Q92793 (CBP_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2442 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. Ref.11 Ref.17 Ref.27 Ref.29
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 activiy via recruitment of HDAC2 to DAAX 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. 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.30 Ref.31 Ref.33 Ref.34 Ref.37
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.29 Ref.32
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.35 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 MLL/HRX; 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.47 Ref.48 Ref.49 Ref.50
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 process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing 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 Reference proteome
Gene Ontology (GO)
Biological_process	N-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 embryonic digit morphogenesis Traceable author statement PubMed 11001584. Source: BHF-UCL germ-line stem cell maintenance Inferred from electronic annotation. Source: Compara homeostatic process Non-traceable author statement PubMed 15261140. Source: UniProtKB innate immune response 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 small molecule metabolic process Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	condensed chromosome outer kinetochore Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay Ref.29. Source: UniProtKB histone acetyltransferase complex Inferred from electronic annotation. Source: Compara nuclear body Inferred from direct assay Ref.32. Source: UniProtKB nuclear chromatin Inferred from direct assay PubMed 21539536. Source: BHF-UCL transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	MRF 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 transcription factor activity involved in negative regulation of transcription Inferred from direct assay PubMed 21539536. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Compara 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.44. Source: UniProtKB signal transducer activity Traceable author statement PubMed 7913207PubMed 8028671. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	2	EBI-81215,EBI-608057
DAXX	Q9UER7	2	EBI-81215,EBI-77321
FOXO1	Q12778	2	EBI-81215,EBI-1108782
IFNAR2	P48551	4	EBI-81215,EBI-958408
IRF3	Q14653	3	EBI-81215,EBI-2650369
KAT2B	Q92831	3	EBI-81215,EBI-477430
MTDH	Q86UE4	2	EBI-81215,EBI-1046588
NAP1L1	P55209	3	EBI-81215,EBI-356392
NCOA6	Q14686	2	EBI-81215,EBI-78670
RELA	Q04206	3	EBI-81215,EBI-73886
TP53	P04637	6	EBI-81215,EBI-366083

