P45481 (CBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CREB-binding protein
EC=2.3.1.48

Gene names

Name:	Crebbp
Synonyms:	Cbp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2441 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 DAAX. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Bromodomain Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Transferase
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-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 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML 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 transcription factor complex Inferred from direct assay PubMed 12464179PubMed 16606840. Source: MGI
Molecular_function	DNA binding Inferred from direct assay PubMed 15681609. Source: MGI MRF binding 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 transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P88946	6	EBI-296306,EBI-936023	From a different organism.
Ctnnb1	Q02248	2	EBI-296306,EBI-397872
DDX5	P17844	3	EBI-296306,EBI-351962	From a different organism.
Khdrbs1	Q60749	7	EBI-296306,EBI-519077
SREBF1	P36956-1	2	EBI-296306,EBI-948328	From a different organism.
TP53	P04637	6	EBI-296306,EBI-366083	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2441

2441

CREB-binding protein

PRO_0000211191

Regions

Domain

586 – 665

80

KIX

Domain

1104 – 1176

73

Bromo

Zinc finger

346 – 432

87

TAZ-type 1

Zinc finger

1702 – 1745

44

ZZ-type

Zinc finger

1766 – 1847

82

TAZ-type 2

Region

226 – 409

184

Interaction with SRCAP By similarity

Compositional bias

1062 – 1065

4

Poly-Glu

Compositional bias

1556 – 1563

8

Poly-Glu

Compositional bias

1944 – 1949

6

Poly-Pro

Compositional bias

1968 – 1971

4

Poly-Gln

Compositional bias

2082 – 2086

5

Poly-Gln

Compositional bias

2200 – 2216

17

Poly-Gln

Compositional bias

2296 – 2299

4

Poly-Gln

Sites

Metal binding

362

1

Zinc 1

Metal binding

366

1

Zinc 1

Metal binding

379

1

Zinc 1

Metal binding

384

1

Zinc 1

Metal binding

393

1

Zinc 2

Metal binding

397

1

Zinc 2

Metal binding

403

1

Zinc 2

Metal binding

408

1

Zinc 2

Metal binding

417

1

Zinc 3

Metal binding

421

1

Zinc 3

Metal binding

426

1

Zinc 3

Metal binding

429

1

Zinc 3

Amino acid modifications

Modified residue

120

1

Phosphoserine By similarity

Modified residue

600

1

Omega-N-methylated arginine Probable

Modified residue

624

1

Omega-N-methylated arginine Probable

Modified residue

1015

1

N6-acetyllysine By similarity

Modified residue

1031

1

Phosphoserine By similarity

Modified residue

1217

1

N6-acetyllysine By similarity

Modified residue

1383

1

Phosphoserine; by IKKA By similarity

Modified residue

1387

1

Phosphoserine; by IKKA By similarity

Modified residue

1584

1

N6-acetyllysine By similarity

Modified residue

1587

1

N6-acetyllysine By similarity

Modified residue

1592

1

N6-acetyllysine By similarity

Modified residue

1593

1

N6-acetyllysine By similarity

Modified residue

1596

1

N6-acetyllysine By similarity

Modified residue

1598

1

N6-acetyllysine By similarity

Modified residue

1742

1

N6-acetyllysine By similarity

Modified residue

1745

1

N6-acetyllysine By similarity

Modified residue

2064

1

Phosphoserine By similarity

Modified residue

2077

1

Phosphoserine By similarity

Modified residue

2080

1

Phosphoserine By similarity

Cross-link

999

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13

Cross-link

1034

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13

Cross-link

1057

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13

Experimental info

Mutagenesis

600

1

R → N: Abolishes binding to CREB. Ref.4 Ref.6

Mutagenesis

999

1

K → 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

Mutagenesis

1015

1

K → R: No change in sumoylation. Ref.6 Ref.13

Mutagenesis

1034

1

K → 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

Mutagenesis

1043

1

K → R: No change in sumoylation. Ref.6 Ref.13

Mutagenesis

1053

1

K → R: No change in sumoylation. Ref.6 Ref.13

