UniProt ID | MERTK_RAT | |
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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. |
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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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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108 | N-linked_Glycosylation | EHKSVKFNCSINIPN CCCCEEEEEEEECCC | 16.95 | - | |
165 | N-linked_Glycosylation | TSVQRSDNGSYICKM EEEEECCCCCEEEEE | 42.42 | - | |
202 | N-linked_Glycosylation | TKQPESVNVTRNTAF CCCCCCEECCCCCEE | 38.43 | - | |
210 | N-linked_Glycosylation | VTRNTAFNLTCQAVG CCCCCEEEEEEEECC | 31.79 | - | |
229 | N-linked_Glycosylation | VNIFWVQNSSRVNEN EEEEEEECCCCCCCC | 32.12 | - | |
289 | N-linked_Glycosylation | PTEVHILNSTAHSIL CCEEEEEECCCCHHH | 36.39 | - | |
311 | N-linked_Glycosylation | DGYSPLQNCSIQVKE CCCCCCCCCEEEEEE | 29.23 | - | |
324 | N-linked_Glycosylation | KEADQLSNGSVMVFN EEHHHCCCCCEEEEE | 56.18 | - | |
331 | N-linked_Glycosylation | NGSVMVFNTSASPHL CCCEEEEECCCCCCE | 23.01 | - | |
349 | N-linked_Glycosylation | QQLQALANYSVTVSC HHHHHHHCCEEEEEE | 30.38 | - | |
384 | N-linked_Glycosylation | APAVAPLNITVFLNE CCCCCCEEEEEEEEC | 27.16 | - | |
390 | N-linked_Glycosylation | LNITVFLNESSNNLE EEEEEEEECCCCCEE | 35.32 | - | |
437 | N-linked_Glycosylation | LSEEVSQNGSWAQVP HCHHHHHCCCEECCC | 38.67 | - | |
449 | N-linked_Glycosylation | QVPVQMHNATCTVRI CCCEEECCCEEEEEE | 31.44 | - | |
534 | Phosphorylation | TKFGGAFSEEDSQLV CCCCCCCCHHHHEEE | 39.27 | 23984901 | |
538 | Phosphorylation | GAFSEEDSQLVVNYR CCCCHHHHEEEEEHH | 28.79 | 23984901 | |
740 | Phosphorylation | CVADFGLSKKIYSGD EEEEECCCCCCCCCC | 32.08 | 23984901 | |
744 | Phosphorylation | FGLSKKIYSGDYYRQ ECCCCCCCCCCCCCC | 18.58 | - | |
748 | Phosphorylation | KKIYSGDYYRQGRIA CCCCCCCCCCCCCCC | 12.22 | - | |
749 | Phosphorylation | KIYSGDYYRQGRIAK CCCCCCCCCCCCCCC | 10.95 | - | |
851 | Ubiquitination | VLRLQLEKLSESLPD HHHHHHHHHHHCCCC | 66.94 | - | |
867 | Phosphorylation | QDKESIIYINTQLLE CCCCEEEEEEHHHHH | 6.10 | 22276854 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of MERTK_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of MERTK_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of MERTK_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Oops, there are no PPI records of MERTK_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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