| UniProt ID | MATK_HUMAN | |
|---|---|---|
| UniProt AC | P42679 | |
| Protein Name | Megakaryocyte-associated tyrosine-protein kinase | |
| Gene Name | MATK | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 507 | |
| Subcellular Localization | Cytoplasm . Membrane . In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation. | |
| Protein Description | 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.. | |
| Protein Sequence | MAGRGSLVSWRAFHGCDSAEELPRVSPRFLRAWHPPPVSARMPTRRWAPGTQCITKCEHTRPKPGELAFRKGDVVTILEACENKSWYRVKHHTSGQEGLLAAGALREREALSADPKLSLMPWFHGKISGQEAVQQLQPPEDGLFLVRESARHPGDYVLCVSFGRDVIHYRVLHRDGHLTIDEAVFFCNLMDMVEHYSKDKGAICTKLVRPKRKHGTKSAEEELARAGWLLNLQHLTLGAQIGEGEFGAVLQGEYLGQKVAVKNIKCDVTAQAFLDETAVMTKMQHENLVRLLGVILHQGLYIVMEHVSKGNLVNFLRTRGRALVNTAQLLQFSLHVAEGMEYLESKKLVHRDLAARNILVSEDLVAKVSDFGLAKAERKGLDSSRLPVKWTAPEALKHGKFTSKSDVWSFGVLLWEVFSYGRAPYPKMSLKEVSEAVEKGYRMEPPEGCPGPVHVLMSSCWEAEPARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQEP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 4 | Methylation | ----MAGRGSLVSWR ----CCCCCCCEEHH | 23.22 | - | |
| 11 | Methylation | RGSLVSWRAFHGCDS CCCCEEHHHHCCCCC | 21.62 | - | |
| 18 | Phosphorylation | RAFHGCDSAEELPRV HHHCCCCCHHHCCCC | 41.47 | 28450419 | |
| 18 (in isoform 2) | Phosphorylation | - | 41.47 | - | |
| 26 | Phosphorylation | AEELPRVSPRFLRAW HHHCCCCCHHHHHHC | 16.19 | 23401153 | |
| 27 (in isoform 2) | Phosphorylation | - | 28.34 | - | |
| 31 | Methylation | RVSPRFLRAWHPPPV CCCHHHHHHCCCCCC | 32.68 | - | |
| 75 | Ubiquitination | AFRKGDVVTILEACE EEECCCEEEEEHHHC | 3.07 | 21890473 | |
| 76 | Phosphorylation | FRKGDVVTILEACEN EECCCEEEEEHHHCC | 21.50 | - | |
| 85 | Phosphorylation | LEACENKSWYRVKHH EHHHCCCCEEEEEEC | 40.70 | - | |
| 87 | Phosphorylation | ACENKSWYRVKHHTS HHCCCCEEEEEECCC | 16.78 | - | |
| 116 | Ubiquitination | EALSADPKLSLMPWF HHHCCCCCHHHCCCC | 51.78 | 21890473 | |
| 117 | Ubiquitination | ALSADPKLSLMPWFH HHCCCCCHHHCCCCC | 6.06 | 21890473 | |
| 117 (in isoform 2) | Ubiquitination | - | 6.06 | - | |
| 118 | Phosphorylation | LSADPKLSLMPWFHG HCCCCCHHHCCCCCC | 28.84 | 27461979 | |
| 217 | Ubiquitination | PKRKHGTKSAEEELA CCCCCCCCCHHHHHH | 52.87 | - | |
| 308 | Phosphorylation | YIVMEHVSKGNLVNF EEEEECCCCCCHHHH | 36.43 | - | |
| 333 | Phosphorylation | TAQLLQFSLHVAEGM HHHHHHHHHHHHHCH | 12.47 | 28387310 | |
| 345 | Phosphorylation | EGMEYLESKKLVHRD HCHHHHHHCCHHCHH | 32.28 | 28387310 | |
| 384 | Phosphorylation | ERKGLDSSRLPVKWT HHCCCCCCCCCCCCC | 37.19 | 24719451 | |
| 441 | Phosphorylation | SEAVEKGYRMEPPEG HHHHHHCCCCCCCCC | 20.18 | 29496907 | |
| 484 | Phosphorylation | KLARELRSAGAPASV HHHHHHHHCCCCCCC | 43.61 | 29396449 | |
| 490 | Phosphorylation | RSAGAPASVSGQDAD HHCCCCCCCCCCCCC | 18.76 | 29396449 | |
| 492 | Phosphorylation | AGAPASVSGQDADGS CCCCCCCCCCCCCCC | 28.39 | 29978859 | |
| 499 | Phosphorylation | SGQDADGSTSPRSQE CCCCCCCCCCCCCCC | 26.68 | 23401153 | |
| 500 (in isoform 2) | Phosphorylation | - | 48.56 | 27251275 | |
| 500 | Phosphorylation | GQDADGSTSPRSQEP CCCCCCCCCCCCCCC | 48.56 | 25159151 | |
| 501 | Phosphorylation | QDADGSTSPRSQEP- CCCCCCCCCCCCCC- | 21.73 | 17525332 | |
| 504 | Phosphorylation | DGSTSPRSQEP---- CCCCCCCCCCC---- | 42.13 | 17525332 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MATK_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MATK_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| NTRK1_HUMAN | NTRK1 | physical | 10329710 | |
| PAXI_HUMAN | PXN | physical | 10080957 | |
| KIT_HUMAN | KIT | physical | 7536744 | |
| SRC_HUMAN | SRC | physical | 7530249 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY. | |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501 AND SER-504, ANDMASS SPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY. | |