Megakaryocyte-associated tyrosine kinase: Difference between revisions

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{{Infobox_gene}}
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'''Megakaryocyte-associated tyrosine-protein kinase''' is an [[enzyme]] that in humans is encoded by the ''MATK'' [[gene]].<ref name="pmid8288563">{{cite journal |vauthors=Bennett BD, Cowley S, Jiang S, London R, Deng B, Grabarek J, Groopman JE, Goeddel DV, Avraham H | title = Identification and characterization of a novel tyrosine kinase from megakaryocytes | journal = J Biol Chem | volume = 269 | issue = 2 | pages = 1068–74 |date=February 1994 | pmid = 8288563 | pmc =  | doi =  }}</ref><ref name="pmid7530249">{{cite journal |vauthors=Avraham S, Jiang S, Ota S, Fu Y, Deng B, Dowler LL, White RA, Avraham H | title = Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product | journal = J Biol Chem | volume = 270 | issue = 4 | pages = 1833–42 |date=February 1995 | pmid = 7530249 | pmc =  | doi =10.1074/jbc.270.4.1833 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MATK megakaryocyte-associated tyrosine kinase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4145| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_MATK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jwo.
| PDB = {{PDB2|1jwo}}, {{PDB2|1x6g}}
| Name = Megakaryocyte-associated tyrosine kinase
| HGNCid = 6906
| Symbol = MATK
| AltSymbols =; CHK; CTK; DKFZp434N1212; HHYLTK; HYL; HYLTK; Lsk; MGC1708; MGC2101
| OMIM = 600038
| ECnumber =
| Homologene = 48104
| MGIid = 99259
  | GeneAtlas_image1 = PBB_GE_MATK_206267_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4145
    | Hs_Ensembl = ENSG00000007264
    | Hs_RefseqProtein = NP_002369
    | Hs_RefseqmRNA = NM_002378
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 3728968
    | Hs_GenLoc_end = 3740345
    | Hs_Uniprot = P42679
    | Mm_EntrezGene = 17179
    | Mm_Ensembl = ENSMUSG00000004933
    | Mm_RefseqmRNA = NM_010768
    | Mm_RefseqProtein = NP_034898
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 80660674
    | Mm_GenLoc_end = 80666110
    | Mm_Uniprot = P70223
  }}
}}
'''Megakaryocyte-associated tyrosine kinase''', also known as '''MATK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MATK megakaryocyte-associated tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4145| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: MATK megakaryocyte-associated tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4145| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}
==Interactions==
Megakaryocyte-associated tyrosine kinase has been shown to [[Protein-protein interaction|interact]] with [[CD117]]<ref name=pmid7536744>{{cite journal |doi=10.1074/jbc.270.16.9661 |last=Jhun |first=B H |authorlink= |author2=Rivnay B |author3=Price D |author4=Avraham H  |date=April 1995  |title=The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit |journal=J. Biol. Chem. |volume=270 |issue=16 |pages=9661–6 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 7536744 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9038210>{{cite journal |doi=10.1074/jbc.272.9.5915 |last=Price |first=D J |authorlink= |author2=Rivnay B |author3=Fu Y |author4=Jiang S |author5=Avraham S |author6=Avraham H  |date=February 1997  |title=Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes |journal=J. Biol. Chem. |volume=272 |issue=9 |pages=5915–20 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9038210 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[TrkA]].<ref name=pmid10329710>{{cite journal |doi=10.1074/jbc.274.21.15059 |last=Yamashita |first=H |authorlink= |author2=Avraham S |author3=Jiang S |author4=Dikic I |author5=Avraham H  |date=May 1999 |title=The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells |journal=J. Biol. Chem. |volume=274 |issue=21 |pages=15059–65 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10329710 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Okada M, Nada S, Yamanashi Y, ''et al.'' |title=CSK: a protein-tyrosine kinase involved in regulation of src family kinases. |journal=J. Biol. Chem. |volume=266 |issue= 36 |pages= 24249-52 |year= 1992 |pmid= 1722201 |doi=  }}
