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P45481 (CBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2441 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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers By similarity. Ref.6 Ref.8 Ref.12 Ref.13

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. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. 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 FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with MECOM and MTDH By similarity. Interacts with CITED1 (via C-terminus). Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region). Interacts with phosphorylated CREB1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK and ARNTL/BMAL1. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17

Subcellular location

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

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. Ref.8

Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B By similarity.

Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX. Ref.13

Sequence similarities

Contains 1 bromo domain.

Contains 1 KIX domain.

Contains 2 TAZ-type zinc fingers.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainBromodomain
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
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 sequence or structural similarity. Source: UniProtKB

germ-line stem cell maintenance

Inferred from mutant phenotype PubMed 17936260. Source: MGI

histone acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 10733899. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 16012757. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10733899. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12464179. Source: MGI

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from sequence orthology PubMed 17332504. Source: MGI

condensed chromosome outer kinetochore

Inferred from direct assay PubMed 14519686. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone acetyltransferase complex

Inferred from direct assay PubMed 9742083. Source: MGI

nuclear chromatin

Inferred from direct assay PubMed 15187136PubMed 16427017. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11963968PubMed 12496368PubMed 15509593. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 12464179PubMed 16606840. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15681609. Source: MGI

MRF binding

Inferred from sequence or structural similarity. Source: UniProtKB

acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 15832170. Source: MGI

histone acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10610177Ref.7PubMed 10733899PubMed 11799127PubMed 16332960. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 10075717. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P889466EBI-296306,EBI-936023From a different organism.
COPS2P612012EBI-296306,EBI-1050386From a different organism.
Creb1Q011472EBI-296306,EBI-2291098
Ctnnb1Q022483EBI-296306,EBI-397872
DDX5P178443EBI-296306,EBI-351962From a different organism.
HIST2H4BP628052EBI-296306,EBI-302023From a different organism.
Khdrbs1Q607497EBI-296306,EBI-519077
KMT2AQ031647EBI-296306,EBI-591370From a different organism.
SREBF1P36956-12EBI-296306,EBI-948328From a different organism.
TP53P046376EBI-296306,EBI-366083From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 24412440CREB-binding protein
PRO_0000211191

Regions

Domain586 – 66580KIX
Domain1104 – 117673Bromo
Zinc finger346 – 43287TAZ-type 1
Zinc finger1702 – 174544ZZ-type
Zinc finger1766 – 184782TAZ-type 2
Region226 – 409184Interaction with SRCAP By similarity
Compositional bias1062 – 10654Poly-Glu
Compositional bias1556 – 15638Poly-Glu
Compositional bias1944 – 19496Poly-Pro
Compositional bias1968 – 19714Poly-Gln
Compositional bias2082 – 20865Poly-Gln
Compositional bias2200 – 221617Poly-Gln
Compositional bias2296 – 22994Poly-Gln

Sites

Metal binding3621Zinc 1
Metal binding3661Zinc 1
Metal binding3791Zinc 1
Metal binding3841Zinc 1
Metal binding3931Zinc 2
Metal binding3971Zinc 2
Metal binding4031Zinc 2
Metal binding4081Zinc 2
Metal binding4171Zinc 3
Metal binding4211Zinc 3
Metal binding4261Zinc 3
Metal binding4291Zinc 3

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1201Phosphoserine By similarity
Modified residue6001Omega-N-methylated arginine Probable
Modified residue6241Omega-N-methylated arginine Probable
Modified residue6561N6-acetyllysine Ref.16
Modified residue10151N6-acetyllysine By similarity
Modified residue10311Phosphoserine By similarity
Modified residue12171N6-acetyllysine Ref.16
Modified residue13831Phosphoserine; by IKKA By similarity
Modified residue13871Phosphoserine; by IKKA By similarity
Modified residue15841N6-acetyllysine By similarity
Modified residue15871N6-acetyllysine By similarity
Modified residue15921N6-acetyllysine By similarity
Modified residue15931N6-acetyllysine By similarity
Modified residue15961N6-acetyllysine Ref.16
Modified residue15981N6-acetyllysine Ref.16
Modified residue17421N6-acetyllysine By similarity
Modified residue17451N6-acetyllysine Ref.16
Modified residue20641Phosphoserine By similarity
Modified residue20771Phosphoserine By similarity
Modified residue20801Phosphoserine By similarity
Cross-link999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13
Cross-link1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13
Cross-link1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13

