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P45481

- CBP_MOUSE

UniProt

P45481 - CBP_MOUSE

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Protein

CREB-binding protein

Gene
Crebbp, Cbp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers By similarity.4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi362 – 3621Zinc 1
Metal bindingi366 – 3661Zinc 1
Metal bindingi379 – 3791Zinc 1
Metal bindingi384 – 3841Zinc 1
Metal bindingi393 – 3931Zinc 2
Metal bindingi397 – 3971Zinc 2
Metal bindingi403 – 4031Zinc 2
Metal bindingi408 – 4081Zinc 2
Metal bindingi417 – 4171Zinc 3
Metal bindingi421 – 4211Zinc 3
Metal bindingi426 – 4261Zinc 3
Metal bindingi429 – 4291Zinc 3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri346 – 43287TAZ-type 1Add
BLAST
Zinc fingeri1702 – 174544ZZ-typeAdd
BLAST
Zinc fingeri1766 – 184782TAZ-type 2Add
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. chromatin binding Source: MGI
  3. DNA binding Source: MGI
  4. histone acetyltransferase activity Source: UniProtKB
  5. MRF binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. transcription coactivator activity Source: UniProtKB
  8. transcription factor binding Source: UniProtKB
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. germ-line stem cell maintenance Source: MGI
  2. histone acetylation Source: UniProtKB
  3. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  4. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  7. regulation of transcription, DNA-templated Source: MGI
  8. rhythmic process Source: UniProtKB-KW
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196520. Pre-NOTCH Transcription and Translation.
REACT_226917. HATs acetylate histones.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48)
Gene namesi
Name:Crebbp
Synonyms:Cbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1098280. Crebbp.

Subcellular locationi

Cytoplasm By similarity. Nucleus
Note: Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus By similarity.

GO - Cellular componenti

  1. condensed chromosome outer kinetochore Source: MGI
  2. cytoplasm Source: UniProtKB-SubCell
  3. histone acetyltransferase complex Source: MGI
  4. nuclear chromatin Source: BHF-UCL
  5. nucleoplasm Source: Reactome
  6. nucleus Source: MGI
  7. PML body Source: MGI
  8. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi600 – 6001R → N: Abolishes binding to CREB. 2 Publications
Mutagenesisi999 – 9991K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-1034 and R-1057. 2 Publications
Mutagenesisi1015 – 10151K → R: No change in sumoylation. 2 Publications
Mutagenesisi1034 – 10341K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1057. 2 Publications
Mutagenesisi1043 – 10431K → R: No change in sumoylation. 2 Publications
Mutagenesisi1053 – 10531K → R: No change in sumoylation. 2 Publications
Mutagenesisi1057 – 10571K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1034. 2 Publications
Mutagenesisi1061 – 10611K → R: No change in sumoylation. 2 Publications
Mutagenesisi1087 – 10871K → R: No change in sumoylation. 1 Publication
Mutagenesisi1690 – 16912LC → KL: Abolishes histone acetyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 24412440CREB-binding proteinPRO_0000211191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei120 – 1201Phosphoserine By similarity
Modified residuei600 – 6001Omega-N-methylated arginine Inferred
Modified residuei624 – 6241Omega-N-methylated arginine Inferred
Modified residuei656 – 6561N6-acetyllysine1 Publication
Cross-linki999 – 999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)1 Publication
Modified residuei1015 – 10151N6-acetyllysine By similarity
Modified residuei1031 – 10311Phosphoserine By similarity
Cross-linki1034 – 1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)1 Publication
Cross-linki1057 – 1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)1 Publication
Modified residuei1217 – 12171N6-acetyllysine1 Publication
Modified residuei1383 – 13831Phosphoserine; by IKKA By similarity
Modified residuei1387 – 13871Phosphoserine; by IKKA By similarity
Modified residuei1584 – 15841N6-acetyllysine By similarity
Modified residuei1587 – 15871N6-acetyllysine By similarity
Modified residuei1592 – 15921N6-acetyllysine By similarity
Modified residuei1593 – 15931N6-acetyllysine By similarity
Modified residuei1596 – 15961N6-acetyllysine1 Publication
Modified residuei1598 – 15981N6-acetyllysine1 Publication
Modified residuei1742 – 17421N6-acetyllysine By similarity
Modified residuei1745 – 17451N6-acetyllysine1 Publication
Modified residuei2064 – 20641Phosphoserine By similarity
Modified residuei2077 – 20771Phosphoserine By similarity
Modified residuei2080 – 20801Phosphoserine By similarity

