Megakaryocyte-associated tyrosine kinase

For the plant gene, see maturase K.

Megakaryocyte-associated tyrosine-protein kinase is an enzyme that in humans is encoded by the MATK gene.

MATK
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1JWO, 1X6G, 3US4
Identifiers
Aliases	MATK, CHK, CTK, HHYLTK, HYL, HYLTK, Lsk, Megakaryocyte-associated tyrosine kinase
External IDs	OMIM: 600038; MGI: 99259; HomoloGene: 48104; GeneCards: MATK; OMA:MATK - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.3 Start 3,777,970 bp End 3,802,129 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 39.72 cM|10 C1 Start 81,088,769 bp End 81,099,199 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte cingulate gyrus anterior cingulate cortex right frontal lobe Brodmann area 9 amygdala prefrontal cortex nucleus accumbens putamen caudate nucleus Top expressed in superior frontal gyrus primary visual cortex dentate gyrus of hippocampal formation granule cell lumbar subsegment of spinal cord entorhinal cortex perirhinal cortex hippocampus proper olfactory tubercle subiculum lateral septal nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity non-membrane spanning protein tyrosine kinase activity kinase activity protein binding protein tyrosine kinase activity signaling receptor binding ATP binding Cellular component cytoplasm cytosol membrane extrinsic component of cytoplasmic side of plasma membrane Biological process cell differentiation phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway protein phosphorylation positive regulation of cell population proliferation peptidyl-tyrosine autophosphorylation mesoderm development cell population proliferation innate immune response ERBB2 signaling pathway peptidyl-tyrosine phosphorylation regulation of cell population proliferation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4145 17179 Ensembl ENSG00000007264 ENSMUSG00000004933 UniProt P42679 P41242 RefSeq (mRNA) NM_002378 NM_139354 NM_139355 NM_001285853 NM_001285854 NM_001285855 NM_010768 RefSeq (protein) NP_002369 NP_647611 NP_647612 NP_001272782 NP_001272783 NP_001272784 NP_034898 Location (UCSC) Chr 19: 3.78 – 3.8 Mb Chr 10: 81.09 – 81.1 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene has amino acid sequence similarity to Csk tyrosine kinase and has the structural features of the CSK subfamily: SRC homology SH2 and SH3 domains, a catalytic domain, a unique N terminus, lack of myristylation signals, lack of a negative regulatory phosphorylation site, and lack of an autophosphorylation site. This protein is thought to play a significant role in the signal transduction of hematopoietic cells. It is able to phosphorylate and inactivate Src family kinases, and may play an inhibitory role in the control of T-cell proliferation. This protein might be involved in signaling in some cases of breast cancer. Three alternatively spliced transcript variants that encode different isoforms have been described for this gene.

Interactions

Megakaryocyte-associated tyrosine kinase has been shown to interact with CD117 and TrkA.

Further reading

• Okada M, Nada S, Yamanashi Y, et al. (1992). "CSK: a protein-tyrosine kinase involved in regulation of src family kinases". J. Biol. Chem. 266 (36): 24249–52. doi:10.1016/S0021-9258(18)54220-4. PMID 1722201.
• McVicar DW, Lal BK, Lloyd A, et al. (1994). "Molecular cloning of lsk, a carboxyl-terminal src kinase (csk) related gene, expressed in leukocytes". Oncogene. 9 (7): 2037–44. PMID 7516063.
• Jhun BH, Rivnay B, Price D, Avraham H (1995). "The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit". J. Biol. Chem. 270 (16): 9661–6. doi:10.1074/jbc.270.16.9661. PMID 7536744.
• Hamaguchi I, Iwama A, Yamaguchi N, et al. (1994). "Characterization of mouse non-receptor tyrosine kinase gene, HYL". Oncogene. 9 (11): 3371–4. PMID 7936664.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Sakano S, Iwama A, Inazawa J, et al. (1994). "Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)". Oncogene. 9 (4): 1155–61. PMID 8134117.
• Zrihan-Licht S, Lim J, Keydar I, et al. (1997). "Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells". J. Biol. Chem. 272 (3): 1856–63. doi:10.1074/jbc.272.3.1856. PMID 8999872.
• Price DJ, Rivnay B, Fu Y, et al. (1997). "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes". J. Biol. Chem. 272 (9): 5915–20. doi:10.1074/jbc.272.9.5915. PMID 9038210.
• Hirao A, Hamaguchi I, Suda T, Yamaguchi N (1997). "Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets". EMBO J. 16 (9): 2342–51. doi:10.1093/emboj/16.9.2342. PMC 1169835. PMID 9171348.
• Grgurevich S, Linnekin D, Musso T, et al. (1997). "The Csk-like proteins Lsk, Hyl, and Matk represent the same Csk homologous kinase (Chk) and are regulated by stem cell factor in the megakaryoblastic cell line MO7e". Growth Factors. 14 (2–3): 103–15. doi:10.3109/08977199709021514. PMID 9255603.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Grgurevich S, Mikhael A, McVicar DW (1999). "The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells". Biochem. Biophys. Res. Commun. 256 (3): 668–75. doi:10.1006/bbrc.1999.0398. PMID 10080957.
• Yamashita H, Avraham S, Jiang S, et al. (1999). "The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells". J. Biol. Chem. 274 (21): 15059–65. doi:10.1074/jbc.274.21.15059. PMID 10329710.
• McShan GD, Zagozdzon R, Park SY, et al. (2002). "Csk homologous kinase associates with RAFTK/Pyk2 in breast cancer cells and negatively regulates its activation and breast cancer cell migration". Int. J. Oncol. 21 (1): 197–205. doi:10.3892/ijo.21.1.197. PMID 12063569.
• Kim S, Zagozdzon R, Meisler A, et al. (2002). "Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer". J. Biol. Chem. 277 (39): 36465–70. doi:10.1074/jbc.M206018200. PMID 12122014.
• Zagozdzon R, Bougeret C, Fu Y, Avraham HK (2003). "Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells". Int. J. Oncol. 21 (6): 1347–52. doi:10.3892/ijo.21.6.1347. PMID 12429987.
• 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.
• Mikkola ET, Bergman M (2003). "Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK". FEBS Lett. 544 (1–3): 11–4. doi:10.1016/S0014-5793(03)00405-8. PMID 12782282. S2CID 2653632.