Experimental info

Mutagenesis6001R → N: Abolishes binding to CREB. Ref.4 Ref.6
Mutagenesis9991K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-1034 and R-1057. Ref.6 Ref.13
Mutagenesis10151K → R: No change in sumoylation. Ref.6 Ref.13
Mutagenesis10341K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1057. Ref.6 Ref.13
Mutagenesis10431K → R: No change in sumoylation. Ref.6 Ref.13
Mutagenesis10531K → R: No change in sumoylation. Ref.6 Ref.13
Mutagenesis10571K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1034. Ref.6 Ref.13
Mutagenesis10611K → R: No change in sumoylation. Ref.6 Ref.13
Mutagenesis10871K → R: No change in sumoylation. Ref.6
Mutagenesis1690 – 16912LC → KL: Abolishes histone acetyltransferase activity. Ref.6
Sequence conflict4001G → P in AAB28651. Ref.1
Sequence conflict5301I → V in AAB28651. Ref.1
Sequence conflict6701S → T in AAB28651. Ref.1
Sequence conflict8261V → E in AAB28651. Ref.1
Sequence conflict9781S → T in AAB28651. Ref.1
Sequence conflict11591W → R in AAB28651. Ref.1
Sequence conflict12391E → G in AAB28651. Ref.1
Sequence conflict14171N → D in AAB28651. Ref.1
Sequence conflict14291R → C in AAB28651. Ref.1
Sequence conflict14661G → V in AAB28651. Ref.1
Sequence conflict14701G → A in AAB28651. Ref.1
Sequence conflict1850 – 18512KL → NV in AAB28651. Ref.1
Sequence conflict18591R → C in AAB28651. Ref.1
Sequence conflict19871A → D in AAB28651. Ref.1
Sequence conflict20601P → N in AAB28651. Ref.1
Sequence conflict23811S → T in AAB28651. Ref.1

Secondary structure

.............................................................. 2441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45481 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: D89AF52B7BD33347

FASTA2,441265,494
        10         20         30         40         50         60 
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP 

        70         80         90        100        110        120 
DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS 

       130        140        150        160        170        180 
PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF 

       190        200        210        220        230        240 
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE 

       250        260        270        280        290        300 
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ 

       310        320        330        340        350        360 
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL 

       370        380        390        400        410        420 
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN 

       430        440        450        460        470        480 
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM 

       490        500        510        520        530        540 
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ 

       550        560        570        580        590        600 
PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 

       610        620        630        640        650        660 
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI 

       670        680        690        700        710        720 
QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM 

       730        740        750        760        770        780 
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN 

       790        800        810        820        830        840 
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP 

       850        860        870        880        890        900 
QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP 

       910        920        930        940        950        960 
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT 

       970        980        990       1000       1010       1020 
PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS 

      1030       1040       1050       1060       1070       1080 
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ 

      1090       1100       1110       1120       1130       1140 
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK 

      1150       1160       1170       1180       1190       1200 
RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC 

      1210       1220       1230       1240       1250       1260 
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ 

      1270       1280       1290       1300       1310       1320 
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR 

      1330       1340       1350       1360       1370       1380 
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF 

      1390       1400       1410       1420       1430       1440 
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF 

      1450       1460       1470       1480       1490       1500 
FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL 

      1510       1520       1530       1540       1550       1560 
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE 

      1570       1580       1590       1600       1610       1620 
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ 

      1630       1640       1650       1660       1670       1680 
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS 

      1690       1700       1710       1720       1730       1740 
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT 

      1750       1760       1770       1780       1790       1800 
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK 

      1810       1820       1830       1840       1850       1860 
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL 

      1870       1880       1890       1900       1910       1920 
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA 

      1930       1940       1950       1960       1970       1980 
GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN 

      1990       2000       2010       2020       2030       2040 
GMPPGRAGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV 

      2050       2060       2070       2080       2090       2100 
MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 

      2110       2120       2130       2140       2150       2160 
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP 

      2170       2180       2190       2200       2210       2220 
AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS 

