ID MATK_HUMAN Reviewed; 507 AA. AC P42679; B3KNZ9; Q9NST8; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-JAN-2026, entry version 230. DE RecName: Full=Megakaryocyte-associated tyrosine-protein kinase; DE EC=2.7.10.2; DE AltName: Full=CSK homologous kinase; DE Short=CHK; DE AltName: Full=Hematopoietic consensus tyrosine-lacking kinase; DE AltName: Full=Protein kinase HYL; DE AltName: Full=Tyrosine-protein kinase CTK; GN Name=MATK; Synonyms=CTK, HYL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8134117; RA Sakano S., Iwama A., Inazawa J., Ariyama T., Ohno M., Suda T.; RT "Molecular cloning of a novel non-receptor tyrosine kinase, HYL RT (hematopoietic consensus tyrosine-lacking kinase)."; RL Oncogene 9:1155-1161(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Megakaryocyte; RX PubMed=8288563; DOI=10.1016/s0021-9258(17)42222-8; RA Bennett B.D., Cowley S., Jiang S., London R., Deng B., Grabarek J., RA Groopman J.E., Goeddel D.V., Avraham H.; RT "Identification and characterization of a novel tyrosine kinase from RT megakaryocytes."; RL J. Biol. Chem. 269:1068-1074(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7530249; DOI=10.1074/jbc.270.4.1833; RA Avraham S., Jiang S., Ota S., Fu Y., Deng B., Dowler L.L., White R.A., RA Avraham H.; RT "Structural and functional studies of the intracellular tyrosine kinase RT MATK gene and its translated product."; RL J. Biol. Chem. 270:1833-1842(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP CHARACTERIZATION. RX PubMed=7936664; RA Hamaguchi I., Iwama A., Yamaguchi N., Sakano S., Matsuda Y., Suda T.; RT "Characterization of mouse non-receptor tyrosine kinase gene, HYL."; RL Oncogene 9:3371-3374(1994). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Platelet; RX PubMed=9171348; DOI=10.1093/emboj/16.9.2342; RA Hirao A., Hamaguchi I., Suda T., Yamaguchi N.; RT "Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of RT CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets."; RL EMBO J. 16:2342-2351(1997). RN [11] RP INTERACTION WITH KIT. RX PubMed=9038210; DOI=10.1074/jbc.272.9.5915; RA Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.; RT "Direct association of Csk homologous kinase (CHK) with the RT diphosphorylated site Tyr568/570 of the activated c-KIT in RT megakaryocytes."; RL J. Biol. Chem. 272:5915-5920(1997). RN [12] RP REVIEW ON ROLE IN KIT SIGNALING. RX PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055; RA Roskoski R. Jr.; RT "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."; RL Biochem. Biophys. Res. Commun. 337:1-13(2005). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP STRUCTURE BY NMR OF 39-108. RG RIKEN structural genomics initiative (RSGI); RT "Solution structures of the SH3 domain of human megakaryocyte-associated RT tyrosine-protein kinase."; RL Submitted (NOV-2005) to the PDB data bank. RN [20] RP VARIANTS [LARGE SCALE ANALYSIS] THR-354; THR-496 AND GLN-503. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Could play a significant role in the signal transduction of CC hematopoietic cells. May regulate tyrosine kinase activity of SRC- CC family members in brain by specifically phosphorylating their C- CC terminal regulatory tyrosine residue which acts as a negative CC regulatory site. It may play an inhibitory role in the control of T- CC cell proliferation. {ECO:0000269|PubMed:9171348}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBUNIT: Interacts with KIT. {ECO:0000269|PubMed:9038210}. CC -!- INTERACTION: CC P42679; P10275: AR; NbExp=4; IntAct=EBI-751664, EBI-608057; CC P42679; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-751664, EBI-11282723; CC P42679; P04626: ERBB2; NbExp=2; IntAct=EBI-751664, EBI-641062; CC P42679; P08238: HSP90AB1; NbExp=2; IntAct=EBI-751664, EBI-352572; CC P42679; Q92876: KLK6; NbExp=3; IntAct=EBI-751664, EBI-2432309; CC P42679; Q5S007: LRRK2; NbExp=2; IntAct=EBI-751664, EBI-5323863; CC P42679; P62258: YWHAE; NbExp=2; IntAct=EBI-751664, EBI-356498; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9171348}. Membrane CC {ECO:0000269|PubMed:9171348}. Note=In platelets, 90% of MATK localizes CC to the membrane fraction, and translocates to the cytoskeleton upon CC thrombin stimulation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P42679-1; Sequence=Displayed; CC Name=2; CC IsoId=P42679-2; Sequence=VSP_043123; CC Name=3; CC IsoId=P42679-3; Sequence=VSP_044277; CC -!