GRM2_RAT - dbPTM
GRM2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRM2_RAT
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.
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
203N-linked_GlycosylationAEILRFFNWTYVSTV
HHHHHHCCCEEEEEE
27.71-
286N-linked_GlycosylationLAATQRLNASFTWVA
HHHHHHHHCEEEEEE
35.41-
338N-linked_GlycosylationFQSLDPWNNSRNPWF
HHHCCCCCCCCCHHH
41.82-
402N-linked_GlycosylationMHRALCPNTTHLCDA
HHHHHCCCCHHHHHC
57.52-
547N-linked_GlycosylationCGLGYWPNASLTGCF
CCCCCCCCCCEECCE
28.19-
675PhosphorylationAQRPRFISPASQVAI
CCCCCCCCHHHHHHH
16.2322817900
843PhosphorylationGSAAPRASANLGQGS
CCCCCCHHCCCCCCC
20.9722817900
867PhosphorylationNGREVVDSTTSSL--
CCEEEECCCCCCC--
23.2128551015
868PhosphorylationGREVVDSTTSSL---
CEEEECCCCCCC---
26.6628551015
869PhosphorylationREVVDSTTSSL----
EEEECCCCCCC----
21.9228551015
870PhosphorylationEVVDSTTSSL-----
EEECCCCCCC-----
29.7228551015
871PhosphorylationVVDSTTSSL------
EECCCCCCC------
35.6928551015

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
675SPhosphorylationKinasePRKACAP27791
GPS
843SPhosphorylationKinasePRKACAP27791
GPS
843SPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRM2_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 GRM2_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RANB9_HUMANRANBP9physical
18555800
KCC2A_RATCamk2aphysical
15494036
GRASP_RATGraspphysical
11850456

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRM2_RAT

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Related Literatures of Post-Translational Modification

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