MERTK_HUMAN - dbPTM
MERTK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MERTK_HUMAN
UniProt AC Q12866
Protein Name Tyrosine-protein kinase Mer
Gene Name MERTK
Organism Homo sapiens (Human).
Sequence Length 999
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3..
Protein Sequence MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM
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
45O-linked_GlycosylationPFPGSLQTDHTPLLS
CCCCCCCCCCCCCCC		34.73OGP
84O-linked_GlycosylationNVAIPQVTSVESKPL
CCCCCCCEECCCCCC		23.08OGP
88PhosphorylationPQVTSVESKPLPPLA
CCCEECCCCCCCCCC		37.1024719451
114N-linked_GlycosylationEHKGVKFNCSISVPN
CCCCCEEEEEEECCC		16.95UniProtKB CARBOHYD
170N-linked_GlycosylationTSVQRSDNGSYICKM
EEEEECCCCCEEEEE		42.42UniProtKB CARBOHYD
186UbiquitinationINNEEIVSDPIYIEV
ECCEEEECCCEEEEE		43.2422817900
207N-linked_GlycosylationTKQPESMNVTRNTAF
CCCCCCCCCCCCCEE		41.09UniProtKB CARBOHYD
214UbiquitinationNVTRNTAFNLTCQAV
CCCCCCEEEEEEEEC		7.8727667366
215N-linked_GlycosylationVTRNTAFNLTCQAVG
CCCCCEEEEEEEECC		31.79UniProtKB CARBOHYD
234N-linked_GlycosylationVNIFWVQNSSRVNEQ
EEEEEEECCCCCCCC		32.12UniProtKB CARBOHYD
294N-linked_GlycosylationPTEVSIRNSTAHSIL
CCEEEEECCCCHHHE		41.88UniProtKB CARBOHYD
316N-linked_GlycosylationDGYSPFRNCSIQVKE
CCCCCCCCCEEEEEE		25.02UniProtKB CARBOHYD
329N-linked_GlycosylationKEADPLSNGSVMIFN
EECCCCCCCCEEEEE		55.21UniProtKB CARBOHYD
336N-linked_GlycosylationNGSVMIFNTSALPHL
CCCEEEEECCCCCHH		23.38UniProtKB CARBOHYD
354N-linked_GlycosylationKQLQALANYSIGVSC
HHHHHHHCCCCCCCC		31.75UniProtKB CARBOHYD
356UbiquitinationLQALANYSIGVSCMN
HHHHHCCCCCCCCCH		16.8122817900
360UbiquitinationANYSIGVSCMNEIGW
HCCCCCCCCCHHCCH		11.4822817900
389N-linked_GlycosylationAPSVAPLNVTVFLNE
CCCCCCEEEEEEECC		26.76UniProtKB CARBOHYD
395N-linked_GlycosylationLNVTVFLNESSDNVD
EEEEEEECCCCCCEE		35.32UniProtKB CARBOHYD
442N-linked_GlycosylationLLEEVGQNGSRARIS
HHHHHHHCCCEEEEE		44.47UniProtKB CARBOHYD
442N-linked_GlycosylationLLEEVGQNGSRARIS
HHHHHHHCCCEEEEE		44.4716335952
451UbiquitinationSRARISVQVHNATCT
CEEEEEEEEECCEEE		24.7821890473
454N-linked_GlycosylationRISVQVHNATCTVRI
EEEEEEECCEEEEEE		37.78UniProtKB CARBOHYD
458PhosphorylationQVHNATCTVRIAAVT
EEECCEEEEEEEEEE		14.4119664995
528UbiquitinationISLAIRKRVQETKFG
HHHHHHHHHHHCCCC		26.0422817900
539PhosphorylationTKFGNAFTEEDSELV
CCCCCCCCHHCHHHH		35.7328857561
543PhosphorylationNAFTEEDSELVVNYI
CCCCHHCHHHHHHHH		35.7927422710
549PhosphorylationDSELVVNYIAKKSFC
CHHHHHHHHHCHHHH		7.2222322096
552UbiquitinationLVVNYIAKKSFCRRA
HHHHHHHCHHHHHHH		39.12-
556UbiquitinationYIAKKSFCRRAIELT
HHHCHHHHHHHHHHH		3.5727667366
563PhosphorylationCRRAIELTLHSLGVS
HHHHHHHHHHHCCCC		15.0527732954
566PhosphorylationAIELTLHSLGVSEEL
HHHHHHHHCCCCHHH		29.9027732954
570PhosphorylationTLHSLGVSEELQNKL
HHHHCCCCHHHHHHH		24.4527732954
591UbiquitinationRNLLILGKILGEGEF
CCHHHHHHHHCCCCC		31.1721906983
607UbiquitinationSVMEGNLKQEDGTSL
CCCCCCEECCCCCEE		56.49-
613PhosphorylationLKQEDGTSLKVAVKT
