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P45481

- CBP_MOUSE

UniProt

P45481 - CBP_MOUSE

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Protein

CREB-binding protein

Gene

Crebbp

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

Catalytic activityi

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

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
Binding sitei1494 – 14941Acetyl-CoA; via carbonyl oxygenBy similarity
Binding sitei1499 – 14991Acetyl-CoABy similarity
Binding sitei1503 – 15031Acetyl-CoABy similarity

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. transcription coactivator activity Source: UniProtKB
  7. transcription factor binding Source: UniProtKB
  8. 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_226917. HATs acetylate histones.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_268602. Pre-NOTCH Transcription and Translation.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48By similarity)
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-KW
  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. 1 Publication
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. 1 Publication
Mutagenesisi1015 – 10151K → R: No change in sumoylation. 1 Publication
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. 1 Publication
Mutagenesisi1043 – 10431K → R: No change in sumoylation. 1 Publication
Mutagenesisi1053 – 10531K → R: No change in sumoylation. 1 Publication
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. 1 Publication
Mutagenesisi1061 – 10611K → R: No change in sumoylation. 1 Publication
Mutagenesisi1087 – 10871K → R: No change in sumoylation.
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
Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53.By similarity

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. Interacts with ASF1A and ASF1B; this promotes histone acetylation. Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4 (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. 23 interactions.
MINTiMINT-203452.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Domaini1324 – 1701378CBP/p300-type HATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 409184Interaction with SRCAPBy similarityAdd
BLAST
Regioni1125 – 117147Interaction with histoneBy similarityAdd
BLAST
Regioni1163 – 118119Interaction with ASF1ABy similarityAdd
BLAST
Regioni1434 – 14363Interaction with histoneBy similarity
Regioni1435 – 14373Acetyl-CoA bindingBy similarity
Regioni1447 – 14482Acetyl-CoA bindingBy similarity

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 CBP/p300-type HAT (histone acetyltransferase) 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.
InParanoidiP45481.

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.
PS51727. CBP_P300_HAT. 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

        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL
60 70 80 90 100
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG
110 120 130 140 150
QAQGQPNSTN MASLGAMGKS PLNQGDSSTP NLPKQAASTS GPTPPASQAL
160 170 180 190 200
NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA
210 220 230 240 250
QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA
260 270 280 290 300
GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ
310 320 330 340 350
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR
360 370 380 390 400
KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG
410 420 430 440 450
KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS
460 470 480 490 500
GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ
510 520 530 540 550
PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL
560 570 580 590 600
PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
610 620 630 640 650
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY
660 670 680 690 700
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV
710 720 730 740 750
RPPNGPLPLP VNRMQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV
760 770 780 790 800
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS
810 820 830 840 850
SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP QASQLPCPPV
860 870 880 890 900
TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP
910 920 930 940 950
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP
960 970 980 990 1000
TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT
1010 1020 1030 1040 1050
EVQTDDAEPE PTESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE
1060 1070 1080 1090 1100
EKKPEVKVEA KEEEENSSND TASQSTSPSQ PRKKIFKPEE LRQALMPTLE
1110 1120 1130 1140 1150
ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE
1160 1170 1180 1190 1200
PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
1210 1220 1230 1240 1250
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV
1260 1270 1280 1290 1300
TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD
1310 1320 1330 1340 1350
IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ
1360 1370 1380 1390 1400
NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF
1410 1420 1430 1440 1450
EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF FRPRCLRTAV
1460 1470 1480 1490 1500
YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
1510 1520 1530 1540 1550
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL
1560 1570 1580 1590 1600
EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS
1610 1620 1630 1640 1650
ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI
1660 1670 1680 1690 1700
VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG
1710 1720 1730 1740 1750
QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL
1760 1770 1780 1790 1800
DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
1810 1820 1830 1840 1850
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK
1860 1870 1880 1890 1900
LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST
1910 1920 1930 1940 1950
PQTPQPPAQP QPSPVNMSPA GFPNVARTQP PTIVSAGKPT NQVPAPPPPA
1960 1970 1980 1990 2000
QPPPAAVEAA RQIEREAQQQ QHLYRANINN GMPPGRAGMG TPGSQMTPVG
2010 2020 2030 2040 2050
LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA
2060 2070 2080 2090 2100
GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
2110 2120 2130 2140 2150
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV
2160 2170 2180 2190 2200
PRPGVPPPQP AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ
2210 2220 2230 2240 2250
HQQQQQQQQQ QQQQQQNSAS LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ
2260 2270 2280 2290 2300
QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA DSTPNIQQAL QQRILQQQQM
2310 2320 2330 2340 2350
KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN QVRSPAPVQS
2360 2370 2380 2390 2400
PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG
2410 2420 2430 2440
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 23 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.
InParanoidi P45481.

Enzyme and pathway databases

Reactomei REACT_226917. HATs acetylate histones.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_268602. Pre-NOTCH Transcription and Translation.
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.
PS51727. CBP_P300_HAT. 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: November 26, 2014
This is version 163 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