Post-translational modificationi

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.1 Publication
Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B By similarity.
Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP45481.
PaxDbiP45481.
PRIDEiP45481.

PTM databases

PhosphoSiteiP45481.

Expressioni

Gene expression databases

CleanExiMM_CREBBP.
GenevestigatoriP45481.

Interactioni

Subunit structurei

Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with MECOM and MTDH By similarity. Interacts with CITED1 (via C-terminus). Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region). Interacts with phosphorylated CREB1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK and ARNTL/BMAL1.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P889466EBI-296306,EBI-936023From a different organism.
COPS2P612012EBI-296306,EBI-1050386From a different organism.
Creb1Q011472EBI-296306,EBI-2291098
Ctnnb1Q022483EBI-296306,EBI-397872
DDX5P178443EBI-296306,EBI-351962From a different organism.
HIST2H4BP628052EBI-296306,EBI-302023From a different organism.
Khdrbs1Q607497EBI-296306,EBI-519077
KMT2AQ031647EBI-296306,EBI-591370From a different organism.
SREBF1P36956-12EBI-296306,EBI-948328From a different organism.
TP53P046376EBI-296306,EBI-366083From a different organism.

Protein-protein interaction databases

DIPiDIP-5974N.
IntActiP45481. 21 interactions.
MINTiMINT-203452.

Structurei

Secondary structure

1
2441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni343 – 3453
Helixi347 – 37226
Beta strandi374 – 3763
Helixi384 – 39613
Helixi400 – 4023
Helixi406 – 42015
Turni423 – 4253
Helixi429 – 4335
Helixi436 – 4383
Helixi590 – 5945
Helixi597 – 61115
Turni617 – 6193
Helixi622 – 64221
Helixi646 – 66419
Turni667 – 6715
Turni1709 – 17113
Beta strandi1713 – 172614
Helixi1731 – 17377
Beta strandi1741 – 17466
Helixi1765 – 178521
Helixi1794 – 180815
Helixi1812 – 18154
Helixi1818 – 183316
Helixi1844 – 18496
Beta strandi2061 – 20644
Helixi2068 – 20758
Beta strandi2076 – 20794
Helixi2088 – 20914
Helixi2097 – 21004
Helixi2102 – 21043
Beta strandi2106 – 21083

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F81NMR-A1764-1850[»]
1JJSNMR-A2067-2112[»]
1KBHNMR-B2059-2117[»]
1KDXNMR-A586-666[»]
1L8CNMR-A345-439[»]
1R8UNMR-B340-439[»]
1SB0NMR-A586-672[»]
1TOTNMR-A1700-1751[»]
1U2NNMR-A340-439[»]
2AGHNMR-B586-672[»]
2C52NMR-A2059-2117[»]
2KA4NMR-A340-439[»]
2KA6NMR-A1764-1855[»]
2KKJNMR-A2059-2117[»]
2L14NMR-A2059-2117[»]
2LQHNMR-A586-672[»]
2LQINMR-A586-672[»]
2LWWNMR-A340-439[»]
4I9OX-ray2.00A586-672[»]
DisProtiDP00348.
ProteinModelPortaliP45481.
SMRiP45481. Positions 340-439, 586-672, 1082-1751, 1764-1855, 2066-2112.

