STK38

From Wikipedia, the free encyclopedia

Serine/threonine kinase 38

Identifiers

STK38; NDR1; NDR

External IDs

OMIM: 606964 MGI: 2442572 HomoloGene: 56033

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• protein amino acid phosphorylation • protein kinase cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_007271 (mRNA)
NP_009202 (protein)

XM_973705 (mRNA)
XP_978799 (protein)

Location

Chr 6: 36.57 - 36.62 Mb

Chr 17: 28.7 - 28.74 Mb

Pubmed search

[1]

[2]

Serine/threonine kinase 38, also known as STK38, is a human gene.^[1]

[edit] References

^ Entrez Gene: STK38 serine/threonine kinase 38.

[edit] Further reading

Millward T, Cron P, Hemmings BA (1995). "Molecular cloning and characterization of a conserved nuclear serine(threonine) protein kinase.". Proc. Natl. Acad. Sci. U.S.A. 92 (11): 5022–6. PMID 7761441.
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.