STK38

STK38
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1PSB
Identifiers
Aliases	STK38, NDR, NDR1, serine/threonine kinase 38
External IDs	OMIM: 606964; MGI: 2442572; HomoloGene: 56033; GeneCards: STK38; OMA:STK38 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.31 Start 36,493,892 bp End 36,547,479 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 A3.3 Start 29,189,854 bp End 29,226,969 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in palpebral conjunctiva oocyte secondary oocyte granulocyte nasal epithelium amniotic fluid epithelium of nasopharynx mononuclear cell monocyte mucosa of paranasal sinus Top expressed in granulocyte conjunctival fornix thymus blood lacrimal gland submandibular gland spleen body of femur medullary collecting duct ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function mitogen-activated protein kinase kinase kinase binding transferase activity nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding magnesium ion binding metal ion binding kinase activity cadherin binding Cellular component cytoplasm nucleus cytosol Biological process protein phosphorylation intracellular signal transduction peptidyl-serine phosphorylation negative regulation of MAP kinase activity phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11329 106504 Ensembl ENSG00000112079 ENSMUSG00000024006 UniProt Q15208 Q91VJ4 RefSeq (mRNA) NM_001305102 NM_007271 NM_134115 NM_001357173 RefSeq (protein) NP_001292031 NP_009202 NP_598876 NP_001344102 Location (UCSC) Chr 6: 36.49 – 36.55 Mb Chr 17: 29.19 – 29.23 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003Natur.425..805M. 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. S2CID 2371325.
• 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. S2CID 33475235.
• 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.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Serine/threonine-protein kinase 38