MERTK_RAT - dbPTM
MERTK_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MERTK_RAT
UniProt AC P57097
Protein Name Tyrosine-protein kinase Mer
Gene Name Mertk
Organism Rattus norvegicus (Rat).
Sequence Length 994
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 (By similarity)..
Protein Sequence MVLAPLLLGLLLLSALWNGGTAEKEEEIKPDQPFSGPLPGSLPADHRPFFAPHSSGDQLSPSQTGRSHPAHTATPQMTSAASNLLPPVAFKNTIGRIVLSEHKSVKFNCSINIPNVYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSITSVQRSDNGSYICKMKVNDREVVSDPIYVEVQGLPYFTKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNENPERSPSVLTVAGLTETAVFSCEAHNDKGLTVSKGVQINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEADQLSNGSVMVFNTSASPHLYEVQQLQALANYSVTVSCRNEIGWSAVSPWILASTTEGAPAVAPLNITVFLNESSNNLEIRWTKPPIKRQDGELVGYRISHVWESAGTSKELSEEVSQNGSWAQVPVQMHNATCTVRIAVITKGGIGPFSEPVDVAIPEHSRVDYAPSSTPAPGNTESMLIILGCFCGFVLMGLILYLSLAIKRRVQETKFGGAFSEEDSQLVVNYRAKKSFCRRAIELTLQSLGVSEELQNKLEDVVVDRNLLILGKVLGEGEFGSVMEGNLKQEDGTSQKVAVKTMKLDNFSLREIEEFLSEAACMKDFNHPNVIRLLGVCIELSSQGIPKPMVILPFMKYGDLHTFLLYSRIESVPKSIPLQTLLKFMVDIAQGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDDLYEIMYSCWSADPLDRPTFSVLRLQLEKLSESLPDAQDKESIIYINTQLLESCEGLANRSSLAGLDMNIDPDSIIASCTAGAAVSVVMAEVHENNLHEERYILNGGNEEWEDVASTPFATVTAGKDGVLPEDRLTKNGISWSHHSTLPLGSPSPDELLFADDSSGDSEVLM
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
108N-linked_GlycosylationEHKSVKFNCSINIPN
CCCCEEEEEEEECCC
16.95-
165N-linked_GlycosylationTSVQRSDNGSYICKM
EEEEECCCCCEEEEE
42.42-
202N-linked_GlycosylationTKQPESVNVTRNTAF
CCCCCCEECCCCCEE
38.43-
210N-linked_GlycosylationVTRNTAFNLTCQAVG
CCCCCEEEEEEEECC
31.79-
229N-linked_GlycosylationVNIFWVQNSSRVNEN
EEEEEEECCCCCCCC
32.12-
289N-linked_GlycosylationPTEVHILNSTAHSIL
CCEEEEEECCCCHHH
36.39-
311N-linked_GlycosylationDGYSPLQNCSIQVKE
CCCCCCCCCEEEEEE
29.23-
324N-linked_GlycosylationKEADQLSNGSVMVFN
EEHHHCCCCCEEEEE
56.18-
331N-linked_GlycosylationNGSVMVFNTSASPHL
CCCEEEEECCCCCCE
23.01-
349N-linked_GlycosylationQQLQALANYSVTVSC
HHHHHHHCCEEEEEE
30.38-
384N-linked_GlycosylationAPAVAPLNITVFLNE
CCCCCCEEEEEEEEC
27.16-
390N-linked_GlycosylationLNITVFLNESSNNLE
EEEEEEEECCCCCEE
35.32-
437N-linked_GlycosylationLSEEVSQNGSWAQVP
HCHHHHHCCCEECCC
38.67-
449N-linked_GlycosylationQVPVQMHNATCTVRI
CCCEEECCCEEEEEE
31.44-
534PhosphorylationTKFGGAFSEEDSQLV
CCCCCCCCHHHHEEE
39.2723984901
538PhosphorylationGAFSEEDSQLVVNYR
CCCCHHHHEEEEEHH
28.7923984901
740PhosphorylationCVADFGLSKKIYSGD
EEEEECCCCCCCCCC
32.0823984901
744PhosphorylationFGLSKKIYSGDYYRQ
ECCCCCCCCCCCCCC
18.58-
748PhosphorylationKKIYSGDYYRQGRIA
CCCCCCCCCCCCCCC
12.22-
749PhosphorylationKIYSGDYYRQGRIAK
CCCCCCCCCCCCCCC
10.95-
851UbiquitinationVLRLQLEKLSESLPD
HHHHHHHHHHHCCCC
66.94-
867PhosphorylationQDKESIIYINTQLLE
CCCCEEEEEEHHHHH
6.1022276854

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

Oops, there are no upstream regulatory protein records of MERTK_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MERTK_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MERTK_RAT

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Related Literatures of Post-Translational Modification

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