UniProtKB - P45481 (CBP_MOUSE)

BLAST

>sp|P45481|CBP_MOUSE CREB-binding protein OS=Mus musculus OX=10090 GN=Crebbp PE=1 SV=3
MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVP
DAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKS
PLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANF
NQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAE
TLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQ
SMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLL
LHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKN
CTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSM
QRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQ
PPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLR
SHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKI
QKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGM
NSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHAN
NIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAP
QASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTP
TPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGT
PLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRS
EMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQ
PRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIK
RKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYC
CGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQ
TTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPR
KENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRF
VDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHF
FRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRL
QEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQE
EEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQ
KLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFS
SLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHT
HKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMK
RVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRL
QQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPA
GFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINN
GMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPV
MSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAA
FIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQP
AMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSAS
LAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGA
DSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSN
QVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLG
NPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL

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History
Entry version 203 (10 Oct 2018)
Sequence version 3 (27 Jul 2011)
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Protein

CREB-binding protein

Gene

Crebbp

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -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). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity).By similarity4 Publications

Catalytic activityⁱ

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N₆-acetyl-L-lysine.By similarity

Sites

Feature key	Position(s)	DescriptionActions	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	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: MGI
Inferred from direct assayⁱ
- 12496368
activating transcription factor binding Source: MGI
cAMP response element binding protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 9413984
chromatin binding
Source: MGI
Inferred from direct assayⁱ
- 15832170
damaged DNA binding Source: UniProtKB
disordered domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11823864
- 14594809
DNA binding
Source: MGI
Inferred from direct assayⁱ
- 15681609
histone acetyltransferase activity
Source: MGI
Inferred from direct assayⁱ
- 11115394
- 11867645
MRF binding Source: UniProtKB
p53 binding Source: MGI
peroxisome proliferator activated receptor binding Source: MGI
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11583620
- 14594809
protein heterodimerization activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11823864
proximal promoter sequence-specific DNA binding Source: MGI
RNA polymerase II regulatory region sequence-specific DNA binding
Source: MGI
Inferred from direct assayⁱ
- 21402781
RNA polymerase II transcription factor binding
Source: MGI
Inferred from physical interactionⁱ
- 7913207
SMAD binding Source: MGI
TFIIB-class transcription factor binding
Source: MGI
Inferred from physical interactionⁱ
- 7913207
transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding
Source: MGI
Inferred from direct assayⁱ
- 22780989
transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: MGI
transcriptional repressor activity, RNA polymerase II transcription factor binding Source: MGI
transcription coactivator activity
Source: MGI
Inferred from direct assayⁱ
- 7913207
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 10075717
zinc ion binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 14594809

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell proliferation Source: MGI
cellular response to hepatocyte growth factor stimulus
Source: MGI
Inferred from direct assayⁱ
- 21072211
cellular response to UV Source: UniProtKB
cellular response to virus
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11583620
germ-line stem cell population maintenance
Source: MGI
Inferred from mutant phenotypeⁱ
- 17936260
histone acetylation Source: UniProtKB
negative regulation of interferon-beta biosynthetic process
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11583620
negative regulation of transcription by RNA polymerase II Source: MGI
negative regulation of viral process
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11583620
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
Inferred from direct assayⁱ
- 7913207
positive regulation of DNA-binding transcription factor activity
Source: UniProtKB
Traceable author statementⁱ
- 10733899
positive regulation of G1/S transition of mitotic cell cycle Source: MGI
positive regulation of gene expression
Source: MGI
Inferred from genetic interactionⁱ
- 22523253
positive regulation of NIK/NF-kappaB signaling Source: MGI
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 10733899
positive regulation of transcription by RNA polymerase II
Source: MGI
Inferred from genetic interactionⁱ
- 16012757
protein acetylation Source: MGI
protein destabilization Source: UniProtKB
regulation of transcription, DNA-templated
Source: MGI
Inferred from direct assayⁱ
- 12464179
rhythmic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, Acyltransferase, Transferase
Biological process	Biological rhythms, Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: CREB-binding protein (EC:2.3.1.48By similarity)
Gene namesⁱ	Name:Crebbp Synonyms:Cbp
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Unplaced

Organism-specific databases

MGIⁱ	MGI:1098280 Crebbp

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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	CREB-binding proteinAdd BLAST		2440

Amino acid modifications

Feature key	Position(s)	DescriptionActions	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	Omega-N-methylated arginine1 Publication	1
Modified residueⁱ	624	Omega-N-methylated arginine1 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

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

EPDⁱ	P45481
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P45481
PaxDbⁱ	P45481
PRIDEⁱ	P45481

