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]

CREBBP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1JSP, 1LIQ, 1RDT, 1WO3, 1WO4, 1WO5, 1WO6, 1WO7, 2D82, 2KJE, 2KWF, 2L84, 2L85, 2LXS, 2LXT, 2RNY, 3DWY, 3P1C, 3P1D, 3P1E, 3P1F, 3SVH, 4A9K, 4N3W, 4N4F, 4NR4, 4NR5, 4NR6, 4NR7, 4NYV, 4NYW, 4NYX, 4OUF, 4TQN, 4TS8, 4WHU, 5JEM, 5I8B, 5I89, 5I86, 4YK0, 5CGP, 5I8G, 2N1A, 5I83, 1ZOQ, 5DBM
Identifiers
Aliases	CREBBP, AW558298, CBP, CBP/p300, KAT3A, p300/CBP, RSTS, CREB binding protein, RSTS1, MKHK1
External IDs	OMIM: 600140 MGI: 1098280 HomoloGene: 68393 GeneCards: CREBBP
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 3,725,054 bp[1] End 3,880,713 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16 A1|16 2.4 cM Start 4,081,328 bp[2] End 4,213,997 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • GO:0001105 transcription coactivator activity • MRF binding • RNA polymerase II transcription factor binding • zinc ion binding • p53 binding • transcription factor binding • chromatin binding • GO:0001158 core promoter proximal region sequence-specific DNA binding • GO:0001104 transcription coregulator activity • signal transducer activity • metal ion binding • histone acetyltransferase activity • RNA polymerase II activating transcription factor binding • damaged DNA binding • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific • GO:0001948 protein binding • acetyltransferase activity • transferase activity, transferring acyl groups • peptide N-acetyltransferase activity • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001106 transcription corepressor activity Cellular component • cytoplasm • nucleoplasm • nuclear chromatin • histone acetyltransferase complex • cell nucleus • nuclear body Biological process • Notch signaling pathway • response to hypoxia • regulation of transcription, DNA-templated • rhythmic process • cellular response to UV • embryonic digit morphogenesis • N-terminal peptidyl-lysine acetylation • stimulatory C-type lectin receptor signaling pathway • negative regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • positive regulation of transcription, DNA-templated • regulation of smoothened signaling pathway • histone acetylation • regulation of transcription from RNA polymerase II promoter in response to hypoxia • regulation of cellular response to heat • transcription initiation from RNA polymerase II promoter • GO:0022415 viral process • positive regulation of type I interferon production • signal transduction • protein acetylation • homeostatic process • beta-catenin-TCF complex assembly • regulation of apoptotic process • positive regulation of transcription from RNA polymerase II promoter • regulation of lipid metabolic process • protein destabilization • regulation of myeloid cell differentiation • positive regulation of transcription of Notch receptor target • positive regulation of transforming growth factor beta receptor signaling pathway • positive regulation of Notch signaling pathway • macromolecular complex assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
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 Mb	Chr 16: 4.08 – 4.21 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/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:

• TF2,[16]
• AR,[17][18][19][20]
• AIRE,[21][22]
• BRCA1,[23][24][25][26][27]
• C-jun,[16]
• CSK,[28]
• Ccaat-enhancer-binding proteins,[29]
• CDX2,[30]
• CREB1,[16][17][31][32][33][34][35][36][37][38]
• CSNK2A2,[39]
• CUTL1,[40]
• CSNK2A1,[39]
• CDK8,[41]
• EBF1,[42]
• EVI1,[43]
• ESR1,[23][44]
• FOXO1,[45]
• GLI3,[46]
• GTF2B,[23][47]
• HIF1A,[48][49][50]
• HIPK2,[51]
• HNF1A,[52]
• HOXB7,[53]
• HNF4A,[54][55]
• ING1,[56]
• KHDRBS1,[57]
• KLF1,[58]
• KLF13,[59]
• KLF4,[60]
• Ku70,[61]
• MAF,[62]
• MLL,[37][63]
• MKL2,[64]
• MSX1,[65]
• MYBL2,[66]
• MYB,[34][66]
• MyoD,[67][68]
• NCOA1,[44][69]
• NCOA3,[69][70]
• NCOA6,[71][72]
• NEUROG1,[73]
• NFATC4,[74]
• NFE2L2,[75]
• NFE2,[76]
• NPAS4,[77]
• NR3C1,[78]
• NUP98,[79]
• P53,[35][80][81]
• PCAF,[41][47]
• POLR2A,[41]
• PPARGC1A,[82]
• PTMA,[83]
• PML,[84][85][86]
• RBBP4,[36]
• RELA,[20][87][88][89][90]
• RPS6KA3,[91]
• SERTAD1,[92]
• SMARCA4,[27][93]
• SMAD1,[73][94]
• SMARCB1[41]
• SREBF1,[95]
• SREBF2,[95]
• SS18L1,[96]
• STAT1,[97]
• STAT2,[98]
• STAT6,[99][100]
• SRF,[84]
• TCF3,[101]
• TGS1,[102]
• TRERF1,[103]
• TDG,[47] and
• Zif268.[104]

References

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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. S2CID 10931640.
• 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. S2CID 25323034.
• 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. S2CID 8408278.
• 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.

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
• Human CREBBP genome location and CREBBP gene details page in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.