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Q6JHU9 (CBP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CREB-binding protein
EC=2.3.1.48
Gene names
Name:Crebbp
Synonyms:Cbp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length2442 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5, DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAAX. Interacts with MAF. Interacts with MTDH. 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) By similarity. Interacts with MECOM. Interacts with CITED1 (via C-terminus) Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity By similarity.

Subcellular location

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

Tissue specificity

Expressed in hypothalamus and cortex. Ref.1

Induction

Up-regulated by IL-1 treatment. Ref.1

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-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 By similarity.

Sequence similarities

Contains 1 bromo domain.

Contains 1 KIX domain.

Contains 2 TAZ-type zinc fingers.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Transferase
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from direct assay PubMed 12477714. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15598887. Source: RGD

regulation of S phase

Inferred from mutant phenotype PubMed 18496732. Source: RGD

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone acetyltransferase complex

Inferred from electronic annotation. Source: InterPro

transcription factor complex

Inferred from direct assay PubMed 15632413. Source: RGD

   Molecular_functionMRF binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome proliferator activated receptor binding

Inferred from direct assay PubMed 12095700. Source: RGD

transcription coactivator activity

Traceable author statement PubMed 12477714. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24422442CREB-binding protein
PRO_0000409385

Regions

Domain586 – 66580KIX
Domain1104 – 117673Bromo
Zinc finger346 – 43287TAZ-type 1
Zinc finger1702 – 174544ZZ-type
Zinc finger1766 – 184782TAZ-type 2
Region226 – 409184Interaction with SRCAP By similarity
Coiled coil1548 – 157528 Potential
Compositional bias682 – 961280Pro-rich
Compositional bias1556 – 15638Poly-Glu
Compositional bias1853 – 2370518Gln-rich
Compositional bias1879 – 2065187Pro-rich
Compositional bias1944 – 19496Poly-Pro
Compositional bias1968 – 19714Poly-Gln
Compositional bias2082 – 20865Poly-Gln
Compositional bias2200 – 221718Poly-Gln
Compositional bias2297 – 23004Poly-Gln

Sites

Metal binding3621Zinc 1 By similarity
Metal binding3661Zinc 1 By similarity
Metal binding3791Zinc 1 By similarity
Metal binding3841Zinc 1 By similarity
Metal binding3931Zinc 2 By similarity
Metal binding3971Zinc 2 By similarity
Metal binding4031Zinc 2 By similarity
Metal binding4081Zinc 2 By similarity
Metal binding4171Zinc 3 By similarity
Metal binding4211Zinc 3 By similarity
Metal binding4261Zinc 3 By similarity
Metal binding4291Zinc 3 By similarity

Amino acid modifications

Modified residue1201Phosphoserine By similarity
Modified residue6001Omega-N-methylated arginine By similarity
Modified residue6241Omega-N-methylated arginine By similarity
Modified residue10151N6-acetyllysine By similarity
Modified residue10311Phosphoserine By similarity
Modified residue12171N6-acetyllysine By similarity
Modified residue13831Phosphoserine; by IKKA By similarity
Modified residue13871Phosphoserine; by IKKA By similarity
Modified residue15841N6-acetyllysine By similarity
Modified residue15871N6-acetyllysine By similarity
Modified residue15921N6-acetyllysine By similarity
Modified residue15931N6-acetyllysine By similarity
Modified residue15961N6-acetyllysine By similarity
Modified residue15981N6-acetyllysine By similarity
Modified residue17421N6-acetyllysine By similarity
Modified residue17451N6-acetyllysine By similarity
Modified residue20641Phosphoserine By similarity
Modified residue20771Phosphoserine By similarity
Modified residue20801Phosphoserine By similarity
Cross-link999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6JHU9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2E77EF213C72C024

FASTA2,442265,424
        10         20         30         40         50         60 
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP 

        70         80         90        100        110        120 
DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG QAQGQPNSTS MASLGAMGKS 

       130        140        150        160        170        180 
PLNPGDSSTP SLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF 