*{{cite journal   |vauthors=Okada M, Nada S, Yamanashi Y, etal |title=CSK: a protein-tyrosine kinase involved in regulation of src family kinases. |journal=J. Biol. Chem. |volume=266 |issue= 36 |pages= 24249–52 |year= 1992 |pmid= 1722201 |doi=  }}
*{{cite journal | author=McVicar DW, Lal BK, Lloyd A, ''et al.'' |title=Molecular cloning of lsk, a carboxyl-terminal src kinase (csk) related gene, expressed in leukocytes. |journal=Oncogene |volume=9 |issue= 7 |pages= 2037-44 |year= 1994 |pmid= 7516063 |doi=  }}
*{{cite journal   |vauthors=McVicar DW, Lal BK, Lloyd A, etal |title=Molecular cloning of lsk, a carboxyl-terminal src kinase (csk) related gene, expressed in leukocytes. |journal=Oncogene |volume=9 |issue= 7 |pages= 2037–44 |year= 1994 |pmid= 7516063 |doi=  }}
*{{cite journal  | author=Avraham S, Jiang S, Ota S, ''et al.'' |title=Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product. |journal=J. Biol. Chem. |volume=270 |issue= 4 |pages= 1833-42 |year= 1995 |pmid= 7530249 |doi= }}
*{{cite journal  |vauthors=Jhun BH, Rivnay B, Price D, Avraham H |title=The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit. |journal=J. Biol. Chem. |volume=270 |issue= 16 |pages= 9661–6 |year= 1995 |pmid= 7536744 |doi=10.1074/jbc.270.16.9661 }}
*{{cite journal | author=Jhun BH, Rivnay B, Price D, Avraham H |title=The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit. |journal=J. Biol. Chem. |volume=270 |issue= 16 |pages= 9661-6 |year= 1995 |pmid= 7536744 |doi=  }}
*{{cite journal   |vauthors=Hamaguchi I, Iwama A, Yamaguchi N, etal |title=Characterization of mouse non-receptor tyrosine kinase gene, HYL. |journal=Oncogene |volume=9 |issue= 11 |pages= 3371–4 |year= 1994 |pmid= 7936664 |doi=  }}
*{{cite journal  | author=Hamaguchi I, Iwama A, Yamaguchi N, ''et al.'' |title=Characterization of mouse non-receptor tyrosine kinase gene, HYL. |journal=Oncogene |volume=9 |issue= 11 |pages= 3371-4 |year= 1994 |pmid= 7936664 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal   |vauthors=Sakano S, Iwama A, Inazawa J, etal |title=Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase). |journal=Oncogene |volume=9 |issue= 4 |pages= 1155–61 |year= 1994 |pmid= 8134117 |doi=  }}
*{{cite journal | author=Sakano S, Iwama A, Inazawa J, ''et al.'' |title=Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase). |journal=Oncogene |volume=9 |issue= 4 |pages= 1155-61 |year= 1994 |pmid= 8134117 |doi=  }}
*{{cite journal   |vauthors=Zrihan-Licht S, Lim J, Keydar I, etal |title=Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1856–63 |year= 1997 |pmid= 8999872 |doi=10.1074/jbc.272.3.1856 }}
*{{cite journal | author=Bennett BD, Cowley S, Jiang S, ''et al.'' |title=Identification and characterization of a novel tyrosine kinase from megakaryocytes. |journal=J. Biol. Chem. |volume=269 |issue= 2 |pages= 1068-74 |year= 1994 |pmid= 8288563 |doi= }}
*{{cite journal   |vauthors=Price DJ, Rivnay B, Fu Y, etal |title=Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 5915–20 |year= 1997 |pmid= 9038210 |doi=10.1074/jbc.272.9.5915  }}
*{{cite journal  | author=Zrihan-Licht S, Lim J, Keydar I, ''et al.'' |title=Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1856-63 |year= 1997 |pmid= 8999872 |doi=  }}
*{{cite journal  |vauthors=Hirao A, Hamaguchi I, Suda T, Yamaguchi N |title=Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets. |journal=EMBO J. |volume=16 |issue= 9 |pages= 2342–51 |year= 1997 |pmid= 9171348 |doi= 10.1093/emboj/16.9.2342 | pmc=1169835 }}
*{{cite journal | author=Price DJ, Rivnay B, Fu Y, ''et al.'' |title=Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 5915-20 |year= 1997 |pmid= 9038210 |doi=  }}
*{{cite journal   |vauthors=Grgurevich S, Linnekin D, Musso T, etal |title=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. |journal=Growth Factors |volume=14 |issue= 2-3 |pages= 103–15 |year= 1997 |pmid= 9255603 |doi=10.3109/08977199709021514 }}
*{{cite journal | author=Hirao A, Hamaguchi I, Suda T, Yamaguchi N |title=Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets. |journal=EMBO J. |volume=16 |issue= 9 |pages= 2342-51 |year= 1997 |pmid= 9171348 |doi= 10.1093/emboj/16.9.2342 }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal  | author=Grgurevich S, Linnekin D, Musso T, ''et al.'' |title=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. |journal=Growth Factors |volume=14 |issue= 2-3 |pages= 103-15 |year= 1997 |pmid= 9255603 |doi= }}
