- 同
- CBP
WordNet
- executed with proper legal authority; "a binding contract"
- the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
- strip sewn over or along an edge for reinforcement or decoration
- the capacity to attract and hold something
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
PrepTutorEJDIC
- 義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
- 蛋白(たんばく)質
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/05/12 00:19:44」(JST)
[Wiki en表示]
See also: p300-CBP coactivator family
| CREB binding protein |
PDB rendering based on 1f81. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
|
1JSP, 1LIQ, 1RDT, 1WO3, 1WO4, 1WO5, 1WO6, 1WO7, 1ZOQ, 2D82, 2KJE, 2KWF, 2L84, 2L85, 2RNY, 3DWY, 3P1C, 3P1D, 3P1E, 3P1F, 3SVH, 4A9K
|
|
|
| Identifiers |
| Symbols |
CREBBP; CBP; KAT3A; RSTS |
| External IDs |
OMIM: 600140 MGI: 1098280 HomoloGene: 68393 ChEMBL: 5747 GeneCards: CREBBP Gene |
| EC number |
2.3.1.48 |
| Gene Ontology |
| Molecular function |
• core promoter proximal region sequence-specific DNA binding
• RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription
• RNA polymerase II transcription factor binding
• RNA polymerase II activating transcription factor binding
• RNA polymerase II transcription coactivator activity
• RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription
• p53 binding
• chromatin binding
• sequence-specific DNA binding transcription factor activity
• transcription coactivator activity
• histone acetyltransferase activity
• signal transducer activity
• protein binding
• transcription factor binding
• zinc ion binding
• acetyltransferase activity
• MRF binding
|
| Cellular component |
• histone acetyltransferase complex
• nuclear chromatin
• condensed chromosome outer kinetochore
• nucleus
• nucleoplasm
• transcription factor complex
• cytoplasm
• nuclear body
|
| Biological process |
• negative regulation of transcription from RNA polymerase II promoter
• response to hypoxia
• regulation of transcription, DNA-dependent
• transcription initiation from RNA polymerase II promoter
• protein complex assembly
• signal transduction
• Notch signaling pathway
• regulation of smoothened signaling pathway
• gene expression
• histone acetylation
• N-terminal peptidyl-lysine acetylation
• virus-host interaction
• germ-line stem cell maintenance
• cellular response to stress
• homeostatic process
• embryonic digit morphogenesis
• cellular lipid metabolic process
• small molecule metabolic process
• innate immune response
• positive regulation of transcription, DNA-dependent
• regulation of transcription from RNA polymerase II promoter in response to hypoxia
• cellular response to hypoxia
|
| Sources: Amigo / QuickGO |
|
| RNA expression pattern |
|
|
| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
|
| Entrez |
1387 |
12914 |
|
| Ensembl |
ENSG00000005339 |
ENSMUSG00000022521 |
|
| UniProt |
Q92793 |
F8VPR5 |
|
| RefSeq (mRNA) |
NM_001079846 |
NM_001025432 |
|
| RefSeq (protein) |
NP_001073315 |
NP_001020603 |
|
| Location (UCSC) |
Chr 16:
3.78 – 3.93 Mb |
Chr 16:
4.08 – 4.21 Mb |
|
| PubMed search |
[2] |
[3] |
|
|
|
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
- 1 Function
- 2 Clinical significance
- 3 Interactions
- 4 References
- 5 Further reading
- 6 External links
|
Function [edit]
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 [edit]
Mutations in this gene cause Rubinstein-Taybi syndrome (RTS).[8] Chromosomal translocations involving this gene have been associated with acute myeloid leukemia.[6][9]
