GRM_DROME - dbPTM
GRM_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRM_DROME
UniProt AC P91685
Protein Name Metabotropic glutamate receptor
Gene Name mGluR
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 976
Subcellular Localization Cell membrane
Multi-pass membrane protein .
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..
Protein Sequence MKQKNNNGTILVVVMVLSWSRVVDLKSPSNTHTQDSVSVSLPGDIILGGLFPVHEKGEGAPCGPKVYNRGVQRLEAMLYAIDRVNNDPNILPGITIGVHILDTCSRDTYALNQSLQFVRASLNNLDTSGYECADGSSPQLRKNASSGPVFGVIGGSYSSVSLQVANLLRLFHIPQVSPASTAKTLSDKTRFDLFARTVPPDTFQSVALVDILKNFNWSYVSTIHSEGSYGEYGIEALHKEATERNVCIAVAEKVPSAADDKVFDSIISKLQKKPNARGVVLFTRAEDARRILQAAKRANLSQPFHWIASDGWGKQQKLLEGLEDIAEGAITVELQSEIIADFDRYMMQLTPETNQRNPWFAEYWEDTFNCVLTSLSVKPDTSNSANSTDNKIGVKAKTECDDSYRLSEKVGYEQESKTQFVVDAVYAFAYALHNLHNDRCNTQSDQTTETRKHLQSESVWYRKISTDTKSQACPDMANYDGKEFYNNYLLNVSFIDLAGSEVKFDRQGDGLARYDILNYQRQENSSGYQYKVIGKWFNGLQLNSETVVWNKETEQPTSACSLPCEVGMIKKQQGDTCCWICDSCESFEYVYDEFTCKDCGPGLWPYADKLSCYALDIQYMKWNSLFALIPMAIAIFGIALTSIVIVLFAKNHDTPLVRASGRELSYTLLFGILVCYCNTFALIAKPTIGSCVLQRFGIGVGFSIIYSALLTKTNRISRIFHSASKSAQRLKYISPQSQVVITTSLIAIQVLITMIWMVVEPPGTRFYYPDRREVILKCKIQDMSFLFSQLYNMILITICTIYAIKTRKIPENFNESKFIGFTMYTTCIIWLAFVPIYFGTGNSYEVQTTTLCISISLSASVALVCLYSPKVYILVFHPDKNVRKLTMNSTVYRRSAAAVAQGAPTSSGYSRTHAPGTSALTGGAVGTNASSSTLPTQNSPHLDEASAQTNVAHKTNGEFLPEVGERVEPICHIVNK
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
112N-linked_GlycosylationSRDTYALNQSLQFVR
CCHHHHHHHHHHHHH
22.6317893096
143N-linked_GlycosylationSSPQLRKNASSGPVF
CCHHHHHHCCCCCEE
38.32-
216N-linked_GlycosylationVDILKNFNWSYVSTI
HHHHHHCCCEEEEEE
35.86-
299N-linked_GlycosylationLQAAKRANLSQPFHW
HHHHHHCCCCCCCEE
44.23-
386N-linked_GlycosylationPDTSNSANSTDNKIG
CCCCCCCCCCCCCCC
45.31-
456PhosphorylationETRKHLQSESVWYRK
HHHHHHHHHCEEEEE
37.8922817900
461PhosphorylationLQSESVWYRKISTDT
HHHHCEEEEECCCCC
10.4022817900
491N-linked_GlycosylationFYNNYLLNVSFIDLA
HHHHEEEEEEEEECC
25.45-
524N-linked_GlycosylationLNYQRQENSSGYQYK
EEEECCCCCCCCEEE
32.89-

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 GRM_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 GRM_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FMR1_DROMEFmr1genetic
19036865
FMR1_DROMEFmr1genetic
18280750
KCC2A_DROMECaMKIIgenetic
21515581

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, AND MASSSPECTROMETRY.

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