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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.
29-SEP-2021, entry version 211.
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:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- SUBUNIT: Interacts with KIT. {ECO:0000269|PubMed:9038210}.
-!- INTERACTION:
P42679; P10275: AR; NbExp=4; IntAct=EBI-751664, EBI-608057;
P42679; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-751664, EBI-11282723;
P42679; P04626: ERBB2; NbExp=2; IntAct=EBI-751664, EBI-641062;
P42679; P08238: HSP90AB1; NbExp=2; IntAct=EBI-751664, EBI-352572;
P42679; Q92876: KLK6; NbExp=3; IntAct=EBI-751664, EBI-2432309;
P42679; 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;
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]
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; -.
SMR; P42679; -.
BioGRID; 110315; 30.
IntAct; P42679; 15.
STRING; 9606.ENSP00000378485; -.
BindingDB; P42679; -.
ChEMBL; CHEMBL4175; -.
DrugBank; DB12010; Fostamatinib.
DrugCentral; P42679; -.
iPTMnet; P42679; -.
PhosphoSitePlus; P42679; -.
BioMuta; MATK; -.
DMDM; 1169123; -.
CPTAC; CPTAC-1790; -.
EPD; P42679; -.
jPOST; P42679; -.
MassIVE; P42679; -.
MaxQB; P42679; -.
PaxDb; P42679; -.
PeptideAtlas; P42679; -.
PRIDE; P42679; -.
ProteomicsDB; 55524; -. [P42679-1]
ProteomicsDB; 55525; -. [P42679-2]
ProteomicsDB; 82579; -.
Antibodypedia; 1174; 360 antibodies.
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; -.
GeneCards; MATK; -.
HGNC; HGNC:6906; MATK.
HPA; ENSG00000007264; Tissue enhanced (blood, bone marrow, brain).
MIM; 600038; gene.
neXtProt; NX_P42679; -.
OpenTargets; ENSG00000007264; -.
PharmGKB; PA30649; -.
VEuPathDB; HostDB:ENSG00000007264; -.
eggNOG; KOG0197; Eukaryota.
GeneTree; ENSGT00940000160775; -.
HOGENOM; CLU_000288_7_2_1; -.
InParanoid; P42679; -.
OMA; FHYRVIY; -.
OrthoDB; 491765at2759; -.
PhylomeDB; P42679; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
PathwayCommons; P42679; -.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SignaLink; P42679; -.
SIGNOR; P42679; -.
BioGRID-ORCS; 4145; 19 hits in 1044 CRISPR screens.
EvolutionaryTrace; P42679; -.
GeneWiki; Megakaryocyte-associated_tyrosine_kinase; -.
GenomeRNAi; 4145; -.
Pharos; P42679; Tbio.
PRO; PR:P42679; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; P42679; protein.
Bgee; ENSG00000007264; Expressed in granulocyte and 212 other tissues.
ExpressionAtlas; P42679; baseline and differential.
Genevisible; P42679; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:RHEA.
GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
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; PK_Tyr_Ser-Thr; 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; Cytoplasm; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
CHAIN 1..507
/note="Megakaryocyte-associated tyrosine-protein kinase"
/id="PRO_0000088073"
DOMAIN 48..110
/note="SH3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
DOMAIN 122..211
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
DOMAIN 235..482
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 241..249
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 482..507
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 493..507
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 352
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 262
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 501
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
VAR_SEQ 1..41
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_044277"
VAR_SEQ 1..24
/note="MAGRGSLVSWRAFHGCDSAEELPR -> MQGHFPAERREGRPRRGTRGQQQL
L (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_043123"
VARIANT 354
/note="A -> T (in an ovarian mucinous carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041679"
VARIANT 496
/note="A -> T (in dbSNP:rs35351680)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041680"
VARIANT 503
/note="R -> Q (in a colorectal adenocarcinoma sample;
somatic mutation; dbSNP:rs778726488)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041681"
CONFLICT 107..108
/note="ER -> DG (in Ref. 1; AAA16703)"
/evidence="ECO:0000305"
CONFLICT 400
/note="Missing (in Ref. 1; AAA16703)"
/evidence="ECO:0000305"
CONFLICT 466..507
/note="ARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQEP -> PAGHPS
ANWPRSWPGSYAVQVPQPPSQGRTPTVHLAPKPGALTPPGGPWPQRTERVESAAWGH
(in Ref. 1; AAA16703)"
/evidence="ECO:0000305"
STRAND 52..57
/evidence="ECO:0007829|PDB:1X6G"
STRAND 59..61
/evidence="ECO:0007829|PDB:1X6G"
STRAND 74..79
/evidence="ECO:0007829|PDB:1X6G"
STRAND 83..91
/evidence="ECO:0007829|PDB:1X6G"
TURN 92..94
