Megakaryocyte-associated tyrosine kinase

Protein-coding gene in the species Homo sapiens

More reference expression dataBioGPS


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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Megakaryocyte-associated tyrosine-protein kinase is an enzyme that in humans is encoded by the MATK gene.^[5]^[6]^[7]

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.^[7]

Interactions

Megakaryocyte-associated tyrosine kinase has been shown to interact with CD117^[8]^[9] and TrkA.^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000007264 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000004933 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Bennett BD, Cowley S, Jiang S, London R, Deng B, Grabarek J, Groopman JE, Goeddel DV, Avraham H (February 1994). "Identification and characterization of a novel tyrosine kinase from megakaryocytes". J Biol Chem. 269 (2): 1068–74. doi:10.1016/S0021-9258(17)42222-8. PMID 8288563.
^ Avraham S, Jiang S, Ota S, Fu Y, Deng B, Dowler LL, White RA, Avraham H (February 1995). "Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product". J Biol Chem. 270 (4): 1833–42. doi:10.1074/jbc.270.4.1833. PMID 7530249.
^ ^a ^b "Entrez Gene: MATK megakaryocyte-associated tyrosine kinase".
^ Jhun, B H; Rivnay B; Price D; Avraham H (April 1995). "The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit". J. Biol. Chem. 270 (16). UNITED STATES: 9661–6. doi:10.1074/jbc.270.16.9661. ISSN 0021-9258. PMID 7536744.
^ Price, D J; Rivnay B; Fu Y; Jiang S; Avraham S; Avraham H (February 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). UNITED STATES: 5915–20. doi:10.1074/jbc.272.9.5915. ISSN 0021-9258. PMID 9038210.
^ Yamashita, H; Avraham S; Jiang S; Dikic I; Avraham H (May 1999). "The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells". J. Biol. Chem. 274 (21). UNITED STATES: 15059–65. doi:10.1074/jbc.274.21.15059. ISSN 0021-9258. PMID 10329710.

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.

PDB gallery

1jwo: Crystal Structure Analysis of the SH2 Domain of the Csk Homologous Kinase CHK
1x6g: Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase.

Protein kinases: tyrosine kinases (EC 2.7.10)

Receptor tyrosine kinases (EC 2.7.10.1)

Growth factor receptors

EGF receptor family	EGFR ERBB2 ERBB3 ERBB4
Insulin receptor family	IGF1R INSR INSRR
PDGF receptor family	CSF1R FLT3 KIT PDGFR (PDGFRA PDGFRB)
FGF receptor family	FGFR1 FGFR2 FGFR3 FGFR4
VEGF receptors family	VEGFR1 VEGFR2 VEGFR3
HGF receptor family	MET RON
Trk receptor family	NTRK1 NTRK2 NTRK3

EPH receptor family

LTK receptor family

TIE receptor family

ROR receptor family

ROR1
ROR2

DDR receptor family

DDR1
DDR2

PTK7 receptor family

PTK7

RYK receptor family

MuSK receptor family

MUSK

ROS receptor family

ROS1

AATYK receptor family

AATYK
AATYK2

AXL receptor family

RET receptor family

uncategorised

STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)

ABL family	ABL1 ARG
ACK family	ACK1 TNK1
CSK family	CSK MATK
FAK family	FAK PYK2
FES family	FES FER
FRK family	FRK BRK SRMS
JAK family	JAK1 JAK2 JAK3 TYK2
SRC-A family	SRC FGR FYN YES1
SRC-B family	BLK HCK LCK LYN
TEC family	TEC BMX BTK ITK TXK
SYK family	SYK ZAP70

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)