UniProt ID | GRM2_RAT | |
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UniProt AC | P31421 | |
Protein Name | Metabotropic glutamate receptor 2 | |
Gene Name | Grm2 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 872 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Cell junction, synapse. Cell projection, dendrite. |
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Protein Description | G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization.. | |
Protein Sequence | MESLLGFLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEECGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHSDAPTAVTGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAATQRLNASFTWVASDGWGALESVVAGSERAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEERFHCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTHLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTDDEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSFIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFVFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVAAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAPRASANLGQGSGSQFVPTVCNGREVVDSTTSSL | |
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 |
---|---|---|---|---|---|
203 | N-linked_Glycosylation | AEILRFFNWTYVSTV HHHHHHCCCEEEEEE | 27.71 | - | |
286 | N-linked_Glycosylation | LAATQRLNASFTWVA HHHHHHHHCEEEEEE | 35.41 | - | |
338 | N-linked_Glycosylation | FQSLDPWNNSRNPWF HHHCCCCCCCCCHHH | 41.82 | - | |
402 | N-linked_Glycosylation | MHRALCPNTTHLCDA HHHHHCCCCHHHHHC | 57.52 | - | |
547 | N-linked_Glycosylation | CGLGYWPNASLTGCF CCCCCCCCCCEECCE | 28.19 | - | |
675 | Phosphorylation | AQRPRFISPASQVAI CCCCCCCCHHHHHHH | 16.23 | 22817900 | |
843 | Phosphorylation | GSAAPRASANLGQGS CCCCCCHHCCCCCCC | 20.97 | 22817900 | |
867 | Phosphorylation | NGREVVDSTTSSL-- CCEEEECCCCCCC-- | 23.21 | 28551015 | |
868 | Phosphorylation | GREVVDSTTSSL--- CEEEECCCCCCC--- | 26.66 | 28551015 | |
869 | Phosphorylation | REVVDSTTSSL---- EEEECCCCCCC---- | 21.92 | 28551015 | |
870 | Phosphorylation | EVVDSTTSSL----- EEECCCCCCC----- | 29.72 | 28551015 | |
871 | Phosphorylation | VVDSTTSSL------ EECCCCCCC------ | 35.69 | 28551015 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of GRM2_RAT !! |
* 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 GRM2_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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