UniProtKB - P45481 (CBP_MOUSE)
Histone lysine acetyltransferase CREBBP
Crebbp
Functioni
Catalytic activityi
- EC:2.3.1.48By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 362 | Zinc 1 | 1 | |
Metal bindingi | 366 | Zinc 1 | 1 | |
Metal bindingi | 379 | Zinc 1 | 1 | |
Metal bindingi | 384 | Zinc 1 | 1 | |
Metal bindingi | 393 | Zinc 2 | 1 | |
Metal bindingi | 397 | Zinc 2 | 1 | |
Metal bindingi | 403 | Zinc 2 | 1 | |
Metal bindingi | 408 | Zinc 2 | 1 | |
Metal bindingi | 417 | Zinc 3 | 1 | |
Metal bindingi | 421 | Zinc 3 | 1 | |
Metal bindingi | 426 | Zinc 3 | 1 | |
Metal bindingi | 429 | Zinc 3 | 1 | |
Binding sitei | 1494 | Acetyl-CoA; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 1499 | Acetyl-CoABy similarity | 1 | |
Binding sitei | 1503 | Acetyl-CoABy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 346 – 432 | TAZ-type 1PROSITE-ProRule annotationAdd BLAST | 87 | |
Zinc fingeri | 1702 – 1745 | ZZ-typePROSITE-ProRule annotationAdd BLAST | 44 | |
Zinc fingeri | 1766 – 1847 | TAZ-type 2PROSITE-ProRule annotationAdd BLAST | 82 |
GO - Molecular functioni
- acetyltransferase activity Source: UniProtKB
- activating transcription factor binding Source: MGI
- cAMP response element binding protein binding Source: CAFA
- chromatin binding Source: MGI
- chromatin DNA binding Source: GO_Central
- damaged DNA binding Source: UniProtKB
- disordered domain specific binding Source: CAFA
- DNA binding Source: MGI
- histone acetyltransferase activity Source: MGI
- MRF binding Source: UniProtKB
- p53 binding Source: MGI
- peptide-lysine-N-acetyltransferase activity Source: MGI
- peroxisome proliferator activated receptor binding Source: MGI
- protein domain specific binding Source: CAFA
- RNA polymerase II transcription factor binding Source: MGI
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- SMAD binding Source: MGI
- TFIIB-class transcription factor binding Source: MGI
- transcription coactivator activity Source: MGI
- transcription corepressor activity Source: MGI
- transcription factor binding Source: UniProtKB
- zinc ion binding Source: CAFA
GO - Biological processi
- cell population proliferation Source: MGI
- cellular response to hepatocyte growth factor stimulus Source: MGI
- cellular response to UV Source: UniProtKB
- cellular response to virus Source: CAFA
- face morphogenesis Source: ARUK-UCL
- germ-line stem cell population maintenance Source: MGI
- histone acetylation Source: UniProtKB
- histone glutamine methylation Source: UniProtKB
- negative regulation of interferon-beta production Source: CAFA
- negative regulation of transcription by RNA polymerase II Source: MGI
- negative regulation of viral process Source: CAFA
- N-terminal peptidyl-lysine acetylation Source: UniProtKB
- positive regulation of cell adhesion molecule production Source: MGI
- positive regulation of CREB transcription factor activity Source: MGI
- positive regulation of DNA-binding transcription factor activity Source: UniProtKB
- positive regulation of G1/S transition of mitotic cell cycle Source: MGI
- positive regulation of gene expression Source: MGI
- positive regulation of NIK/NF-kappaB signaling Source: MGI
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: MGI
- positive regulation of transforming growth factor beta receptor signaling pathway Source: MGI
- protein acetylation Source: MGI
- protein destabilization Source: UniProtKB
- regulation of transcription, DNA-templated Source: MGI
- rhythmic process Source: UniProtKB-KW
Keywordsi
Molecular function | Activator, Acyltransferase, Transferase |
Biological process | Biological rhythms, Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-1234158, Regulation of gene expression by Hypoxia-inducible Factor R-MMU-201722, Formation of the beta-catenin:TCF transactivating complex R-MMU-2122947, NOTCH1 Intracellular Domain Regulates Transcription R-MMU-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production R-MMU-3371568, Attenuation phase R-MMU-350054, Notch-HLH transcription pathway R-MMU-400206, Regulation of lipid metabolism by PPARalpha R-MMU-5621575, CD209 (DC-SIGN) signaling R-MMU-8866907, Activation of the TFAP2 (AP-2) family of transcription factors R-MMU-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells R-MMU-8941856, RUNX3 regulates NOTCH signaling R-MMU-9018519, Estrogen-dependent gene expression R-MMU-918233, TRAF3-dependent IRF activation pathway R-MMU-933541, TRAF6 mediated IRF7 activation R-MMU-9617629, Regulation of FOXO transcriptional activity by acetylation |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Crebbp Synonyms:Cbp |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1098280, Crebbp |
