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Gene Ontology Classifications
mitogen-activated protein kinase 1

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Mapk1. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes 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. One study also suggests that this protein acts as a transcriptional repressor independent of its kinase activity. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene. [provided by RefSeq, Jan 2014]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
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  2. Baxter RM et al. (2002) Role of the nude gene in epithelial terminal differentiation. J Invest Dermatol, 118:303-9. (PubMed:11841548)
  3. Boucherat O et al. (2014) Crucial requirement of ERK/MAPK signaling in respiratory tract development. Development, 141:3197-211. (PubMed:25100655)
  4. Castelli M et al. (2004) MAP kinase phosphatase 3 (MKP3) interacts with and is phosphorylated by protein kinase CK2alpha. J Biol Chem, 279:44731-9. (PubMed:15284227)
  5. Corson LB et al. (2003) Spatial and temporal patterns of ERK signaling during mouse embryogenesis. Development, 130:4527-37. (PubMed:12925581)
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  8. Fan M et al. (2004) Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1alpha: modulation by p38 MAPK. Genes Dev, 18:278-89. (PubMed:14744933)
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  10. Fisher CE et al. (2001) Erk MAP kinase regulates branching morphogenesis in the developing mouse kidney. Development, 128:4329-38. (PubMed:11684667)
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  12. Ge L et al. (2003) A beta-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis. J Biol Chem, 278:34418-26. (PubMed:12821670)
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  20. Jin SX et al. (2010) Long-term potentiation in the CA1 hippocampus induced by NR2A subunit-containing NMDA glutamate receptors is mediated by Ras-GRF2/Erk map kinase signaling. PLoS One, 5:e11732. (PubMed:20661302)
  21. Kamda JD et al. (2009) Phosphoinositide 3-kinase-dependent inhibition of dendritic cell interleukin-12 production by Giardia lamblia. Infect Immun, 77:685-93. (PubMed:19047410)
  22. Kim MY et al. (2005) Presenilin acts as a positive regulator of basal level activity of ERK through the Raf-MEK1 signaling pathway. Biochem Biophys Res Commun, 332:609-13. (PubMed:15896720)
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  26. Nojima H et al. (2008) IQGAP3 regulates cell proliferation through the Ras/ERK signalling cascade. Nat Cell Biol, 10:971-8. (PubMed:18604197)
  27. Noshita N et al. (2002) Copper/zinc superoxide dismutase attenuates neuronal cell death by preventing extracellular signal-regulated kinase activation after transient focal cerebral ischemia in mice. J Neurosci, 22:7923-30. (PubMed:12223545)
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  33. Round JL et al. (2007) Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors. Nat Immunol, 8:154-61. (PubMed:17187070)
  34. Sohaskey ML et al. (2002) Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes. Mol Biol Cell, 13:454-68. (PubMed:11854404)
  35. Soond SM et al. (2008) ERK and the F-box protein betaTRCP target STAT1 for degradation. J Biol Chem, 283:16077-83. (PubMed:18378670)
  36. Stanciu M et al. (2002) Prolonged Nuclear Retention of Activated Extracellular Signal-regulated Protein Kinase Promotes Cell Death Generated by Oxidative Toxicity or Proteasome Inhibition in a Neuronal Cell Line. J Biol Chem, 277:4010-7. (PubMed:11726647)
  37. Tarrega C et al. (2005) ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1. J Biol Chem, 280:37885-94. (PubMed:16148006)
  38. Wilm B et al. (2004) The forkhead genes, Foxc1 and Foxc2, regulate paraxial versus intermediate mesoderm cell fate. Dev Biol, 271:176-89. (PubMed:15196959)
  39. Yeo M et al. (2003) A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J Biol Chem, 278:26078-85. (PubMed:12721286)
  40. You H et al. (2004) p53-dependent inhibition of FKHRL1 in response to DNA damage through protein kinase SGK1. Proc Natl Acad Sci U S A, 101:14057-62. (PubMed:15383658)
  41. Zuniga A et al. (1999) Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. J Biol Chem, 274:21900-7. (PubMed:10419510)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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