CREB-binding protein

CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene.[5][6] 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 KIX domain (CREB and MYB interaction domain), 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.[7][8]

See also: p300-CBP coactivator family
CREBBP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCREBBP, AW558298, CBP, CBP/p300, KAT3A, p300/CBP, RSTS, CREB binding protein, RSTS1, MKHK1
External IDsOMIM: 600140 MGI: 1098280 HomoloGene: 68393 GeneCards: CREBBP
Gene location (Human)
Chr.Chromosome 16 (human)[1]
Band16p13.3Start3,725,054 bp[1]
End3,880,713 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1387

12914

Ensembl

ENSG00000005339

ENSMUSG00000022521

UniProt

Q92793

P45481

RefSeq (mRNA)

NM_001079846
NM_004380

NM_001025432

RefSeq (protein)

NP_001073315
NP_004371

n/a

Location (UCSC)Chr 16: 3.73 – 3.88 MbChr 16: 4.08 – 4.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

This gene is ubiquitously expressed and is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein [Ref] 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 [9] 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.[10] 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,[11]

Posttranslational modification

Homeodomain interacting protein kinase 2 (HIPK2) phosphorylates several regions of CBP close to the N-terminal and close to the C-terminal region as well. Out of the described phosphoacceptor sites, serines 2361, 2363, 2371, 2376, and 2381 are responsible for the HIPK2-induced mobility shift of the CBP C-terminal activation domain that is also visible in Polyacrylamide gel electrophoresis (PAGE) experiments. However, activation of CBP by HIPK2 is not mediated by this phosphorylation but rather by counteracting the repressive action of the cell cycle regulatory domain 1 (CRD1) of CBP, located between amino acids 977 and 1076.[12]

Clinical significance

Mutations in this gene cause Rubinstein-Taybi syndrome (RTS).[13] Chromosomal translocations involving this gene have been associated with acute myeloid leukemia.[10][14] 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.

Small molecule inhibition

A small molecule inhibitor (I-CBP112) binding to the bromodomain domain of CBP/p300 has been developed for leukemia therapy.[15]

Interactions

CREB-binding protein has been shown to interact with:

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References
  1. GRCh38: Ensembl release 89: ENSG00000005339 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000022521 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  8. 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/%5B%5D
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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 Progress in Hormone Research. 52: 103–19, discussion 119–20. PMID 9238849.
  • Marcello A, Zoppé M, Giacca M (March 2001). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator". IUBMB Life. 51 (3): 175–81. doi:10.1080/152165401753544241. PMID 11547919.
  • Matt T (2002). "Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP)". Acta Medica Austriaca. 29 (3): 77–9. doi:10.1046/j.1563-2571.2002.02010.x. PMID 12168567.
  • Combes R, Balls M, Bansil L, Barratt M, Bell D, Botham P, Broadhead C, Clothier R, George E, Fentem J, Jackson M, Indans I, Loizu G, Navaratnam V, Pentreath V, Phillips B, Stemplewski H, Stewart J (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. 30 (4): 365–406. doi:10.1177/026119290203000403. PMID 12234245. S2CID 26326825.
  • Minghetti L, Visentin S, Patrizio M, Franchini L, Ajmone-Cat MA, Levi G (May 2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions". Neurochemical Research. 29 (5): 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295.
  • Kino T, Pavlakis GN (April 2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1". DNA and Cell Biology. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.
  • Greene WC, Chen LF (2004). "Regulation of NF-kappaB action by reversible acetylation". Novartis Foundation Symposium. Novartis Foundation Symposia. 259: 208–17, discussion 218–25. doi:10.1002/0470862637.ch15. ISBN 9780470862612. PMID 15171256.
  • Liou LY, Herrmann CH, Rice AP (September 2004). "HIV-1 infection and regulation of Tat function in macrophages". The International Journal of Biochemistry & Cell Biology. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343.
  • Pugliese A, Vidotto V, Beltramo T, Petrini S, Torre D (2005). "A review of HIV-1 Tat protein biological effects". Cell Biochemistry and Function. 23 (4): 223–7. doi:10.1002/cbf.1147. PMID 15473004.
  • Bannwarth S, Gatignol A (January 2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host". Current HIV Research. 3 (1): 61–71. doi:10.2174/1570162052772924. PMID 15638724.
  • Le Rouzic E, Benichou S (February 2005). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
  • Gibellini D, Vitone F, Schiavone P, Re MC (April 2005). "HIV-1 tat protein and cell proliferation and survival: a brief review". The New Microbiologica. 28 (2): 95–109. PMID 16035254.
  • Hetzer C, Dormeyer W, Schnölzer M, Ott M (October 2005). "Decoding Tat: the biology of HIV Tat posttranslational modifications". Microbes and Infection. 7 (13): 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164.
  • Peruzzi F (January 2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis". Frontiers in Bioscience. 11: 708–17. doi:10.2741/1829. PMID 16146763. S2CID 12438136.

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