dbPTM

GRM3_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRM3_RAT
UniProt AC	P31422
Protein Name	Metabotropic glutamate receptor 3
Gene Name	Grm3
Organism	Rattus norvegicus (Rat).
Sequence Length	879
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. Signaling inhibits adenylate cyclase activity..
Protein Sequence	MKMLTRLQILMLALFSKGFLLSLGDHNFMRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDNYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAANRVNASFTWVASDGWGAQESIVKGSEHVAYGAITLELASHPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRQVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKEYLLKINFTAPFNPNKGADSIVKFDTFGDGMGRYNVFNLQQTGGKYSYLKVGHWAETLSLDVDSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPYEYLVDEFTCMDCGPGQWPTADLSGCYNLPEDYIKWEDAWAIGPVTIACLGFLCTCIVITVFIKHNNTPLVKASGRELCYILLFGVSLSYCMTFFFIAKPSPVICALRRLGLGTSFAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILETPGTRRYTLPEKRETVILKCNVKDSSMLISLTYDVVLVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIVLFQPQKNVVTHRLHLNRFSVSGTATTYSQSSASTYVPTVCNGREVLDSTTSSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
209	N-linked_Glycosylation	AEILRFFNWTYVSTV HHHHHHCCCEEEEEC	27.71	17360426
292	N-linked_Glycosylation	IAAANRVNASFTWVA HHHHHCCCEEEEEEE	26.99	-
414	N-linked_Glycosylation	MQRTLCPNTTKLCDA HHHHHCCCHHHHHHH	60.42	-
439	N-linked_Glycosylation	KEYLLKINFTAPFNP HHEEEEEEEECCCCC	26.99	24090084
845	Phosphorylation	RLHLNRFSVSGTATT EEEECEEEEECEEEE	16.49	22817900
874	Phosphorylation	NGREVLDSTTSSL-- CCCHHHHCCCCCC--	29.44	27097102
875	Phosphorylation	GREVLDSTTSSL--- CCHHHHCCCCCC---	30.29	28551015
876	Phosphorylation	REVLDSTTSSL---- CHHHHCCCCCC----	21.92	27097102
877	Phosphorylation	EVLDSTTSSL----- HHHHCCCCCC-----	29.72	27097102
878	Phosphorylation	VLDSTTSSL------ HHHCCCCCC------	35.69	27097102

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
845	S	Phosphorylation	Kinase	PRKACA	P27791	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRM3_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 GRM3_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
KCC2A_RAT	Camk2a	physical	15494036

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GRM3_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structures of the extracellular regions of the group II/IIImetabotropic glutamate receptors."; Muto T., Tsuchiya D., Morikawa K., Jingami H.; Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-575, GLYCOSYLATION ATASN-209, AND DISULFIDE BONDS.	17360426 [Abstract]