[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1281467 [NCBI, ExPASy, EBI, Israel, Japan]
Seger R.,
Seger D.,
Lozeman F.J.,
Ahn N.G.,
Graves L.M.,
Campbell J.S.,
Ericsson L.,
Harrylock M.,
Jensen A.M.,
Krebs E.G.;
"Human T-cell mitogen-activated protein kinase kinases are related to yeast signal transduction kinases.";
J. Biol. Chem. 267:25628-25631(1992).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8388392 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng C.-F.,
Guan K.-L.;
"Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2.";
J. Biol. Chem. 268:11435-11439(1993).
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[3]
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PHOSPHORYLATION AT SER-218 AND SER-222, AND MUTAGENESIS.
PubMed=8131746 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng C.-F.,
Guan K.-L.;
"Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues.";
EMBO J. 13:1123-1131(1994).
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[4]
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CLEAVAGE BY ANTHRAX LETHAL FACTOR, AND PROTEIN SEQUENCE OF 9-17.
DOI=10.1126/science.280.5364.734; PubMed=9563949 [NCBI, ExPASy, EBI, Israel, Japan]
Duesbery N.S.,
Webb C.P.,
Leppla S.H.,
Gordon V.M.,
Klimpel K.R.,
Copeland T.D.,
Ahn N.G.,
Oskarsson M.K.,
Fukasawa K.,
Paull K.D.,
Vande Woude G.F.;
"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor.";
Science 280:734-737(1998).
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[5]
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CLEAVAGE BY ANTHRAX LETHAL FACTOR.
DOI=10.1042/0264-6021:3520739; PubMed=11104681 [NCBI, ExPASy, EBI, Israel, Japan]
Vitale G.,
Bernardi L.,
Napolitani G.,
Mock M.,
Montecucco C.;
"Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor.";
Biochem. J. 352:739-745(2000).
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[6]
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INTERACTION WITH YOPJ, AND ACETYLATION.
DOI=10.1126/science.1126867; PubMed=16728640 [NCBI, ExPASy, EBI, Israel, Japan]
Mukherjee S.,
Keitany G.,
Li Y.,
Wang Y.,
Ball H.L.,
Goldsmith E.J.,
Orth K.;
"Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation.";
Science 312:1211-1214(2006).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J.,
Jaensch L.,
Nimtz M.,
Dieterich G.,
Hornberger R.,
Keri G.,
Wehland J.,
Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
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[8]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; THR-286 AND THR-386, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H.,
Olsen J.V.,
Bairlein M.,
Gnad F.,
Oppermann F.S.,
Korner R.,
Greff Z.,
Keri G.,
Stemmann O.,
Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
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[9]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[10]
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VARIANTS CFC SYNDROME SER-53 AND CYS-130.
DOI=10.1126/science.1124642; PubMed=16439621 [NCBI, ExPASy, EBI, Israel, Japan]
Rodriguez-Viciana P.,
Tetsu O.,
Tidyman W.E.,
Estep A.L.,
Conger B.A.,
Cruz M.S.,
McCormick F.,
Rauen K.A.;
"Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome.";
Science 311:1287-1290(2006).
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- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates ERK1 and ERK2 MAP kinases.
- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
- ENZYME REGULATION: Activated by phosphorylation.
- SUBUNIT: Interacts with MORG1 (By similarity). Interacts with Yersinia yopJ.
- INTERACTION:
Q9NR09:BIRC6; NbExp=1; IntAct=EBI-492564, EBI-1765160;
P04049:RAF1; NbExp=1; IntAct=EBI-492564, EBI-365996;
Q96RU8:TRIB1; NbExp=1; IntAct=EBI-492564, EBI-492555;
Q96RU7:TRIB3; NbExp=1; IntAct=EBI-492564, EBI-492476;
- PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF or MEKK1) regulates positively the kinase activity.
- PTM: Acetylation by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.
- DISEASE: Defects in MAP2K1 are a cause of cardiofaciocutaneous syndrome (CFC syndrome) [MIM:115150]; also known as cardio-facio-cutaneous syndrome. CFC syndrome is characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. The inheritance of CFC syndrome is autosomal dominant.
- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
- SIMILARITY: Contains 1 protein kinase domain.
- WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=MAP2K1";.
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