GRM2_HUMAN - dbPTM
GRM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRM2_HUMAN
UniProt AC Q14416
Protein Name Metabotropic glutamate receptor 2
Gene Name GRM2
Organism Homo sapiens (Human).
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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization..
Protein Sequence MGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTVCNGREVVDSTTSSL
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
109PhosphorylationALDFVRASLSRGADG
HHHHHHHHHHCCCCC
19.1327174698
111PhosphorylationDFVRASLSRGADGSR
HHHHHHHHCCCCCCC
26.6027174698
203N-linked_GlycosylationAEILRFFNWTYVSTV
HHHHHHCCCEEEEEE
27.71UniProtKB CARBOHYD
246PhosphorylationEKVGRAMSRAAFEGV
HHHHHHHHHHHHHHH
20.13-
286N-linked_GlycosylationLAASQRLNASFTWVA
HHHHHHHCCCEEEEE
35.41UniProtKB CARBOHYD
288PhosphorylationASQRLNASFTWVASD
HHHHHCCCEEEEECC
23.3326853621
338N-linked_GlycosylationFQSLDPWNNSRNPWF
HHHCCCCCCCCCHHH
41.82UniProtKB CARBOHYD
402N-linked_GlycosylationMHRALCPNTTRLCDA
HHHHHCCCHHHHHHH
53.75UniProtKB CARBOHYD
457PhosphorylationIGRYNIFTYLRAGSG
CCCCCCEEEEECCCC
20.18-
501PhosphorylationPLPASRCSEPCLQNE
CCCHHHCCCCHHHCC
43.39-
547N-linked_GlycosylationCGLGYWPNASLTGCF
CCCCCCCCCCEECCE
28.19UniProtKB CARBOHYD
734PhosphorylationSMLGSLAYNVLLIAL
HHHHHHHHHHHHHHH
15.88-
745PhosphorylationLIALCTLYAFKTRKC
HHHHHHHHHHHCCCC
7.58-
749PhosphorylationCTLYAFKTRKCPENF
HHHHHHHCCCCCCCC
28.98-
850PhosphorylationSSSLGQGSGSQFVPT
HHHCCCCCCCCCCCE
27.6432142685

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 GRM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRM2_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 GRM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQL1_HUMANUBQLN1physical
25416956
NADL2_HUMANNAALADL2physical
25416956
GRIP1_HUMANGRIP1physical
11891216
SDCB1_HUMANSDCBPphysical
11891216

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRM2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP