GRIA3_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRIA3_RAT
• UniProt AC: P19492
• Protein Name: Glutamate receptor 3
• Gene Name: Gria3
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 888
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane ; Multi-pass membrane protein . Interaction with CNIH2 and CNIH3 promotes cell surface expression.
• Protein Description: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity)..
• Protein Sequence: MGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLSYYKWEKFVYLYDTERGFSVLQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSSSSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI

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
57	N-linked_Glycosylation	QLYNTNQNTTEKPFH EEECCCCCCCCCCEE	51.54	-
260	N-linked_Glycosylation	RVMHGGANITGFQIV HHHCCCCCCEEEEEE	35.31	21317871
374	N-linked_Glycosylation	DTYGRRTNYTIDVYE ECCCCCCCEEEEEEE	30.09	21317871
409	N-linked_Glycosylation	FSDQQISNDSSSSEN CCCCCCCCCCCCCCC	55.61	-
416	N-linked_Glycosylation	NDSSSSENRTIVVTT CCCCCCCCCEEEEEE	48.63	-
615	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	-
657	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
722	Phosphorylation	GVARVRKSKGKFAFL HHHHHHHCCCCEEEE	35.76	22817900
841	S-palmitoylation	MVALIEFCYKSRAES HHHHHHHHHHHHHHH	2.44	-
861	Ubiquitination	TKNTQNFKPAPATNT CCCCCCCCCCCCCCC	48.06	-
866	Phosphorylation	NFKPAPATNTQNYAT CCCCCCCCCCCCCEE	37.43	-
868	Phosphorylation	KPAPATNTQNYATYR CCCCCCCCCCCEEEC	17.52	-
871	Phosphorylation	PATNTQNYATYREGY CCCCCCCCEEECCCC	7.18	-
873	Phosphorylation	TNTQNYATYREGYNV CCCCCCEEECCCCCE	16.86	-
874	Phosphorylation	NTQNYATYREGYNVY CCCCCEEECCCCCEE	9.86	-
878	Phosphorylation	YATYREGYNVYGTES CEEECCCCCEECCCC	9.19	-
881	Phosphorylation	YREGYNVYGTESVKI ECCCCCEECCCCCCC	18.07	-
885	Phosphorylation	YNVYGTESVKI---- CCEECCCCCCC----	28.66	16099093
887	Ubiquitination	VYGTESVKI------ EECCCCCCC------	52.56	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of GRIA3_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
615	C	Palmitoylation	Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression.	-
841	C	Palmitoylation	In contrast, Cys-841 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GRIA3_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of GRIA3_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Dynamics and allosteric potential of the AMPA receptor N-terminaldomain.";
Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I.,Greger I.H.;
EMBO J. 30:972-982(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-403, SUBUNIT, DISULFIDEBOND, AND GLYCOSYLATION AT ASN-260 AND ASN-374.
PubMed: 21317871