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P45481

- CBP_MOUSE

UniProt

P45481 - CBP_MOUSE

Protein

CREB-binding protein

Gene

Crebbp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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.By similarity

    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 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1702 – 174544ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1766 – 184782TAZ-type 2PROSITE-ProRule annotationAdd
    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

    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.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

    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 – 11RemovedBy similarity
    Chaini2 – 24412440CREB-binding proteinPRO_0000211191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei120 – 1201PhosphoserineBy similarity
    Modified residuei600 – 6001Omega-N-methylated arginine1 Publication
    Modified residuei624 – 6241Omega-N-methylated arginine1 Publication
    Modified residuei656 – 6561N6-acetyllysine1 Publication
    Cross-linki999 – 999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
    Modified residuei1015 – 10151N6-acetyllysineBy similarity
    Modified residuei1031 – 10311PhosphoserineBy similarity
    Cross-linki1034 – 1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
    Cross-linki1057 – 1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
    Modified residuei1217 – 12171N6-acetyllysine1 Publication
    Modified residuei1383 – 13831Phosphoserine; by IKKABy similarity
    Modified residuei1387 – 13871Phosphoserine; by IKKABy similarity
    Modified residuei1584 – 15841N6-acetyllysineBy similarity
    Modified residuei1587 – 15871N6-acetyllysineBy similarity
    Modified residuei1592 – 15921N6-acetyllysineBy similarity
    Modified residuei1593 – 15931N6-acetyllysineBy similarity
    Modified residuei1596 – 15961N6-acetyllysine1 Publication
    Modified residuei1598 – 15981N6-acetyllysine1 Publication
    Modified residuei1742 – 17421N6-acetyllysineBy similarity
    Modified residuei1745 – 17451N6-acetyllysine1 Publication
    Modified residuei2064 – 20641PhosphoserineBy similarity
    Modified residuei2077 – 20771PhosphoserineBy similarity
    Modified residuei2080 – 20801PhosphoserineBy 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.By similarity14 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45481.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini586 – 66580KIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini1104 – 117673BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni226 – 409184Interaction with SRCAPBy 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.PROSITE-ProRule annotation
    Contains 1 KIX domain.PROSITE-ProRule annotation
    Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri346 – 43287TAZ-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1702 – 174544ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1766 – 184782TAZ-type 2PROSITE-ProRule annotationAdd
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti400 – 4001G → P in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti530 – 5301I → V in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti670 – 6701S → T in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti826 – 8261V → E in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti978 – 9781S → T in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1159 – 11591W → R in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1239 – 12391E → G in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1417 – 14171N → D in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1429 – 14291R → C in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1466 – 14661G → V in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1470 – 14701G → A in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1850 – 18512KL → NV in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1859 – 18591R → C in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti1987 – 19871A → D in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti2060 – 20601P → N in AAB28651. (PubMed:8413673)Curated
    Sequence conflicti2381 – 23811S → T in AAB28651. (PubMed:8413673)Curated

    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

    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: October 1, 2014
    This is version 161 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