MATK_HUMAN - dbPTM
MATK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Methylation----MAGRGSLVSWR
----CCCCCCCEEHH
23.22-
11MethylationRGSLVSWRAFHGCDS
CCCCEEHHHHCCCCC
21.62-
18PhosphorylationRAFHGCDSAEELPRV
HHHCCCCCHHHCCCC
41.4728450419
18 (in isoform 2)Phosphorylation-41.47-
26PhosphorylationAEELPRVSPRFLRAW
HHHCCCCCHHHHHHC
16.1923401153
27 (in isoform 2)Phosphorylation-28.34-
31MethylationRVSPRFLRAWHPPPV
CCCHHHHHHCCCCCC
32.68-
75UbiquitinationAFRKGDVVTILEACE
EEECCCEEEEEHHHC
3.0721890473
76PhosphorylationFRKGDVVTILEACEN
EECCCEEEEEHHHCC
21.50-
85PhosphorylationLEACENKSWYRVKHH
EHHHCCCCEEEEEEC
40.70-
87PhosphorylationACENKSWYRVKHHTS
HHCCCCEEEEEECCC
16.78-
116UbiquitinationEALSADPKLSLMPWF
HHHCCCCCHHHCCCC
51.7821890473
117UbiquitinationALSADPKLSLMPWFH
HHCCCCCHHHCCCCC
6.0621890473
117 (in isoform 2)Ubiquitination-6.06-
118PhosphorylationLSADPKLSLMPWFHG
HCCCCCHHHCCCCCC
28.8427461979
217UbiquitinationPKRKHGTKSAEEELA
CCCCCCCCCHHHHHH
52.87-
308PhosphorylationYIVMEHVSKGNLVNF
EEEEECCCCCCHHHH
36.43-
333PhosphorylationTAQLLQFSLHVAEGM
HHHHHHHHHHHHHCH
12.4728387310
345PhosphorylationEGMEYLESKKLVHRD
HCHHHHHHCCHHCHH
32.2828387310
384PhosphorylationERKGLDSSRLPVKWT
HHCCCCCCCCCCCCC
37.1924719451
441PhosphorylationSEAVEKGYRMEPPEG
HHHHHHCCCCCCCCC
20.1829496907
484PhosphorylationKLARELRSAGAPASV
HHHHHHHHCCCCCCC
43.6129396449
490PhosphorylationRSAGAPASVSGQDAD
HHCCCCCCCCCCCCC
18.7629396449
492PhosphorylationAGAPASVSGQDADGS
CCCCCCCCCCCCCCC
28.3929978859
499PhosphorylationSGQDADGSTSPRSQE
CCCCCCCCCCCCCCC
26.6823401153
500 (in isoform 2)Phosphorylation-48.5627251275
500PhosphorylationGQDADGSTSPRSQEP
CCCCCCCCCCCCCCC
48.5625159151
501PhosphorylationQDADGSTSPRSQEP-
CCCCCCCCCCCCCC-
21.7317525332
504PhosphorylationDGSTSPRSQEP----
CCCCCCCCCCC----
42.1317525332

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MATK_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NTRK1_HUMANNTRK1physical
10329710
PAXI_HUMANPXNphysical
10080957
KIT_HUMANKITphysical
7536744
SRC_HUMANSRCphysical
7530249

Drug and Disease Associations
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.
Regulatory Network of MATK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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