MAPK1
La MAP quinasa 1, también conocida como MAPK1, p42MAPK y ERK2, es una enzima codificada en humanos por el gen mapk1.[1]
MAP quinasa 1 | ||||
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![]() Estructura tridimensional de la proteína MAPK1. | ||||
Estructuras disponibles | ||||
PDB |
Lista de códigos PDB 1erk
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Identificadores | ||||
Símbolos | MAPK1 (HGNC: 6871) p38, ERK, p40, ERK2, ERT1, MAPK2, P42MAPK, PRKM1, PRKM2, p41, p41mapk | |||
Identificadores externos | ||||
Locus | Cr. 22 q11.21-q11.22 | |||
Ortólogos | ||||
Especies |
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Entrez |
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UniProt |
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RefSeq (ARNm) |
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La MAPK1 pertenece a la familia de las MAP quinasas. Las MAP quinasas actúan como punto de integración de múltiples señales bioquímicas, y están implicadas en una amplia variedad de procesos celulares tales como proliferación celular, diferenciación celular, regulación de la transcripción y desarrollo. La activación de esta quinasa requiere su fosforilación por otras quinasas. Tras la activación, MAPK1 se trasloca al núcleo de las células estimuladas, donde fosforilará diversas dianas nucleares. Se han descrito dos variantes transcripcionales de este gen, que codifican la misma proteína, diferenciándose únicamente en los UTRs.[2]
Interacciones
La proteína MAPK1 ha demostrado ser capaz de interaccionar con:
- TSC2[3]
- PEA15[4]
- DUSP1[5][6]
- NEK2[7]
- DUSP3[8]
- STAT5A[9][10]
- MAPK14[11][12]
- FHL2[13]
- TNIP1[14]
- RPS6KA3[15][16]
- RPS6KA2[15][17]
- MAP2K1[11][18][19][20][21][22]
- RPS6KA1[16][17][23]
- PTPN7[24][25]
- MKNK1[26]
- CIITA[27]
- TOB1[28]
- PEBP1[19]
- DUSP22[29]
- Myc[30][31][32]
- ADAM17[33]
- SORBS3[34]
- ELK1[23][35]
- VAV1[36][37]
- HDAC4[38]
- MKNK2[26][39]
- MAP3K1[40]
- UBR5[23]
Véase también
- MAP quinasas (MAPK)
- ERK
Referencias
- Owaki H, Makar R, Boulton TG, Cobb MH, Geppert TD (febrero de 1992). «Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs». Biochem. Biophys. Res. Commun. 182 (3): 1416-22. PMID 1540184. doi:10.1016/0006-291X(92)91891-S.
- «Entrez Gene: MAPK1 mitogen-activated protein kinase 1».
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- Tanoue, T; Maeda R; Adachi M; Nishida E (Feb. de 2001). «Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions». EMBO J. (England) 20 (3): 466-79. ISSN 0261-4189. PMID 11157753. doi:10.1093/emboj/20.3.466.
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- Zhang, Shengliang; Fukushi Masaya, Hashimoto Shinichi, Gao Chongfeng, Huang Lin, Fukuyo Yayoi, Nakajima Takuma, Amagasa Teruo, Enomoto Shoji, Koike Katsuro, Miura Osamu, Yamamoto Naoki, Tsuchida Nobuo (Sep. de 2002). «A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling». Biochem. Biophys. Res. Commun. (United States) 297 (1): 17-23. ISSN 0006-291X. PMID 12220502.
- Zhao, Y; Bjorbaek C, Moller D E (Nov. de 1996). «Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases». J. Biol. Chem. (UNITED STATES) 271 (47): 29773-9. ISSN 0021-9258. PMID 8939914.
- Smith, J A; Poteet-Smith C E, Malarkey K, Sturgill T W (Jan. de 1999). «Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo». J. Biol. Chem. (UNITED STATES) 274 (5): 2893-8. ISSN 0021-9258. PMID 9915826.
- Roux, Philippe P; Richards Stephanie A, Blenis John (Jul. de 2003). «Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity». Mol. Cell. Biol. (United States) 23 (14): 4796-804. ISSN 0270-7306. PMID 12832467.
- Robinson, Fred L; Whitehurst Angelique W, Raman Malavika, Cobb Melanie H (Apr. de 2002). «Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1». J. Biol. Chem. (United States) 277 (17): 14844-52. ISSN 0021-9258. PMID 11823456. doi:10.1074/jbc.M107776200.
- Yeung, K; Janosch P, McFerran B, Rose D W, Mischak H, Sedivy J M, Kolch W (mayo. de 2000). «Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein». Mol. Cell. Biol. (UNITED STATES) 20 (9): 3079-85. ISSN 0270-7306. PMID 10757792.
- Wunderlich, W; Fialka I, Teis D, Alpi A, Pfeifer A, Parton R G, Lottspeich F, Huber L A (Feb. de 2001). «A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment». J. Cell Biol. (United States) 152 (4): 765-76. ISSN 0021-9525. PMID 11266467.
- Xu Be; Stippec S, Robinson F L, Cobb M H (Jul. de 2001). «Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking». J. Biol. Chem. (United States) 276 (28): 26509-15. ISSN 0021-9258. PMID 11352917. doi:10.1074/jbc.M102769200.
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