CREB-binding protein - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q92793 (CBP_HUMAN)

Last modified February 9, 2010. Version 130. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
CREB-binding protein
EC=2.3.1.48

Gene names

Name:	CREBBP
Synonyms:	CBP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	2442 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Ref.9
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 phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with MAF, SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, 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 ZCCHC12 By similarity. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activiy via recruitment of HDAC2 to DAAX By similarity. 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. Ref.9 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.32
Subcellular location	Nucleus. Note: Recruited to nuclear bodies by SS18L1/CREST.
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 upon DNA damage, probably by ATM or ATR. Ref.31 Ref.33 Ref.35 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 MYST3/MOZ; translocation t(11;16)(q23;p13.3) with MLL/HRX; translocation t(10;16)(q22;p13) with MYST4/MORF. MYST3-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Defects in CREBBP are a cause of Rubinstein-Taybi syndrome (RSTS) [MIM:180849]. RSTS is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Ref.41 Ref.42 Ref.43 Ref.44
Sequence similarities	Contains 1 bromo domain. Contains 1 KIX domain. Contains 2 TAZ-type zinc fingers. Contains 1 ZZ-type zinc finger.

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Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Disease mutation
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
Gene Ontology (GO)
Biological process	N-terminal peptidyl-lysine acetylation Inferred from direct assay. Source: UniProtKB histone acetylation Ref.39 Inferred from direct assay. Source: UniProtKB homeostatic process Non-traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Traceable author statement. Source: ProtInc response to hypoxia Traceable author statement. Source: UniProtKB signal transduction Non-traceable author statement. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: ProtInc nuclear body Ref.28 Inferred from direct assay. Source: UniProtKB
Molecular function	MyoD binding Inferred from direct assay. Source: UniProtKB histone acetyltransferase activity Ref.39 Inferred from direct assay. Source: UniProtKB p53 binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc transcription coactivator activity Ref.6 Inferred from direct assay. Source: UniProtKB transcription factor activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
DAXX	Q9UER7	1	EBI-81215,EBI-77321
HTT	P42858	1	EBI-81215,EBI-466029
IFNAR2	P48551	3	EBI-81215,EBI-958408
KAT2B	Q92831	2	EBI-81215,EBI-477430
MTDH	Q86UE4	1	EBI-81215,EBI-1046588
NAP1L1	P55209	2	EBI-81215,EBI-356392
NCOA6	Q14686	1	EBI-81215,EBI-78670
RELA	Q04206	1	EBI-81215,EBI-73886
RPA2	P15927	1	EBI-81215,EBI-621404
TP53	P04637	3	EBI-81215,EBI-366083

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 2442

2441

CREB-binding protein

PRO_0000211190

Regions

Domain

587 – 666

KIX

Domain

1103 – 1175

Bromo

Zinc finger

347 – 433

TAZ-type 1

Zinc finger

1701 – 1744

ZZ-type

Zinc finger

1765 – 1846

TAZ-type 2

Region

227 – 410

184

Interaction with SRCAP

Region

1460 – 1891

432

Interaction with TRERF1

Compositional bias

1061 – 1064

Poly-Glu

Compositional bias

1199 – 1487

289

Cys/His-rich

Compositional bias

1555 – 1562

Poly-Glu

Compositional bias

1943 – 1948

Poly-Pro

Compositional bias

1967 – 1970

Poly-Gln

Compositional bias

2081 – 2085

Poly-Gln

Compositional bias

2199 – 2216

Poly-Gln

Compositional bias

2245 – 2248

Poly-Gln

Compositional bias

2297 – 2300

Poly-Gln

Sites

Site

29 – 30

Breakpoint for translocation to form MYST4-CREBBP

Site

266 – 267

Breakpoint for translocation to form MYST3-CREBBP

Amino acid modifications

Modified residue

N-acetylalanine Ref.35

Modified residue

121

Phosphoserine Ref.33

Modified residue

124

Phosphoserine Ref.31

Modified residue

274

Phosphoserine Ref.35

Modified residue

601

Omega-N-methylated arginine By similarity

Modified residue

625

Omega-N-methylated arginine By similarity

Modified residue

1001

Phosphothreonine Ref.31

Modified residue

1014

N6-acetyllysine Ref.37

Modified residue

1030

Phosphoserine Ref.31

Modified residue

1072

Phosphoserine Ref.31

Modified residue

1216

N6-acetyllysine Ref.37

Modified residue

1583

N6-acetyllysine Ref.37

Modified residue

1588

N6-acetyllysine Ref.30

Modified residue

1591

N6-acetyllysine Ref.37 Ref.30

Modified residue

1592

N6-acetyllysine Ref.37 Ref.30

Modified residue

1595

N6-acetyllysine Ref.37 Ref.30

Modified residue

1597

N6-acetyllysine Ref.37 Ref.30

Modified residue

1741

N6-acetyllysine Ref.37

Modified residue

1744

N6-acetyllysine Ref.37

Modified residue

1755

Phosphoserine Ref.31

Modified residue

2063

Phosphoserine Ref.33 Ref.35 Ref.36

Modified residue

2076

Phosphoserine Ref.33

Modified residue

2079

Phosphoserine Ref.33 Ref.35

Cross-link

998

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Cross-link

1033

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Cross-link

1056

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Natural variations

Natural variant

1175

Y → C in RSTS; mild form. dbSNP rs28937315. Ref.42

VAR_037305

Natural variant

1278

E → K in RSTS; abolishes acetyltransferase activity. Ref.43 Ref.44

VAR_035080

Natural variant

1378

R → P in RSTS; abolishes acetyltransferase activity and the ability of transactivate CREB. Ref.41

VAR_015578

Natural variant

1414

V → I: dbSNP rs130015.

VAR_027953

Natural variant

1447

T → I in RSTS. Ref.44

VAR_035081

Natural variant

1450

Y → H in RSTS. Ref.44

VAR_035082

Natural variant

1470

H → R in RSTS. Ref.44

VAR_035083

Natural variant

1664

R → H in RSTS; abolishes acetyltransferase activity. Ref.43 Ref.44

VAR_035084

Experimental info

Sequence conflict

1511 – 1513

FAE → NSG in AAC51340. Ref.2

Sequence conflict

1724 – 1725

ED → VV in AAC51340. Ref.2

Sequence conflict

1770

L → V in AAC51770. Ref.1

Sequence conflict

1789

N → F in AAC51340. Ref.2

Sequence conflict

1812

T → P in AAC51340. Ref.2

Secondary structure

2442

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q92793-1 [UniParc].

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

2,442

265,351

        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

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References

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[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: 9238046] [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: 9177780] [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]	"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: 8782817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-405, CHROMOSOMAL TRANSLOCATION WITH MYST3.
[5]	"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: 11157802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-83, CHROMOSOMAL TRANSLOCATION WITH MYST4.
[6]	"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: 8684459] [Abstract] Cited for: INTERACTION WITH PCAF.
[7]	"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: 8917528] [Abstract] Cited for: INTERACTION WITH HIF1A AND EP300.
[8]	"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: 9528808] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[9]	"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: 9707565] [Abstract] Cited for: INTERACTION WITH KLF1, FUNCTION.
[10]	"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: 10347196] [Abstract] Cited for: INTERACTION WITH SRCAP.
[11]	"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: 10077561] [Abstract] Cited for: INTERACTION WITH PML.
[12]	"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: 10490106] [Abstract] Cited for: ACETYLATION OF NCOA3.
[13]	"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: 10866662] [Abstract] Cited for: INTERACTION WITH NCOA6.
[14]	"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: 11154691] [Abstract] Cited for: INTERACTION WITH MAFG, ACETYLATION OF MAFG.
[15]	"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: 11514544] [Abstract] Cited for: INTERACTION WITH NFATC4.
[16]	"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: 11568182] [Abstract] Cited for: INTERACTION WITH MECOM.
[17]	"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: 11463834] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[18]	"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: 11559821] [Abstract] Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
[19]	"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: 11349124] [Abstract] Cited for: INTERACTION WITH TRERF1.
[20]	"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: 11481323] [Abstract] Cited for: INTERACTION WITH PELP1.
[21]	"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: 11864910] [Abstract] Cited for: INTERACTION WITH SPIB.
[22]	"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: 11744733] [Abstract] Cited for: INTERACTION WITH CITED4.
[23]	"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: 11971985] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH NCOA2; NCOA3; IKKA; IKKB AND IKBKG.
[24]	"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: 12738767] [Abstract] Cited for: INTERACTION WITH IRF2, ACETYLATION OF IRF2.
[25]	"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: 12730195] [Abstract] Cited for: INTERACTION WITH N4BP2.
[26]	"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: 15075319] [Abstract] Cited for: INTERACTION WITH ELF3.
[27]	"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: 15126506] [Abstract] Cited for: INTERACTION WITH MLLT7.
[28]	"The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies." Pradhan A., Liu Y. Neurosci. Lett. 370:191-195(2004) [PubMed: 15488321] [Abstract] Cited for: SUBCELLULAR LOCATION.
[29]	"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: 14716005] [Abstract] Cited for: INTERACTION WITH SS18L1/CREST.
[30]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1588; LYS-1591; LYS-1592; LYS-1595 AND LYS-1597, MASS SPECTROMETRY. Tissue: Epithelium.
[31]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; THR-1001; SER-1030; SER-1072 AND SER-1755, MASS SPECTROMETRY.
[32]	"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: 18316612] [Abstract] Cited for: INTERACTION WITH MTDH.
[33]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-2063; SER-2076 AND SER-2079, MASS SPECTROMETRY.
[34]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[35]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-2063 AND SER-2079, MASS SPECTROMETRY.
[36]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2063, MASS SPECTROMETRY. Tissue: T-cell.
[37]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1014; LYS-1216; LYS-1583; LYS-1591; LYS-1592; LYS-1595; LYS-1597; LYS-1741 AND LYS-1744, MASS SPECTROMETRY.
[38]	"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: 11959977] [Abstract] Cited for: STRUCTURE BY NMR OF 345-439 IN COMPLEX WITH 776-826 OF HIF1A.
[39]	"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: 11742995] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MYST3.
[40]	"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: 14744133] [Abstract] Cited for: STRUCTURE BY NMR OF 589-679 IN COMPLEX WITH HIV-1 TAT.
[41]	"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: 11331617] [Abstract] Cited for: VARIANT RSTS PRO-1378.
[42]	"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: 12114483] [Abstract] Cited for: VARIANT RSTS CYS-1175.
[43]	"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: 12566391] [Abstract] Cited for: VARIANTS RSTS LYS-1278 AND HIS-1664, CHARACTERIZATION OF VARIANTS RSTS LYS-1278 AND HIS-1664.
[44]	"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: 15706485] [Abstract] Cited for: VARIANTS RSTS LYS-1278; ILE-1447; HIS-1450; ARG-1470 AND HIS-1664.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

