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Protein

CREB-binding protein

Gene

Crebbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER).By similarity4 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi362Zinc 11
Metal bindingi366Zinc 11
Metal bindingi379Zinc 11
Metal bindingi384Zinc 11
Metal bindingi393Zinc 21
Metal bindingi397Zinc 21
Metal bindingi403Zinc 21
Metal bindingi408Zinc 21
Metal bindingi417Zinc 31
Metal bindingi421Zinc 31
Metal bindingi426Zinc 31
Metal bindingi429Zinc 31
Binding sitei1494Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1499Acetyl-CoABy similarity1
Binding sitei1503Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

GO - Molecular functioni

GO - Biological processi

  • cellular response to hepatocyte growth factor stimulus Source: MGI
  • cellular response to UV Source: UniProtKB
  • germ-line stem cell population maintenance Source: MGI
  • histone acetylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • N-terminal peptidyl-lysine acetylation Source: UniProtKB
  • positive regulation of CREB transcription factor activity Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein acetylation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • rhythmic process 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

ReactomeiR-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-3214847. HATs acetylate histones.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

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
Proteomesi
  • UP000000589 Componenti: 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

  • condensed chromosome outer kinetochore Source: MGI
  • cytoplasm Source: MGI
  • histone acetyltransferase complex Source: MGI
  • nuclear body Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PML body Source: MGI
  • RNA polymerase II transcription factor complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi600R → N: Abolishes binding to CREB. 1 Publication1
Mutagenesisi999K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-1034 and R-1057. 1 Publication1
Mutagenesisi1015K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1034K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1057. 1 Publication1
Mutagenesisi1043K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1053K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1057K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1034. 1 Publication1
Mutagenesisi1061K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1087K → R: No change in sumoylation. 1
Mutagenesisi1690 – 1691LC → KL: Abolishes histone acetyltransferase activity. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002111912 – 2441CREB-binding proteinAdd BLAST2440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei120PhosphoserineCombined sources1
Modified residuei219Omega-N-methylarginineBy similarity1
Modified residuei600Omega-N-methylated arginine1 Publication1
Modified residuei624Omega-N-methylated arginine1 Publication1
Modified residuei656N6-acetyllysineCombined sources1
Cross-linki999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei1015N6-acetyllysineBy similarity1
Modified residuei1031PhosphoserineBy similarity1
Cross-linki1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei1077PhosphoserineBy similarity1
Modified residuei1217N6-acetyllysineCombined sources1
Modified residuei1383Phosphoserine; by IKKABy similarity1
Modified residuei1387Phosphoserine; by IKKABy similarity1
Modified residuei1584N6-acetyllysineBy similarity1
Modified residuei1592N6-acetyllysineBy similarity1
Modified residuei1593N6-acetyllysineBy similarity1
Modified residuei1596N6-acetyllysineCombined sources1
Modified residuei1598N6-acetyllysineCombined sources1
Modified residuei1742N6-acetyllysineBy similarity1
Modified residuei1745N6-acetyllysineCombined sources1
Modified residuei1764PhosphoserineBy similarity1
Modified residuei2064PhosphoserineCombined sources1
Modified residuei2077PhosphoserineBy similarity1
Modified residuei2080PhosphoserineBy similarity1
Modified residuei2350PhosphoserineCombined sources1

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

EPDiP45481.
MaxQBiP45481.
PaxDbiP45481.
PRIDEiP45481.

PTM databases

iPTMnetiP45481.
PhosphoSitePlusiP45481.

Expressioni

Gene expression databases

CleanExiMM_CREBBP.

Interactioni

Subunit structurei

Interacts (via transactivation domain and C-terminus) with PCNA; the interaction occurs on chromatin in UV-irradiated damaged cells (By similarity). 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.
BUB1BO605663EBI-296306,EBI-1001438From 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.
SNAI1O958637EBI-296306,EBI-1045459From a different organism.
SREBF1P36956-12EBI-296306,EBI-948328From a different organism.
TP53P046376EBI-296306,EBI-366083From a different organism.

GO - Molecular functioni

  • MRF binding Source: UniProtKB
  • p53 binding Source: MGI
  • RNA polymerase II transcription factor binding Source: MGI
  • TFIIB-class transcription factor binding Source: MGI
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-5974N.
IntActiP45481. 26 interactors.
MINTiMINT-203452.
STRINGi10090.ENSMUSP00000023165.