Miscellaneous databases

EvolutionaryTraceiP45481.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini586 – 66580KIXAdd
BLAST
Domaini1104 – 117673BromoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 409184Interaction with SRCAP By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1062 – 10654Poly-Glu
Compositional biasi1556 – 15638Poly-Glu
Compositional biasi1944 – 19496Poly-Pro
Compositional biasi1968 – 19714Poly-Gln
Compositional biasi2082 – 20865Poly-Gln
Compositional biasi2200 – 221617Poly-GlnAdd
BLAST
Compositional biasi2296 – 22994Poly-Gln

Sequence similaritiesi

Contains 1 bromo domain.
Contains 1 KIX domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri346 – 43287TAZ-type 1Add
BLAST
Zinc fingeri1702 – 174544ZZ-typeAdd
BLAST
Zinc fingeri1766 – 184782TAZ-type 2Add
BLAST

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.

Family and domain databases

Gene3Di1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProiIPR001487. 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]
PfamiPF00439. 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]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P45481-1 [UniParc]FASTAAdd to Basket

« Hide

MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL     50
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG 100
QAQGQPNSTN MASLGAMGKS PLNQGDSSTP NLPKQAASTS GPTPPASQAL 150
NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA 200
QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA 250
GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ 300
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR 350
KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG 400
KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS 450
GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ 500
PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL 550
PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 600
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY 650
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV 700
RPPNGPLPLP VNRMQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV 750
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS 800
SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP QASQLPCPPV 850
TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP 900
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP 950
TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT 1000
EVQTDDAEPE PTESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE 1050
EKKPEVKVEA KEEEENSSND TASQSTSPSQ PRKKIFKPEE LRQALMPTLE 1100
ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE 1150
PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC 1200
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV 1250
TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD 1300
IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ 1350
NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF 1400
EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF FRPRCLRTAV 1450
YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL 1500
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL 1550
EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS 1600
ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI 1650
VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG 1700
QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL 1750
DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK 1800
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK 1850
LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST 1900
PQTPQPPAQP QPSPVNMSPA GFPNVARTQP PTIVSAGKPT NQVPAPPPPA 1950
QPPPAAVEAA RQIEREAQQQ QHLYRANINN GMPPGRAGMG TPGSQMTPVG 2000
LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA 2050
GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 2100
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV 2150
PRPGVPPPQP AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ 2200
HQQQQQQQQQ QQQQQQNSAS LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ 2250
QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA DSTPNIQQAL QQRILQQQQM 2300
KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN QVRSPAPVQS 2350
PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG 2400
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L 2441
Length:2,441
Mass (Da):265,494
Last modified:July 27, 2011 - v3
Checksum:iD89AF52B7BD33347
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti400 – 4001G → P in AAB28651. 1 Publication
Sequence conflicti530 – 5301I → V in AAB28651. 1 Publication
Sequence conflicti670 – 6701S → T in AAB28651. 1 Publication
Sequence conflicti826 – 8261V → E in AAB28651. 1 Publication
Sequence conflicti978 – 9781S → T in AAB28651. 1 Publication
Sequence conflicti1159 – 11591W → R in AAB28651. 1 Publication
Sequence conflicti1239 – 12391E → G in AAB28651. 1 Publication
Sequence conflicti1417 – 14171N → D in AAB28651. 1 Publication
Sequence conflicti1429 – 14291R → C in AAB28651. 1 Publication
Sequence conflicti1466 – 14661G → V in AAB28651. 1 Publication
Sequence conflicti1470 – 14701G → A in AAB28651. 1 Publication
Sequence conflicti1850 – 18512KL → NV in AAB28651. 1 Publication
Sequence conflicti1859 – 18591R → C in AAB28651. 1 Publication
Sequence conflicti1987 – 19871A → D in AAB28651. 1 Publication
Sequence conflicti2060 – 20601P → N in AAB28651. 1 Publication
Sequence conflicti2381 – 23811S → T in AAB28651. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S66385 mRNA. Translation: AAB28651.1.
AC132380 Genomic DNA. No translation available.
CCDSiCCDS27915.1.
PIRiS39161.
UniGeneiMm.132238.
Mm.392384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S66385 mRNA. Translation: AAB28651.1 .
AC132380 Genomic DNA. No translation available.
CCDSi CCDS27915.1.
PIRi S39161.
UniGenei Mm.132238.
Mm.392384.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F81 NMR - A 1764-1850 [» ]
1JJS NMR - A 2067-2112 [» ]
1KBH NMR - B 2059-2117 [» ]
1KDX NMR - A 586-666 [» ]
1L8C NMR - A 345-439 [» ]
1R8U NMR - B 340-439 [» ]
1SB0 NMR - A 586-672 [» ]
1TOT NMR - A 1700-1751 [» ]
1U2N NMR - A 340-439 [» ]
2AGH NMR - B 586-672 [» ]
2C52 NMR - A 2059-2117 [» ]
2KA4 NMR - A 340-439 [» ]
2KA6 NMR - A 1764-1855 [» ]
2KKJ NMR - A 2059-2117 [» ]
2L14 NMR - A 2059-2117 [» ]
2LQH NMR - A 586-672 [» ]
2LQI NMR - A 586-672 [» ]
2LWW NMR - A 340-439 [» ]
4I9O X-ray 2.00 A 586-672 [» ]
DisProti DP00348.
ProteinModelPortali P45481.
SMRi P45481. Positions 340-439, 586-672, 1082-1751, 1764-1855, 2066-2112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-5974N.
IntActi P45481. 21 interactions.
MINTi MINT-203452.

