MELK

MELK
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4BKY, 4BKZ, 4D2P, 4D2T, 4D2V, 4D2W, 4IXP, 4UMP, 4UMQ, 4UMR, 4UMT, 4UMU, 5IHA, 5IHC, 5IH9, 5IH8
Identifiers
Aliases	MELK, HPK38, maternal embryonic leucine zipper kinase
External IDs	MGI: 106924 HomoloGene: 32111 GeneCards: MELK
EC number	2.7.10.2
Gene ontology Molecular function • transferase activity • nucleotide binding • calcium ion binding • protein kinase activity • non-membrane spanning protein tyrosine kinase activity • kinase activity • protein serine/threonine kinase activity • protein binding • ATP binding • lipid binding Cellular component • cytoplasm • membrane • plasma membrane • cell cortex • nucleus Biological process • intrinsic apoptotic signaling pathway in response to oxidative stress • hemopoiesis • intracellular signal transduction • phosphorylation • protein phosphorylation • G2/M transition of mitotic cell cycle • neural precursor cell proliferation • positive regulation of apoptotic process • protein autophosphorylation • cell cycle • cell proliferation • apoptotic process • peptidyl-tyrosine phosphorylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9833	17279
Ensembl	ENSG00000165304	ENSMUSG00000035683
UniProt	Q14680	Q61846
RefSeq (mRNA)	NM_001256685 NM_001256687 NM_001256688 NM_001256689 NM_001256690 NM_001256691 NM_001256692 NM_001256693 NM_014791	NM_010790
RefSeq (protein)	NP_001243614.1 NP_001243616.1 NP_001243617.1 NP_001243618.1 NP_001243619.1 NP_001243621.1 NP_001243622.1 NP_055606.1	NP_034920.2
Location (UCSC)	Chr 9: 36.57 – 36.68 Mb	Chr 4: 44.3 – 44.36 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Maternal embryonic leucine zipper kinase is an enzyme that in humans is encoded by the MELK gene.^[3][4][5]

Interactions

MELK has been shown to interact with CDC25B.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. "Entrez Gene: MELK maternal embryonic leucine zipper kinase".
6. 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, Mann M (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, Bollen M (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, Stalmans W, Bollen M (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.