CREB binding protein

From Wikipedia, the free encyclopedia

See also: P300/CBP

CREB binding protein (Rubinstein-Taybi syndrome)

PDB rendering based on 1f81.

Available structures: 1f81, 1jjs, 1jsp, 1kbh, 1kdx, 1l3e, 1l8c, 1liq, 1p4q, 1r8u, 1sb0, 1tot, 1u2n, 1zoq, 2agh, 2c52, 2d82

Identifiers

Symbol(s)

CREBBP; CBP; RSTS; RTS

External IDs

OMIM: 600140 MGI: 1098280 HomoloGene: 68393

Gene ontology
Molecular Function:	• transcription factor activity • transcription coactivator activity • histone acetyltransferase activity • signal transducer activity • protein binding • zinc ion binding • acetyltransferase activity • transferase activity • metal ion binding • MyoD binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• response to hypoxia • regulation of transcription, DNA-dependent • protein complex assembly • signal transduction • histone acetylation • homeostatic process • positive regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001079846 (mRNA)
NP_001073315 (protein)

NM_001025432 (mRNA)
NP_001020603 (protein)

Location

Chr 16: 3.72 - 3.87 Mb

Chr 16: 4 - 4.13 Mb

Pubmed search

[1]

[2]

CREB binding protein (Rubinstein-Taybi syndrome), also known as CREBBP, is a human gene.

[edit] 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. PMID 9238849.
Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.". IUBMB Life 51 (3): 175–81. PMID 11547919.
Matt T (2002). "Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP).". Acta Med. Austriaca 29 (3): 77–9. PMID 12168567.
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. PMID 12234245.
Minghetti L, Visentin S, Patrizio M, et al. (2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions.". Neurochem. Res. 29 (5): 965–78. PMID 15139295.
Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.
Greene WC, Chen LF (2004). "Regulation of NF-kappaB action by reversible acetylation.". Novartis Found. Symp. 259: 208–17; discussion 218–25. PMID 15171256.
Liou LY, Herrmann CH, Rice AP (2005). "HIV-1 infection and regulation of Tat function in macrophages.". Int. J. Biochem. Cell Biol. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343.
Pugliese A, Vidotto V, Beltramo T, et al. (2005). "A review of HIV-1 Tat protein biological effects.". Cell Biochem. Funct. 23 (4): 223–7. doi:10.1002/cbf.1147. PMID 15473004.
Bannwarth S, Gatignol A (2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host.". Curr. HIV Res. 3 (1): 61–71. PMID 15638724.
Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle.". Retrovirology 2: 11. doi:10.1186/1742-4690-2-11. PMID 15725353.
Gibellini D, Vitone F, Schiavone P, Re MC (2005). "HIV-1 tat protein and cell proliferation and survival: a brief review.". New Microbiol. 28 (2): 95–109. PMID 16035254.
Hetzer C, Dormeyer W, Schnölzer M, Ott M (2006). "Decoding Tat: the biology of HIV Tat posttranslational modifications.". Microbes Infect. 7 (13): 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164.
Peruzzi F (2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis.". Front. Biosci. 11: 708–17. PMID 16146763.