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Q6JHU9

- CBP_RAT

UniProt

Q6JHU9 - CBP_RAT

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Protein

CREB-binding protein

Gene
Crebbp, Cbp
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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.

Catalytic activityi

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

Sites

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

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. activating transcription factor binding Source: RGD
  3. histone acetyltransferase activity Source: UniProtKB
  4. MRF binding Source: UniProtKB
  5. peroxisome proliferator activated receptor binding Source: RGD
  6. protein binding Source: UniProtKB
  7. SMAD binding Source: RGD
  8. transcription coactivator activity Source: RGD
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell proliferation Source: RGD
  2. histone acetylation Source: UniProtKB
  3. positive regulation of G1/S transition of mitotic cell cycle Source: RGD
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  6. regulation of transcription, DNA-templated Source: RGD
  7. rhythmic process Source: UniProtKB-KW
  8. 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

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48)
Gene namesi
Name:Crebbp
Synonyms:Cbp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2401. Crebbp.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. histone acetyltransferase complex Source: InterPro
  3. nucleus Source: RGD
  4. protein complex Source: RGD
  5. transcription factor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 24422441CREB-binding proteinPRO_0000409385Add
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 By similarity
Modified residuei624 – 6241Omega-N-methylated arginine By similarity
Modified residuei656 – 6561N6-acetyllysine By similarity
Cross-linki999 – 999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
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) By similarity
Cross-linki1057 – 1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Modified residuei1217 – 12171N6-acetyllysine By similarity
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-acetyllysine By similarity
Modified residuei1598 – 15981N6-acetyllysine By similarity
Modified residuei1742 – 17421N6-acetyllysine By similarity
Modified residuei1745 – 17451N6-acetyllysine By similarity
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 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.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6JHU9.

PTM databases

PhosphoSiteiQ6JHU9.

Expressioni

Tissue specificityi

Expressed in hypothalamus and cortex.1 Publication

Inductioni

Up-regulated by IL-1 treatment.1 Publication

Gene expression databases

GenevestigatoriQ6JHU9.

Interactioni

Subunit structurei

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 DAXX. 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. Interacts with NPAS2, CLOCK and ARNTL/BMAL1 By similarity.

Protein-protein interaction databases

IntActiQ6JHU9. 1 interaction.
MINTiMINT-7292086.

Structurei

3D structure databases

ProteinModelPortaliQ6JHU9.
SMRiQ6JHU9. Positions 340-439, 586-672, 1085-1198, 1324-1751, 1764-1850, 2066-2112.

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1548 – 157528 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi682 – 961280Pro-richAdd
BLAST
Compositional biasi1556 – 15638Poly-Glu
Compositional biasi1853 – 2370518Gln-richAdd
BLAST
Compositional biasi1879 – 2065187Pro-richAdd
BLAST
Compositional biasi1944 – 19496Poly-Pro
Compositional biasi1968 – 19714Poly-Gln
Compositional biasi2082 – 20865Poly-Gln
Compositional biasi2200 – 221718Poly-GlnAdd
BLAST
Compositional biasi2297 – 23004Poly-Gln

Sequence similaritiesi

Contains 1 bromo domain.
Contains 1 KIX domain.

Keywords - Domaini

Bromodomain, Coiled coil, 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.

Q6JHU9-1 [UniParc]FASTAAdd to Basket

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MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL     50
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG 100
QAQGQPNSTS MASLGAMGKS PLNPGDSSTP SLPKQAASTS GPTPPASQAL 150
NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA 200
QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA 250
GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ 300
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA 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 MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 600
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY 650
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV 700
RPPNGPLSLP VNRVQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV 750
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS 800
SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP QTSQLPCPPV 850
TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP 900
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP 950
TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT 1000
EVQTDDAEPD PAESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE 1050
EKKPEVKVEA KEEEENSANG 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 FGMHVQEYGS DCPPPNTRRV 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 GFPSVARTQP PTIVSAGKPT NQVPAPPPPA 1950
QPPPAAVEAA RQIEREGQQQ QHLYRANINN GMPPGRAGMG TPGSQMAPVG 2000
LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA 2050
GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 2100
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV 2150
PRPGVPPPQQ AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ 2200
HQQQQQQQQQ QQQQQQQSSA SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM 2250
QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ 2300
MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ 2350
SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL 2400
GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL 2442
Length:2,442
Mass (Da):265,424
Last modified:July 5, 2004 - v1
Checksum:i2E77EF213C72C024
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY462245 mRNA. Translation: AAR23149.1.
UniGeneiRn.12815.

Genome annotation databases

UCSCiRGD:2401. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY462245 mRNA. Translation: AAR23149.1 .
UniGenei Rn.12815.

3D structure databases

ProteinModelPortali Q6JHU9.
SMRi Q6JHU9. Positions 340-439, 586-672, 1085-1198, 1324-1751, 1764-1850, 2066-2112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q6JHU9. 1 interaction.
MINTi MINT-7292086.

PTM databases

PhosphoSitei Q6JHU9.

Proteomic databases

PaxDbi Q6JHU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2401. rat.

Organism-specific databases

RGDi 2401. Crebbp.

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.

Miscellaneous databases

NextBioi 13957143.
PROi Q6JHU9.

Gene expression databases

Genevestigatori Q6JHU9.

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

  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.

Entry informationi

Entry nameiCBP_RAT
AccessioniPrimary (citable) accession number: Q6JHU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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