MATK_HUMAN
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 03-AUG-2022, entry version 214.
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=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, 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 -!- 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}.
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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_002369.2; NM_002378.3. [P42679-2]
DR RefSeq; NP_647611.1; NM_139354.2. [P42679-3]
DR RefSeq; NP_647612.1; NM_139355.2. [P42679-1]
DR RefSeq; XP_011526320.1; XM_011528018.1. [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; 31.
DR IntAct; P42679; 15.
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 EPD; P42679; -.
DR jPOST; P42679; -.
DR MassIVE; P42679; -.
DR MaxQB; P42679; -.
DR PaxDb; P42679; -.
DR PeptideAtlas; P42679; -.
DR PRIDE; P42679; -.
DR ProteomicsDB; 55524; -. [P42679-1]
DR ProteomicsDB; 55525; -. [P42679-2]
DR ProteomicsDB; 82579; -.
DR Antibodypedia; 1174; 362 antibodies from 32 providers.
DR DNASU; 4145; -.
DR Ensembl; ENST00000310132.11; ENSP00000308734.5; ENSG00000007264.15. [P42679-1]
DR Ensembl; ENST00000395040.6; ENSP00000378481.1; ENSG00000007264.15. [P42679-3]
DR Ensembl; ENST00000395045.6; ENSP00000378485.1; ENSG00000007264.15. [P42679-2]
DR Ensembl; ENST00000619596.4; ENSP00000483213.1; ENSG00000007264.15. [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 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 neXtProt; NX_P42679; -.
DR OpenTargets; ENSG00000007264; -.
DR PharmGKB; PA30649; -.
DR VEuPathDB; HostDB:ENSG00000007264; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000160775; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P42679; -.
DR OMA; IMKLCWE; -.
DR OrthoDB; 491765at2759; -.
DR PhylomeDB; P42679; -.
DR TreeFam; TF351634; -.
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 BioGRID-ORCS; 4145; 26 hits in 1112 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 172 other tissues.
DR ExpressionAtlas; P42679; baseline and differential.
DR Genevisible; P42679; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR CDD; cd09937; SH2_csk_like; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035027; Csk-like_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Reference proteome;
KW SH2 domain; SH3 domain; Transferase; 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 493..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