*{{cite journal  |vauthors=Grgurevich S, Mikhael A, McVicar DW |title=The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 3 |pages= 668–75 |year= 1999 |pmid= 10080957 |doi= 10.1006/bbrc.1999.0398 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Yamashita H, Avraham S, Jiang S, etal |title=The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 15059–65 |year= 1999 |pmid= 10329710 |doi=10.1074/jbc.274.21.15059 }}
*{{cite journal | author=Grgurevich S, Mikhael A, McVicar DW |title=The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 3 |pages= 668-75 |year= 1999 |pmid= 10080957 |doi= 10.1006/bbrc.1999.0398 }}
*{{cite journal   |vauthors=McShan GD, Zagozdzon R, Park SY, etal |title=Csk homologous kinase associates with RAFTK/Pyk2 in breast cancer cells and negatively regulates its activation and breast cancer cell migration. |journal=Int. J. Oncol. |volume=21 |issue= 1 |pages= 197–205 |year= 2002 |pmid= 12063569 |doi= 10.3892/ijo.21.1.197}}
*{{cite journal | author=Yamashita H, Avraham S, Jiang S, ''et al.'' |title=The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 15059-65 |year= 1999 |pmid= 10329710 |doi= }}
*{{cite journal   |vauthors=Kim S, Zagozdzon R, Meisler A, etal |title=Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36465–70 |year= 2002 |pmid= 12122014 |doi= 10.1074/jbc.M206018200 }}
*{{cite journal  | author=McShan GD, Zagozdzon R, Park SY, ''et al.'' |title=Csk homologous kinase associates with RAFTK/Pyk2 in breast cancer cells and negatively regulates its activation and breast cancer cell migration. |journal=Int. J. Oncol. |volume=21 |issue= 1 |pages= 197-205 |year= 2002 |pmid= 12063569 |doi=  }}
*{{cite journal  |vauthors=Zagozdzon R, Bougeret C, Fu Y, Avraham HK |title=Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells. |journal=Int. J. Oncol. |volume=21 |issue= 6 |pages= 1347–52 |year= 2003 |pmid= 12429987 |doi=  10.3892/ijo.21.6.1347}}
*{{cite journal | author=Kim S, Zagozdzon R, Meisler A, ''et al.'' |title=Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36465-70 |year= 2002 |pmid= 12122014 |doi= 10.1074/jbc.M206018200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  | author=Zagozdzon R, Bougeret C, Fu Y, Avraham HK |title=Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells. |journal=Int. J. Oncol. |volume=21 |issue= 6 |pages= 1347-52 |year= 2003 |pmid= 12429987 |doi= }}
*{{cite journal  |vauthors=Mikkola ET, Bergman M |title=Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK. |journal=FEBS Lett. |volume=544 |issue= 1-3 |pages= 11–4 |year= 2003 |pmid= 12782282 |doi=10.1016/S0014-5793(03)00405-8 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Mikkola ET, Bergman M |title=Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK. |journal=FEBS Lett. |volume=544 |issue= 1-3 |pages= 11-4 |year= 2003 |pmid= 12782282 |doi= }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=4145}}
{{Tyrosine kinases}}
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[[Category:Human proteins]]
[[Category:Tyrosine kinases]]


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Revision as of 19:51, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Megakaryocyte-associated tyrosine-protein kinase is an enzyme that in humans is encoded by the MATK gene.[1][2][3]

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.[3]

Interactions

Megakaryocyte-associated tyrosine kinase has been shown to interact with CD117[4][5] and TrkA.[6]

References

  1. ↑ 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. PMID 8288563.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: MATK megakaryocyte-associated tyrosine kinase".
  4. ↑ 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. UNITED STATES. 270 (16): 9661–6. doi:10.1074/jbc.270.16.9661. ISSN 0021-9258. PMID 7536744.
  5. ↑ 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. UNITED STATES. 272 (9): 5915–20. doi:10.1074/jbc.272.9.5915. ISSN 0021-9258. PMID 9038210.
  6. ↑ 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. UNITED STATES. 274 (21): 15059–65. doi:10.1074/jbc.274.21.15059. ISSN 0021-9258. PMID 10329710.

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.
  • 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.
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