/evidence="ECO:0007829|PDB:1X6G"
STRAND 97..101
/evidence="ECO:0007829|PDB:1X6G"
HELIX 102..104
/evidence="ECO:0007829|PDB:1X6G"
STRAND 105..107
/evidence="ECO:0007829|PDB:1X6G"
STRAND 123..126
/evidence="ECO:0007829|PDB:1JWO"
HELIX 129..135
/evidence="ECO:0007829|PDB:3US4"
STRAND 144..148
/evidence="ECO:0007829|PDB:3US4"
STRAND 150..152
/evidence="ECO:0007829|PDB:3US4"
STRAND 156..162
/evidence="ECO:0007829|PDB:3US4"
STRAND 165..174
/evidence="ECO:0007829|PDB:3US4"
STRAND 177..188
/evidence="ECO:0007829|PDB:3US4"
HELIX 189..198
/evidence="ECO:0007829|PDB:3US4"
STRAND 203..205
/evidence="ECO:0007829|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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WP1493: Carbon assimilation C4 pathway
WP1714: Tyrosine metabolism
WP253: Glycolysis
WP1844: MAP kinase cascade
WP32: Translation Factors
WP1653: Galactose metabolism
WP1946: Cori Cycle
WP1567: Glycolysis and Gluconeogenesis
WP1703: Streptomycin biosynthesis
WP1681: Pantothenate and CoA biosynthesis
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1701: Starch and sucrose metabolism
WP1619: Amino sugar and nucleotide sugar metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1676: Non-homologous end-joining
WP1663: Homologous recombination
WP1687: Phenylalanine, tyrosine and tryptophan biosynthesi
WP1644: DNA replication
WP1909: Signal regulatory protein (SIRP) family interactions
WP1654: gamma-Hexachlorocyclohexane degradation
WP2032: TSH signaling pathway
WP1438: Influenza A virus infection
WP1692: Protein export
WP346: Protein Modifications
WP1700: Selenoamino acid metabolism

Related Genes :
[CSK] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase CYL)
[Csk] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK)
[LYN JTK8] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (Lck/Yes-related novel protein tyrosine kinase) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[KIT SCFR] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Piebald trait protein) (PBT) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (p145 c-kit) (v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog) (CD antigen CD117)
[csk-1 Y48G1C.2] Tyrosine-protein kinase csk-1 (EC 2.7.10.2) (C-terminal src kinase)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[LCK] Tyrosine-protein kinase Lck (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (Protein YT16) (Proto-oncogene Lck) (T cell-specific protein-tyrosine kinase) (p56-LCK)
[Csk] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase)
[Lck Lsk-t] Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)
[Flt3 Flk-2 Flt-3] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase 2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Tyrosine-protein kinase receptor flk-2) (CD antigen CD135)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[SYK] Tyrosine-protein kinase SYK (EC 2.7.10.2) (Spleen tyrosine kinase) (p72-Syk)
[KDR FLK1 VEGFR2] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor) (KDR) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[Flt1 Emrk2 Flt Vegfr1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Embryonic receptor kinase 2) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase receptor FLT)
[Melk Kiaa0175 Pk38] Maternal embryonic leucine zipper kinase (EC 2.7.11.1) (Protein kinase PK38) (mPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2)
[Lyn] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[Ptk2b Fak2 Pyk2 Raftk] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[Tek Hyk Tie-2 Tie2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)
[FLT1 FLT FRT VEGFR1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase FRT) (Tyrosine-protein kinase receptor FLT) (FLT) (Vascular permeability factor receptor)
[Kdr Flk-1 Flk1] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase NYK) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[Syk ptk72 Sykb] Tyrosine-protein kinase SYK (EC 2.7.10.2) (Spleen tyrosine kinase)
[FLT3 CD135 FLK2 STK1] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1) (CD antigen CD135)
[JAK2] Tyrosine-protein kinase JAK2 (EC 2.7.10.2) (Janus kinase 2) (JAK-2)
[Itk Emt Tlk Tsk] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (IL-2-inducible T-cell kinase) (Kinase EMT) (Kinase TLK) (T-cell-specific kinase)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[Jak2] Tyrosine-protein kinase JAK2 (EC 2.7.10.2) (Janus kinase 2) (JAK-2)
[TEK TIE2 VMCM VMCM1] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (hTIE2) (p140 TEK) (CD antigen CD202b)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)

Bibliography :