GRIA3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRIA3_MOUSE
• UniProt AC: Q9Z2W9
• Protein Name: Glutamate receptor 3
• Gene Name: Gria3
• Organism: Mus musculus (Mouse).
• 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: MGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGYYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDIQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDIVLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSSSSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRTPVNLAVLKLSEQGILDKLKNKWWYDKGECGAKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI

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 HHHCCCCCEEEEEEE	35.31	-
372	Dimethylation	QFDTYGRRTNYTIDV EEECCCCCCCEEEEE	23.98	-
374	N-linked_Glycosylation	DTYGRRTNYTIDVYE ECCCCCCCEEEEEEE	30.09	-
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	-
688	Phosphorylation	TKEFFRRSKIAVYEK CHHHHHHHHHHHHHH	24.94	-
699	Phosphorylation	VYEKMWSYMKSAEPS HHHHHHHHHHHCCCC	7.95	20139300
702	Phosphorylation	KMWSYMKSAEPSVFT HHHHHHHHCCCCCCE	22.72	23984901
706	Phosphorylation	YMKSAEPSVFTKTTA HHHHCCCCCCEEECC	22.74	23984901
709	Phosphorylation	SAEPSVFTKTTADGV HCCCCCCEEECCCHH	25.89	20139300
711	Phosphorylation	EPSVFTKTTADGVAR CCCCCEEECCCHHHH	24.94	23984901
712	Phosphorylation	PSVFTKTTADGVARV CCCCEEECCCHHHHH	25.06	23984901
722	Phosphorylation	GVARVRKSKGKFAFL HHHHHHHCCCCEEEE	35.76	-
758	Phosphorylation	GNLDSKGYGVATPKG CCCCCCCCCCCCCCC	16.50	-
841	S-palmitoylation	MVALIEFCYKSRAES HHHHHHHHHHHHHHH	2.44	16129400
861	Ubiquitination	TKNTQNFKPAPATNT CCCCCCCCCCCCCCC	48.06	-
866	Phosphorylation	NFKPAPATNTQNYAT CCCCCCCCCCCCCEE	37.43	29899451
868	Phosphorylation	KPAPATNTQNYATYR CCCCCCCCCCCEEEC	17.52	29899451
871	Phosphorylation	PATNTQNYATYREGY CCCCCCCCEEECCCC	7.18	29899451
874	Phosphorylation	NTQNYATYREGYNVY CCCCCEEECCCCCEE	9.86	29899451
881	Phosphorylation	YREGYNVYGTESVKI ECCCCCEECCCCCCC	18.07	25521595
885	Phosphorylation	YNVYGTESVKI---- CCEECCCCCCC----	28.66	29899451

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

Oops, there are no upstream regulatory protein records of GRIA3_MOUSE !!

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).	16129400

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_MOUSE	Sqstm1	physical	19004011

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Palmitoylation

"Differential regulation of AMPA receptor subunit trafficking bypalmitoylation of two distinct sites.";
Hayashi T., Rumbaugh G., Huganir R.L.;
Neuron 47:709-723(2005).
Cited for: PALMITOYLATION AT CYS-841.
PubMed: 16129400

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-871 AND TYR-881, ANDMASS SPECTROMETRY.
PubMed: 18034455