Interactions [edit]
CREB-binding protein has been shown to interact with:
- Activating transcription factor 2[10]
- Androgen receptor[11][12][13][14]
- Autoimmune regulator[15][16]
- BRCA1[17][18][19][20][21]
- BRCA2[7]
- C-jun[10]
- C-src tyrosine kinase[22]
- Casein kinase 2, alpha 1[23]
- Ccaat-enhancer-binding proteins[24]
- CDX2[25]
- CREB1[10][11][26][27][28][29][30][31][32][33]
- CSNK2A2[23]
- CUTL1[34]
- Cyclin-dependent kinase 8[35]
- EBF1[36]
- Estrogen receptor alpha[17][37]
- EVI1[38]
- FOXO1[39]
- GLI3[40]
- Glucocorticoid receptor[41]
- Hepatocyte nuclear factor 4 alpha[42][43]
- HIF1A[44][45][46]
- HIPK2[47]
- HNF1A[48]
- HOXB7[49]
- ING1[50]
- KHDRBS1[51]
- KLF13[52]
- KLF4[53]
- Ku70[54]
- MAF[55]
- MLL[32][56]
- Mothers against decapentaplegic homolog 1[57][58]
- MSX1[59]
- MYB[29][60]
- MYBL2[60]
- MyoD[61][62]
- NCOA6[63][64]
- NEUROG1[58]
- NFATC4[65]
- NFE2[66]
- NFE2L2[67]
- Nuclear receptor coactivator 1[37][68]
- Nuclear receptor coactivator 3[68][69]
- NUP98[70]
- P53[30][71][72]
- PCAF[35][73]
- POLR2A[35]
- PPARGC1A[74]
- Promyelocytic leukemia protein[75][76][77]
- PTMA[78]
- RBBP4[31]
- RELA[14][79][80][81][82]
- RPS6KA3[83]
- SERTAD1[84]
- Serum response factor[75]
- SMARCB1[35]
- SMARCA4[21][85]
- SREBF1[86]
- SREBF2[86]
- SS18L1[87]
- STAT1[88]
- STAT2[89]
- STAT6[90][91]
- TCF3[92]
- TGS1[93]
- Thymine-DNA glycosylase[73]
- Transcription Factor II B[17][73]
- TRERF1[94]
- Zif268.[95]
References [edit]
- ^ 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. Bibcode:1993Natur.365..855C. doi:10.1038/365855a0. PMID 8413673.
- ^ 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. PMID 8586450.
- ^ 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. Bibcode:2007PNAS..104.7009T. doi:10.1073/pnas.0702010104. PMC 1855428. PMID 17438265. ; Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953. ; Piskacek M (2009-11-05). "9aaTAD is a common transactivation domain recruits multiple general coactivators TAF9, MED15, CBP/p300 and GCN5". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3488.2. ; Piskacek M (2009-11-05). "9aaTADs mimic DNA to interact with a pseudo-DNA Binding Domain KIX of Med15 (Molecular Chameleons)". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3939.1. ; Piskacek M; Piskacek, Martin (2009-11-20). "9aaTAD Prediction result (2006)". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3984.1.
- ^ 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]
- ^ a b "Entrez Gene: CREBBP (CREB-binding protein)".
- ^ a b Siddique H, Rao VN, Reddy ES (Aug 2009). "CBP-mediated post-translational N-glycosylation of BRCA2". Int J Oncol. 35 (2): 16387–91. PMID 19578754.
- ^ 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. Bibcode:1995Natur.376..348P. doi:10.1038/376348a0. PMID 7630403.
- ^ 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. doi:10.1002/gcc.10174. PMID 12619164.
- ^ a b c Sano, Y; Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. (UNITED STATES) 273 (44): 29098–105. doi:10.1074/jbc.273.44.29098. ISSN 0021-9258. PMID 9786917.
- ^ a b Kim, J; Jia L, Stallcup M R, Coetzee G A (Feb. 2005). "The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus". J. Mol. Endocrinol. (England) 34 (1): 107–18. doi:10.1677/jme.1.01701. ISSN 0952-5041. PMID 15691881.
- ^ Frønsdal, K; Engedal N, Slagsvold T, Saatcioglu F (Nov. 1998). "CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1". J. Biol. Chem. (UNITED STATES) 273 (48): 31853–9. doi:10.1074/jbc.273.48.31853. ISSN 0021-9258. PMID 9822653.