- TISSUE SPECIFICITY: Expressed in various myeloid cell lines, detected CC in brain and lung. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L18974; AAA16703.1; -; mRNA. DR EMBL; X77278; CAA54493.1; -; mRNA. DR EMBL; S75164; AAC60645.1; -; Genomic_DNA. DR EMBL; S75145; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75147; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75166; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75168; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75151; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75153; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75155; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75156; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75158; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75159; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; S75162; AAC60645.1; JOINED; Genomic_DNA. DR EMBL; AK055395; BAG51511.1; -; mRNA. DR EMBL; AL137754; CAB70906.2; -; mRNA. DR EMBL; AC005777; AAC62843.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69285.1; -; Genomic_DNA. DR EMBL; BC000114; AAH00114.1; -; mRNA. DR EMBL; BC003109; AAH03109.1; -; mRNA. DR CCDS; CCDS12113.1; -. [P42679-2] DR CCDS; CCDS12114.1; -. [P42679-1] DR CCDS; CCDS42468.1; -. [P42679-3] DR PIR; A49865; A49865. DR PIR; A55625; A55625. DR RefSeq; NP_001427506.1; NM_001440577.1. [P42679-1] DR RefSeq; NP_002369.2; NM_002378.3. [P42679-2] DR RefSeq; NP_647611.1; NM_139354.3. [P42679-3] DR RefSeq; NP_647612.1; NM_139355.3. [P42679-1] DR PDB; 1JWO; X-ray; 2.50 A; A=117-213. DR PDB; 1X6G; NMR; -; A=41-108. DR PDB; 3US4; X-ray; 1.50 A; A=117-213. DR PDBsum; 1JWO; -. DR PDBsum; 1X6G; -. DR PDBsum; 3US4; -. DR AlphaFoldDB; P42679; -. DR SMR; P42679; -. DR BioGRID; 110315; 33. DR FunCoup; P42679; 601. DR IntAct; P42679; 20. DR MINT; P42679; -. DR STRING; 9606.ENSP00000378485; -. DR BindingDB; P42679; -. DR ChEMBL; CHEMBL4175; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; P42679; -. DR iPTMnet; P42679; -. DR PhosphoSitePlus; P42679; -. DR BioMuta; MATK; -. DR DMDM; 1169123; -. DR CPTAC; CPTAC-1790; -. DR jPOST; P42679; -. DR MassIVE; P42679; -. DR PaxDb; 9606-ENSP00000378485; -. DR PeptideAtlas; P42679; -. DR ProteomicsDB; 55524; -. [P42679-1] DR ProteomicsDB; 55525; -. [P42679-2] DR ProteomicsDB; 82579; -. DR Pumba; P42679; -. DR Antibodypedia; 1174; 359 antibodies from 32 providers. DR DNASU; 4145; -. DR Ensembl; ENST00000310132.11; ENSP00000308734.5; ENSG00000007264.16. [P42679-1] DR Ensembl; ENST00000395040.6; ENSP00000378481.1; ENSG00000007264.16. [P42679-3] DR Ensembl; ENST00000395045.6; ENSP00000378485.1; ENSG00000007264.16. [P42679-2] DR Ensembl; ENST00000619596.4; ENSP00000483213.1; ENSG00000007264.16. [P42679-2] DR GeneID; 4145; -. DR KEGG; hsa:4145; -. DR MANE-Select; ENST00000310132.11; ENSP00000308734.5; NM_139355.3; NP_647612.1. DR UCSC; uc002lyt.4; human. [P42679-1] DR AGR; HGNC:6906; -. DR ClinPGx; PA30649; -. DR CTD; 4145; -. DR DisGeNET; 4145; -. DR GeneCards; MATK; -. DR HGNC; HGNC:6906; MATK. DR HPA; ENSG00000007264; Tissue enhanced (bone marrow, brain). DR MIM; 600038; gene. DR OpenTargets; ENSG00000007264; -. DR VEuPathDB; HostDB:ENSG00000007264; -. DR eggNOG; KOG0197; Eukaryota. DR GeneTree; ENSGT00940000160775; -. DR HOGENOM; CLU_000288_7_2_1; -. DR InParanoid; P42679; -. DR OMA; HDSGQEG; -. DR OrthoDB; 346907at2759; -. DR PAN-GO; P42679; 1 GO annotation based on evolutionary models. DR PhylomeDB; P42679; -. DR BRENDA; 2.7.10.2; 2681. DR PathwayCommons; P42679; -. DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling. DR