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2442

2442

CREB-binding protein

PRO_0000211190

Regions

Domain

587 – 666

80

KIX

Domain

1103 – 1175

73

Bromo

Zinc finger

347 – 433

87

TAZ-type 1

Zinc finger

1701 – 1744

44

ZZ-type

Zinc finger

1765 – 1846

82

TAZ-type 2

Region

227 – 410

184

Interaction with SRCAP

Region

1460 – 1891

432

Interaction with TRERF1

Compositional bias

1061 – 1064

4

Poly-Glu

Compositional bias

1199 – 1487

289

Cys/His-rich

Compositional bias

1555 – 1562

8

Poly-Glu

Compositional bias

1943 – 1948

6

Poly-Pro

Compositional bias

1967 – 1970

4

Poly-Gln

Compositional bias

2081 – 2085

5

Poly-Gln

Compositional bias

2199 – 2216

18

Poly-Gln

Compositional bias

2245 – 2248

4

Poly-Gln

Compositional bias

2297 – 2300

4

Poly-Gln

Sites

Metal binding

363

1

Zinc 1 By similarity

Metal binding

367

1

Zinc 1 By similarity

Metal binding

380

1

Zinc 1 By similarity

Metal binding

385

1

Zinc 1 By similarity

Metal binding

394

1

Zinc 2 By similarity

Metal binding

398

1

Zinc 2 By similarity

Metal binding

404

1

Zinc 2 By similarity

Metal binding

409

1

Zinc 2 By similarity

Metal binding

418

1

Zinc 3 By similarity

Metal binding

422

1

Zinc 3 By similarity

Metal binding

427

1

Zinc 3 By similarity

Metal binding

430

1

Zinc 3 By similarity

Site

29 – 30

2

Breakpoint for translocation to form KAT6B-CREBBP

Site

266 – 267

2

Breakpoint for translocation to form KAT6A-CREBBP

Amino acid modifications

Modified residue

121

1

Phosphoserine Ref.38 Ref.41

Modified residue

601

1

Omega-N-methylated arginine By similarity

Modified residue

625

1

Omega-N-methylated arginine By similarity

Modified residue

1014

1

N6-acetyllysine Ref.40

Modified residue

1030

1

Phosphoserine Ref.36

Modified residue

1216

1

N6-acetyllysine Ref.40

Modified residue

1382

1

Phosphoserine; by IKKA Ref.35

Modified residue

1386

1

Phosphoserine; by IKKA Ref.35

Modified residue

1583

1

N6-acetyllysine Ref.40

Modified residue

1586

1

N6-acetyllysine Ref.40

Modified residue

1591

1

N6-acetyllysine Ref.40

Modified residue

1592

1

N6-acetyllysine Ref.40

Modified residue

1595

1

N6-acetyllysine Ref.40

Modified residue

1597

1

N6-acetyllysine Ref.40

Modified residue

1741

1

N6-acetyllysine Ref.40

Modified residue

1744

1

N6-acetyllysine Ref.40

Modified residue

2063

1

Phosphoserine Ref.38 Ref.39

Modified residue

2076

1

Phosphoserine Ref.38

Modified residue

2079

1

Phosphoserine Ref.38

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

Alternative sequence

406 – 444

39

VAHCA…RNQQT → A in isoform 2.

VSP_045700

Natural variant

1175

1

Y → C in RSTS1; mild form. Ref.48
Corresponds to variant rs28937315 [ dbSNP | Ensembl ].

VAR_037305

Natural variant

1278

1

E → K in RSTS1; abolishes acetyltransferase activity. Ref.49 Ref.50

VAR_035080

Natural variant

1378

1

R → P in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB. Ref.47

VAR_015578

Natural variant

1414

1

V → I.
Corresponds to variant rs130015 [ dbSNP | Ensembl ].

VAR_027953

Natural variant

1447

1

T → I in RSTS1. Ref.50

VAR_035081

Natural variant

1450

1

Y → H in RSTS1. Ref.50

VAR_035082

Natural variant

1470

1

H → R in RSTS1. Ref.50

VAR_035083

Natural variant

1664

1

R → H in RSTS1; abolishes acetyltransferase activity. Ref.49 Ref.50

VAR_035084

Experimental info

Sequence conflict

1511 – 1513

3

FAE → NSG in AAC51340. Ref.2

Sequence conflict

1724 – 1725

2

ED → VV in AAC51340. Ref.2

Sequence conflict

1770

1

L → V in AAC51770. Ref.1

Sequence conflict

1789

1

N → F in AAC51340. Ref.2

Sequence conflict

1812

1

T → P in AAC51340. Ref.2

Secondary structure

1

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2442

Helix Strand Turn

Details...