- ^ Ishitani, Ken; Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki (Jul. 2003). "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. (United States) 306 (3): 660–5. doi:10.1016/S0006-291X(03)01021-0. ISSN 0006-291X. PMID 12810069.
- ^ a b Aarnisalo, P; Palvimo J J, Jänne O A (Mar. 1998). "CREB-binding protein in androgen receptor-mediated signaling". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5): 2122–7. Bibcode:1998PNAS...95.2122A. doi:10.1073/pnas.95.5.2122. ISSN 0027-8424. PMC 19270. PMID 9482849.
- ^ Pitkänen, J; Doucas V, Sternsdorf T, Nakajima T, Aratani S, Jensen K, Will H, Vähämurto P, Ollila J, Vihinen M, Scott H S, Antonarakis S E, Kudoh J, Shimizu N, Krohn K, Peterson P (Jun. 2000). "The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein". J. Biol. Chem. (UNITED STATES) 275 (22): 16802–9. doi:10.1074/jbc.M908944199. ISSN 0021-9258. PMID 10748110.
- ^ Iioka, Takashi; Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo (Aug. 2003). "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain". J. Bone Miner. Res. (United States) 18 (8): 1419–29. doi:10.1359/jbmr.2003.18.8.1419. ISSN 0884-0431. PMID 12929931.
- ^ a b c Fan, Saijun; Ma Yong Xian, Wang Chenguang, Yuan Ren-Qi, Meng Qinghui, Wang Ji-An, Erdos Michael, Goldberg Itzhak D, Webb Paul, Kushner Peter J, Pestell Richard G, Rosen Eliot M (Jan. 2002). "p300 Modulates the BRCA1 inhibition of estrogen receptor activity". Cancer Res. (United States) 62 (1): 141–51. ISSN 0008-5472. PMID 11782371.
- ^ Pao, G M; Janknecht R, Ruffner H, Hunter T, Verma I M (Feb. 2000). "CBP/p300 interact with and function as transcriptional coactivators of BRCA1". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (3): 1020–5. Bibcode:2000PNAS...97.1020P. doi:10.1073/pnas.97.3.1020. ISSN 0027-8424. PMC 15508. PMID 10655477.
- ^ Chai, Y L; Cui J, Shao N, Shyam E, Reddy P, Rao V N (Jan. 1999). "The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter". Oncogene (ENGLAND) 18 (1): 263–8. doi:10.1038/sj.onc.1202323. ISSN 0950-9232. PMID 9926942.
- ^ Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (Jul. 2003). "BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit". J. Biol. Chem. (United States) 278 (29): 26333–41. doi:10.1074/jbc.M303076200. ISSN 0021-9258. PMID 12700228.
- ^ a b Neish, A S; Anderson S F, Schlegel B P, Wei W, Parvin J D (Feb. 1998). "Factors associated with the mammalian RNA polymerase II holoenzyme". Nucleic Acids Res. (ENGLAND) 26 (3): 847–53. doi:10.1093/nar/26.3.847. ISSN 0305-1048. PMC 147327. PMID 9443979.
- ^ Kawabuchi, M; Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M (Apr. 2000). "Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases". Nature (ENGLAND) 404 (6781): 999–1003. doi:10.1038/35010121. ISSN 0028-0836. PMID 10801129.
- ^ a b Yamaguchi, Y; Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (Aug. 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. (ENGLAND) 26 (16): 3854–61. doi:10.1093/nar/26.16.3854. ISSN 0305-1048. PMC 147779. PMID 9685505.
- ^ Kovacs KA, Steinmann M; Magistretti PJ, Halfon O, Cardinaux JR (Sept. 2003). "CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation". J Biol. Chem. (UNITED STATES) 278 (38): 36959–65. doi:10.1074/jbc.M303147200. ISSN 0021-9258. PMID 12857754.
