Wikipedia

MAPK1

(Redirected from P42 MAP kinase)

Mitogen-activated protein kinase 1 (MAPK 1), also known as ERK2, is an enzyme that in humans is encoded by the MAPK1 gene.[5]

MAPK1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMAPK1, ERK, ERK-2, ERK2, ERT1, MAPK2, P42MAPK, PRKM1, PRKM2, p38, p40, p41, p41mapk, p42-MAPK, mitogen-activated protein kinase 1, NS13
External IDsOMIM: 176948; MGI: 1346858; HomoloGene: 37670; GeneCards: MAPK1; OMA:MAPK1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

5594

26413

Ensembl

ENSG00000100030

ENSMUSG00000063358

UniProt

P28482

P63085

RefSeq (mRNA)

NM_138957
NM_002745

NM_001038663
NM_011949
NM_001357115
NM_028991

RefSeq (protein)

NP_002736
NP_620407

NP_001033752
NP_036079
NP_001344044

Location (UCSC)Chr 22: 21.76 – 21.87 MbChr 16: 16.8 – 16.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene.[6] MAPK1 contains multiple amino acid sites that are phosphorylated and ubiquitinated.[7]

Interactions

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MAPK1 has been shown to interact with:

Clinical significance

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Mutations in MAPK1 are implicated in many types of cancer.[45]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100030 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000063358 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Owaki H, Makar R, Boulton TG, Cobb MH, Geppert TD (February 1992). "Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs". Biochem. Biophys. Res. Commun. 182 (3): 1416–22. doi:10.1016/0006-291X(92)91891-S. PMID 1540184.
  6. ^ "Entrez Gene: MAPK1 mitogen-activated protein kinase 1".
  7. ^ "ERK2 (human)". www.phosphosite.org. Retrieved 2020-10-31.
  8. ^ Díaz-Rodríguez E, Montero JC, Esparís-Ogando A, Yuste L, Pandiella A (June 2002). "Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding". Mol. Biol. Cell. 13 (6): 2031–44. doi:10.1091/mbc.01-11-0561. PMC 117622. PMID 12058067.
  9. ^ Voong LN, Slater AR, Kratovac S, Cressman DE (April 2008). "Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator". J. Biol. Chem. 283 (14): 9031–9. doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089.
  10. ^ Slack DN, Seternes OM, Gabrielsen M, Keyse SM (May 2001). "Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1". J. Biol. Chem. 276 (19): 16491–500. doi:10.1074/jbc.M010966200. PMID 11278799.
  11. ^ Calvisi DF, Pinna F, Meloni F, Ladu S, Pellegrino R, Sini M, Daino L, Simile MM, De Miglio MR, Virdis P, Frau M, Tomasi ML, Seddaiu MA, Muroni MR, Feo F, Pascale RM (June 2008). "Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma". Cancer Res. 68 (11): 4192–200. doi:10.1158/0008-5472.CAN-07-6157. PMID 18519678.
  12. ^ Todd JL, Tanner KG, Denu JM (May 1999). "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway". J. Biol. Chem. 274 (19): 13271–80. doi:10.1074/jbc.274.19.13271. PMID 10224087.
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  14. ^ Cano E, Hazzalin CA, Kardalinou E, Buckle RS, Mahadevan LC (November 1995). "Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction". J. Cell Sci. 108 (11): 3599–609. doi:10.1242/jcs.108.11.3599. PMID 8586671.
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  17. ^ a b Sanz-Moreno V, Casar B, Crespo P (May 2003). "p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels". Mol. Cell. Biol. 23 (9): 3079–90. doi:10.1128/mcb.23.9.3079-3090.2003. PMC 153192. PMID 12697810.
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  22. ^ Chen Z, Cobb MH (May 2001). "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2". J. Biol. Chem. 276 (19): 16070–5. doi:10.1074/jbc.M100681200. PMID 11279118.
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  24. ^ Tanoue T, Maeda R, Adachi M, Nishida E (February 2001). "Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions". EMBO J. 20 (3): 466–79. doi:10.1093/emboj/20.3.466. PMC 133461. PMID 11157753.
  25. ^ a b Waskiewicz AJ, Flynn A, Proud CG, Cooper JA (April 1997). "Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2". EMBO J. 16 (8): 1909–20. doi:10.1093/emboj/16.8.1909. PMC 1169794. PMID 9155017.
  26. ^ Scheper GC, Parra JL, Wilson M, Van Kollenburg B, Vertegaal AC, Han ZG, Proud CG (August 2003). "The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization". Mol. Cell. Biol. 23 (16): 5692–705. doi:10.1128/mcb.23.16.5692-5705.2003. PMC 166352. PMID 12897141.
  27. ^ Jin Z, Gao F, Flagg T, Deng X (September 2004). "Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation". J. Biol. Chem. 279 (38): 40209–19. doi:10.1074/jbc.M404056200. PMID 15210690.
  28. ^ Gupta S, Davis RJ (October 1994). "MAP kinase binds to the NH2-terminal activation domain of c-Myc". FEBS Lett. 353 (3): 281–5. Bibcode:1994FEBSL.353..281G. doi:10.1016/0014-5793(94)01052-8. PMID 7957875. S2CID 45404088.
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  30. ^ Lou Y, Xie W, Zhang DF, Yao JH, Luo ZF, Wang YZ, Shi YY, Yao XB (August 2004). "Nek2A specifies the centrosomal localization of Erk2". Biochem. Biophys. Res. Commun. 321 (2): 495–501. doi:10.1016/j.bbrc.2004.06.171. PMID 15358203.
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  32. ^ Pettiford SM, Herbst R (February 2000). "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene. 19 (7): 858–69. doi:10.1038/sj.onc.1203408. PMID 10702794. S2CID 24843974.
  33. ^ Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T (April 1999). "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 274 (17): 11693–700. doi:10.1074/jbc.274.17.11693. PMID 10206983.
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  35. ^ a b Roux PP, Richards SA, Blenis J (July 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. 23 (14): 4796–804. doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
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Further reading

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