Structurei

Secondary structure

12441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni343 – 345Combined sources3
Helixi347 – 372Combined sources26
Beta strandi374 – 376Combined sources3
Helixi384 – 396Combined sources13
Helixi400 – 402Combined sources3
Helixi406 – 420Combined sources15
Turni423 – 425Combined sources3
Helixi429 – 433Combined sources5
Helixi436 – 438Combined sources3
Helixi590 – 594Combined sources5
Helixi597 – 611Combined sources15
Turni617 – 619Combined sources3
Helixi622 – 642Combined sources21
Helixi646 – 664Combined sources19
Turni667 – 671Combined sources5
Turni1709 – 1711Combined sources3
Beta strandi1713 – 1726Combined sources14
Helixi1731 – 1737Combined sources7
Beta strandi1741 – 1746Combined sources6
Helixi1765 – 1785Combined sources21
Helixi1794 – 1808Combined sources15
Helixi1812 – 1815Combined sources4
Helixi1818 – 1833Combined sources16
Beta strandi1840 – 1843Combined sources4
Helixi1844 – 1849Combined sources6
Beta strandi2061 – 2064Combined sources4
Helixi2068 – 2075Combined sources8
Beta strandi2076 – 2079Combined sources4
Helixi2088 – 2091Combined sources4
Helixi2097 – 2100Combined sources4
Helixi2102 – 2104Combined sources3
Beta strandi2106 – 2108Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5HOUNMR-A340-439[»]
5HP0NMR-A1764-1857[»]
5HPDNMR-A1764-1855[»]
DisProtiDP00348.
ProteinModelPortaliP45481.
SMRiP45481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45481.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini586 – 665KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1104 – 1176BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1324 – 1701CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST378

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 409Interaction with SRCAPBy similarityAdd BLAST184
Regioni1125 – 1171Interaction with histoneBy similarityAdd BLAST47
Regioni1163 – 1181Interaction with ASF1ABy similarityAdd BLAST19
Regioni1434 – 1436Interaction with histoneBy similarity3
Regioni1435 – 1437Acetyl-CoA bindingBy similarity3
Regioni1447 – 1448Acetyl-CoA bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1062 – 1065Poly-Glu4
Compositional biasi1556 – 1563Poly-Glu8
Compositional biasi1944 – 1949Poly-Pro6
Compositional biasi1968 – 1971Poly-Gln4
Compositional biasi2082 – 2086Poly-Gln5
Compositional biasi2200 – 2216Poly-GlnAdd BLAST17
Compositional biasi2296 – 2299Poly-Gln4

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)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiP45481.

Family and domain databases

CDDicd15802. RING_CBP-p300. 1 hit.
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.
IPR031162. CBP_P300_HAT.
IPR013178. Histone_AcTrfase_Rtt109/CBP.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR010303. RING_CBP-p300.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. HAT_KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 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)DescriptionActionsGraphical viewLength
Sequence conflicti400G → P in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti530I → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti670S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti826V → E in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti978S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1159W → R in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1239E → G in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1417N → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1429R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1466G → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1470G → A in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1850 – 1851KL → NV in AAB28651 (PubMed:8413673).Curated2
Sequence conflicti1859R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1987A → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2060P → N in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2381S → T in AAB28651 (PubMed:8413673).Curated1

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.
CCDSiCCDS27915.1.
PIRiS39161.
UniGeneiMm.132238.
Mm.392384.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5HOUNMR-A340-439[»]
5HP0NMR-A1764-1857[»]
5HPDNMR-A1764-1855[»]
DisProtiDP00348.
ProteinModelPortaliP45481.
SMRiP45481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-5974N.
IntActiP45481. 26 interactors.
MINTiMINT-203452.
STRINGi10090.ENSMUSP00000023165.

PTM databases

iPTMnetiP45481.
PhosphoSitePlusiP45481.

Proteomic databases

EPDiP45481.
MaxQBiP45481.
PaxDbiP45481.
PRIDEiP45481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1098280. Crebbp.

Phylogenomic databases

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiP45481.

Enzyme and pathway databases

ReactomeiR-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-3214847. HATs acetylate histones.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

ChiTaRSiCrebbp. mouse.
EvolutionaryTraceiP45481.
PROiP45481.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CREBBP.

Family and domain databases

CDDicd15802. RING_CBP-p300. 1 hit.
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.
IPR031162. CBP_P300_HAT.
IPR013178. Histone_AcTrfase_Rtt109/CBP.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR010303. RING_CBP-p300.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. HAT_KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM01250. KAT11. 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]
ProtoNetiSearch...

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 30, 2016
This is version 185 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.