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Megakaryocyte-associated tyrosine-protein kinase (EC 2.7.10.2) (CSK homologous kinase) (CHK) (Hematopoietic consensus tyrosine-lacking kinase) (Protein kinase HYL) (Tyrosine-protein kinase CTK)

 MATK_HUMAN              Reviewed;         507 AA.
P42679; B3KNZ9; Q9NST8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 186.
RecName: Full=Megakaryocyte-associated tyrosine-protein kinase;
EC=2.7.10.2;
AltName: Full=CSK homologous kinase;
Short=CHK;
AltName: Full=Hematopoietic consensus tyrosine-lacking kinase;
AltName: Full=Protein kinase HYL;
AltName: Full=Tyrosine-protein kinase CTK;
Name=MATK; Synonyms=CTK, HYL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8134117;
Sakano S., Iwama A., Inazawa J., Ariyama T., Ohno M., Suda T.;
"Molecular cloning of a novel non-receptor tyrosine kinase, HYL
(hematopoietic consensus tyrosine-lacking kinase).";
Oncogene 9:1155-1161(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Megakaryocyte;
PubMed=8288563;
Bennett B.D., Cowley S., Jiang S., London R., Deng B., Grabarek J.,
Groopman J.E., Goeddel D.V., Avraham H.;
"Identification and characterization of a novel tyrosine kinase from
megakaryocytes.";
J. Biol. Chem. 269:1068-1074(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7530249; DOI=10.1074/jbc.270.4.1833;
Avraham S., Jiang S., Ota S., Fu Y., Deng B., Dowler L.L., White R.A.,
Avraham H.;
"Structural and functional studies of the intracellular tyrosine
kinase MATK gene and its translated product.";
J. Biol. Chem. 270:1833-1842(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
CHARACTERIZATION.
PubMed=7936664;
Hamaguchi I., Iwama A., Yamaguchi N., Sakano S., Matsuda Y., Suda T.;
"Characterization of mouse non-receptor tyrosine kinase gene, HYL.";
Oncogene 9:3371-3374(1994).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Platelet;
PubMed=9171348; DOI=10.1093/emboj/16.9.2342;
Hirao A., Hamaguchi I., Suda T., Yamaguchi N.;
"Translocation of the Csk homologous kinase (Chk/Hyl) controls
activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated
platelets.";
EMBO J. 16:2342-2351(1997).
[11]
INTERACTION WITH KIT.
PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
"Direct association of Csk homologous kinase (CHK) with the
diphosphorylated site Tyr568/570 of the activated c-KIT in
megakaryocytes.";
J. Biol. Chem. 272:5915-5920(1997).
[12]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
STRUCTURE BY NMR OF 39-108.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the SH3 domain of human megakaryocyte-
associated tyrosine-protein kinase.";
Submitted (NOV-2005) to the PDB data bank.
[20]
VARIANTS [LARGE SCALE ANALYSIS] THR-354; THR-496 AND GLN-503.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Could play a significant role in the signal transduction
of hematopoietic cells. May regulate tyrosine kinase activity of
SRC-family members in brain by specifically phosphorylating their
C-terminal regulatory tyrosine residue which acts as a negative
regulatory site. It may play an inhibitory role in the control of
T-cell proliferation. {ECO:0000269|PubMed:9171348}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts with KIT. {ECO:0000269|PubMed:9038210}.
-!- INTERACTION:
P10275:AR; NbExp=4; IntAct=EBI-751664, EBI-608057;
P04626:ERBB2; NbExp=2; IntAct=EBI-751664, EBI-641062;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-751664, EBI-352572;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-751664, EBI-5323863;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9171348}.
Membrane {ECO:0000269|PubMed:9171348}. Note=In platelets, 90% of
MATK localizes to the membrane fraction, and translocates to the
cytoskeleton upon thrombin stimulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P42679-1; Sequence=Displayed;
Name=2;
IsoId=P42679-2; Sequence=VSP_043123;
Note=No experimental confirmation available.;
Name=3;
IsoId=P42679-3; Sequence=VSP_044277;
-!- TISSUE SPECIFICITY: Expressed in various myeloid cell lines,
detected in brain and lung.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; L18974; AAA16703.1; -; mRNA.
EMBL; X77278; CAA54493.1; -; mRNA.
EMBL; S75164; AAC60645.1; -; Genomic_DNA.
EMBL; S75145; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75147; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75166; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75168; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75151; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75153; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75155; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75156; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75158; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75159; AAC60645.1; JOINED; Genomic_DNA.
EMBL; S75162; AAC60645.1; JOINED; Genomic_DNA.
EMBL; AK055395; BAG51511.1; -; mRNA.
EMBL; AL137754; CAB70906.2; -; mRNA.
EMBL; AC005777; AAC62843.1; -; Genomic_DNA.
EMBL; CH471139; EAW69285.1; -; Genomic_DNA.
EMBL; BC000114; AAH00114.1; -; mRNA.
EMBL; BC003109; AAH03109.1; -; mRNA.
CCDS; CCDS12113.1; -. [P42679-2]
CCDS; CCDS12114.1; -. [P42679-1]
CCDS; CCDS42468.1; -. [P42679-3]
PIR; A49865; A49865.
