STK38

Serine/threonine kinase 38
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1PSB​
Identifiers
Symbols	STK38 ; NDR; NDR1
External IDs	OMIM: 606964 MGI: 2442572 HomoloGene: 56033 ChEMBL: 1075155 GeneCards: STK38 Gene
EC number	2.7.11.1
Gene ontology Molecular function • magnesium ion binding • protein serine/threonine kinase activity • protein binding • ATP binding • mitogen-activated protein kinase kinase kinase binding Cellular component • nucleus • cytoplasm • MLL5-L complex Biological process • cellular protein modification process • protein phosphorylation • intracellular signal transduction • negative regulation of MAP kinase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11329	106504
Ensembl	ENSG00000112079	ENSMUSG00000024006
UniProt	Q15208	Q91VJ4
RefSeq (mRNA)	NM_001305102	NM_134115
RefSeq (protein)	NP_001292031	NP_598876
Location (UCSC)	Chr 6: 36.49 – 36.55 Mb	Chr 17: 28.97 – 29.01 Mb
PubMed search

Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene.^[1][2]

References

1. Millward T, Cron P, Hemmings BA (Jun 1995). "Molecular cloning and characterization of a conserved nuclear serine(threonine) protein kinase". Proc Natl Acad Sci U S A 92 (11): 5022–6. doi:10.1073/pnas.92.11.5022. PMC 41840. PMID 7761441.
2. "Entrez Gene: STK38 serine/threonine kinase 38".

Further reading

• Tripodis N, Mason R, Humphray SJ, et al. (1999). "Physical map of human 6p21.2-6p21.3: region flanking the centromeric end of the major histocompatibility complex". Genome Res. 8 (6): 631–43. doi:10.1101/gr.8.6.631. PMC 310739. PMID 9647638.
• Millward TA, Heizmann CW, Schäfer BW, Hemmings BA (1998). "Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins". EMBO J. 17 (20): 5913–22. doi:10.1093/emboj/17.20.5913. PMC 1170919. PMID 9774336.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tamaskovic R, Bichsel SJ, Rogniaux H, et al. (2003). "Mechanism of Ca2+-mediated regulation of NDR protein kinase through autophosphorylation and phosphorylation by an upstream kinase". J. Biol. Chem. 278 (9): 6710–8. doi:10.1074/jbc.M210590200. PMID 12493777.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• Bhattacharya S, Large E, Heizmann CW, et al. (2004). "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase". Biochemistry 42 (49): 14416–26. doi:10.1021/bi035089a. PMID 14661952.
• Devroe E, Erdjument-Bromage H, Tempst P, Silver PA (2004). "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases". J. Biol. Chem. 279 (23): 24444–51. doi:10.1074/jbc.M401999200. PMID 15067004.
• Bichsel SJ, Tamaskovic R, Stegert MR, Hemmings BA (2005). "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein". J. Biol. Chem. 279 (34): 35228–35. doi:10.1074/jbc.M404542200. PMID 15197186.
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Devroe E, Silver PA, Engelman A (2005). "HIV-1 incorporates and proteolytically processes human NDR1 and NDR2 serine-threonine kinases". Virology 331 (1): 181–9. doi:10.1016/j.virol.2004.10.023. PMID 15582665.
• Amente S, Napolitano G, Licciardo P, et al. (2005). "Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation". FEBS Lett. 579 (3): 683–9. doi:10.1016/j.febslet.2004.12.045. PMID 15670829.
• Hergovich A, Bichsel SJ, Hemmings BA (2005). "Human NDR kinases are rapidly activated by MOB proteins through recruitment to the plasma membrane and phosphorylation". Mol. Cell. Biol. 25 (18): 8259–72. doi:10.1128/MCB.25.18.8259-8272.2005. PMC 1234321. PMID 16135814.
• Hergovich A, Lamla S, Nigg EA, Hemmings BA (2007). "Centrosome-associated NDR kinase regulates centrosome duplication". Mol. Cell 25 (4): 625–34. doi:10.1016/j.molcel.2007.01.020. PMID 17317633.