EECCCCCEEEEEEEE		31.5522817900
619UbiquitinationTSLKVAVKTMKLDNS
CEEEEEEEEEECCCC		32.9127667366
622UbiquitinationKVAVKTMKLDNSSQR
EEEEEEEECCCCCHH		58.90-
645PhosphorylationAACMKDFSHPNVIRL
HHHCCCCCCHHHHHH		48.44-
681PhosphorylationMKYGDLHTYLLYSRL
CEECCHHHHHHHHCC		24.1421609022
685PhosphorylationDLHTYLLYSRLETGP
CHHHHHHHHCCCCCC		6.8021609022
686PhosphorylationLHTYLLYSRLETGPK
HHHHHHHHCCCCCCC		30.2924719451
698UbiquitinationGPKHIPLQTLLKFMV
CCCCCCHHHHHHHHH		25.4222817900
699PhosphorylationPKHIPLQTLLKFMVD
CCCCCHHHHHHHHHH		41.56-
702UbiquitinationIPLQTLLKFMVDIAL
CCHHHHHHHHHHHHH		34.2322817900
745PhosphorylationCVADFGLSKKIYSGD
EEEEECCCCCCCCCC		32.0830108239
749PhosphorylationFGLSKKIYSGDYYRQ
ECCCCCCCCCCCCCC		18.5821945579
750PhosphorylationGLSKKIYSGDYYRQG
CCCCCCCCCCCCCCC		28.7621945579
753PhosphorylationKKIYSGDYYRQGRIA
CCCCCCCCCCCCCCC		12.2221945579
754PhosphorylationKIYSGDYYRQGRIAK
CCCCCCCCCCCCCCC		10.9521945579
761UbiquitinationYRQGRIAKMPVKWIA
CCCCCCCCCCCEEEE		41.1722817900
765UbiquitinationRIAKMPVKWIAIESL
CCCCCCCEEEEHHHH		27.3221906983
775MethylationAIESLADRVYTSKSD
EHHHHHHHCCCCHHH		20.1018938715
775DimethylationAIESLADRVYTSKSD
EHHHHHHHCCCCHHH		20.10-
777PhosphorylationESLADRVYTSKSDVW
HHHHHHCCCCHHHHH		13.24-
793UbiquitinationFGVTMWEIATRGMTP
HCEEHHHHHHCCCCC		2.5421890473
856UbiquitinationVLRLQLEKLLESLPD
HHHHHHHHHHHCCCC		67.9523000965
872PhosphorylationRNQADVIYVNTQLLE
HCCCCEEEEEHHHHH		6.36-
923UbiquitinationTAEVHDSKPHEGRYI
EEEEECCCCCCCCEE		57.35-
929PhosphorylationSKPHEGRYILNGGSE
CCCCCCCEEECCCCC		22.1822817900
935PhosphorylationRYILNGGSEEWEDLT
CEEECCCCCCHHCCC		33.4721602930
968PhosphorylationRLVRNGVSWSHSSML
HHHHCCCCCCCCCCC		25.0219369195
970PhosphorylationVRNGVSWSHSSMLPL
HHCCCCCCCCCCCCC		13.1419369195
979PhosphorylationSSMLPLGSSLPDELL
CCCCCCCCCCCCCEE		36.0619369195
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
749YPhosphorylationKinaseMERTKQ12866
PhosphoELM
753YPhosphorylationKinaseMERTKQ12866
PhosphoELM
754YPhosphorylationKinaseMERTKQ12866
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MERTK_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 MERTK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITB5_HUMANITGB5genetic
15673687
MERTK_HUMANMERTKphysical
15673687
ACK1_HUMANTNK2physical
16288044
Drug and Disease Associations
Kegg Disease
H00527 Retinitis pigmentosa (RP)
OMIM Disease
613862Retinitis pigmentosa 38 (RP38)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MERTK_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-442, AND MASSSPECTROMETRY.
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-543; SER-613; TYR-929;SER-935; SER-968; SER-970 AND SER-979, AND MASS SPECTROMETRY.
"Identification of the major autophosphorylation sites of Nyk/Mer, anNCAM-related receptor tyrosine kinase.";
Ling L., Templeton D., Kung H.J.;
J. Biol. Chem. 271:18355-18362(1996).
Cited for: AUTOPHOSPHORYLATION AT TYR-749; TYR-753 AND TYR-754.

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