MAP2K3: Difference between revisions

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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. It phosphorylates and thus activates MAPK14/p38-MAPK. This kinase can be activated by insulin, and is necessary for the expression of glucose transporter. Expression of RAS oncogene is found to result in the accumulation of the active form of this kinase, which thus leads to the constitutive activation of MAPK14, and confers oncogenic transformation of primary cells. The inhibition of this kinase is involved in the pathogenesis of Yersina pseudotuberculosis. Multiple alternatively spliced transcript variants that encode distinct isoforms have been reported for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MAP2K3 mitogen-activated protein kinase kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5606| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. It phosphorylates and thus activates MAPK14/p38-MAPK. This kinase can be activated by insulin, and is necessary for the expression of glucose transporter. Expression of RAS oncogene is found to result in the accumulation of the active form of this kinase, which thus leads to the constitutive activation of MAPK14, and confers oncogenic transformation of primary cells. The inhibition of this kinase is involved in the pathogenesis of Yersinia pseudotuberculosis. Multiple alternatively spliced transcript variants that encode distinct isoforms have been reported for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MAP2K3 mitogen-activated protein kinase kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5606| accessdate = }}</ref>
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*{{cite journal  |vauthors=Ben-Levy R, Hooper S, Wilson R, etal |title=Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2 |journal=Curr. Biol. |volume=8 |issue= 19 |pages= 1049–57 |year= 1999 |pmid= 9768359 |doi=10.1016/S0960-9822(98)70442-7  }}
*{{cite journal  |vauthors=Ben-Levy R, Hooper S, Wilson R, etal |title=Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2 |journal=Curr. Biol. |volume=8 |issue= 19 |pages= 1049–57 |year= 1999 |pmid= 9768359 |doi=10.1016/S0960-9822(98)70442-7  }}
*{{cite journal  |vauthors=Doza YN, Cuenda A, Thomas GM, etal |title=Activation of the MAP kinase homologue RK requires the phosphorylation of Thr-180 and Tyr-182 and both residues are phosphorylated in chemically stressed KB cells |journal=FEBS Lett. |volume=364 |issue= 2 |pages= 223–8 |year= 1995 |pmid= 7750576 |doi=10.1016/0014-5793(95)00346-B  }}
*{{cite journal  |vauthors=Doza YN, Cuenda A, Thomas GM, etal |title=Activation of the MAP kinase homologue RK requires the phosphorylation of Thr-180 and Tyr-182 and both residues are phosphorylated in chemically stressed KB cells |journal=FEBS Lett. |volume=364 |issue= 2 |pages= 223–8 |year= 1995 |pmid= 7750576 |doi=10.1016/0014-5793(95)00346-B  }}
*{{cite journal  |vauthors=Dérijard B, Raingeaud J, Barrett T, etal |title=Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms |journal=Science |volume=267 |issue= 5198 |pages= 682–5 |year= 1995 |pmid= 7839144 |doi=10.1126/science.7839144  }}
*{{cite journal  |vauthors=Dérijard B, Raingeaud J, Barrett T, etal |title=Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms |journal=Science |volume=267 |issue= 5198 |pages= 682–5 |year= 1995 |pmid= 7839144 |doi=10.1126/science.7839144  |bibcode=1995Sci...267..682D }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Zheng CF, Guan KL |title=Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 23933–9 |year= 1993 |pmid= 8226933 |doi=  }}
*{{cite journal  |vauthors=Zheng CF, Guan KL |title=Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 23933–9 |year= 1993 |pmid= 8226933 |doi=  }}
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*{{cite journal  |vauthors=Majka M, Ratajczak J, Kowalska MA, Ratajczak MZ |title=Binding of stromal derived factor-1alpha (SDF-1alpha) to CXCR4 chemokine receptor in normal human megakaryoblasts but not in platelets induces phosphorylation of mitogen-activated protein kinase p42/44 (MAPK), ELK-1 transcription factor and serine/threonine kinase AKT |journal=Eur. J. Haematol. |volume=64 |issue= 3 |pages= 164–72 |year= 2000 |pmid= 10997882 |doi=10.1034/j.1600-0609.2000.90112.x  }}
*{{cite journal  |vauthors=Majka M, Ratajczak J, Kowalska MA, Ratajczak MZ |title=Binding of stromal derived factor-1alpha (SDF-1alpha) to CXCR4 chemokine receptor in normal human megakaryoblasts but not in platelets induces phosphorylation of mitogen-activated protein kinase p42/44 (MAPK), ELK-1 transcription factor and serine/threonine kinase AKT |journal=Eur. J. Haematol. |volume=64 |issue= 3 |pages= 164–72 |year= 2000 |pmid= 10997882 |doi=10.1034/j.1600-0609.2000.90112.x  }}
*{{cite journal  |vauthors=Fleming Y, Armstrong CG, Morrice N, etal |title=Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7 |journal=Biochem. J. |volume=352 Pt 1 |issue=  Pt 1|pages= 145–54 |year= 2001 |pmid= 11062067 |doi=  10.1042/0264-6021:3520145| pmc=1221441  }}
*{{cite journal  |vauthors=Fleming Y, Armstrong CG, Morrice N, etal |title=Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7 |journal=Biochem. J. |volume=352 Pt 1 |issue=  Pt 1|pages= 145–54 |year= 2001 |pmid= 11062067 |doi=  10.1042/0264-6021:3520145| pmc=1221441  }}
*{{cite journal  |vauthors=Venter JC, Adams MD, Myers EW, etal |title=The sequence of the human genome |journal=Science |volume=291 |issue= 5507 |pages= 1304–51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal  |vauthors=Venter JC, Adams MD, Myers EW, etal |title=The sequence of the human genome |journal=Science |volume=291 |issue= 5507 |pages= 1304–51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 |bibcode=2001Sci...291.1304V }}
*{{cite journal  |vauthors=Chen Z, Cobb MH |title=Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2 |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16070–5 |year= 2001 |pmid= 11279118 |doi= 10.1074/jbc.M100681200 }}
*{{cite journal  |vauthors=Chen Z, Cobb MH |title=Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2 |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16070–5 |year= 2001 |pmid= 11279118 |doi= 10.1074/jbc.M100681200 }}
}}
}}

