CREB-binding protein
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Lua error in Module:Infobox_gene at line 33: attempt to index field 'wikibase' (a nil value). CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene.[1][2] The CREB protein carries out its function by activating transcription, where interaction with transcription factors is managed by one or more CREB domains: the nuclear receptor interaction domain (RID), the CREB and MYB interaction domain (KIX), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3) and the interferon response binding domain (IBiD). The CREB protein domains, KIX, TAZ1 and TAZ2, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53.[3][4]
Contents
Function
This gene is ubiquitously expressed and is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein that binds to cAMP-response element-binding protein (CREB), this gene is now known to play critical roles in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. The protein encoded by this gene has intrinsic histone acetyltransferase activity [5] and also acts as a scaffold to stabilize additional protein interactions with the transcription complex. This protein acetylates both histone and non-histone proteins. This protein shares regions of very high-sequence similarity with protein EP300 in its bromodomain, cysteine-histidine-rich regions, and histone acetyltransferase domain.[6] Recent results suggest that novel CBP-mediated post-translational N-glycosylation activity alters the conformation of CBP-interacting proteins, leading to regulation of gene expression, cell growth and differentiation,[7]
Clinical significance
Mutations in this gene cause Rubinstein-Taybi syndrome (RTS).[8] Chromosomal translocations involving this gene have been associated with acute myeloid leukemia.[6][9] Hypothalamic expression of this gene in mice correlates with mouse lifespan, and when CBP is inhibited in C. elegans by RNAi, there is a proportional fold-change decrease in lifespan.
Interactions
CREB-binding protein has been shown to interact with:
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- TF2,[10]
- AR,[11][12][13][14]
- AIRE,[15][16]
- BRCA1,[17][18][19][20][21]
- C-jun,[10]
- CSK,[22]
- Ccaat-enhancer-binding proteins,[23]
- CDX2,[24]
- CREB1,[10][11][25][26][27][28][29][30][31][32]
- CSNK2A2,[33]
- CUTL1,[34]
- CSNK2A1,[33]
- CDK8,[35]
- EBF1,[36]
- EVI1,[37]
- ESR1,[17][38]
- FOXO1,[39]
- GLI3,[40]
- GTF2B,[17][41]
- HIF1A,[42][43][44]
- HIPK2,[45]
- HNF1A,[46]
- HOXB7,[47]
- HNF4A,[48][49]
- ING1,[50]
- KHDRBS1,[51]
- KLF13,[52]
- KLF4,[53]
- Ku70,[54]
- MAF,[55]
- MLL,[31][56]
- MSX1,[57]
- MYBL2,[58]
- MYB,[28][58]
- MyoD,[59][60]
- NCOA1,[38][61]
- NCOA3,[61][62]
- NCOA6,[63][64]
- NEUROG1,[65]
- NFATC4,[66]
- NFE2L2,[67]
- NFE2,[68]
- NR3C1,[69]
- NUP98,[70]
- P53,[29][71][72]
- PCAF,[35][41]
- POLR2A,[35]
- PPARGC1A,[73]
- PTMA,[74]
- PML,[75][76][77]
- RBBP4,[30]
- RELA,[14][78][79][80][81]
- RPS6KA3,[82]
- SERTAD1,[83]
- SMARCA4,[21][84]
- SMAD1,[65][85]
- SMARCB1[35]
- SREBF1,[86]
- SREBF2,[86]
- SS18L1,[87]
- STAT1,[88]
- STAT2,[89]
- STAT6,[90][91]
- SRF,[75]
- TCF3,[92]
- TGS1,[93]
- TRERF1,[94]
- TDG,[41] and
- Zif268.[95]
References
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
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- ↑ The prediction for 9aaTADs (for both acidic and hydrophilic transactivation domains) is available online from ExPASy http://us.expasy.org/tools/ and EMBnet Spain http://www.es.embnet.org/Services/EMBnetAT/htdoc/9aatad/
- ↑ Ogryzko VV et al. "The transcriptional coactivators p300 and CBP are histone acetyltransferases". Cell. 1996 87(5):953-9.[1]
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Further reading
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External links
- GeneReviews/NCBI/NIH/UW entry on Rubinstein-Taybi Syndrome
- CREBBP protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- NURSA C39
- Drosophila nejire - The Interactive Fly
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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