MAPK1

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

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

Function

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

MAPK1 has been shown to interact with:

Clinical significance

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

See also

References

  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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  19. ^ a b Yeung K, Janosch P, McFerran B, Rose DW, Mischak H, Sedivy JM, Kolch W (May 2000). "Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein". Mol. Cell. Biol. 20 (9): 3079–85. doi:10.1128/mcb.20.9.3079-3085.2000. PMC 85596. PMID 10757792.
  20. ^ Wunderlich W, Fialka I, Teis D, Alpi A, Pfeifer A, Parton RG, Lottspeich F, Huber LA (February 2001). "A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment". J. Cell Biol. 152 (4): 765–76. doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.
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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.
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