STK38
Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene.[5][6]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000112079 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024006 - Ensembl, May 2017
- ↑ "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. PMC 41840
. PMID 7761441. doi:10.1073/pnas.92.11.5022. - ↑ "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. PMC 310739 . PMID 9647638. doi:10.1101/gr.8.6.631.
- 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. PMC 1170919 . PMID 9774336. doi:10.1093/emboj/17.20.5913.
- 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- 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. PMID 12493777. doi:10.1074/jbc.M210590200.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. PMID 14574404. doi:10.1038/nature02055.
- 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. PMID 14661952. doi:10.1021/bi035089a.
- 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. PMID 15067004. doi:10.1074/jbc.M401999200.
- 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. PMID 15197186. doi:10.1074/jbc.M404542200.
- 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. PMID 15324660. doi:10.1016/j.cub.2004.07.051.
- 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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
- 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. PMID 15582665. doi:10.1016/j.virol.2004.10.023.
- 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. PMID 15670829. doi:10.1016/j.febslet.2004.12.045.
- 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. PMC 1234321 . PMID 16135814. doi:10.1128/MCB.25.18.8259-8272.2005.
- Hergovich A, Lamla S, Nigg EA, Hemmings BA (2007). "Centrosome-associated NDR kinase regulates centrosome duplication". Mol. Cell. 25 (4): 625–34. PMID 17317633. doi:10.1016/j.molcel.2007.01.020.
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