- ^ Lorentz, O; Suh E R, Taylor J K, Boudreau F, Traber P G (Mar. 1999). "CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity". J. Biol. Chem. (UNITED STATES) 274 (11): 7196–9. doi:10.1074/jbc.274.11.7196. ISSN 0021-9258. PMID 10066780. (Retracted. If this is intentional, please replace
{{Retracted}} with {{Retracted|intentional=yes}}.)
- ^ Shi, Yuling; Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S (Apr. 2004). "Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (16): 5898–903. Bibcode:2004PNAS..101.5898S. doi:10.1073/pnas.0307718101. ISSN 0027-8424. PMC 395895. PMID 15073328.
- ^ Shimomura, A; Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (Jul. 1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein". J. Biol. Chem. (UNITED STATES) 271 (30): 17957–60. doi:10.1074/jbc.271.30.17957. ISSN 0021-9258. PMID 8663317.
- ^ Radhakrishnan, I; Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. 1997). "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions". Cell (UNITED STATES) 91 (6): 741–52. doi:10.1016/S0092-8674(00)80463-8. ISSN 0092-8674. PMID 9413984.
- ^ a b Zor, Tsaffrir; Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. 2002). "Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators". J. Biol. Chem. (United States) 277 (44): 42241–8. doi:10.1074/jbc.M207361200. ISSN 0021-9258. PMID 12196545.
- ^ a b Giebler, H A; Lemasson I, Nyborg J K (Jul. 2000). "p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation". Mol. Cell. Biol. (UNITED STATES) 20 (13): 4849–58. doi:10.1128/MCB.20.13.4849-4858.2000. ISSN 0270-7306. PMC 85936. PMID 10848610.
- ^ a b Zhang, Q; Vo N, Goodman R H (Jul. 2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. (UNITED STATES) 20 (14): 4970–8. doi:10.1128/MCB.20.14.4970-4978.2000. ISSN 0270-7306. PMC 85947. PMID 10866654.
- ^ a b Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). "MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein". Mol. Cell. Biol. (United States) 21 (7): 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. ISSN 0270-7306. PMC 86859. PMID 11259575.
- ^ Ledo, Fran; Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM". EMBO J. (England) 21 (17): 4583–92. doi:10.1093/emboj/cdf440. ISSN 0261-4189. PMC 126180. PMID 12198160.
- ^ Li, S; Aufiero B, Schiltz R L, Walsh M J (Jun. 2000). "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (13): 7166–71. Bibcode:2000PNAS...97.7166L. doi:10.1073/pnas.130028697. ISSN 0027-8424. PMC 16517. PMID 10852958.
- ^ a b c d Cho, H; Orphanides G, Sun X, Yang X J, Ogryzko V, Lees E, Nakatani Y, Reinberg D (Sep. 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol. (UNITED STATES) 18 (9): 5355–63. ISSN 0270-7306. PMC 109120. PMID 9710619.
- ^ Zhao, Fang; McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom (Jun. 2003). "Inhibition of p300/CBP by early B-cell factor". Mol. Cell. Biol. (United States) 23 (11): 3837–46. doi:10.1128/MCB.23.11.3837-3846.2003. ISSN 0270-7306. PMC 155219. PMID 12748286.
- ^ a b Sheppard, H M; Harries J C, Hussain S, Bevan C, Heery D M (Jan. 2001). "Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1". Mol. Cell. Biol. (UNITED STATES) 21 (1): 39–50. doi:10.1128/MCB.21.1.39-50.2001. ISSN 0270-7306. PMC 86566. PMID 11113179.
- ^ Chakraborty, S; Senyuk V, Sitailo S, Chi Y, Nucifora G (Nov. 2001). "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles". J. Biol. Chem. (United States) 276 (48): 44936–43. doi:10.1074/jbc.M106733200. ISSN 0021-9258. PMID 11568182.
- ^ Nasrin, N; Ogg S, Cahill C M, Biggs W, Nui S, Dore J, Calvo D, Shi Y, Ruvkun G, Alexander-Bridges M C (Sep. 2000). "DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (19): 10412–7. Bibcode:2000PNAS...9710412N. doi:10.1073/pnas.190326997. ISSN 0027-8424. PMC 27038. PMID 10973497.
- ^ Dai, P; Akimaru H, Tanaka Y, Maekawa T, Nakafuku M, Ishii S (Mar. 1999). "Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3". J. Biol. Chem. (UNITED STATES) 274 (12): 8143–52. doi:10.1074/jbc.274.12.8143. ISSN 0021-9258. PMID 10075717.
- ^ Almlöf, T; Wallberg A E, Gustafsson J A, Wright A P (Jun. 1998). "Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors". Biochemistry (UNITED STATES) 37 (26): 9586–94. doi:10.1021/bi973029x. ISSN 0006-2960. PMID 9649342.
- ^ Yoshida, E; Aratani S, Itou H, Miyagishi M, Takiguchi M, Osumu T, Murakami K, Fukamizu A (Dec. 1997). "Functional association between CBP and HNF4 in trans-activation". Biochem. Biophys. Res. Commun. (UNITED STATES) 241 (3): 664–9. doi:10.1006/bbrc.1997.7871. ISSN 0006-291X. PMID 9434765.
- ^ Dell, H; Hadzopoulou-Cladaras M (Mar. 1999). "CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression". J. Biol. Chem. (UNITED STATES) 274 (13): 9013–21. doi:10.1074/jbc.274.13.9013. ISSN 0021-9258. PMID 10085149.
- ^ Ema, M; Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, Poellinger L, Fujii-Kuriyama Y (Apr. 1999). "Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300". EMBO J. (ENGLAND) 18 (7): 1905–14. doi:10.1093/emboj/18.7.1905. ISSN 0261-4189. PMC 1171276. PMID 10202154.
- ^ Bhattacharya, S; Michels C L, Leung M K, Arany Z P, Kung A L, Livingston D M (Jan. 1999). "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1". Genes Dev. (UNITED STATES) 13 (1): 64–75. doi:10.1101/gad.13.1.64. ISSN 0890-9369. PMC 316375. PMID 9887100.
- ^ Park, Young-Kwon; Ahn Dae-Ro, Oh Myoungsuk, Lee Taekyoung, Yang Eun Gyeong, Son Miwon, Park Hyunsung (Jul. 2008). "Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation". Mol. Pharmacol. (United States) 74 (1): 236–45. doi:10.1124/mol.108.045278. PMID 18426857.
- ^ Hofmann, Thomas G; Möller Andreas, Sirma Hüaeyin, Zentgraf Hanswalter, Taya Yoichi, Dröge Wulf, Will Hans, Schmitz M Lienhard (Jan. 2002). "Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2". Nat. Cell Biol. (England) 4 (1): 1–10. doi:10.1038/ncb715. ISSN 1465-7392. PMID 11740489.
- ^ Soutoglou, E; Papafotiou G, Katrakili N, Talianidis I (Apr. 2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins". J. Biol. Chem. (UNITED STATES) 275 (17): 12515–20. doi:10.1074/jbc.275.17.12515. ISSN 0021-9258. PMID 10777539.
- ^ Chariot, A; van Lint C, Chapelier M, Gielen J, Merville M P, Bours V (Jul. 1999). "CBP and histone deacetylase inhibition enhance the transactivation potential of the HOXB7 homeodomain-containing protein". Oncogene (ENGLAND) 18 (27): 4007–14. doi:10.1038/sj.onc.1202776. ISSN 0950-9232. PMID 10435624.
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- ^ Kasper, L H; Brindle P K, Schnabel C A, Pritchard C E, Cleary M L, van Deursen J M (Jan. 1999). "CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity". Mol. Cell. Biol. (UNITED STATES) 19 (1): 764–76. ISSN 0270-7306. PMC 83933. PMID 9858599.
- ^ Ito, Akihiro; Kawaguchi Yoshiharu, Lai Chun-Hsiang, Kovacs Jeffrey J, Higashimoto Yuichiro, Appella Ettore, Yao Tso-Pang (Nov. 2002). "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". EMBO J. (England) 21 (22): 6236–45. doi:10.1093/emboj/cdf616. ISSN 0261-4189. PMC 137207. PMID 12426395.
- ^ Livengood, Jill A; Scoggin Kirsten E S, Van Orden Karen, McBryant Steven J, Edayathumangalam Rajeswari S, Laybourn Paul J, Nyborg Jennifer K (Mar. 2002). "p53 Transcriptional activity is mediated through the SRC1-interacting domain of CBP/p300". J. Biol. Chem. (United States) 277 (11): 9054–61. doi:10.1074/jbc.M108870200. ISSN 0021-9258. PMID 11782467.
- ^ a b c Tini, Marc; Benecke Arndt, Um Soo-Joong, Torchia Joseph, Evans Ronald M, Chambon Pierre (Feb. 2002). "Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription". Mol. Cell (United States) 9 (2): 265–77. doi:10.1016/S1097-2765(02)00453-7. ISSN 1097-2765. PMID 11864601.
- ^ Puigserver, P; Adelmant G, Wu Z, Fan M, Xu J, O'Malley B, Spiegelman B M (Nov. 1999). "Activation of PPARgamma coactivator-1 through transcription factor docking". Science (UNITED STATES) 286 (5443): 1368–71. doi:10.1126/science.286.5443.1368. ISSN 0036-8075. PMID 10558993.
- ^ a b Matsuzaki, Kazuhito; Minami Takeshi, Tojo Masahide, Honda Yoshiomi, Saitoh Noriko, Nagahiro Shinji, Saya Hideyuki, Nakao Mitsuyoshi (Mar. 2003). "PML-nuclear bodies are involved in cellular serum response". Genes Cells (England) 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. ISSN 1356-9597. PMID 12622724.
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- ^ Karetsou, Zoe; Kretsovali Adroniki, Murphy Carol, Tsolas Orestes, Papamarcaki Thomais (Apr. 2002). "Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription". EMBO Rep. (England) 3 (4): 361–6. doi:10.1093/embo-reports/kvf071. ISSN 1469-221X. PMC 1084059. PMID 11897665.
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- ^ Merienne, K; Pannetier S, Harel-Bellan A, Sassone-Corsi P (Oct. 2001). "Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities". Mol. Cell. Biol. (United States) 21 (20): 7089–96. doi:10.1128/MCB.21.20.7089-7096.2001. ISSN 0270-7306. PMC 99884. PMID 11564891.
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- ^ Zhang, J J; Vinkemeier U, Gu W, Chakravarti D, Horvath C M, Darnell J E (Dec. 1996). "Two contact regions between Stat1 and CBP/p300 in interferon gamma signaling". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 93 (26): 15092–6. Bibcode:1996PNAS...9315092Z. doi:10.1073/pnas.93.26.15092. ISSN 0027-8424. PMC 26361. PMID 8986769.
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Further reading [edit]
- 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. doi:10.1080/152165401753544241. 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. doi:10.1046/j.1563-2571.2002.02010.x. 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. doi:10.1023/B:NERE.0000021241.90133.89. 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. doi:10.1002/0470862637.ch15. 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. doi:10.2174/1570162052772924. 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. PMC 554975. 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. doi:10.2741/1829. PMID 16146763.
