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
RCSB PDB, PDBe, PDBsum
Identificadores
Símbolos CREBBP (HGNC: 2348) CBP; RSTS; RTS
Identificadores
externos
 Bases de datos de enzimas
IntEnz: entrada en IntEnz
BRENDA: entrada en BRENDA
ExPASy: NiceZime view
KEGG: entrada en KEEG
PRIAM: perfil PRIAM
ExplorEnz: entrada en ExplorEnz
MetaCyc: vía metabólica
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]
[editar datos en Wikidata]

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[editar]

Este gen esta 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[editar]

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[editar]

La proteína CREBBP ha demostrado ser capaz de interaccionar con:

Véase también[editar]

Referencias[editar]

  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. 
  23. ↑ Shimomura, A; Ogawa Y; Kitani T; Fujisawa H; Hagiwara M (Jul. de 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. ISSN 0021-9258. PMID 8663317. doi:10.1074/jbc.271.30.17957. 
  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. 
  28. ↑ a b Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. de 2001). «MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein». Mol. Cell. Biol. (United States) 21 (7): 2249-58. ISSN 0270-7306. PMC 86859. PMID 11259575. doi:10.1128/MCB.21.7.2249-2258.2001. 
  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. 
  30. ↑ Li, S; Aufiero B, Schiltz R L, Walsh M J (Jun. de 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. ISSN 0027-8424. PMC 16517. PMID 10852958. doi:10.1073/pnas.130028697. 
  31. ↑ a b c d Cho, H; Orphanides G, Sun X, Yang X J, Ogryzko V, Lees E, Nakatani Y, Reinberg D (Sep. de 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. 
  32. ↑ Zhao, Fang; McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom (Jun. de 2003). «Inhibition of p300/CBP by early B-cell factor». Mol. Cell. Biol. (United States) 23 (11): 3837-46. ISSN 0270-7306. PMC 155219. PMID 12748286. doi:10.1128/MCB.23.11.3837-3846.2003. 
  33. ↑ a b Sheppard, H M; Harries J C, Hussain S, Bevan C, Heery D M (Jan. de 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. ISSN 0270-7306. PMC 86566. PMID 11113179. doi:10.1128/MCB.21.1.39-50.2001. 
  34. ↑ Chakraborty, S; Senyuk V; Sitailo S; Chi Y; Nucifora G (Nov. de 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. ISSN 0021-9258. PMID 11568182. doi:10.1074/jbc.M106733200. 
  35. ↑ Nasrin, N; Ogg S, Cahill C M, Biggs W, Nui S, Dore J, Calvo D, Shi Y, Ruvkun G, Alexander-Bridges M C (Sep. de 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. ISSN 0027-8424. PMC 27038. PMID 10973497. doi:10.1073/pnas.190326997. 
  36. ↑ Dai, P; Akimaru H; Tanaka Y; Maekawa T; Nakafuku M; Ishii S (Mar. de 1999). «Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3». J. Biol. Chem. (UNITED STATES) 274 (12): 8143-52. ISSN 0021-9258. PMID 10075717. doi:10.1074/jbc.274.12.8143. 
  37. ↑ Almlöf, T; Wallberg A E, Gustafsson J A, Wright A P (Jun. de 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. ISSN 0006-2960. PMID 9649342. doi:10.1021/bi973029x. 
  38. ↑ Yoshida, E; Aratani S; Itou H; Miyagishi M; Takiguchi M; Osumu T; Murakami K; Fukamizu A (Dec. de 1997). «Functional association between CBP and HNF4 in trans-activation». Biochem. Biophys. Res. Commun. (UNITED STATES) 241 (3): 664-9. ISSN 0006-291X. PMID 9434765. doi:10.1006/bbrc.1997.7871. 
  39. ↑ Dell, H; Hadzopoulou-Cladaras M (Mar. de 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. ISSN 0021-9258. PMID 10085149. doi:10.1074/jbc.274.13.9013. 
  40. ↑ Ema, M; Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, Poellinger L, Fujii-Kuriyama Y (Apr. de 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. ISSN 0261-4189. PMC 1171276. PMID 10202154. doi:10.1093/emboj/18.7.1905. 
  41. ↑ Bhattacharya, S; Michels C L, Leung M K, Arany Z P, Kung A L, Livingston D M (Jan. de 1999). «Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1». Genes Dev. (UNITED STATES) 13 (1): 64-75. ISSN 0890-9369. PMC 316375. PMID 9887100. doi:10.1101/gad.13.1.64. 
  42. ↑ Park, Young-Kwon; Ahn Dae-Ro, Oh Myoungsuk, Lee Taekyoung, Yang Eun Gyeong, Son Miwon, Park Hyunsung (Jul. de 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. PMID 18426857. doi:10.1124/mol.108.045278. 
  43. ↑ Hofmann, Thomas G; Möller Andreas, Sirma Hüaeyin, Zentgraf Hanswalter, Taya Yoichi, Dröge Wulf, Will Hans, Schmitz M Lienhard (Jan. de 2002). «Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2». Nat. Cell Biol. (England) 4 (1): 1-10. ISSN 1465-7392. PMID 11740489. doi:10.1038/ncb715. 
  44. ↑ Soutoglou, E; Papafotiou G; Katrakili N; Talianidis I (Apr. de 2000). «Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins». J. Biol. Chem. (UNITED STATES) 275 (17): 12515-20. ISSN 0021-9258. PMID 10777539. doi:10.1074/jbc.275.17.12515. 
  45. ↑ Chariot, A; van Lint C, Chapelier M, Gielen J, Merville M P, Bours V (Jul. de 1999). «CBP and histone deacetylase inhibition enhance the transactivation potential of the HOXB7 homeodomain-containing protein». Oncogene (ENGLAND) 18 (27): 4007-14. ISSN 0950-9232. PMID 10435624. doi:10.1038/sj.onc.1202776. 
  46. ↑ Vieyra, Diego; Loewith Robbie, Scott Michelle, Bonnefin Paul, Boisvert Francois-Michel, Cheema Parneet, Pastyryeva Svitlana, Meijer Maria, Johnston Randal N, Bazett-Jones David P, McMahon Steven, Cole Michael D, Young Dallan, Riabowol Karl (Aug. de 2002). «Human ING1 proteins differentially regulate histone acetylation». J. Biol. Chem. (United States) 277 (33): 29832-9. ISSN 0021-9258. PMID 12015309. doi:10.1074/jbc.M200197200. 
  47. ↑ Hong, Wei; Resnick Ross J, Rakowski Carrie, Shalloway David, Taylor Steven J, Blobel Gerd A (Nov. de 2002). «Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68». Mol. Cancer Res. (United States) 1 (1): 48-55. ISSN 1541-7786. PMID 12496368. 
  48. ↑ Song, Chao-Zhong; Keller Kimberly, Murata Ken, Asano Haruhiko, Stamatoyannopoulos George (Mar. de 2002). «Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2». J. Biol. Chem. (United States) 277 (9): 7029-36. ISSN 0021-9258. PMC 2808425. PMID 11748222. doi:10.1074/jbc.M108826200. 
  49. ↑ Geiman, D E; Ton-That H, Johnson J M, Yang V W (Mar. de 2000). «Transactivation and growth suppression by the gut-enriched Krüppel-like factor (Krüppel-like factor 4) are dependent on acidic amino acid residues and protein-protein interaction». Nucleic Acids Res. (ENGLAND) 28 (5): 1106-13. PMC 102607. PMID 10666450. doi:10.1093/nar/28.5.1106. 
  50. ↑ Barlev, N A; Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman J L, Berger S L (Mar. de 1998). «Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex». Mol. Cell. Biol. (UNITED STATES) 18 (3): 1349-58. ISSN 0270-7306. PMC 108848. PMID 9488450. 
  51. ↑ Chen, Qin; Dowhan Dennis H, Liang Dongcai, Moore David D, Overbeek Paul A (Jul. de 2002). «CREB-binding protein/p300 co-activation of crystallin gene expression». J. Biol. Chem. (United States) 277 (27): 24081-9. ISSN 0021-9258. PMID 11943779. doi:10.1074/jbc.M201821200. 
  52. ↑ Goto, Natalie K; Zor Tsaffrir, Martinez-Yamout Maria, Dyson H Jane, Wright Peter E (Nov. de 2002). «Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain». J. Biol. Chem. (United States) 277 (45): 43168-74. ISSN 0021-9258. PMID 12205094. doi:10.1074/jbc.M207660200. 
  53. ↑ Pearson, K L; Hunter T; Janknecht R (Dec. de 1999). «Activation of Smad1-mediated transcription by p300/CBP». Biochim. Biophys. Acta (NETHERLANDS) 1489 (2-3): 354-64. ISSN 0006-3002. PMID 10673036. 
  54. ↑ a b Sun, Y; Nadal-Vicens M, Misono S, Lin M Z, Zubiaga A, Hua X, Fan G, Greenberg M E (Feb. de 2001). «Neurogenin promotes neurogenesis and inhibits glial differentiation by independent mechanisms». Cell (United States) 104 (3): 365-76. ISSN 0092-8674. PMID 11239394. doi:10.1016/S0092-8674(01)00224-0. 
  55. ↑ Shetty, S; Takahashi T; Matsui H; Ayengar R; Raghow R (mayo. de 1999). «Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300)». Biochem. J. (ENGLAND). 339 ( Pt 3): 751-8. ISSN 0264-6021. PMC 1220213. PMID 10215616. doi:10.1042/0264-6021:3390751. 
  56. ↑ a b Bessa, M; Saville M K, Watson R J (Jun. de 2001). «Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator». Oncogene (England) 20 (26): 3376-86. ISSN 0950-9232. PMID 11423988. doi:10.1038/sj.onc.1204439. 
  57. ↑ Polesskaya, A; Naguibneva I, Duquet A, Bengal E, Robin P, Harel-Bellan A (Aug. de 2001). «Interaction between acetylated MyoD and the bromodomain of CBP and/or p300». Mol. Cell. Biol. (United States) 21 (16): 5312-20. ISSN 0270-7306. PMC 87255. PMID 11463815. doi:10.1128/MCB.21.16.5312-5320.2001. 
  58. ↑ Sartorelli, V; Huang J; Hamamori Y; Kedes L (Feb. de 1997). «Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C». Mol. Cell. Biol. (UNITED STATES) 17 (2): 1010-26. ISSN 0270-7306. PMC 231826. PMID 9001254. 
  59. ↑ Lee, S K; Anzick S L, Choi J E, Bubendorf L, Guan X Y, Jung Y K, Kallioniemi O P, Kononen J, Trent J M, Azorsa D, Jhun B H, Cheong J H, Lee Y C, Meltzer P S, Lee J W (Nov. de 1999). «A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo». J. Biol. Chem. (UNITED STATES) 274 (48): 34283-93. ISSN 0021-9258. PMID 10567404. doi:10.1074/jbc.274.48.34283. 
  60. ↑ Lee, S K; Jung S Y, Kim Y S, Na S Y, Lee Y C, Lee J W (Feb. de 2001). «Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2». Mol. Endocrinol. (United States) 15 (2): 241-54. ISSN 0888-8809. PMID 11158331. doi:10.1210/me.15.2.241. 
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