Beta strand

133 – 135

3

Helix

377 – 379

3

Turn

383 – 388

6

Helix

391 – 395

5

Turn

593 – 596

4

Helix

598 – 612

15

Turn

618 – 622

5

Helix

624 – 642

19

Helix

647 – 669

23

Turn

670 – 672

3

Helix

1087 – 1102

16

Turn

1105 – 1108

4

Helix

1109 – 1111

3

Helix

1117 – 1120

4

Helix

1125 – 1128

4

Helix

1135 – 1143

9

Beta strand

1146 – 1149

4

Helix

1150 – 1167

18

Turn

1169 – 1171

3

Helix

1173 – 1196

24

Helix

1765 – 1784

20

Helix

1793 – 1805

13

Turn

1811 – 1815

5

Helix

1817 – 1832

16

Helix

1841 – 1853

13

Helix

2066 – 2072

7

Helix

2080 – 2091

12

Helix

2094 – 2103

10

Turn

2104 – 2106

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 3BEA9B8558BA1A5E	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
	Isoform 2 [UniParc]. Checksum: F95ED9F12B5DEDFB	FASTA	2,404	260,993
	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 GKACQAILGS PASGIQNTIG 430 440 450 460 470 480 SVGTGQQNAT SLSNPNPIDP SSMQRAYAAL GLPYMNQPQT QLQPQVPGQQ PAQPQTHQQM 490 500 510 520 530 540 RTLNPLGNNP MNIPAGGITT DQQPPNLISE SALPTSLGAT NPLMNDGSNS GNIGTLSTIP 550 560 570 580 590 600 TAAPPSSTGV RKGWHEHVTQ DLRSHLVHKL VQAIFPTPDP AALKDRRMEN LVAYAKKVEG 610 620 630 640 650 660 DMYESANSRD EYYHLLAEKI YKIQKELEEK RRSRLHKQGI LGNQPALPAP GAQPPVIPQA 670 680 690 700 710 720 QPVRPPNGPL SLPVNRMQVS QGMNSFNPMS LGNVQLPQAP MGPRAASPMN HSVQMNSMGS 730 740 750 760 770 780 VPGMAISPSR MPQPPNMMGA HTNNMMAQAP AQSQFLPQNQ FPSSSGAMSV GMGQPPAQTG 790 800 810 820 830 840 VSQGQVPGAA LPNPLNMLGP QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHTTPPGMT 850 860 870 880 890 900 PPQPAAPTQP STPVSSSGQT PTPTPGSVPS ATQTQSTPTV QAAAQAQVTP QPQTPVQPPS 910 920 930 940 950 960 VATPQSSQQQ PTPVHAQPPG TPLSQAAASI DNRVPTPSSV ASAETNSQQP GPDVPVLEMK 970 980 990 1000 1010 1020 TETQAEDTEP DPGESKGEPR SEMMEEDLQG ASQVKEETDI AEQKSEPMEV DEKKPEVKVE 1030 1040 1050 1060 1070 1080 VKEEEESSSN GTASQSTSPS QPRKKIFKPE ELRQALMPTL EALYRQDPES LPFRQPVDPQ 1090 1100 1110 1120 1130 1140 LLGIPDYFDI VKNPMDLSTI KRKLDTGQYQ EPWQYVDDVW LMFNNAWLYN RKTSRVYKFC 1150 1160 1170 1180 1190 1200 SKLAEVFEQE IDPVMQSLGY CCGRKYEFSP QTLCCYGKQL CTIPRDAAYY SYQNRYHFCE 1210 1220 1230 1240 1250 1260 KCFTEIQGEN VTLGDDPSQP QTTISKDQFE KKKNDTLDPE PFVDCKECGR KMHQICVLHY 1270 1280 1290 1300 1310 1320 DIIWPSGFVC DNCLKKTGRP RKENKFSAKR LQTTRLGNHL EDRVNKFLRR QNHPEAGEVF 1330 1340 1350 1360 1370 1380 VRVVASSDKT VEVKPGMKSR FVDSGEMSES FPYRTKALFA FEEIDGVDVC FFGMHVQEYG 1390 1400 1410 1420 1430 1440 SDCPPPNTRR VYISYLDSIH FFRPRCLRTA VYHEILIGYL EYVKKLGYVT GHIWACPPSE 1450 1460 1470 1480 1490 1500 GDDYIFHCHP PDQKIPKPKR LQEWYKKMLD KAFAERIIHD YKDIFKQATE DRLTSAKELP 1510 1520 1530 1540 1550 1560 YFEGDFWPNV LEESIKELEQ EEEERKKEES TAASETTEGS QGDSKNAKKK NNKKTNKNKS 1570 1580 1590 1600 1610 1620 SISRANKKKP SMPNVSNDLS QKLYATMEKH KEVFFVIHLH AGPVINTLPP IVDPDPLLSC 1630 1640 1650 1660 1670 1680 DLMDGRDAFL TLARDKHWEF SSLRRSKWST LCMLVELHTQ GQDRFVYTCN ECKHHVETRW 1690 1700 1710 1720 1730 1740 HCTVCEDYDL CINCYNTKSH AHKMVKWGLG LDDEGSSQGE PQSKSPQESR RLSIQRCIQS 1750 1760 1770 1780 1790 1800 LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPV CKQLIALCCY HAKHCQENKC 1810 1820 1830 1840 1850 1860 PVPFCLNIKH KLRQQQIQHR LQQAQLMRRR MATMNTRNVP QQSLPSPTSA PPGTPTQQPS 1870 1880 1890 1900 1910 1920 TPQTPQPPAQ PQPSPVSMSP AGFPSVARTQ PPTTVSTGKP TSQVPAPPPP AQPPPAAVEA 1930 1940 1950 1960 1970 1980 ARQIEREAQQ QQHLYRVNIN NSMPPGRTGM GTPGSQMAPV SLNVPRPNQV SGPVMPSMPP 1990 2000 2010 2020 2030 2040 GQWQQAPLPQ QQPMPGLPRP VISMQAQAAV AGPRMPSVQP PRSISPSALQ DLLRTLKSPS 2050 2060 2070 2080 2090 2100 SPQQQQQVLN ILKSNPQLMA AFIKQRTAKY VANQPGMQPQ PGLQSQPGMQ PQPGMHQQPS 2110 2120 2130 2140 2150 2160 LQNLNAMQAG VPRPGVPPQQ QAMGGLNPQG QALNIMNPGH NPNMASMNPQ YREMLRRQLL 2170 2180 2190 2200 2210 2220 QQQQQQQQQQ QQQQQQQQGS AGMAGGMAGH GQFQQPQGPG GYPPAMQQQQ RMQQHLPLQG 2230 2240 2250 2260 2270 2280 SSMGQMAAQM GQLGQMGQPG LGADSTPNIQ QALQQRILQQ QQMKQQIGSP GQPNPMSPQQ 2290 2300 2310 2320 2330 2340 HMLSGQPQAS HLPGQQIATS LSNQVRSPAP VQSPRPQSQP PHSSPSPRIQ PQPSPHHVSP 2350 2360 2370 2380 2390 2400 QTGSPHPGLA VTMASSIDQG HLGNPEQSAM LPQLNTPSRS ALSSELSLVG DTTGDTLEKF VEGL

