| General information | | DisProt: | DP00348 | | Name: | CREB-binding protein | | Synonym(s): | CBP_MOUSE
EC 2.3.1.48
CBP
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P45481 | | UniGene: | Mm.132238 | | SwissProt: | CBP_MOUSE | | TrEMBL: | | | NCBI (GI): | 1345703 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 2441 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP - 60
DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS - 120
PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF - 180
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE - 240
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ - 300
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL - 360
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAP KACQVAHCAS SRQIISHWKN - 420
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM - 480
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSV PAGGITTDQQ - 540
PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR - 600
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI - 660
QKELEEKRRT RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM - 720
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN - 780
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQEPGAA LPNPLNMLAP - 840
QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP - 900
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT - 960
PLSQAAASID NRVPTPSTVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS - 1020
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ - 1080
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK - 1140
RKLDTGQYQE PWQYVDDVRL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC - 1200
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCGK CFTEIQGENV TLGDDPSQPQ - 1260
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR - 1320
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF - 1380
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQDTAL IAPHQIQGCV YISYLDSIHF - 1440
FRPRCLRTAV YHEILIGYLE YVKKLVYVTA HIWACPPSEG DDYIFHCHPP DQKIPKPKRL - 1500
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE - 1560
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ - 1620
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS - 1680
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT - 1740
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK - 1800
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHN VRQQQIQHCL - 1860
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA - 1920
GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN - 1980
GMPPGRDGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV - 2040
MSMQAQAAVA GPRMPNVQPN RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA - 2100
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP - 2160
AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS - 2220
LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA - 2280
DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN - 2340
QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG TPHPGLAVTM ASSMDQGHLG - 2400
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
|
| Functional narrative |
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.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | ACTR binding domain | | Location: | 2059 - 2117 | | Length: | 59 | | Region sequence: |
PNRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQ | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (304 K; d11-Tris (pH 6.6) 10 mM; NaCl 50 mM)
| References:
- Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. "Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators." Nature. 2002; 415(6871): 549-53. PubMed: 11823864
| Comments:
|
| Region 2 | | Type: | Disordered | | Name: | | | Location: | 2083 - 2086 | | Length: | 4 | | Region sequence: |
QQQQ | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via an order to disorder transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; )
- Circular dichroism (CD) spectroscopy, far-UV (293 K; KCl 50 mM; Potassium phosphate (pH 7.0) 10 mM)
| References:
- Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E. "A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies." Mol Cell. 2001; 8(3): 581-90. PubMed: 11583620
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 2113 - 2152 | | Length: | 40 | | Region sequence: |
QPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPR | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (304 K; d11-Tris (pH 6.6) 10 mM; NaCl 50 mM)
| References:
- Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. "Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators." Nature. 2002; 415(6871): 549-53. PubMed: 11823864
| Comments:
|
| Comments |
Additional UniGene ID: Mm.392384
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