PTM databases

iPTMnetⁱ	P45481
PhosphoSitePlusⁱ	P45481

Expressionⁱ

Gene expression databases

CleanExⁱ	MM_CREBBP

CleanExⁱ

MM_CREBBP

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 (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).By similarity14 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P03254	3	EBI-296306,EBI-8599077	From Human adenovirus C serotype 2.
	P03255	2	EBI-296306,EBI-2603114	From Human adenovirus C serotype 5.
	P88946	6	EBI-296306,EBI-936023	From Human herpesvirus 8 type M.
Arntl	Q9WTL8-4	2	EBI-296306,EBI-644568
BCL6	P41182	2	EBI-296306,EBI-765407	From Homo sapiens.
BUB1B	O60566	3	EBI-296306,EBI-1001438	From Homo sapiens.
COPS2	P61201	2	EBI-296306,EBI-1050386	From Homo sapiens.
Creb1	Q01147	2	EBI-296306,EBI-2291098
Ctnnb1	Q02248	3	EBI-296306,EBI-397872
DDX5	P17844	3	EBI-296306,EBI-351962	From Homo sapiens.
Ets1	P27577	3	EBI-296306,EBI-4289053
FUS	P35637	4	EBI-296306,EBI-400434	From Homo sapiens.
HIST2H4B	P62805	2	EBI-296306,EBI-302023	From Homo sapiens.
Khdrbs1	Q60749	7	EBI-296306,EBI-519077
KMT2A	Q03164	7	EBI-296306,EBI-591370	From Homo sapiens.
Rela	Q04207	9	EBI-296306,EBI-644400
SNAI1	O95863	7	EBI-296306,EBI-1045459	From Homo sapiens.
TP53	P04637	9	EBI-296306,EBI-366083	From Homo sapiens.
Trim28	Q62318-1	2	EBI-296306,EBI-6876996

GO - Molecular functionⁱ

activating transcription factor binding Source: MGI
cAMP response element binding protein binding
Source: CAFA
Inferred from physical interactionⁱ
- 9413984
disordered domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11823864
- 14594809
MRF binding Source: UniProtKB
p53 binding Source: MGI
peroxisome proliferator activated receptor binding Source: MGI
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 11583620
- 14594809
protein heterodimerization activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11823864
RNA polymerase II transcription factor binding
Source: MGI
Inferred from physical interactionⁱ
- 7913207
SMAD binding Source: MGI
TFIIB-class transcription factor binding
Source: MGI
Inferred from physical interactionⁱ
- 7913207
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 10075717

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

CORUMⁱ	P45481
Database of interacting proteins More...DIPⁱ	DIP-5974N
IntActⁱ	P45481, 39 interactors
Molecular INTeraction database More...MINTⁱ	P45481
STRINGⁱ	10090.ENSMUSP00000023165

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	343 – 345	Combined sources	3
Helixⁱ	347 – 372	Combined sources	26
Beta strandⁱ	374 – 376	Combined sources	3
Helixⁱ	384 – 396	Combined sources	13
Helixⁱ	400 – 402	Combined sources	3
Helixⁱ	406 – 420	Combined sources	15
Turnⁱ	423 – 425	Combined sources	3
Helixⁱ	429 – 433	Combined sources	5
Helixⁱ	436 – 438	Combined sources	3
Helixⁱ	590 – 594	Combined sources	5
Helixⁱ	597 – 611	Combined sources	15
Turnⁱ	617 – 619	Combined sources	3
Helixⁱ	622 – 642	Combined sources	21
Helixⁱ	646 – 664	Combined sources	19
Turnⁱ	667 – 671	Combined sources	5
Helixⁱ	1088 – 1103	Combined sources	16
Turnⁱ	1106 – 1109	Combined sources	4
Helixⁱ	1110 – 1112	Combined sources	3
Helixⁱ	1118 – 1121	Combined sources	4
Helixⁱ	1126 – 1129	Combined sources	4
Helixⁱ	1136 – 1144	Combined sources	9
Helixⁱ	1151 – 1168	Combined sources	18
Helixⁱ	1174 – 1197	Combined sources	24
Beta strandⁱ	1281 – 1283	Combined sources	3
Turnⁱ	1285 – 1287	Combined sources	3
Beta strandⁱ	1290 – 1292	Combined sources	3
Helixⁱ	1293 – 1296	Combined sources	4
Turnⁱ	1300 – 1302	Combined sources	3
Helixⁱ	1310 – 1314	Combined sources	5
Helixⁱ	1334 – 1350	Combined sources	17
Beta strandⁱ	1358 – 1371	Combined sources	14
Helixⁱ	1374 – 1380	Combined sources	7
Turnⁱ	1381 – 1384	Combined sources	4
Beta strandⁱ	1388 – 1403	Combined sources	16
Beta strandⁱ	1406 – 1418	Combined sources	13
Beta strandⁱ	1429 – 1437	Combined sources	9
Helixⁱ	1444 – 1446	Combined sources	3
Helixⁱ	1447 – 1465	Combined sources	19
Beta strandⁱ	1469 – 1473	Combined sources	5
Beta strandⁱ	1483 – 1487	Combined sources	5
Helixⁱ	1497 – 1513	Combined sources	17
Beta strandⁱ	1518 – 1522	Combined sources	5
Helixⁱ	1523 – 1530	Combined sources	8
Helixⁱ	1535 – 1537	Combined sources	3
Helixⁱ	1545 – 1555	Combined sources	11
Turnⁱ	1709 – 1711	Combined sources	3
Beta strandⁱ	1713 – 1726	Combined sources	14
Helixⁱ	1731 – 1737	Combined sources	7
Beta strandⁱ	1741 – 1746	Combined sources	6
Helixⁱ	1765 – 1785	Combined sources	21
Helixⁱ	1794 – 1808	Combined sources	15
Helixⁱ	1812 – 1815	Combined sources	4
Helixⁱ	1818 – 1833	Combined sources	16
Beta strandⁱ	1840 – 1843	Combined sources	4
Helixⁱ	1844 – 1849	Combined sources	6
Beta strandⁱ	2061 – 2064	Combined sources	4
Helixⁱ	2068 – 2075	Combined sources	8
Beta strandⁱ	2076 – 2079	Combined sources	4
Helixⁱ	2088 – 2091	Combined sources	4
Helixⁱ	2097 – 2100	Combined sources	4
Helixⁱ	2102 – 2104	Combined sources	3
Beta strandⁱ	2106 – 2108	Combined sources	3