SignaLink; P42679; -. DR SIGNOR; P42679; -. DR Agora; ENSG00000007264; -. DR BioGRID-ORCS; 4145; 33 hits in 1190 CRISPR screens. DR EvolutionaryTrace; P42679; -. DR GeneWiki; Megakaryocyte-associated_tyrosine_kinase; -. DR GenomeRNAi; 4145; -. DR Pharos; P42679; Tbio. DR PRO; PR:P42679; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P42679; protein. DR Bgee; ENSG00000007264; Expressed in granulocyte and 173 other cell types or tissues. DR ExpressionAtlas; P42679; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR CDD; cd05083; PTKc_Chk; 1. DR CDD; cd09937; SH2_csk_like; 1. DR CDD; cd11811; SH3_CHK; 1. DR FunFam; 1.10.510.10:FF:000376; Tyrosine-protein kinase; 1. DR FunFam; 2.30.30.40:FF:000145; Tyrosine-protein kinase; 1. DR FunFam; 3.30.200.20:FF:000053; Tyrosine-protein kinase; 1. DR FunFam; 3.30.505.10:FF:000023; Tyrosine-protein kinase; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR035027; Csk-like_SH2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050198; Non-receptor_tyrosine_kinases. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase; KW Membrane; Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; SH2 domain; SH3 domain; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1..507 FT /note="Megakaryocyte-associated tyrosine-protein kinase" FT /id="PRO_0000088073" FT DOMAIN 48..110 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 122..211 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 235..482 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 482..507 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 491..507 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 352 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 241..249 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..41 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_044277" FT VAR_SEQ 1..24 FT /note="MAGRGSLVSWRAFHGCDSAEELPR -> MQGHFPAERREGRPRRGTRGQQQL FT L (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043123" FT VARIANT 354 FT /note="A -> T (in an ovarian mucinous carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041679" FT VARIANT 496 FT /note="A -> T (in dbSNP:rs35351680)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041680" FT VARIANT 503 FT /note="R -> Q (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs778726488)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041681" FT CONFLICT 107..108 FT /note="ER -> DG (in Ref. 1; AAA16703)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="Missing (in Ref. 1; AAA16703)" FT /evidence="ECO:0000305" FT CONFLICT 466..507 FT /note="ARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQEP -> PAGHPS FT ANWPRSWPGSYAVQVPQPPSQGRTPTVHLAPKPGALTPPGGPWPQRTERVESAAWGH FT (in Ref. 1; AAA16703)" FT /evidence="ECO:0000305" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:1X6G" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:1X6G" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1X6G" FT STRAND 123..126 FT /evidence="ECO:0007829|PDB:1JWO" FT HELIX 129..135 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 156..162 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 165..174 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 177..188 FT /evidence="ECO:0007829|PDB:3US4" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:3US4" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:3US4" SQ SEQUENCE 507 AA; 56469 MW; 85721C6E024575EF CRC64; MAGRGSLVSW RAFHGCDSAE ELPRVSPRFL RAWHPPPVSA RMPTRRWAPG TQCITKCEHT RPKPGELAFR KGDVVTILEA CENKSWYRVK HHTSGQEGLL AAGALREREA LSADPKLSLM PWFHGKISGQ EAVQQLQPPE DGLFLVRESA RHPGDYVLCV SFGRDVIHYR VLHRDGHLTI DEAVFFCNLM DMVEHYSKDK GAICTKLVRP KRKHGTKSAE EELARAGWLL NLQHLTLGAQ IGEGEFGAVL QGEYLGQKVA VKNIKCDVTA QAFLDETAVM TKMQHENLVR LLGVILHQGL YIVMEHVSKG NLVNFLRTRG RALVNTAQLL QFSLHVAEGM EYLESKKLVH RDLAARNILV SEDLVAKVSD FGLAKAERKG LDSSRLPVKW TAPEALKHGK FTSKSDVWSF GVLLWEVFSY GRAPYPKMSL KEVSEAVEKG YRMEPPEGCP GPVHVLMSSC WEAEPARRPP FRKLAEKLAR ELRSAGAPAS VSGQDADGST SPRSQEP //