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 21, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Mapk1
  • participates in the following biological processes:
    • B cell receptor signaling pathway ^[24]
    • cytosine metabolic process ^[3]
    • lipopolysaccharide-mediated signaling pathway ^[13]
    • mammary gland epithelial cell proliferation ^[21]
    • MAPK cascade ^{[23, 24, 27]}
    • organ morphogenesis ^[8]
    • peptidyl-serine phosphorylation ^[18]
    • protein phosphorylation ^{[2, 3, 6, 29]}
    • response to DNA damage stimulus ^[32]
    • response to exogenous dsRNA ^[13]
    • response to lipopolysaccharide ^[13]
    • signal transduction by phosphorylation ^{[12, 17, 18, 22, 23, 24, 27]}
    • T cell receptor signaling pathway ^[23]
  • performs the following molecular functions:
    • kinase activity ^{[3, 14]}
    • MAP kinase activity ^{[12, 17, 18, 22, 23, 24, 27]}
    • protein kinase activity ^{[6, 29]}
    • RNA polymerase II carboxy-terminal domain kinase activity ^[31]
  • is located in the following cellular components:
    • cytoplasm ^{[4, 22, 30]}
    • cytosol ^{[1, 16, 26]}
    • mitochondrion ^[1]
    • nucleus ^{[4, 20, 30]}
    • pseudopodium ^[10]
• The gene product of Mapk1 has been shown to bind to the gene products of Dlg1, Dlg4, Dusp6, Hivep1, Micalcl, Mknk2, Nupl1, Rps6ka4. ^{[3, 7, 9, 19, 25, 28]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Mapk1
  • participates in the following biological processes:
    • labyrinthine layer blood vessel development ^[11]
    • peptidyl-serine phosphorylation ^[18]
    • protein phosphorylation ^[17]
    • signal transduction by phosphorylation ^{[2, 18]}
  • performs the following molecular functions:
    • MAP kinase activity ^{[2, 18]}
    • phosphotyrosine binding ^[15]
  • is located in the following cellular components:
    • intracellular ^{[2, 18]}
• Researchers have inferred, based on genetic interactions, that the gene product of Mapk1
  • participates in the following biological processes:
    • negative regulation of cell differentiation based on interactions with Iapp ^[5]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Mapk1:
  • participates in the following biological processes:
    • ERBB signaling pathway
    • ERK1 and ERK2 cascade
    • intracellular signal transduction
    • MAPK cascade
    • MAPK import into nucleus
    • peptidyl-serine phosphorylation
    • positive regulation of peptidyl-threonine phosphorylation
    • positive regulation of translation
    • protein phosphorylation
    • response to chemical stimulus
    • response to epidermal growth factor stimulus
    • response to estrogen stimulus
    • response to toxic substance
    • sensory perception of pain
    • signal transduction
    • signal transduction by phosphorylation
  • performs the following molecular functions:
    • ATP binding
    • MAP kinase activity
    • mitogen-activated protein kinase kinase kinase binding
    • phosphatase binding
    • protein serine/threonine kinase activity
    • transcription factor binding
  • is located in the following cellular components:
    • axon part
    • cytoplasm
    • cytosol
    • dendrite cytoplasm
    • microtubule cytoskeleton
    • nucleoplasm
    • nucleus
    • perikaryon
    • protein complex

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Summary text based on GO annotations supported by structural data

• Mapk1 encodes a protein or proteins that contain the following InterPro domains: Mitogen-activated protein (MAP) kinase, conserved site, Mitogen-activated protein (MAP) kinase, ERK1/2, Protein kinase, ATP binding site, Protein kinase, catalytic domain, Protein kinase-like domain, Serine/threonine- / dual specificity protein kinase, catalytic domain, Serine/threonine-protein kinase, active site, indicating that the gene product:
  • performs the following molecular functions:
    • transferase activity, transferring phosphorus-containing groups

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Mapk1 indicates that it:
  • participates in the following biological processes:
    • apoptotic process
    • cell cycle
    • phosphorylation
  • performs the following molecular functions:
    • nucleotide binding
    • transferase activity

