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STK38: Wikis


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Serine/threonine kinase 38
Symbols STK38; NDR1; NDR
External IDs OMIM606964 MGI2442572 HomoloGene56033 GeneCards: STK38 Gene
RNA expression pattern
PBB GE STK38 202951 at tn.png
More reference expression data
Species Human Mouse
Entrez 11329 106504
Ensembl ENSG00000112079 ENSMUSG00000024006
UniProt Q15208 Q8BJS2
RefSeq (mRNA) NM_007271 XM_973705
RefSeq (protein) NP_009202 XP_978799
Location (UCSC) Chr 6:
36.57 - 36.62 Mb
Chr 17:
28.7 - 28.74 Mb
PubMed search [1] [2]

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


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. 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. 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. 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. 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. 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.  


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