Latest revision as of 20:38, 27 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Dual specificity mitogen-activated protein kinase kinase 3 is an enzyme that in humans is encoded by the MAP2K3 gene.[1]

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. It phosphorylates and thus activates MAPK14/p38-MAPK. This kinase can be activated by insulin, and is necessary for the expression of glucose transporter. Expression of RAS oncogene is found to result in the accumulation of the active form of this kinase, which thus leads to the constitutive activation of MAPK14, and confers oncogenic transformation of primary cells. The inhibition of this kinase is involved in the pathogenesis of Yersinia pseudotuberculosis. Multiple alternatively spliced transcript variants that encode distinct isoforms have been reported for this gene.[2]

Interactions

MAP2K3 has been shown to interact with TAOK2[3] and PLCB2.[4]

References

  1. Rampoldi L, Zimbello R, Bortoluzzi S, Tiso N, Valle G, Lanfranchi G, Danieli GA (Mar 1998). "Chromosomal localization of four MAPK signaling cascade genes: MEK1, MEK3, MEK4 and MEKK5". Cytogenet Cell Genet. 78 (3–4): 301–3. doi:10.1159/000134677. PMID 9465908.
  2. "Entrez Gene: MAP2K3 mitogen-activated protein kinase kinase 3".
  3. Chen, Z; Cobb M H (May 2001). "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2". J. Biol. Chem. United States. 276 (19): 16070–5. doi:10.1074/jbc.M100681200. ISSN 0021-9258. PMID 11279118.
  4. Barr, Alastair J; Marjoram Robin; Xu Jing; Snyderman Ralph (Apr 2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. United States. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. ISSN 0006-291X. PMID 12054652.

Further reading