P300/CBP entry

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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.

IPI

IPI00023339.

PIR

S39162.

RefSeq

NP_001073315.1.
NP_004371.2.

UniGene

Hs.459759

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JSP	NMR	-	B	1081-1197	[»]
1LIQ	NMR	-	A	376-402	[»]
1WO3	NMR	-	A	394-398	[»]
1WO4	NMR	-	A	394-398	[»]
1WO5	NMR	-	A	394-398	[»]
1WO6	NMR	-	A	133-138	[»]
1WO7	NMR	-	A	133-138	[»]
1ZOQ	X-ray	2.37	C/D	2065-2111	[»]
2D82	NMR	-	A	1081-1197	[»]
2KJE	NMR	-	A	1763-1854	[»]
2RNY	NMR	-	A	1081-1197	[»]
3DWY	X-ray	1.98	A/B	1081-1197	[»]

SMR

Q92793. Positions 341-440, 587-673, 1323-1701, 1699-1750.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-952N.

IntAct

Q92793. 25 interactions.

STRING

Q92793.

PTM databases

PhosphoSite

Q92793.

Proteomic databases

PRIDE

Q92793.

Genome annotation databases

Ensembl

ENST00000262367; ENSP00000262367; ENSG00000005339; Homo sapiens. [Genome view]

GeneID

1387.

KEGG

hsa:1387.

UCSC

uc002cvv.1. human.

Organism-specific databases

CTD

1387.

GeneCards

GC16M003716.

H-InvDB

HIX0026954.

HGNC

HGNC:2348. CREBBP.

HPA

CAB004212.

MIM

180849. phenotype.
600140. gene.

Orphanet

783. Rubinstein-Taybi syndrome.

PharmGKB

PA26866.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14101.

HOGENOM

HBG402903.

HOVERGEN

Q92793.

OMA

VTQSPLH.

OrthoDB

EOG9WWV3Q.

PhylomeDB

Q92793.

Enzyme and pathway databases

BRENDA

2.3.1.48. 247.

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hnf3apathway. FOXA1 transcription factor network.
foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
hif1_tfpathway. HIF-1-alpha transcription factor network.
ifngpathway. IFN-gamma pathway.
il12_stat4pathway. IL12 signaling mediated by STAT4.
ps1pathway. Presenilin action in Notch and Wnt signaling.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).

Reactome

REACT_602. Metabolism of lipids and lipoproteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92793.

Bgee

Q92793.

CleanEx

HS_CREBBP.

Genevestigator

Q92793.

GermOnline

ENSG00000005339. Homo sapiens.

Family and domain databases

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR003101. KIX.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:1.10.246.20. KIX. 1 hit.
G3DSA:1.10.1630.10. Nuc_rcpt_coact_CREBbp. 1 hit.
G3DSA:1.20.1020.10. Znf_TAZ. 2 hits.

Pfam

PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 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]

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 Resources

NextBio

5635.

SOURCE

Search...

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Entry information

Entry name

CBP_HUMAN

Accession

Primary (citable) accession number: Q92793
Secondary accession number(s): O00147, Q16376

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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Relevant documents

Human chromosome 16

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents