CREBBP

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Proteína de unión a CREB

Estructura tridimensional de la proteína CREBBP.
Estructuras disponibles
PDB

Buscar ortólogos: PDBe, RCSB PDBe, RCSB

 Lista de códigos PDB
1JSP , 1LIQ , 1RDT , 1WO3 , 1WO4 , 1WO5 , 1WO6 , 1WO7 , 2D82 , 2KJE , 2KWF , 2L84 , 2L85 , 2LXS , 2LXT , 2RNY , 3DWY , 3P1C , 3P1D , 3P1E , 3P1F , 3SVH , 4A9K
 Estructuras enzimáticas
Identificadores
Símbolos CREBBP (HGNC: 2348) CBP; RSTS; RTS
Identificadores
externos
Número EC 2.3.1.48
Locus Cr. 16 p13.3
Patrón de expresión de ARNm
ancho=250px
ancho=250px
Más información
Ortólogos
Especies
Humano Ratón
Entrez
1387 12914
Ensembl
Véase HS Véase MM
UniProt
Q92793 F8VPR5
RefSeq
(ARNm)
NM_001079846 NM_001025432
RefSeq
(proteína) NCBI
NP_001073315 NP_001020603
Ubicación (UCSC)
Cr. 16:
3.78 – 3.93 Mb
Cr. 16:
4.08 – 4.21 Mb
PubMed (Búsqueda)
[1]


[2]

La proteína de unión a CREB, también conocido como CREBBP o CBP es una proteína codificada en humanos por el gen CREBBP.[1][2]

Función

Este gen es expresado ubicuamente y está implicado en la co-activación transcripcional de diversos factores de transcripción. El primero fue aislado como una proteína nuclear que se une a proteínas de unión a elementos de respuesta a AMPc (CREB). Este gen es conocido por jugar un papel crítico en el desarrollo embrionario, el control de la proliferación celular y la homeostasis por medio de la reorganización de la cromatina para el reconocimiento de los factores de transcripción. Esta proteína posee una actividad histona acetiltransferasa intrínseca y actúa a su vez como andamio para estabilizar interacciones de proteínas adicionales con el complejo transcripcional. Esta proteína acetila tanto a histonas como a proteínas no histonas. Las CREBBP comparten regiones de una elevada similitud de secuencia con el bromodominio, las regiones ricas en cisteína-histidina y el dominio histona acetiltransferasa de la proteína EP300.[3]

Importancia clínica

Mutaciones en este gen son las causantes del síndrome de Rubinstein-Taybi (RTS).[4]​ Se han asociado diversas traslocaciones cromosómicas de este gen con la leucemia mieloide aguda.[3][5]

Interacciones

La proteína CREBBP ha demostrado ser capaz de interaccionar con:

Véase también

Referencias

  1. Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH (octubre de 1993). «Phosphorylated CREB binds specifically to the nuclear protein CBP». Nature 365 (6449): 855-9. PMID 8413673. doi:10.1038/365855a0. 
  2. Wydner KL, Bhattacharya S, Eckner R, Lawrence JB, Livingston DM (noviembre de 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. 
  3. a b «Entrez Gene: CREBBP (CREB-binding protein)». 
  4. Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ (julio de 1995). «Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP». Nature 376 (6538): 348-51. PMID 7630403. doi:10.1038/376348a0. 
  5. Vizmanos JL, Larráyoz MJ, Lahortiga I, Floristán F, Alvarez C, Odero MD, Novo FJ, Calasanz MJ (abril de 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. PMID 12619164. doi:10.1002/gcc.10174. 
  6. a b c Sano, Y; Tokitou F; Dai P; Maekawa T; Yamamoto T; Ishii S (Oct. de 1998). «CBP alleviates the intramolecular inhibition of ATF-2 function». J. Biol. Chem. (UNITED STATES) 273 (44): 29098-105. ISSN 0021-9258. PMID 9786917. doi:10.1074/jbc.273.44.29098. 
  7. a b Kim, J; Jia L, Stallcup M R, Coetzee G A (Feb. de 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. ISSN 0952-5041. PMID 15691881. doi:10.1677/jme.1.01701. 
  8. Frønsdal, K; Engedal N; Slagsvold T; Saatcioglu F (Nov. de 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. ISSN 0021-9258. PMID 9822653. doi:10.1074/jbc.273.48.31853. 
  9. Ishitani, Ken; Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki (Jul. de 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. ISSN 0006-291X. PMID 12810069. doi:10.1016/S0006-291X(03)01021-0. 
  10. a b Aarnisalo, P; Palvimo J J, Jänne O A (Mar. de 1998). «CREB-binding protein in androgen receptor-mediated signaling». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5): 2122-7. ISSN 0027-8424. PMC 19270. PMID 9482849. doi:10.1073/pnas.95.5.2122. 
  11. 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. de 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. ISSN 0021-9258. PMID 10748110. doi:10.1074/jbc.M908944199. 
  12. Iioka, Takashi; Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo (Aug. de 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. ISSN 0884-0431. PMID 12929931. doi:10.1359/jbmr.2003.18.8.1419. 
  13. 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. de 2002). «p300 Modulates the BRCA1 inhibition of estrogen receptor activity». Cancer Res. (United States) 62 (1): 141-51. ISSN 0008-5472. PMID 11782371. 
  14. Pao, G M; Janknecht R, Ruffner H, Hunter T, Verma I M (Feb. de 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. ISSN 0027-8424. PMC 15508. PMID 10655477. doi:10.1073/pnas.97.3.1020. 
  15. Chai, Y L; Cui J, Shao N, Shyam E, Reddy P, Rao V N (Jan. de 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. ISSN 0950-9232. PMID 9926942. doi:10.1038/sj.onc.1202323. 
  16. Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (Jul. de 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. ISSN 0021-9258. PMID 12700228. doi:10.1074/jbc.M303076200. 
  17. a b Neish, A S; Anderson S F, Schlegel B P, Wei W, Parvin J D (Feb. de 1998). «Factors associated with the mammalian RNA polymerase II holoenzyme». Nucleic Acids Res. (ENGLAND) 26 (3): 847-53. ISSN 0305-1048. PMC 147327. PMID 9443979. doi:10.1093/nar/26.3.847. 
  18. Kawabuchi, M; Satomi Y; Takao T; Shimonishi Y; Nada S; Nagai K; Tarakhovsky A; Okada M (Apr. de 2000). «Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases». Nature (ENGLAND) 404 (6781): 999-1003. ISSN 0028-0836. PMID 10801129. doi:10.1038/35010121. 
  19. a b Yamaguchi, Y; Wada T; Suzuki F; Takagi T; Hasegawa J; Handa H (Aug. de 1998). «Casein kinase II interacts with the bZIP domains of several transcription factors». Nucleic Acids Res. (ENGLAND) 26 (16): 3854-61. ISSN 0305-1048. PMC 147779. PMID 9685505. doi:10.1093/nar/26.16.3854. 
  20. Kovacs KA, Steinmann M; Magistretti PJ; Halfon O; Cardinaux JR (Sept. de 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. ISSN 0021-9258. PMID 12857754. doi:10.1074/jbc.M303147200. 
  21. Lorentz, O; Suh E R, Taylor J K, Boudreau F, Traber P G (Mar. de 1999). «CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity». J. Biol. Chem. (UNITED STATES) 274 (11): 7196-9. ISSN 0021-9258. PMID 10066780. doi:10.1074/jbc.274.11.7196. 
  22. Shi, Yuling; Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S (Apr. de 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. ISSN 0027-8424. PMC 395895. PMID 15073328. doi:10.1073/pnas.0307718101. 
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  24. Radhakrishnan, I; Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. de 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. ISSN 0092-8674. PMID 9413984. doi:10.1016/S0092-8674(00)80463-8. 
  25. a b Zor, Tsaffrir; Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. de 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. ISSN 0021-9258. PMID 12196545. doi:10.1074/jbc.M207361200. 
  26. a b Giebler, H A; Lemasson I, Nyborg J K (Jul. de 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. ISSN 0270-7306. PMC 85936. PMID 10848610. doi:10.1128/MCB.20.13.4849-4858.2000. 
  27. a b Zhang, Q; Vo N, Goodman R H (Jul. de 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. ISSN 0270-7306. PMC 85947. PMID 10866654. doi:10.1128/MCB.20.14.4970-4978.2000. 
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  29. Ledo, Fran; Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. de 2002). «Ca2+-dependent block of CREB-CBP transcription by repressor DREAM». EMBO J. (England) 21 (17): 4583-92. ISSN 0261-4189. PMC 126180. PMID 12198160. doi:10.1093/emboj/cdf440. 
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