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References

1. Baines CP et al. (2002) Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection. Circ Res, 90:390-7. (PubMed:11884367)
2. Baxter RM et al. (2002) Role of the nude gene in epithelial terminal differentiation. J Invest Dermatol, 118:303-9. (PubMed:11841548)
3. 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)
4. Corson LB et al. (2003) Spatial and temporal patterns of ERK signaling during mouse embryogenesis. Development, 130:4527-37. (PubMed:12925581)
5. Dacquin R et al. (2004) Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo. J Cell Biol, 164:509-14. (PubMed:14970190)
6. 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)
7. Fernandez E et al. (2009) Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins. Mol Syst Biol, 5:269. (PubMed:19455133)
8. Fisher CE et al. (2001) Erk MAP kinase regulates branching morphogenesis in the developing mouse kidney. Development, 128:4329-38. (PubMed:11684667)
9. Fuentealba LC et al. (2007) Integrating patterning signals: Wnt/GSK3 regulates the duration of the BMP/Smad1 signal. Cell, 131:980-93. (PubMed:18045539)
10. 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)
11. Hatano N et al. (2003) Essential role for ERK2 mitogen-activated protein kinase in placental development. Genes Cells, 8:847-56. (PubMed:14622137)
12. Higuchi T et al. (2004) MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by binding to a multifunctional docking site of met. Mol Cell Biol, 24:7456-68. (PubMed:15314156)
13. Hoebe K et al. (2003) Identification of Lps2 as a key transducer of MyD88-independent TIR signalling. Nature, 424:743-8. (PubMed:12872135)
14. Holgado-Madruga M et al. (2003) Gab1 is an integrator of cell death versus cell survival signals in oxidative stress. Mol Cell Biol, 23:4471-84. (PubMed:12808090)
15. Ishibe S et al. (2003) Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol Cell, 12:1275-85. (PubMed:14636584)
16. Ishida-Kitagawa N et al. (2012) Siglec-15 protein regulates formation of functional osteoclasts in concert with DNAX-activating protein of 12 kDa (DAP12). J Biol Chem, 287:17493-502. (PubMed:22451653)
17. 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)
18. Lee SH et al. (2008) ERK is a novel regulatory kinase for poly(A) polymerase. Nucleic Acids Res, 36:803-13. (PubMed:18084034)
19. Miura K et al. (2008) Molecular cloning of Ebitein1: a novel extracellular signal-regulated kinase 2-binding protein in testis. Biochem Biophys Res Commun, 368:336-42. (PubMed:18241670)
20. Moosmang S et al. (2005) Role of hippocampal Cav1.2 Ca2+ channels in NMDA receptor-independent synaptic plasticity and spatial memory. J Neurosci, 25:9883-92. (PubMed:16251435)
21. Nojima H et al. (2008) IQGAP3 regulates cell proliferation through the Ras/ERK signalling cascade. Nat Cell Biol, 10:971-8. (PubMed:18604197)
22. 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)
23. Pani G et al. (1996) Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase. J Exp Med, 184:839-52. (PubMed:9064344)
24. Pani G et al. (1997) The motheaten mutation rescues B cell signaling and development in CD45-deficient mice. J Exp Med, 186:581-8. (PubMed:9254656)
25. Papin J et al. (2004) Bioinformatics and cellular signaling. Curr Opin Biotechnol, 15:78-81. (PubMed:15102471)
26. Ribon V et al. (1998) A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes. Mol Cell Biol, 18:872-9. (PubMed:9447983)
27. Richards JD et al. (1996) Reconstitution of B cell antigen receptor-induced signaling events in a nonlymphoid cell line by expressing the Syk prottein-tyrosine kinase. J Biol Chem, 271:6458-66. (PubMed:8626447)
28. 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)
29. Soond SM et al. (2008) ERK and the F-box protein betaTRCP target STAT1 for degradation. J Biol Chem, 283:16077-83. (PubMed:18378670)
30. 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)
31. 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)
32. 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)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

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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