      2230       2240       2250       2260       2270       2280 
LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA 

      2290       2300       2310       2320       2330       2340 
DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN 

      2350       2360       2370       2380       2390       2400 
QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG 

      2410       2420       2430       2440 
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L 

« Hide

References

« Hide 'large scale' references
[1]"Phosphorylated CREB binds specifically to the nuclear protein CBP."
Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R., Goodman R.H.
Nature 365:855-859(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors."
Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.
Cell 85:403-414(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA1.
[4]"Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism."
Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., Hoeger C., Montminy M.R.
Mol. Cell. Biol. 16:694-703(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CREB1, MUTAGENESIS OF ARG-600.
[5]"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA3.
[6]"CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites."
Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.
Mol. Cell. Biol. 19:3496-3505(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GATA1, MUTAGENESIS OF 1690-LYS-CYS-1691.
[7]"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.
[8]"A transcriptional switch mediated by cofactor methylation."
Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, FUNCTION.
[9]"Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells."
Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T.
Genomics 80:601-613(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CITED4.
[10]"CREB-binding protein/p300 co-activation of crystallin gene expression."
Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.
J. Biol. Chem. 277:24081-24089(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAF.
[11]"Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
Rossow K.L., Janknecht R.
Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX5.
[12]"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: FUNCTION IN ACETYLATION OF FOXO1.
[13]"SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx."
Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G., Kwok R.P.S., Shih H.-M.
Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH DAXX, FUNCTION, MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043; LYS-1053; LYS-1057 AND LYS-1061.
[14]"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
Shin S., Janknecht R.
J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX17.
[15]"Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling."
Cho G., Lim Y., Zand D., Golden J.A.
Mol. Cell. Biol. 28:1565-1572(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZCCHC12.
[16]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656; LYS-1217; LYS-1596; LYS-1598 AND LYS-1745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[17]"Machine learning helps identify CHRONO as a circadian clock component."
Anafi R.C., Lee Y., Sato T.K., Venkataraman A., Ramanathan C., Kavakli I.H., Hughes M.E., Baggs J.E., Growe J., Liu A.C., Kim J., Hogenesch J.B.
PLoS Biol. 12:E1001840-E1001840(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARNTL/BMAL1.
[18]"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites."
De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
J. Biol. Chem. 279:3042-3049(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 340-439 IN COMPLEX WITH 220-269 OF CITED2 AND ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S66385 mRNA. Translation: AAB28651.1.
AC132380 Genomic DNA. No translation available.
CCDSCCDS27915.1.
PIRS39161.
UniGeneMm.132238.
Mm.392384.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F81NMR-A1764-1850[»]
1JJSNMR-A2067-2112[»]
1KBHNMR-B2059-2117[»]
1KDXNMR-A586-666[»]
1L8CNMR-A345-439[»]
1R8UNMR-B340-439[»]
1SB0NMR-A586-672[»]
1TOTNMR-A1700-1751[»]
1U2NNMR-A340-439[»]
2AGHNMR-B586-672[»]
2C52NMR-A2059-2117[»]
2KA4NMR-A340-439[»]
2KA6NMR-A1764-1855[»]
2KKJNMR-A2059-2117[»]
2L14NMR-A2059-2117[»]
2LQHNMR-A586-672[»]
2LQINMR-A586-672[»]
2LWWNMR-A340-439[»]
4I9OX-ray2.00A586-672[»]
DisProtDP00348.
ProteinModelPortalP45481.
SMRP45481. Positions 340-439, 586-672, 1082-1751, 1764-1855, 2066-2112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-5974N.
IntActP45481. 21 interactions.
MINTMINT-203452.

PTM databases

PhosphoSiteP45481.

Proteomic databases

MaxQBP45481.
PaxDbP45481.
PRIDEP45481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1098280. Crebbp.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000111353.
HOVERGENHBG000185.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.
REACT_218274. Chromatin organization.

Gene expression databases

CleanExMM_CREBBP.
GenevestigatorP45481.

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. mouse.
EvolutionaryTraceP45481.
PROP45481.
SOURCESearch...

Entry information

Entry nameCBP_MOUSE
AccessionPrimary (citable) accession number: P45481
Secondary accession number(s): E9QPH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot