STK38L

From Wikipedia, the free encyclopedia

Serine/threonine kinase 38 like

Identifiers

STK38L; KIAA0965; NDR2

External IDs

MGI: 1922250 HomoloGene: 56299

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • actin binding • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• cytoplasm • actin cytoskeleton
Biological Process:	• protein amino acid phosphorylation • protein kinase cascade • regulation of cellular component organization and biogenesis

Orthologs

Human

Mouse

Refseq

NM_015000 (mRNA)
NP_055815 (protein)

NM_172734 (mRNA)
NP_766322 (protein)

Location

Chr 12: 27.34 - 27.37 Mb

Chr 6: 146.68 - 146.74 Mb

Pubmed search

[1]

[2]

Serine/threonine kinase 38 like, also known as STK38L, is a human gene.^[1]

[edit] References

^ Entrez Gene: STK38L serine/threonine kinase 38 like.

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Nagase T, Ishikawa K, Suyama M, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 6 (1): 63–70. PMID 10231032.
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.
Stegert MR, Tamaskovic R, Bichsel SJ, et al. (2004). "Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein.". J. Biol. Chem. 279 (22): 23806–12. doi:10.1074/jbc.M402472200. PMID 15037617.
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.
Stegert MR, Hergovich A, Tamaskovic R, et al. (2006). "Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3.". Mol. Cell. Biol. 25 (24): 11019–29. doi:10.1128/MCB.25.24.11019-11029.2005. PMID 16314523.
Suzuki A, Ogura T, Esumi H (2006). "NDR2 acts as the upstream kinase of ARK5 during insulin-like growth factor-1 signaling.". J. Biol. Chem. 281 (20): 13915–21. doi:10.1074/jbc.M511354200. PMID 16488889.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.