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CREB-binding protein

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Title: CREB-binding protein  
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Subject: RBBP4, Histone acetylation and deacetylation, FOXO1, Atrichia with papular lesions, CBP
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CREB-binding protein

CREB binding protein
PDB rendering based on 1f81.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; CBP; KAT3A; RSTS
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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 1
  • Clinical significance 2
  • Interactions 3
  • References 4
  • Further reading 5
  • External links 6

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:

References

  1. ^ Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH (October 1993). "Phosphorylated CREB binds specifically to the nuclear protein CBP". Nature 365 (6449): 855–9.  
  2. ^ Wydner KL, Bhattacharya S, Eckner R, Lawrence JB, Livingston DM (November 1995). "Localization of human CREB-binding protein gene (CREBBP) to 16p13.2-p13.3 by fluorescence in situ hybridization". Genomics 30 (2): 395–6.  
  3. ^ Teufel DP, Freund SM, Bycroft M, Fersht AR (April 2007). "Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53". PNAS 104 (17): 7009–7014.  
  4. ^ 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/
  5. ^ Ogryzko VV et al. "The transcriptional coactivators p300 and CBP are histone acetyltransferases". Cell. 1996 87(5):953-9.[6]
  6. ^ a b "Entrez Gene: CREBBP (CREB-binding protein)". 
  7. ^ Siddique H, Rao VN, Reddy ES (Aug 2009). "CBP-mediated post-translational N-glycosylation of BRCA2". Int J Oncol. 35 (2): 16387–91.  
  8. ^ Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ (July 1995). "Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP". Nature 376 (6538): 348–51.  
  9. ^ Vizmanos JL, Larráyoz MJ, Lahortiga I, Floristán F, Alvarez C, Odero MD, Novo FJ, Calasanz MJ (April 2003). "t(10;16)(q22;p13) and MORF-CREBBP fusion is a recurrent event in acute myeloid leukemia". Genes Chromosomes Cancer 36 (4): 402–5.  
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Further reading

  • Goldman PS, Tran VK, Goodman RH (1997). "The multifunctional role of the co-activator CBP in transcriptional regulation.". Recent Prog. Horm. Res. 52: 103–19; discussion 119–20.  
  • Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.". IUBMB Life 51 (3): 175–81.  
  • Matt T (2002). "Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP).". Acta Med. Austriaca 29 (3): 77–9.  
  • Combes R, Balls M, Bansil L; et al. (2002). "An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991).". Alternatives to laboratory animals : ATLA 30 (4): 365–406.  
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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
  • - The Interactive Flynejire Drosophila

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