LMTK2

LMTK2
Identifiers
Aliases LMTK2, AATYK2, BREK, KPI-2, KPI2, LMR2, PPP1R100, cprk, hBREK, lemur tyrosine kinase 2
External IDs MGI: 3036247 HomoloGene: 8948 GeneCards: LMTK2
Genetically Related Diseases
prostate cancer[1]
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

22853

231876

Ensembl

ENSG00000164715

ENSMUSG00000038970

UniProt

Q8IWU2

Q3TYD6

RefSeq (mRNA)

NM_014916

NM_001081109

RefSeq (protein)

NP_055731.2

NP_001074578.1

Location (UCSC) Chr 7: 98.11 – 98.21 Mb Chr 5: 144.1 – 144.19 Mb
PubMed search [2] [3]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein kinase LMTK2 also known as Lemur tyrosine kinase 2 (LMTK2) is an enzyme that in humans is encoded by the LMTK2 gene.[4][5]

Function

The LMTK2 enzyme belongs to both the protein kinase and the tyrosine kinase families. It contains N-terminus transmembrane helices and a long C-terminal cytoplasmic tail with serine/threonine/tyrosine kinase activity. This protein interacts with several other proteins, such as androgen receptor, inhibitor-2 (Inh2), protein phosphatase-1 (PP1C), p35, and myosin VI. It phosphorylates other proteins, and is itself also phosphorylated when interacting with cyclin-dependent kinase 5 (cdk5)/p35 complex. This protein is involved in nerve growth factor (NGF)-TrkA signalling, and also plays a critical role in endosomal membrane trafficking. Mouse studies suggested an essential role of this protein in spermatogenesis.[5]

Clinical significance

Loss of LMTK2 has been implicated to play a role in development of prostate cancer.[6]

Interactions

LMTK2 has been shown to interact with PPP1CA,[7] Cyclin-dependent kinase 5[8] and PPP1R2.[7]

References

  1. ↑ "Diseases that are genetically associated with LMTK2 view/edit references on wikidata".
  2. ↑ "Human PubMed Reference:".
  3. ↑ "Mouse PubMed Reference:".
  4. ↑ Kawa S, Fujimoto J, Tezuka T, Nakazawa T, Yamamoto T (Mar 2004). "Involvement of BREK, a serine/threonine kinase enriched in brain, in NGF signalling". Genes to Cells. 9 (3): 219–32. doi:10.1111/j.1356-9597.2004.00714.x. PMID 15005709.
  5. 1 2 "Entrez Gene: LMTK2 lemur tyrosine kinase 2".
  6. ↑ Shah K, Bradbury NA (Jun 2015). "Lemur Tyrosine Kinase 2, a novel target in prostate cancer therapy". Oncotarget. 6 (16): 14233–46. PMID 26008968.
  7. 1 2 Wang H, Brautigan DL (Dec 2002). "A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2". The Journal of Biological Chemistry. 277 (51): 49605–12. doi:10.1074/jbc.M209335200. PMID 12393858.
  8. ↑ Kesavapany S, Lau KF, Ackerley S, Banner SJ, Shemilt SJ, Cooper JD, Leigh PN, Shaw CE, McLoughlin DM, Miller CC (Jun 2003). "Identification of a novel, membrane-associated neuronal kinase, cyclin-dependent kinase 5/p35-regulated kinase". The Journal of Neuroscience. 23 (12): 4975–83. PMID 12832520.

Further reading

  • Eeles RA, Kote-Jarai Z, Giles GG, Olama AA, Guy M, Jugurnauth SK, Mulholland S, Leongamornlert DA, Edwards SM, Morrison J, Field HI, Southey MC, Severi G, Donovan JL, Hamdy FC, Dearnaley DP, Muir KR, Smith C, Bagnato M, Ardern-Jones AT, Hall AL, O'Brien LT, Gehr-Swain BN, Wilkinson RA, Cox A, Lewis S, Brown PM, Jhavar SG, Tymrakiewicz M, Lophatananon A, Bryant SL, Horwich A, Huddart RA, Khoo VS, Parker CC, Woodhouse CJ, Thompson A, Christmas T, Ogden C, Fisher C, Jamieson C, Cooper CS, English DR, Hopper JL, Neal DE, Easton DF (Mar 2008). "Multiple newly identified loci associated with prostate cancer susceptibility". Nature Genetics. 40 (3): 316–21. doi:10.1038/ng.90. PMID 18264097. 
  • Chibalina MV, Seaman MN, Miller CC, Kendrick-Jones J, Buss F (Dec 2007). "Myosin VI and its interacting protein LMTK2 regulate tubule formation and transport to the endocytic recycling compartment". Journal of Cell Science. 120 (Pt 24): 4278–88. doi:10.1242/jcs.014217. PMC 2621362Freely accessible. PMID 18029400. 
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 
  • Wang H, Brautigan DL (Nov 2006). "Peptide microarray analysis of substrate specificity of the transmembrane Ser/Thr kinase KPI-2 reveals reactivity with cystic fibrosis transmembrane conductance regulator and phosphorylase". Molecular & Cellular Proteomics. 5 (11): 2124–30. doi:10.1074/mcp.M600188-MCP200. PMID 16887929. 
  • Kesavapany S, Lau KF, Ackerley S, Banner SJ, Shemilt SJ, Cooper JD, Leigh PN, Shaw CE, McLoughlin DM, Miller CC (Jun 2003). "Identification of a novel, membrane-associated neuronal kinase, cyclin-dependent kinase 5/p35-regulated kinase". The Journal of Neuroscience. 23 (12): 4975–83. PMID 12832520. 
  • Wang H, Brautigan DL (Dec 2002). "A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2". The Journal of Biological Chemistry. 277 (51): 49605–12. doi:10.1074/jbc.M209335200. PMID 12393858. 
  • Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jun 1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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