LMTK2

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.

LMTK2
Identifiers
Aliases	LMTK2, AATYK2, BREK, KPI-2, KPI2, LMR2, PPP1R100, cprk, hBREK, lemur tyrosine kinase 2
External IDs	OMIM: 610989; MGI: 3036247; HomoloGene: 8948; GeneCards: LMTK2; OMA:LMTK2 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q21.3 Start 98,106,862 bp End 98,209,638 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 G2 Start 144,037,254 bp End 144,125,022 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus Brodmann area 23 parietal lobe postcentral gyrus superior frontal gyrus primary visual cortex lateral nuclear group of thalamus pons parotid gland Skeletal muscle tissue of rectus abdominis Top expressed in Paneth cell primary motor cortex cingulate gyrus prefrontal cortex olfactory tubercle piriform cortex superior colliculus retinal pigment epithelium subiculum inferior colliculi More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity kinase activity myosin VI binding protein serine/threonine kinase activity protein binding protein phosphatase inhibitor activity ATP binding receptor tyrosine kinase transmembrane signaling receptor activity transmembrane receptor protein tyrosine kinase activity Cellular component integral component of membrane recycling endosome Golgi apparatus membrane early endosome perinuclear region of cytoplasm cytosol growth cone soma cytoplasm integral component of plasma membrane receptor complex Biological process transferrin transport phosphorylation protein phosphorylation early endosome to late endosome transport receptor recycling peptidyl-serine phosphorylation endocytic recycling protein autophosphorylation peptidyl-threonine phosphorylation negative regulation of phosphoprotein phosphatase activity negative regulation of signal transduction peptidyl-tyrosine phosphorylation cell differentiation negative regulation of apoptotic process positive regulation of ERK1 and ERK2 cascade transmembrane receptor protein tyrosine kinase signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 22853 231876 Ensembl ENSG00000164715 ENSMUSG00000038970 UniProt Q8IWU2 Q3TYD6 RefSeq (mRNA) NM_014916 NM_001081109 RefSeq (protein) NP_055731 NP_001074578 Location (UCSC) Chr 7: 98.11 – 98.21 Mb Chr 5: 144.04 – 144.13 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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 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.

Clinical significance

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

Interactions

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

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. S2CID 30968525.
• 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 2621362. 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. S2CID 7827573.
• 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. doi:10.1523/JNEUROSCI.23-12-04975.2003. PMC 6741199. 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.