| Protein Name :
Dual specificity mitogen-activated protein kinase kinase 1
UniProtKB / Swiss-Prot ID : MP2K1_HUMAN
Gene Name (Synonyms) :
MAP2K1, MEK1, PRKMK1
Species : Homo sapiens (Human).
Subcellular Localization : Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle pole body. Cytoplasm. Nucleus. Note=Localizes at centrosomes during prometaphase, midzone during anaphase and midbody during telophase/cytokinesis.
Protein Function : Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator- activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis.
|Predicted Secondary Structure
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| Overview of Protein Modification Sites with Functional and Structural Information
|Accessible Surface Area (ASA)|
Experimental PTM Sites
|Predicted PTM Sites|
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Experimental Post-Translational Modification Sites
|615279||Cardiofaciocutaneous syndrome 3 (CFC3)|
|Related Literatures of Post-Translational Modification|
|"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";|
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; THR-286 ANDTHR-386, AND MASS SPECTROMETRY.
|"Large-scale proteomics analysis of the human kinome.";|
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASSSPECTROMETRY.
|"Activation of MEK family kinases requires phosphorylation of twoconserved Ser/Thr residues.";|
Zheng C.-F., Guan K.-L.;
EMBO J. 13:1123-1131(1994).
Cited for: PHOSPHORYLATION AT SER-218 AND SER-222, AND MUTAGENESIS.
|"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";|
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASSSPECTROMETRY.
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