       190        200        210        220        230        240 
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE 

       250        260        270        280        290        300 
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ 

       310        320        330        340        350        360 
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA TGPTADPEKR KLIQQQLVLL 

       370        380        390        400        410        420 
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN 

       430        440        450        460        470        480 
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM 

       490        500        510        520        530        540 
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ 

       550        560        570        580        590        600 
PPNLISESAL PTSLGATNPL MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 

       610        620        630        640        650        660 
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI 

       670        680        690        700        710        720 
QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV RPPNGPLSLP VNRVQVSQGM 

       730        740        750        760        770        780 
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN 

       790        800        810        820        830        840 
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP 

       850        860        870        880        890        900 
QTSQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP 

       910        920        930        940        950        960 
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT 

       970        980        990       1000       1010       1020 
PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPD PAESKGEPRS 

      1030       1040       1050       1060       1070       1080 
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSANG TASQSTSPSQ 

      1090       1100       1110       1120       1130       1140 
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK 

      1150       1160       1170       1180       1190       1200 
RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC 

      1210       1220       1230       1240       1250       1260 
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ 

      1270       1280       1290       1300       1310       1320 
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR 

      1330       1340       1350       1360       1370       1380 
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF 

      1390       1400       1410       1420       1430       1440 
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQEYGS DCPPPNTRRV YISYLDSIHF 

      1450       1460       1470       1480       1490       1500 
FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL 

      1510       1520       1530       1540       1550       1560 
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE 

      1570       1580       1590       1600       1610       1620 
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ 

      1630       1640       1650       1660       1670       1680 
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS 

      1690       1700       1710       1720       1730       1740 
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT 

      1750       1760       1770       1780       1790       1800 
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK 

      1810       1820       1830       1840       1850       1860 
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL 

      1870       1880       1890       1900       1910       1920 
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA 

      1930       1940       1950       1960       1970       1980 
GFPSVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREGQQQ QHLYRANINN 

      1990       2000       2010       2020       2030       2040 
GMPPGRAGMG TPGSQMAPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV 

      2050       2060       2070       2080       2090       2100 
MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 

      2110       2120       2130       2140       2150       2160 
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQQ 

      2170       2180       2190       2200       2210       2220 
AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQQSSA 

      2230       2240       2250       2260       2270       2280 
SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG 

      2290       2300       2310       2320       2330       2340 
ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS 

      2350       2360       2370       2380       2390       2400 
NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL 

      2410       2420       2430       2440 
GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL

« Hide

References

[1]"Interleukin-1beta induces CREB-binding protein (CBP) mRNA in brain and the sequencing of rat CBP."
Tang C., Sula M.J., Bohnet S., Rehman A., Taishi P., Krueger J.M.
Brain Res. Mol. Brain Res. 137:213-222(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY462245 mRNA. Translation: AAR23149.1.
IPIIPI01018433.
UniGeneRn.12815.

3D structure databases

HSSPHSSP built from PDB template 1KDX based on UniProtKB P45481.
ProteinModelPortalQ6JHU9.
SMRQ6JHU9. Positions 340-439, 586-672, 1085-1198, 1324-1751, 1764-1850, 2066-2112.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-7292086.

PTM databases

PhosphoSiteQ6JHU9.

Proteomic databases

PaxDbQ6JHU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2401. rat.

Organism-specific databases

RGD2401. Crebbp.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000111353.
HOVERGENHBG000185.
OrthoDBEOG4B2SW9.

Gene expression databases

GenevestigatorQ6JHU9.

Family and domain databases

Gene3D1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProIPR001487. 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]
PfamPF00439. 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]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47370. Bromodomain. 1 hit.
SSF47040. KIX. 1 hit.
SSF69125. Nuc_recept_coact. 1 hit.
SSF57933. TAZ_finger. 2 hits.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

NextBio13957143.

Entry information

Entry nameCBP_RAT
AccessionPrimary (citable) accession number: Q6JHU9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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