STK38
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Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene.[3][4]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ 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. - ↑ "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.
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