Subcellular locationi
Nucleus
- histone acetyltransferase complex Source: MGI
- nuclear body Source: MGI
- nuclear chromatin Source: BHF-UCL
- nucleoplasm Source: MGI
- nucleus Source: MGI
- PML body Source: MGI
Other locations
- condensed chromosome outer kinetochore Source: MGI
- cytoplasm Source: MGI
- protein-containing complex Source: CAFA
- RNA polymerase II transcription regulator complex Source: MGI
- transcription regulator complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 600 | R → N: Abolishes binding to CREB. 1 Publication | 1 | |
Mutagenesisi | 999 | K → 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 Publication | 1 | |
Mutagenesisi | 1015 | K → R: No change in sumoylation. 1 Publication | 1 | |
Mutagenesisi | 1034 | K → 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 Publication | 1 | |
Mutagenesisi | 1043 | K → R: No change in sumoylation. 1 Publication | 1 | |
Mutagenesisi | 1053 | K → R: No change in sumoylation. 1 Publication | 1 | |
Mutagenesisi | 1057 | K → 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 Publication | 1 | |
Mutagenesisi | 1061 | K → R: No change in sumoylation. 1 Publication | 1 | |
Mutagenesisi | 1087 | K → R: No change in sumoylation. | 1 | |
Mutagenesisi | 1690 – 1691 | LC → KL: Abolishes histone acetyltransferase activity. 1 Publication | 2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000211191 | 2 – 2441 | Histone lysine acetyltransferase CREBBPAdd BLAST | 2440 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 120 | PhosphoserineCombined sources | 1 | |
Modified residuei | 219 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 600 | Asymmetric dimethylarginine1 Publication | 1 | |
Modified residuei | 624 | Asymmetric dimethylarginine1 Publication | 1 | |
Modified residuei | 656 | N6-acetyllysineCombined sources | 1 | |
Cross-linki | 999 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication | ||
Modified residuei | 1015 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1031 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1034 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication | ||
Cross-linki | 1057 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication | ||
Modified residuei | 1077 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1217 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1383 | Phosphoserine; by IKKABy similarity | 1 | |
Modified residuei | 1387 | Phosphoserine; by IKKABy similarity | 1 | |
Modified residuei | 1584 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1592 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1593 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1596 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1598 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1742 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1745 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1764 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2064 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2077 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2080 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2350 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P45481 |
jPOSTi | P45481 |
MaxQBi | P45481 |
PaxDbi | P45481 |
PRIDEi | P45481 |
PTM databases
iPTMneti | P45481 |
PhosphoSitePlusi | P45481 |
SwissPalmi | P45481 |
Interactioni
Subunit structurei
Interacts with DHX9 (via N-terminus); this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity).
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 with IRF3 (when phosphorylated); forming the dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I interferon genes (By similarity).
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.
Interacts with SMAD4; negatively regulated by ZBTB7A (By similarity).
Forms a complex with KMT2A and CREB1 (By similarity).
Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (By similarity).
