CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018821
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CREB-binding protein 
Protein Synonyms/Alias
  
Gene Name
 CREBBP 
Gene Synonyms/Alias
 CBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13LDGPPNPKRAKLSSPacetylation[1, 2]
635NLVAYAKKVEGDMYEbutyrylation[3]
635NLVAYAKKVEGDMYEpropionylation[3]
663EKIYKIQKELEEKRRbutyrylation[3]
663EKIYKIQKELEEKRRpropionylation[3]
998DVPVLEMKTETQAEDsumoylation[4]
1014EPDPGESKGEPRSEMacetylation[1, 2, 5, 6]
1033LQGASQVKEETDIAEsumoylation[4]
1042ETDIAEQKSEPMEVDacetylation[1]
1056DEKKPEVKVEVKEEEsumoylation[4]
1203LGYCCGRKYEFSPQTacetylation[5]
1216QTLCCYGKQLCTIPRacetylation[1, 2, 5, 6]
1320KKTGRPRKENKFSAKpropionylation[3]
1323GRPRKENKFSAKRLQpropionylation[3]
1327KENKFSAKRLQTTRLpropionylation[3]
1376VEVKPGMKSRFVDSGacetylation[7]
1509WYKKMLDKAFAERIIbutyrylation[3]
1509WYKKMLDKAFAERIIpropionylation[3]
1583EGSQGDSKNAKKKNNacetylation[1, 5, 6]
1586QGDSKNAKKKNNKKTacetylation[1, 5, 6]
1587GDSKNAKKKNNKKTNacetylation[5]
1588DSKNAKKKNNKKTNKacetylation[8]
1591NAKKKNNKKTNKNKSacetylation[5, 6, 8]
1591NAKKKNNKKTNKNKSbutyrylation[3]
1591NAKKKNNKKTNKNKSpropionylation[3]
1592AKKKNNKKTNKNKSSacetylation[5, 6, 8]
1595KNNKKTNKNKSSISRacetylation[1, 5, 6, 8]
1595KNNKKTNKNKSSISRbutyrylation[3, 9]
1597NKKTNKNKSSISRANacetylation[1, 5, 6, 8]
1597NKKTNKNKSSISRANbutyrylation[3]
1597NKKTNKNKSSISRANpropionylation[3]
1605SSISRANKKKPSMPNpropionylation[3]
1606SISRANKKKPSMPNVpropionylation[3]
1620VSNDLSQKLYATMEKacetylation[1, 6]
1736CINCYNTKSHAHKMVacetylation[2]
1741NTKSHAHKMVKWGLGacetylation[1, 2, 5, 6]
1744SHAHKMVKWGLGLDDacetylation[1, 2, 5, 6]
1762SQGEPQSKSPQESRRacetylation[1, 2]
1762SQGEPQSKSPQESRRubiquitination[10]
1806KRVVQHTKGCKRKTNbutyrylation[3]
1806KRVVQHTKGCKRKTNpropionylation[3]
1809VQHTKGCKRKTNGGCbutyrylation[3]
1809VQHTKGCKRKTNGGCpropionylation[3]
1937PTTVSTGKPTSQVPAacetylation[1]
2075QDLLRTLKSPSSPQQubiquitination[11]
2091QQVLNILKSNPQLMAacetylation[1]
2102QLMAAFIKQRTAKYVubiquitination[12, 13]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Lysine propionylation and butyrylation are novel post-translational modifications in histones.
 Chen Y, Sprung R, Tang Y, Ball H, Sangras B, Kim SC, Falck JR, Peng J, Gu W, Zhao Y.
 Mol Cell Proteomics. 2007 May;6(5):812-9. [PMID: 17267393]
 [4] SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx.
 Kuo HY, Chang CC, Jeng JC, Hu HM, Lin DY, Maul GG, Kwok RP, Shih HM.
 Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):16973-8. [PMID: 16287980]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [8] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [9] Molecular characterization of propionyllysines in non-histone proteins.
 Cheng Z, Tang Y, Chen Y, Kim S, Liu H, Li SS, Gu W, Zhao Y.
 Mol Cell Proteomics. 2009 Jan;8(1):45-52. [PMID: 18753126]
 [10] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [11] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [12] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [13] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 587 666 KIX.
 DOMAIN 1103 1175 Bromo.
 ZN_FING 347 433 TAZ-type 1.
 ZN_FING 1701 1744 ZZ-type.
 ZN_FING 1765 1846 TAZ-type 2.
 REGION 227 410 Interaction with SRCAP.
 REGION 1460 1891 Interaction with TRERF1.
 METAL 363 363 Zinc 1 (By similarity).
 METAL 367 367 Zinc 1 (By similarity).
 METAL 380 380 Zinc 1 (By similarity).
 METAL 385 385 Zinc 1 (By similarity).
 METAL 394 394 Zinc 2 (By similarity).
 METAL 398 398 Zinc 2 (By similarity).
 METAL 404 404 Zinc 2 (By similarity).
 METAL 409 409 Zinc 2 (By similarity).
 METAL 418 418 Zinc 3 (By similarity).
 METAL 422 422 Zinc 3 (By similarity).
 METAL 427 427 Zinc 3 (By similarity).
 METAL 430 430 Zinc 3 (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 121 121 Phosphoserine.