PTM databases

PhosphoSitei P45481.

Proteomic databases

MaxQBi P45481.
PaxDbi P45481.
PRIDEi P45481.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1098280. Crebbp.

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.

Enzyme and pathway databases

Reactomei REACT_196520. Pre-NOTCH Transcription and Translation.
REACT_226917. HATs acetylate histones.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi CREBBP. mouse.
EvolutionaryTracei P45481.
PROi P45481.
SOURCEi Search...

Gene expression databases

CleanExi MM_CREBBP.
Genevestigatori P45481.

Family and domain databases

Gene3Di 1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProi 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 ]
Pfami 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 ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphorylated CREB binds specifically to the nuclear protein CBP."
    Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R., Goodman R.H.
    Nature 365:855-859(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors."
    Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.
    Cell 85:403-414(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA1.
  4. "Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism."
    Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., Hoeger C., Montminy M.R.
    Mol. Cell. Biol. 16:694-703(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREB1, MUTAGENESIS OF ARG-600.
  5. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
    Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
    Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA3.
  6. "CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites."
    Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.
    Mol. Cell. Biol. 19:3496-3505(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GATA1, MUTAGENESIS OF 1690-LYS-CYS-1691.
  7. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
    Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
    J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED1.
  8. "A transcriptional switch mediated by cofactor methylation."
    Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
    Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, FUNCTION.
  9. "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells."
    Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T.
    Genomics 80:601-613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED4.
  10. "CREB-binding protein/p300 co-activation of crystallin gene expression."
    Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.
    J. Biol. Chem. 277:24081-24089(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAF.
  11. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
    Rossow K.L., Janknecht R.
    Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5.
  12. "Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity."
    Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T., Miyagishi M., Nakajima T., Fukamizu A.
    Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLATION OF FOXO1.
  13. "SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx."
    Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G., Kwok R.P.S., Shih H.-M.
    Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH DAXX, FUNCTION, MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043; LYS-1053; LYS-1057 AND LYS-1061.
  14. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
    Shin S., Janknecht R.
    J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX17.
  15. "Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling."
    Cho G., Lim Y., Zand D., Golden J.A.
    Mol. Cell. Biol. 28:1565-1572(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZCCHC12.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656; LYS-1217; LYS-1596; LYS-1598 AND LYS-1745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  17. Cited for: INTERACTION WITH ARNTL/BMAL1.
  18. "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites."
    De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
    J. Biol. Chem. 279:3042-3049(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 340-439 IN COMPLEX WITH 220-269 OF CITED2 AND ZINC IONS.

Entry informationi

Entry nameiCBP_MOUSE
AccessioniPrimary (citable) accession number: P45481
Secondary accession number(s): E9QPH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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