ENSP00000262367.

Chemistry

BindingDBQ92793.
ChEMBLCHEMBL5747.

PTM databases

PhosphoSiteQ92793.

Polymorphism databases

DMDM116241283.

Proteomic databases

PaxDbQ92793.
PRIDEQ92793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262367; ENSP00000262367; ENSG00000005339. [Q92793-1]
ENST00000382070; ENSP00000371502; ENSG00000005339. [Q92793-2]
GeneID1387.
KEGGhsa:1387.
UCSCuc002cvv.3. human. [Q92793-1]

Organism-specific databases

CTD1387.
GeneCardsGC16M003775.
HGNCHGNC:2348. CREBBP.
HPACAB004212.
HPA055861.
MIM180849. phenotype.
600140. gene.
neXtProtNX_Q92793.
Orphanet370026. 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.
PharmGKBPA26866.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000111353.
HOVERGENHBG000185.
KOK04498.
OMAPCPPVTQ.
OrthoDBEOG75B84F.
PhylomeDBQ92793.
TreeFamTF101097.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_2155. NICD traffics to nucleus.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkQ92793.

Gene expression databases

ArrayExpressQ92793.
BgeeQ92793.
CleanExHS_CREBBP.
GenevestigatorQ92793.

Family and domain databases

Gene3D1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProIPR001487. 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]
PfamPF00439. 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]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSCREBBP. human.
EvolutionaryTraceQ92793.
GeneWikiCREB-binding_protein.
GenomeRNAi1387.
NextBio5635.
PROQ92793.
SOURCESearch...

Entry information

Entry nameCBP_HUMAN
AccessionPrimary (citable) accession number: Q92793
Secondary accession number(s): D3DUC9 expand/collapse secondary AC list , O00147, Q16376, Q4LE28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM