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Sp1

De Wikipedia, la enciclopedia libre
Factor de transcripción Sp1

Estructura tridimensional de la proteína Sp1.
Estructuras disponibles
PDB

Buscar ortólogos: PDBe, RCSB

 Lista de códigos PDB
1sp1
Identificadores
Símbolo Sp1 (HGNC: 11205)
Identificadores
externos
Locus Cr. 12 q13.13
Ortólogos
Especies
Humano Ratón
Entrez
6667
UniProt
P08047 n/a
RefSeq
(ARNm)
NP_612482 n/a
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Sp1 es un factor de transcripción humano implicado en la expresión génica que tiene lugar durante el desarrollo temprano de un organismo. Sp1 pertenece a la familia de factores de transcripción Sp/KLF. Esta proteína tiene 785 aminoácidos y un peso molecular de 81 kDa.[1]​ La secuencia completa de la proteína puede ser encontrada en la página del NCBI, con el número de acceso NP_612482. Sp1 contiene un motivo de dedos de zinc mediante el cual se une directamente al ADN y favorece la transcripción. Sus dedos de zinc son del tipo Cys2/His2 y reconocen la secuencia consenso 5'-(G/T)GGGCGG(G/A)(G/A)(C/T)-3' (elemento GC). Fue descubierto en 1983 y ha sido modificado desde entonces para formar Sp1C, que tiene un dominio de unión a ADN del tipo dedos de zinc. En el virus SV40, Sp1 se une a las cajas GC en la región reguladora (RR) del genoma.

Sp1 ha sido utilizado en diversos estudios como proteína control para comparar con los niveles aumentados o disminuidos de receptor de aril hidrocarburos y/o de receptor de estrógeno, debido a que se une a ambos y generalmente se mantiene a un nivel constante.[2]​

Interacciones

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La proteína Sp1 ha demostrado ser capaz de interaccionar con:

Referencias

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  1. ↑ véase UniProtKB
  2. ↑ The Aryl Hydrocarbon Receptor Mediates Degradation of Estrogen Receptor αあるふぁ through Activation of Proteasomes. Mark Wormke, Matthew Stoner, Bradley Saville, Kelcey Walker, Maen Abdelrahim, Robert Burghardt, and Stephen Safe. Molecular and Cellular Biology, March 2003, p. 1843-1855, Vol. 23, No. 6. DOI: 10.1128/MCB.23.6.1843-1855.2003
  3. ↑ Krainc, D; Bai G, Okamoto S, Carles M, Kusiak J W, Brent R N, Lipton S A (Oct. de 1998). «Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1». J. Biol. Chem. (UNITED STATES) 273 (40): 26218-24. ISSN 0021-9258. PMID 9748305. 
  4. ↑ Park, So-Youn; Shin Hyun-Mu, Han Tae-Hee (Sep. de 2002). «Synergistic interaction of MEF2D and Sp1 in activation of the CD14 promoter». Mol. Immunol. (England) 39 (1-2): 25-30. ISSN 0161-5890. PMID 12213324. 
  5. ↑ Lin, S Y; Black A R, Kostic D, Pajovic S, Hoover C N, Azizkhan J C (Apr. de 1996). «Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction». Mol. Cell. Biol. (UNITED STATES) 16 (4): 1668-75. ISSN 0270-7306. PMID 8657142. 
  6. ↑ Rotheneder, H; Geymayer S; Haidweger E (Nov. de 1999). «Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter». J. Mol. Biol. (ENGLAND) 293 (5): 1005-15. ISSN 0022-2836. PMID 10547281. doi:10.1006/jmbi.1999.3213. 
  7. ↑ Karlseder, J; Rotheneder H; Wintersberger E (Apr. de 1996). «Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F». Mol. Cell. Biol. (UNITED STATES) 16 (4): 1659-67. ISSN 0270-7306. PMID 8657141. 
  8. ↑ Ström, A C; Forsberg M; Lillhager P; Westin G (Jun. de 1996). «The transcription factors Sp1 and Oct-1 interact physically to regulate human U2 snRNA gene expression». Nucleic Acids Res. (ENGLAND) 24 (11): 1981-6. ISSN 0305-1048. PMID 8668525. 
  9. ↑ a b Gunther, M; Laithier M; Brison O (Jul. de 2000). «A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening». Mol. Cell. Biochem. (NETHERLANDS) 210 (1-2): 131-42. ISSN 0300-8177. PMID 10976766. 
  10. ↑ Wysocka, Joanna; Myers Michael P, Laherty Carol D, Eisenman Robert N, Herr Winship (Apr. de 2003). «Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1». Genes Dev. (United States) 17 (7): 896-911. ISSN 0890-9369. PMID 12670868. doi:10.1101/gad.252103. 
  11. ↑ Kuang, Ping-Ping; Berk John L, Rishikof David C, Foster Judith A, Humphries Donald E, Ricupero Dennis A, Goldstein Ronald H (Jul. de 2002). «NF-kappaB induced by IL-1beta inhibits elastin transcription and myofibroblast phenotype». Am. J. Physiol., Cell Physiol. (United States) 283 (1): C58-65. ISSN 0363-6143. PMID 12055073. doi:10.1152/ajpcell.00314.2001. 
  12. ↑ Sif, S; Gilmore T D (Nov. de 1994). «Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1». J. Virol. (UNITED STATES) 68 (11): 7131-8. ISSN 0022-538X. PMID 7933095. 
  13. ↑ Liu, Yi-Wen; Tseng Hui-Ping, Chen Lei-Chin, Chen Ben-Kuen, Chang Wen-Chang (Jul. de 2003). «Functional cooperation of simian virus 40 promoter factor 1 and CCAAT/enhancer-binding protein beta and delta in lipopolysaccharide-induced gene activation of IL-10 in mouse macrophages». J. Immunol. (United States) 171 (2): 821-8. ISSN 0022-1767. PMID 12847250. 
  14. ↑ a b Foti, Daniela; Iuliano Rodolfo, Chiefari Eusebio, Brunetti Antonio (Apr. de 2003). «A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription». Mol. Cell. Biol. (United States) 23 (8): 2720-32. ISSN 0270-7306. PMID 12665574. 
  15. ↑ 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. PMID 10215616. 
  16. ↑ Galvagni, F; Capo S; Oliviero S (Mar. de 2001). «Sp1 and Sp3 physically interact and co-operate with GABP for the activation of the utrophin promoter». J. Mol. Biol. (England) 306 (5): 985-96. ISSN 0022-2836. PMID 11237613. doi:10.1006/jmbi.2000.4335. 
  17. ↑ a b c Wang, Yi-Ting; Chuang Jian-Ying, Shen Meng-Ru, Yang Wen-Bin, Chang Wen-Chang, Hung Jan-Jong (Jul. de 2008). «Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process». J. Mol. Biol. (England) 380 (5): 869-85. PMID 18572193. doi:10.1016/j.jmb.2008.05.043. 
  18. ↑ Botella, L M; Sánchez-Elsner T, Rius C, Corbí A, Bernabéu C (Sep. de 2001). «Identification of a critical Sp1 site within the endoglin promoter and its involvement in the transforming growth factor-beta stimulation». J. Biol. Chem. (United States) 276 (37): 34486-94. ISSN 0021-9258. PMID 11432852. doi:10.1074/jbc.M011611200. 
  19. ↑ Poncelet, A C; Schnaper H W (Mar. de 2001). «Sp1 and Smad proteins cooperate to mediate transforming growth factor-beta 1-induced alpha 2(I) collagen expression in human glomerular mesangial cells». J. Biol. Chem. (United States) 276 (10): 6983-92. ISSN 0021-9258. PMID 11114293. doi:10.1074/jbc.M006442200. 
  20. ↑ a b Di Padova, Monica; Bruno Tiziana, De Nicola Francesca, Iezzi Simona, D'Angelo Carmen, Gallo Rita, Nicosia Daniela, Corbi Nicoletta, Biroccio Annamaria, Floridi Aristide, Passananti Claudio, Fanciulli Maurizio (Sep. de 2003). «Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter». J. Biol. Chem. (United States) 278 (38): 36496-504. ISSN 0021-9258. PMID 12847090. doi:10.1074/jbc.M306694200. 
  21. ↑ Singh, Jarnail; Murata Kenji, Itahana Yoko, Desprez Pierre-Yves (Mar. de 2002). «Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex». Oncogene (England) 21 (12): 1812-22. ISSN 0950-9232. PMID 11896613. doi:10.1038/sj.onc.1205252. 
  22. ↑ a b Zhang, Ying; Dufau Maria L (Sep. de 2002). «Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex». J. Biol. Chem. (United States) 277 (36): 33431-8. ISSN 0021-9258. PMID 12091390. doi:10.1074/jbc.M204417200. 
  23. ↑ a b Sun, Jian-Min; Chen Hou Yu, Moniwa Mariko, Litchfield David W, Seto Edward, Davie James R (Sep. de 2002). «The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2». J. Biol. Chem. (United States) 277 (39): 35783-6. ISSN 0021-9258. PMID 12176973. doi:10.1074/jbc.C200378200. 
  24. ↑ Won, Jaejoon; Yim Jeongbin, Kim Tae Kook (Oct. de 2002). «Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells». J. Biol. Chem. (United States) 277 (41): 38230-8. ISSN 0021-9258. PMID 12151407. doi:10.1074/jbc.M206064200. 
  25. ↑ Li, Shi-Hua; Cheng Anna L, Zhou Hui, Lam Suzanne, Rao Manjula, Li He, Li Xiao-Jiang (Mar. de 2002). «Interaction of Huntington disease protein with transcriptional activator Sp1». Mol. Cell. Biol. (United States) 22 (5): 1277-87. ISSN 0270-7306. PMID 11839795. 
  26. ↑ Botella, Luisa M; Sánchez-Elsner Tilman, Sanz-Rodriguez Francisco, Kojima Soichi, Shimada Jun, Guerrero-Esteo Mercedes, Cooreman Michael P, Ratziu Vlad, Langa Carmen, Vary Calvin P H, Ramirez Jose R, Friedman Scott, Bernabéu Carmelo (Dec. de 2002). «Transcriptional activation of endoglin and transforming growth factor-beta signaling components by cooperative interaction between Sp1 and KLF6: their potential role in the response to vascular injury». Blood (United States) 100 (12): 4001-10. ISSN 0006-4971. PMID 12433697. doi:10.1182/blood.V100.12.4001. 
  27. ↑ Su, K; Yang X, Roos M D, Paterson A J, Kudlow J E (Jun. de 2000). «Human Sug1/p45 is involved in the proteasome-dependent degradation of Sp1». Biochem. J. (ENGLAND). 348 Pt 2: 281-9. ISSN 0264-6021. PMID 10816420. 
  28. ↑ Takada, Norio; Sanda Takaomi, Okamoto Hiroshi, Yang Jian-Ping, Asamitsu Kaori, Sarol Lilen, Kimura Genjiro, Uranishi Hiroaki, Tetsuka Toshifumi, Okamoto Takashi (Aug. de 2002). «RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions». J. Virol. (United States) 76 (16): 8019-30. ISSN 0022-538X. PMID 12134007. 
  29. ↑ Sugawara, T; Saito M; Fujimoto S (Aug. de 2000). «Sp1 and SF-1 interact and cooperate in the regulation of human steroidogenic acute regulatory protein gene expression». Endocrinology (UNITED STATES) 141 (8): 2895-903. ISSN 0013-7227. PMID 10919277. 
  30. ↑ Biesiada, E; Hamamori Y; Kedes L; Sartorelli V (Apr. de 1999). «Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter». Mol. Cell. Biol. (UNITED STATES) 19 (4): 2577-84. ISSN 0270-7306. PMID 10082523. 
  31. ↑ Lécuyer, Eric; Herblot Sabine, Saint-Denis Marianne, Martin Richard, Begley C Glenn, Porcher Catherine, Orkin Stuart H, Hoang Trang (Oct. de 2002). «The SCL complex regulates c-kit expression in hematopoietic cells through functional interaction with Sp1». Blood (United States) 100 (7): 2430-40. ISSN 0006-4971. PMID 12239153. doi:10.1182/blood-2002-02-0568. 
  32. ↑ Vallian, S; Chin K V, Chang K S (Dec. de 1998). «The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter». Mol. Cell. Biol. (UNITED STATES) 18 (12): 7147-56. ISSN 0270-7306. PMID 9819401. 

Enlaces externos

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SP1

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