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] [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. , 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]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[37]	"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.
[38]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[39]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[40]	"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, MASS SPECTROMETRY.
[41]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"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].
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

P300/CBP entry

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.

IPI

IPI00023339.
IPI01009314.

PIR

S39162.

RefSeq

NP_001073315.1. NM_001079846.1.
NP_004371.2. NM_004380.2.

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	[»]
1RDT	X-ray	2.40	E	58-80	[»]
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	[»]
2KWF	NMR	-	A	587-673	[»]
2L84	NMR	-	A	1081-1197	[»]
2L85	NMR	-	A	1081-1197	[»]
2RNY	NMR	-	A	1081-1197	[»]
3DWY	X-ray	1.98	A/B	1081-1197	[»]
3P1C	X-ray	1.82	A/B	1081-1197	[»]
3P1D	X-ray	1.86	A/B	1081-1197	[»]
3P1E	X-ray	1.80	A/B	1081-1197	[»]
3P1F	X-ray	1.63	A/B	1081-1197	[»]
3SVH	X-ray	1.80	A/B	1081-1197	[»]
4A9K	X-ray	1.81	A/B	1081-1197	[»]

ProteinModelPortal

Q92793.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-952N.

IntAct

Q92793. 42 interactions.

MINT

MINT-104685.

STRING

9606.ENSP00000262367.

PTM databases

PhosphoSite

Q92793.

Polymorphism databases

DMDM

116241283.

Proteomic databases

PaxDb

Q92793.

PRIDE

Q92793.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262367; ENSP00000262367; ENSG00000005339.
ENST00000382070; ENSP00000371502; ENSG00000005339.

GeneID

1387.

KEGG

hsa:1387.

UCSC

uc002cvv.3. human.

Organism-specific databases

CTD

1387.

GeneCards

GC16M003775.

HGNC

HGNC:2348. CREBBP.

HPA

CAB004212.

MIM

180849. phenotype.
600140. gene.

neXtProt

NX_Q92793.

Orphanet

783. Rubinstein-Taybi syndrome.

PharmGKB

PA26866.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000111353.

HOVERGEN

HBG000185.

KO

K04498.

OrthoDB

EOG4B2SW9.

PhylomeDB

Q92793.

Enzyme and pathway databases

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_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.
REACT_2155. NICD traffics to nucleus.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92793.

Bgee

Q92793.

CleanEx

HS_CREBBP.

Genevestigator

Q92793.

GermOnline

ENSG00000005339. Homo sapiens.

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

BindingDB

Q92793.

ChEMBL

CHEMBL5747.

ChiTaRS

CREBBP. human.

EvolutionaryTrace

Q92793.

GenomeRNAi

1387.

NextBio

5635.

SOURCE

Search...

Entry information

Entry name

CBP_HUMAN

Accession

Primary (citable) accession number: Q92793
Secondary accession number(s): D3DUC9 , O00147, Q16376, Q4LE28

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 166 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.