 MOD_RES 601 601 Omega-N-methylated arginine (By
 MOD_RES 625 625 Omega-N-methylated arginine (By
 MOD_RES 1014 1014 N6-acetyllysine.
 MOD_RES 1030 1030 Phosphoserine.
 MOD_RES 1216 1216 N6-acetyllysine.
 MOD_RES 1382 1382 Phosphoserine; by IKKA.
 MOD_RES 1386 1386 Phosphoserine; by IKKA.
 MOD_RES 1583 1583 N6-acetyllysine.
 MOD_RES 1586 1586 N6-acetyllysine.
 MOD_RES 1591 1591 N6-acetyllysine.
 MOD_RES 1592 1592 N6-acetyllysine.
 MOD_RES 1595 1595 N6-acetyllysine.
 MOD_RES 1597 1597 N6-acetyllysine.
 MOD_RES 1741 1741 N6-acetyllysine.
 MOD_RES 1744 1744 N6-acetyllysine.
 MOD_RES 2063 2063 Phosphoserine.
 MOD_RES 2076 2076 Phosphoserine.
 MOD_RES 2079 2079 Phosphoserine.
 CROSSLNK 998 998 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1033 1033 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1056 1056 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Bromodomain; Chromosomal rearrangement; Complete proteome; Cytoplasm; Disease mutation; Host-virus interaction; Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2442 AA 
Protein Sequence
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE LGLLNSGNLV 60
PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG GQAQGQPNSA NMASLSAMGK 120
SPLSQGDSSA PSLPKQAAST SGPTPAASQA LNPQAQKQVG LATSSPATSQ TGPGICMNAN 180
FNQTHPGLLN SNSGHSLINQ ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA 240
ETLTQVSPQM TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK 300
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK RKLIQQQLVL 360
LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA GKACQVAHCA SSRQIISHWK 420
NCTRHDCPVC LPLKNASDKR NQQTILGSPA SGIQNTIGSV GTGQQNATSL SNPNPIDPSS 480
MQRAYAALGL PYMNQPQTQL QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ 540
QPPNLISESA LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL 600
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY YHLLAEKIYK 660
IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP VRPPNGPLSL PVNRMQVSQG 720
MNSFNPMSLG NVQLPQAPMG PRAASPMNHS VQMNSMGSVP GMAISPSRMP QPPNMMGAHT 780
NNMMAQAPAQ SQFLPQNQFP SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA 840
SQLPCPPVTQ SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT 900
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT PVHAQPPGTP 960
LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE TQAEDTEPDP GESKGEPRSE 1020
MMEEDLQGAS QVKEETDIAE QKSEPMEVDE KKPEVKVEVK EEEESSSNGT ASQSTSPSQP 1080
RKKIFKPEEL RQALMPTLEA LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR 1140
KLDTGQYQEP WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC 1200
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT LGDDPSQPQT 1260
TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI IWPSGFVCDN CLKKTGRPRK 1320
ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN HPEAGEVFVR VVASSDKTVE VKPGMKSRFV 1380
DSGEMSESFP YRTKALFAFE EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF 1440
RPRCLRTAVY HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ 1500
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE ESIKELEQEE 1560
EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI SRANKKKPSM PNVSNDLSQK 1620
LYATMEKHKE VFFVIHLHAG PVINTLPPIV DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS 1680
LRRSKWSTLC MLVELHTQGQ DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH 1740
KMVKWGLGLD DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR 1800
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL RQQQIQHRLQ 1860
QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP QTPQPPAQPQ PSPVSMSPAG 1920
FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ PPPAAVEAAR QIEREAQQQQ HLYRVNINNS 1980
MPPGRTGMGT PGSQMAPVSL NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI 2040
SMQAQAAVAG PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF 2100
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP RPGVPPQQQA 2160
MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ QQQQQQQQQQ QQQQQQGSAG 2220
MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG 2280
ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS 2340
NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL 2400
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL 2442 
Gene Ontology
 GO:0000940; C:condensed chromosome outer kinetochore; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0000123; C:histone acetyltransferase complex; IEA:Compara.
 GO:0016604; C:nuclear body; IDA:UniProtKB.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
 GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
 GO:0043426; F:MRF binding; IDA:UniProtKB.
 GO:0001102; F:RNA polymerase II activating transcription factor binding; TAS:BHF-UCL.
 GO:0001078; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:BHF-UCL.
 GO:0001105; F:RNA polymerase II transcription coactivator activity; TAS:BHF-UCL.
 GO:0001191; F:RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription; IDA:BHF-UCL.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
 GO:0030718; P:germ-line stem cell maintenance; IEA:Compara.
 GO:0042592; P:homeostatic process; NAS:UniProtKB.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0006461; P:protein complex assembly; TAS:ProtInc.
 GO:0008589; P:regulation of smoothened signaling pathway; TAS:BHF-UCL.
 GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
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. 
Pfam
 PF00439; Bromodomain
 PF09030; Creb_binding
 PF06001; DUF902
 PF08214; KAT11
 PF02172; KIX
 PF02135; zf-TAZ
 PF00569; ZZ 
SMART
 SM00297; BROMO
 SM00551; ZnF_TAZ
 SM00291; ZnF_ZZ 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50952; KIX
 PS50134; ZF_TAZ
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS
 PR00503; BROMODOMAIN.