Megakaryocyte-associated tyrosine kinase

Megakaryocyte-associated tyrosine kinase
File:PBB Protein MATK image.jpg PDB rendering based on 1jwo.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1jwo​, 1x6g​
Identifiers
Symbols	MATK ; CHK; CTK; DKFZp434N1212; HHYLTK; HYL; HYLTK; Lsk; MGC1708; MGC2101
External IDs	Template:OMIM5 Template:MGI HomoloGene: 48104
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MATK 206267 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Megakaryocyte-associated tyrosine kinase, also known as MATK, is a human gene.

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.

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. PMID 1722201.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Avraham S, Jiang S, Ota S; et al. (1995). "Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product". J. Biol. Chem. 270 (4): 1833–42. PMID 7530249.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 7536744.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bennett BD, Cowley S, Jiang S; et al. (1994). "Identification and characterization of a novel tyrosine kinase from megakaryocytes". J. Biol. Chem. 269 (2): 1068–74. PMID 8288563.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 8999872.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9038210.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9171348.CS1 maint: Multiple names: authors list (link)
• 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. PMID 9255603.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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. PMID 10329710.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12063569.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12429987.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12782282.