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00348
ProteinModelPortalⁱ	P45481
SMRⁱ	P45481
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P45481

EvolutionaryTraceⁱ

P45481

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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	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	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	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-finger

Phylogenomic databases

eggNOGⁱ	KOG1778 Eukaryota COG5076 LUCA
HOGENOMⁱ	HOG000111353
HOVERGENⁱ	HBG000185
InParanoidⁱ	P45481

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15802 RING_CBP-p300, 1 hit
Gene3Dⁱ	1.10.1630.10, 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
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
Pfam protein domain database More...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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show all Align All

P45481-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F8VPR5	F8VPR5_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	2,441	Annotation score:
A0A0U1RQB6	A0A0U1RQB6_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	2,403	Annotation score:
A0A0U1RPL2	A0A0U1RPL2_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	1,107	Annotation score:
A0A0U1RP23	A0A0U1RP23_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	172	Annotation score:
A0A0U1RP46	A0A0U1RP46_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	127	Annotation score:
A0A0U1RPQ3	A0A0U1RPQ3_MOUSE	CREB-binding protein CREB-binding protein	Crebbp	247	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS27915.1
PIRⁱ	S39161
UniGeneⁱ	Mm.132238 Mm.392384

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P45481	CREB-binding protein	)	HUMAN		2442	UniRef90_Q92793
CREB-binding protein		RAT		2442
CREB binding protein		CALJA		2450
Uncharacterized protein		PROCO		2449
Uncharacterized protein		Cebus capucinus imitator		2448
+168

Protein	Similar proteins		Species	Score	Length	Source
P45481	CREB-binding protein	)	HUMAN		2442	UniRef50_Q92793
CREB-binding protein		RAT		2442
CREB binding protein		CALJA		2450
Uncharacterized protein		PROCO		2449
Uncharacterized protein		Cebus capucinus imitator		2448
+337

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
DisProtⁱ	DP00348
ProteinModelPortalⁱ	P45481
SMRⁱ	P45481
ModBaseⁱ	Search...
MobiDBⁱ	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

Proteomic databases

EPDⁱ	P45481
MaxQBⁱ	P45481
PaxDbⁱ	P45481
PRIDEⁱ	P45481

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Organism-specific databases

MGIⁱ	MGI:1098280 Crebbp

Phylogenomic databases

eggNOGⁱ	KOG1778 Eukaryota COG5076 LUCA
HOGENOMⁱ	HOG000111353
HOVERGENⁱ	HBG000185
InParanoidⁱ	P45481

Miscellaneous databases

ChiTaRSⁱ	Crebbp mouse
EvolutionaryTraceⁱ	P45481
Protein Ontology More...PROⁱ	PR:P45481
SOURCEⁱ	Search...

Gene expression databases

CleanExⁱ	MM_CREBBP

CleanExⁱ

MM_CREBBP

Family and domain databases

CDDⁱ	cd15802 RING_CBP-p300, 1 hit
Gene3Dⁱ	1.10.1630.10, 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
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
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...

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:	October 10, 2018
	This is version 203 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, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

UniProtKB

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Help

UniRef

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Supporting data

UniProtKB - P45481 (CBP_MOUSE)

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CREB-binding protein

Crebbp

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