By similarity14 PublicationsBinary interactionsi
Hide detailsP45481
GO - Molecular functioni
- activating transcription factor binding Source: MGI
- cAMP response element binding protein binding Source: CAFA
- disordered domain specific binding Source: CAFA
- MRF binding Source: UniProtKB
- p53 binding Source: MGI
- peroxisome proliferator activated receptor binding Source: MGI
- protein domain specific binding Source: CAFA
- RNA polymerase II transcription factor binding Source: MGI
- SMAD binding Source: MGI
- TFIIB-class transcription factor binding Source: MGI
- transcription factor binding Source: UniProtKB
Protein-protein interaction databases
CORUMi | P45481 |
DIPi | DIP-5974N |
IntActi | P45481, 39 interactors |
MINTi | P45481 |
STRINGi | 10090.ENSMUSP00000023165 |
Miscellaneous databases
RNActi | P45481, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P45481 |
SASBDBi | P45481 |
SMRi | P45481 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P45481 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 586 – 665 | KIXPROSITE-ProRule annotationAdd BLAST | 80 | |
Domaini | 1104 – 1176 | BromoPROSITE-ProRule annotationAdd BLAST | 73 | |
Domaini | 1324 – 1701 | CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST | 378 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 226 – 409 | Interaction with SRCAPBy similarityAdd BLAST | 184 | |
Regioni | 1125 – 1171 | Interaction with histoneBy similarityAdd BLAST | 47 | |
Regioni | 1163 – 1181 | Interaction with ASF1ABy similarityAdd BLAST | 19 | |
Regioni | 1434 – 1436 | Interaction with histoneBy similarity | 3 | |
Regioni | 1435 – 1437 | Acetyl-CoA bindingBy similarity | 3 | |
Regioni | 1447 – 1448 | Acetyl-CoA bindingBy similarity | 2 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1062 – 1065 | Poly-Glu | 4 | |
Compositional biasi | 1556 – 1563 | Poly-Glu | 8 | |
Compositional biasi | 1944 – 1949 | Poly-Pro | 6 | |
Compositional biasi | 1968 – 1971 | Poly-Gln | 4 | |
Compositional biasi | 2082 – 2086 | Poly-Gln | 5 | |
Compositional biasi | 2200 – 2216 | Poly-GlnAdd BLAST | 17 | |
Compositional biasi | 2296 – 2299 | Poly-Gln | 4 |
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 346 – 432 | TAZ-type 1PROSITE-ProRule annotationAdd BLAST | 87 | |
Zinc fingeri | 1702 – 1745 | ZZ-typePROSITE-ProRule annotationAdd BLAST | 44 | |
Zinc fingeri | 1766 – 1847 | TAZ-type 2PROSITE-ProRule annotationAdd BLAST | 82 |
Keywords - Domaini
Bromodomain, Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1778, Eukaryota |
InParanoidi | P45481 |
Family and domain databases
CDDi | cd15802, RING_CBP-p300, 1 hit |
DisProti | DP00348 |
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 2.10.110.40, 1 hit 3.30.40.10, 1 hit 3.30.60.90, 1 hit |
IDEALi | IID50008 |
InterProi | View protein in InterPro IPR001487, Bromodomain IPR036427, Bromodomain-like_sf IPR018359, Bromodomain_CS IPR031162, CBP_P300_HAT IPR013178, Histone_AcTrfase_Rtt109/CBP IPR003101, KIX_dom IPR036529, KIX_dom_sf IPR009110, Nuc_rcpt_coact IPR014744, Nuc_rcpt_coact_CREBbp IPR037073, Nuc_rcpt_coact_CREBbp_sf IPR010303, RING_CBP-p300 IPR038547, RING_CBP-p300_sf IPR035898, TAZ_dom_sf IPR013083, Znf_RING/FYVE/PHD IPR000197, Znf_TAZ IPR000433, Znf_ZZ IPR043145, Znf_ZZ_sf |
Pfami | View protein in Pfam PF00439, 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 |
PRINTSi | PR00503, BROMODOMAIN |
SMARTi | View protein in SMART SM00297, BROMO, 1 hit SM01250, KAT11, 1 hit SM00551, ZnF_TAZ, 2 hits SM00291, ZnF_ZZ, 1 hit |
SUPFAMi | SSF47040, SSF47040, 1 hit SSF47370, SSF47370, 1 hit SSF57933, SSF57933, 2 hits SSF69125, SSF69125, 1 hit |
PROSITEi | View protein in PROSITE 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF8VPR5 | F8VPR5_MOUSE | Histone acetyltransferase | Crebbp | 2,441 | Annotation score: | ||
A0A0U1RQB6 | A0A0U1RQB6_MOUSE | Histone acetyltransferase | Crebbp | 2,403 | Annotation score: | ||
A0A0U1RPL2 | A0A0U1RPL2_MOUSE | Histone acetyltransferase | Crebbp | 1,107 | Annotation score: | ||
A0A0U1RP23 | A0A0U1RP23_MOUSE | Histone acetyltransferase | Crebbp | 172 | Annotation score: | ||
A0A0U1RP46 | A0A0U1RP46_MOUSE | Histone acetyltransferase | Crebbp | 127 | Annotation score: | ||