PIR; A55625; A55625.
RefSeq; NP_002369.2; NM_002378.3. [P42679-2]
RefSeq; NP_647611.1; NM_139354.2. [P42679-3]
RefSeq; NP_647612.1; NM_139355.2. [P42679-1]
RefSeq; XP_011526320.1; XM_011528018.1. [P42679-1]
UniGene; Hs.631845; -.
PDB; 1JWO; X-ray; 2.50 A; A=117-213.
PDB; 1X6G; NMR; -; A=41-108.
PDB; 3US4; X-ray; 1.50 A; A=117-213.
PDBsum; 1JWO; -.
PDBsum; 1X6G; -.
PDBsum; 3US4; -.
ProteinModelPortal; P42679; -.
SMR; P42679; -.
BioGrid; 110315; 14.
IntAct; P42679; 11.
MINT; MINT-1466004; -.
STRING; 9606.ENSP00000378485; -.
BindingDB; P42679; -.
ChEMBL; CHEMBL4175; -.
GuidetoPHARMACOLOGY; 2101; -.
iPTMnet; P42679; -.
PhosphoSitePlus; P42679; -.
BioMuta; MATK; -.
DMDM; 1169123; -.
EPD; P42679; -.
MaxQB; P42679; -.
PaxDb; P42679; -.
PeptideAtlas; P42679; -.
PRIDE; P42679; -.
DNASU; 4145; -.
Ensembl; ENST00000310132; ENSP00000308734; ENSG00000007264. [P42679-1]
Ensembl; ENST00000395040; ENSP00000378481; ENSG00000007264. [P42679-3]
Ensembl; ENST00000395045; ENSP00000378485; ENSG00000007264. [P42679-2]
Ensembl; ENST00000619596; ENSP00000483213; ENSG00000007264. [P42679-2]
GeneID; 4145; -.
KEGG; hsa:4145; -.
UCSC; uc002lyt.4; human. [P42679-1]
CTD; 4145; -.
DisGeNET; 4145; -.
EuPathDB; HostDB:ENSG00000007264.13; -.
GeneCards; MATK; -.
HGNC; HGNC:6906; MATK.
HPA; HPA004847; -.
MIM; 600038; gene.
neXtProt; NX_P42679; -.
OpenTargets; ENSG00000007264; -.
PharmGKB; PA30649; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P42679; -.
KO; K08888; -.
OMA; KAGWLLN; -.
PhylomeDB; P42679; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SignaLink; P42679; -.
SIGNOR; P42679; -.
EvolutionaryTrace; P42679; -.
GeneWiki; Megakaryocyte-associated_tyrosine_kinase; -.
GenomeRNAi; 4145; -.
PRO; PR:P42679; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000007264; -.
CleanEx; HS_MATK; -.
ExpressionAtlas; P42679; baseline and differential.
Genevisible; P42679; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09937; SH2_csk_like; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035027; Csk-like_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
CHAIN 1 507 Megakaryocyte-associated tyrosine-protein
kinase.
/FTId=PRO_0000088073.
DOMAIN 48 110 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 122 211 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 235 482 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 241 249 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 352 352 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 262 262 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 41 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_044277.
VAR_SEQ 1 24 MAGRGSLVSWRAFHGCDSAEELPR -> MQGHFPAERREGR
PRRGTRGQQQLL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043123.
VARIANT 354 354 A -> T (in an ovarian mucinous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041679.
VARIANT 496 496 A -> T (in dbSNP:rs35351680).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041680.
VARIANT 503 503 R -> Q (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs778726488).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041681.
CONFLICT 107 108 ER -> DG (in Ref. 1; AAA16703).
{ECO:0000305}.
CONFLICT 400 400 Missing (in Ref. 1; AAA16703).
{ECO:0000305}.
CONFLICT 466 507 ARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQE
P -> PAGHPSANWPRSWPGSYAVQVPQPPSQGRTPTVHLA
PKPGALTPPGGPWPQRTERVESAAWGH (in Ref. 1;
AAA16703). {ECO:0000305}.
STRAND 52 57 {ECO:0000244|PDB:1X6G}.
STRAND 59 61 {ECO:0000244|PDB:1X6G}.
STRAND 74 79 {ECO:0000244|PDB:1X6G}.
STRAND 83 91 {ECO:0000244|PDB:1X6G}.
TURN 92 94 {ECO:0000244|PDB:1X6G}.
STRAND 97 101 {ECO:0000244|PDB:1X6G}.
HELIX 102 104 {ECO:0000244|PDB:1X6G}.
STRAND 105 107 {ECO:0000244|PDB:1X6G}.
STRAND 123 126 {ECO:0000244|PDB:1JWO}.
HELIX 129 135 {ECO:0000244|PDB:3US4}.
STRAND 144 148 {ECO:0000244|PDB:3US4}.
STRAND 150 152 {ECO:0000244|PDB:3US4}.
STRAND 156 162 {ECO:0000244|PDB:3US4}.
STRAND 165 174 {ECO:0000244|PDB:3US4}.
STRAND 177 188 {ECO:0000244|PDB:3US4}.
HELIX 189 198 {ECO:0000244|PDB:3US4}.
STRAND 203 205 {ECO:0000244|PDB:3US4}.
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


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