MELK
Maternal embryonic leucine zipper kinase is an enzyme that in humans is encoded by the MELK gene.[1][2][3]
Interactions
MELK has been shown to interact with CDC25B.[4]
References
- ↑ Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (Nov 1996). "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.
- ↑ Heyer BS, Warsowe J, Solter D, Knowles BB, Ackerman SL (Aug 1997). "New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse egg and preimplantation embryo". Mol Reprod Dev 47 (2): 148–56. doi:10.1002/(SICI)1098-2795(199706)47:2<148::AID-MRD4>3.0.CO;2-M. PMID 9136115.
- ↑ "Entrez Gene: MELK maternal embryonic leucine zipper kinase".
- ↑ Davezac N, Baldin V, Blot J, Ducommun B, Tassan JP (Oct 2002). "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation". Oncogene 21 (50): 7630–41. doi:10.1038/sj.onc.1205870. PMID 12400006.
Further reading
- Lin ML, Park JH, Nishidate T, Nakamura Y, Katagiri T (2007). "Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family.". Breast Cancer Res. 9 (1): R17. doi:10.1186/bcr1650. PMC 1851384. PMID 17280616.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Beullens M, Vancauwenbergh S, Morrice N, Derua R, Ceulemans H, Waelkens E et al. (2006). "Substrate specificity and activity regulation of protein kinase MELK.". J. Biol. Chem. 280 (48): 40003–11. doi:10.1074/jbc.M507274200. PMID 16216881.
- Vulsteke V, Beullens M, Boudrez A, Keppens S, Van Eynde A, Rider MH et al. (2004). "Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1.". J. Biol. Chem. 279 (10): 8642–7. doi:10.1074/jbc.M311466200. PMID 14699119.
- Davezac N, Baldin V, Blot J, Ducommun B, Tassan JP (2002). "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation.". Oncogene 21 (50): 7630–41. doi:10.1038/sj.onc.1205870. PMID 12400006.
- Seong HA, Gil M, Kim KT, Kim SJ, Ha H (2002). "Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine protein serine/threonine kinase 38 (MPK38).". Biochem. J. 361 (Pt 3): 597–604. doi:10.1042/0264-6021:3610597. PMC 1222342. PMID 11802789.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Gil M, Yang Y, Lee Y, Choi I, Ha H (1997). "Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells". Gene 195 (2): 295–301. doi:10.1016/S0378-1119(97)00181-9. PMID 9305775.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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