Mutagenesis

1057

1

K → 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

Mutagenesis

1061

1

K → R: No change in sumoylation. Ref.6 Ref.13

Mutagenesis

1087

1

K → R: No change in sumoylation. Ref.6

Mutagenesis

1690 – 1691

2

LC → KL: Abolishes histone acetyltransferase activity. Ref.6

Sequence conflict

400

1

G → P in AAB28651. Ref.1

Sequence conflict

530

1

I → V in AAB28651. Ref.1

Sequence conflict

670

1

S → T in AAB28651. Ref.1

Sequence conflict

826

1

V → E in AAB28651. Ref.1

Sequence conflict

978

1

S → T in AAB28651. Ref.1

Sequence conflict

1159

1

W → R in AAB28651. Ref.1

Sequence conflict

1239

1

E → G in AAB28651. Ref.1

Sequence conflict

1417

1

N → D in AAB28651. Ref.1

Sequence conflict

1429

1

R → C in AAB28651. Ref.1

Sequence conflict

1466

1

G → V in AAB28651. Ref.1

Sequence conflict

1470

1

G → A in AAB28651. Ref.1

Sequence conflict

1850 – 1851

2

KL → NV in AAB28651. Ref.1

Sequence conflict

1859

1

R → C in AAB28651. Ref.1

Sequence conflict

1987

1

A → D in AAB28651. Ref.1

Sequence conflict

2060

1

P → N in AAB28651. Ref.1

Sequence conflict

2381

1

S → T in AAB28651. Ref.1

Secondary structure

1

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2441

Helix Strand Turn

Details...

Turn

343 – 345

3

Helix

347 – 372

26

Beta strand

374 – 376

3

Helix

384 – 396

13

Helix

400 – 402

3

Helix

406 – 420

15

Helix

429 – 433

5

Helix

436 – 438

3

Turn

587 – 590

4

Helix

591 – 594

4

Helix

597 – 611

15

Helix

617 – 621

5

Helix

623 – 640

18

Helix

646 – 662

17

Turn

663 – 665

3

Turn

667 – 671

5

Turn

1709 – 1711

3

Beta strand

1713 – 1726

14

Helix

1731 – 1737

7

Beta strand

1741 – 1746

6

Helix

1765 – 1785

21

Helix

1794 – 1808

15

Helix

1812 – 1815

4

Helix

1818 – 1833

16

Helix

1844 – 1849

6

Beta strand

2061 – 2064

4

Helix

2068 – 2075

8

Beta strand

2076 – 2079

4

Helix

2088 – 2091

4

Helix

2097 – 2100

4

Helix

2102 – 2104

3

Beta strand

2106 – 2108

3

Sequences

	Sequence		Length	Mass (Da)
	P45481 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: D89AF52B7BD33347	FASTA	2,441	265,494
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.

IPI

IPI00875480.

PIR

S39161.

UniGene

Mm.132238.
Mm.392384.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F81	NMR	-	A	1764-1850	[»]
1JJS	NMR	-	A	2067-2112	[»]
1KBH	NMR	-	B	2061-2117	[»]
1KDX	NMR	-	A	586-666	[»]
1L8C	NMR	-	A	345-439	[»]
1R8U	NMR	-	B	340-439	[»]
1SB0	NMR	-	A	586-672	[»]
1TOT	NMR	-	A	1700-1751	[»]
1U2N	NMR	-	A	340-439	[»]
2AGH	NMR	-	B	586-672	[»]
2C52	NMR	-	A	2061-2117	[»]
2KA4	NMR	-	A	340-439	[»]
2KA6	NMR	-	A	1764-1855	[»]
2KKJ	NMR	-	A	2061-2117	[»]
2L14	NMR	-	A	2061-2117	[»]
2LQH	NMR	-	A	586-672	[»]
2LQI	NMR	-	A	586-672	[»]
4I9O	X-ray	2.00	A	586-672	[»]

DisProt

DP00348.

ProteinModelPortal

P45481.

SMR

P45481. Positions 340-439, 586-672, 1082-1198, 1324-1751, 1764-1855, 2066-2112.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5974N.

IntAct

P45481. 14 interactions.

MINT

MINT-203452.

PTM databases

PhosphoSite

P45481.

Proteomic databases

PaxDb

P45481.

PRIDE

P45481.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:1098280. Crebbp.

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000111353.

HOVERGEN

HBG000185.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

CleanEx

MM_CREBBP.

Genevestigator

P45481.

GermOnline

ENSMUSG00000022521. Mus musculus.

Family and domain databases

Gene3D

1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.

InterPro

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]

Pfam

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]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF47040. KIX. 1 hit.
SSF69125. Nuc_recept_coact. 1 hit.
SSF57933. TAZ_finger. 2 hits.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

CREBBP. mouse.

EvolutionaryTrace

P45481.

SOURCE

Search...

Entry information

Entry name

CBP_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 147 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program