SCUBA

MELK — Maternal embryonic leucine zipper kinase

MELK belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

MELK's module in each cell type

Cell typeModuleShares the module with
CD8⁺ T cellsMitotic Spindle Assembly
Cell cycle
FBXO5, LRR1, MTFR2, NCAPG2, RAD51AP1, SHCBP1, SKA1, SKA3 +3 moreView in SCUBA
Goblet cellsFOXM1-driven G2/M
Cell cycle
CDCA5, CENPK, DIAPH3, E2F8, ESCO2, FOXM1, IQGAP3, ORC6 +5 moreView in SCUBA

About the gene

SynonymsKIAA0175
Chromosome9: 36572862-36677683
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classDisease related genes, Enzymes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins
Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle

Function

Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.