A0A0U1RPQ3 | A0A0U1RPQ3_MOUSE | Histone lysine acetyltransferase CR... | Crebbp | 247 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 400 | G → P in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 530 | I → V in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 670 | S → T in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 826 | V → E in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 978 | S → T in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1159 | W → R in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1239 | E → G in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1417 | N → D in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1429 | R → C in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1466 | G → V in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1470 | G → A in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1850 – 1851 | KL → NV in AAB28651 (PubMed:8413673).Curated | 2 | |
Sequence conflicti | 1859 | R → C in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 1987 | A → D in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 2060 | P → N in AAB28651 (PubMed:8413673).Curated | 1 | |
Sequence conflicti | 2381 | S → T in AAB28651 (PubMed:8413673).Curated | 1 |
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 |
Similar proteinsi
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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
5HOU | NMR | - | A | 340-439 | [»] | |
5HP0 | NMR | - | A | 1764-1857 | [»] | |
5HPD | NMR | - | A | 1764-1855 | [»] | |
5U4K | NMR | - | A | 586-672 | [»] | |
5U7G | X-ray | 2.40 | A/B | 1079-1556 | [»] | |
5W0I | X-ray | 1.43 | A | 1083-1198 | [»] | |
6DMX | X-ray | 2.80 | B/D/G/I | 586-672 | [»] | |
6DNQ | X-ray | 2.35 | B/D | 586-672 | [»] | |
BMRBi | P45481 | |||||
SASBDBi | P45481 | |||||
SMRi | P45481 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P45481 |
DIPi | DIP-5974N |
IntActi | P45481, 39 interactors |
MINTi | P45481 |
STRINGi | 10090.ENSMUSP00000023165 |
PTM databases
iPTMneti | P45481 |
PhosphoSitePlusi | P45481 |
SwissPalmi | P45481 |
Proteomic databases
EPDi | P45481 |
jPOSTi | P45481 |
MaxQBi | P45481 |
PaxDbi | P45481 |
PRIDEi | P45481 |
Organism-specific databases
MGIi | MGI:1098280, Crebbp |
Phylogenomic databases
eggNOGi | KOG1778, Eukaryota |
InParanoidi | P45481 |
Enzyme and pathway databases
Reactomei | R-MMU-1234158, Regulation of gene expression by Hypoxia-inducible Factor R-MMU-201722, Formation of the beta-catenin:TCF transactivating complex R-MMU-2122947, NOTCH1 Intracellular Domain Regulates Transcription R-MMU-3134973, LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production R-MMU-3371568, Attenuation phase R-MMU-350054, Notch-HLH transcription pathway R-MMU-400206, Regulation of lipid metabolism by PPARalpha R-MMU-5621575, CD209 (DC-SIGN) signaling R-MMU-8866907, Activation of the TFAP2 (AP-2) family of transcription factors R-MMU-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells R-MMU-8941856, RUNX3 regulates NOTCH signaling R-MMU-9018519, Estrogen-dependent gene expression R-MMU-918233, TRAF3-dependent IRF activation pathway R-MMU-933541, TRAF6 mediated IRF7 activation R-MMU-9617629, Regulation of FOXO transcriptional activity by acetylation |
Miscellaneous databases
ChiTaRSi | Crebbp, mouse |
EvolutionaryTracei | P45481 |
PROi | PR:P45481 |
RNActi | P45481, protein |
SOURCEi | Search... |
Family and domain databases
CDDi | cd15802, RING_CBP-p300, 1 hit |
DisProti | DP00348 |
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 2.10.110.40, 1 hit 3.30.40.10, 1 hit 3.30.60.90, 1 hit |
IDEALi | IID50008 |
InterProi | View protein in InterPro IPR001487, Bromodomain IPR036427, Bromodomain-like_sf IPR018359, Bromodomain_CS IPR031162, CBP_P300_HAT IPR013178, Histone_AcTrfase_Rtt109/CBP IPR003101, KIX_dom IPR036529, KIX_dom_sf IPR009110, Nuc_rcpt_coact IPR014744, Nuc_rcpt_coact_CREBbp IPR037073, Nuc_rcpt_coact_CREBbp_sf IPR010303, RING_CBP-p300 IPR038547, RING_CBP-p300_sf IPR035898, TAZ_dom_sf IPR013083, Znf_RING/FYVE/PHD IPR000197, Znf_TAZ IPR000433, Znf_ZZ IPR043145, Znf_ZZ_sf |
Pfami | View protein in Pfam PF00439, 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 |
PRINTSi | PR00503, BROMODOMAIN |
SMARTi | View protein in SMART SM00297, BROMO, 1 hit SM01250, KAT11, 1 hit SM00551, ZnF_TAZ, 2 hits SM00291, ZnF_ZZ, 1 hit |
SUPFAMi | SSF47040, SSF47040, 1 hit SSF47370, SSF47370, 1 hit SSF57933, SSF57933, 2 hits SSF69125, SSF69125, 1 hit |
PROSITEi | View protein in PROSITE 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CBP_MOUSE | |
Accessioni | P45481Primary (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: | February 10, 2021 | |
This is version 220 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references