External links [edit]
- 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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PDB gallery
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1f81: SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP
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1jjs: NMR Structure of IBiD, A Domain of CBP/p300
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1jsp: NMR Structure of CBP Bromodomain in complex with p53 peptide
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1kbh: Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR
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1kdx: KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES
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1l3e: NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex
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1l8c: STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THE CELLULAR HYPOXIC RESPONSE
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1liq: Non-native Solution Structure of a fragment of the CH1 domain of CBP
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1p4q: Solution structure of the CITED2 transactivation domain in complex with the p300 CH1 domain
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1r8u: NMR structure of CBP TAZ1/CITED2 complex
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1sb0: Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb
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1u2n: Structure CBP TAZ1 Domain
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2agh: Structural basis for cooperative transcription factor binding to the CBP coactivator
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2c52: STRUCTURAL DIVERSITY IN CBP P160 COMPLEXES
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2d82: Target Structure-Based Discovery of Small Molecules that Block Human p53 and CREB Binding Protein (CBP) Association
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Transcription coregulators
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| Coactivators |
- ARA (54, 55, 70)
- BCAS3
- CARM1
- p300-CBP (EP300, CREBBP)
- CRTC (1, 2, 3)
- DRIP/TRAP
- MN1
- PCAF
- PNRC (1, 2)
- PPARGC (1A, 1B)
- TGFB1I1
NCOA1 (SRC-1)
- NCOA2 (GRIP1/SRC-2/TIF2)
- NCOA3 (AIB/SRC-3/TRAM-1)
- NCOA4 (ARA70)
- NCOA5 (CIA)
- NCOA6 (RAP250)
- NCOA7 (ERAP140)
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| Corepressors |
- CTBP (1, 2)
- Hairless homolog
- LCOR
- NRIP1 (RIP140)
- PELP-1
- RCOR1
- Rb
- SIN3A
- SIN3B
- Tripartite motif family TRIM (24, 28, 33)
NCOR1
- NCOR2 (SMRT)
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| ATP-dependent remodeling factors |
- Chromatin Structure Remodeling (RSC) Complex
- SWI/SNF
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see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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- Qiu X1, Cheng JC1, Chang HM1, Leung PC2.
- Endocrine-related cancer.Endocr Relat Cancer.2014 Aug;21(4):533-43. doi: 10.1530/ERC-13-0450.
- Elevated expression of cyclooxygenase 2 (COX2 (PTGS2)) has been reported to occur in human ovarian cancer and to be associated with poor prognosis. We have previously demonstrated that COX2-derived prostaglandin E2 (PGE2) promotes human ovarian cancer cell invasion. We had also demonstrated that epi
- PMID 24969217
- Mechanism of raloxifene-induced upregulation of glutamate transporters in rat primary astrocytes.
- Karki P1, Webb A, Zerguine A, Choi J, Son DS, Lee E.
- Glia.Glia.2014 Aug;62(8):1270-83. doi: 10.1002/glia.22679. Epub 2014 Apr 29.
- Raloxifene (RX), a selective estrogen receptor modulator (SERM), exerts neuroprotection in multiple clinical and experimental settings. Astrocytic glutamate transporters GLT-1 (EAAT2) and GLAST (EAAT1) are the main glutamate transporters in the central nervous system, taking up most of excess glutam
- PMID 24782323
Japanese Journal
- CREB-binding protein transcription activation domain for enhanced transgene expression by a positive feedback system
- Kanda Genki,Ochiai Hiroshi,Harashima Hideyoshi,Kamiya Hiroyuki
- Journal of Biotechnology 157(1), 7-11, 2012-01
- … The positive feedback system using a fusion protein of the sequence-specific DNA binding domain of yeast GAL4 and the transcription activation domain of herpes simplex virus VP16 (GAL4-VP16), in which GAL4-VP16 promotes its own expression as well as that of a reporter gene product, is useful for efficient transgene expression from plasmid DNA. …
- NAID 120003811532
- c-Maf suppresses human T-cell leukemia virus type 1 Tax by competing for CREB-binding protein
- HIESHIMA Kunio,NAGAKUBO Daisuke,SHIGETA Akiko,TANAKA Yuetsu,HOSHINO Hiroo,TSUKASAKI Kunihiro,YAMADA Yasuaki,YOSHIE Osamu
- Cancer science 102(4), 890-894, 2011-04-10
- NAID 10029292861
Related Links
- CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene. The CREB protein carries out its function by activating transcription, where interaction with transcription factors is managed ...
- The CREBBP gene provides instructions for making CREB binding protein, which regulates the activity of many genes in tissues throughout the body. This protein plays an essential role in controlling cell growth and division and prompting ...
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