dbPTM

GRIA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA2_MOUSE
UniProt AC	P23819
Protein Name	Glutamate receptor 2
Gene Name	Gria2
Organism	Mus musculus (Mouse).
Sequence Length	883
Subcellular Localization	Cell membrane Multi-pass membrane protein. Endoplasmic reticulum membrane Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein. Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface e
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). Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity)..
Protein Sequence	MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
194	Phosphorylation	KKDETYRSLFQDLEL CCCHHHHHHHHHHHH	24.11	-
256	N-linked_Glycosylation	KIQFGGANVSGFQIV EEEECCCCCCCEEEE	31.59	-
370	N-linked_Glycosylation	DQNGKRINYTINIME CCCCCEEEEEEEEEE	31.74	-
379	Methylation	TINIMELKTNGPRKI EEEEEEECCCCCCCC	27.00	-
406	N-linked_Glycosylation	LTELPSGNDTSGLEN EEECCCCCCCCCCCC	54.44	-
413	N-linked_Glycosylation	NDTSGLENKTVVVTT CCCCCCCCCEEEEEE	50.79	-
610	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	16129400
683	Phosphorylation	TKEFFRRSKIAVFDK CHHHHHHHCCCHHHH	24.94	-
717	Phosphorylation	GVARVRKSKGKYAYL HHHHHHHCCCCEEEE	35.76	-
721	Phosphorylation	VRKSKGKYAYLLEST HHHCCCCEEEEEHHH	14.78	25293948
723	Phosphorylation	KSKGKYAYLLESTMN HCCCCEEEEEHHHHH	14.55	25293948
727	Phosphorylation	KYAYLLESTMNEYIE CEEEEEHHHHHHHHH	32.69	25293948
728	Phosphorylation	YAYLLESTMNEYIEQ EEEEEHHHHHHHHHH	18.03	25293948
732	Phosphorylation	LESTMNEYIEQRKPC EHHHHHHHHHHCCCC	12.54	25293948
836	S-palmitoylation	LVALIEFCYKSRAEA HHHHHHHHHHHHHHH	2.44	16129400
850	Ubiquitination	AKRMKVAKNAQNINP HHHHHHHHHHCCCCC	56.66	22790023
850 (in isoform 4)	Ubiquitination	-	56.66	22790023
858	Phosphorylation	NAQNINPSSSQNSQN HHCCCCCCCCCCCCC	37.83	25521595
859	Phosphorylation	AQNINPSSSQNSQNF HCCCCCCCCCCCCCC	36.88	29899451
860	Phosphorylation	QNINPSSSQNSQNFA CCCCCCCCCCCCCCC	37.41	25521595
863	Phosphorylation	NPSSSQNSQNFATYK CCCCCCCCCCCCEEC	20.90	25521595
868	Phosphorylation	QNSQNFATYKEGYNV CCCCCCCEECCCCEE	30.87	20415495
869	Phosphorylation	NSQNFATYKEGYNVY CCCCCCEECCCCEEE	12.01	20415495
870 (in isoform 4)	Ubiquitination	-	40.07	22790023
870	Ubiquitination	SQNFATYKEGYNVYG CCCCCEECCCCEEEC	40.07	22790023
873	Phosphorylation	FATYKEGYNVYGIES CCEECCCCEEECEEE	11.53	29899451
876	Phosphorylation	YKEGYNVYGIESVKI ECCCCEEECEEEEEC	14.56	20547133
880	Phosphorylation	YNVYGIESVKI---- CEEECEEEEEC----	27.13	10501226
887 (in isoform 3)	Phosphorylation	-		24759943
888 (in isoform 4)	Ubiquitination	-		-
899 (in isoform 3)	Phosphorylation	-		22807455
901 (in isoform 3)	Phosphorylation	-		29899451
903 (in isoform 3)	Phosphorylation	-		22807455
904 (in isoform 3)	Phosphorylation	-		29899451
908 (in isoform 4)	Ubiquitination	-		-
912 (in isoform 3)	Phosphorylation	-		22807455

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
683	S	Phosphorylation	Kinase	PKC	-	Uniprot
717	S	Phosphorylation	Kinase	PKG	-	Uniprot
876	Y	Phosphorylation	Kinase	LYN	P07948	PSP
880	S	Phosphorylation	Kinase	PRKCA	P20444	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
610	C	Palmitoylation	16129400
ZDHHC3/GODZ specifically palmitoylates Cys-610, which leads to Golgi retention and decreased cell surface expression.
836	C	Palmitoylation	16129400
In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis.

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 GRIA2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_MOUSE	Sqstm1	physical	19004011
GRIA1_MOUSE	Gria1	physical	14687553
GRIA3_MOUSE	Gria3	physical	14687553
GRIA1_MOUSE	Gria1	physical	15883194
CCG2_MOUSE	Cacng2	physical	15883194
DLG4_MOUSE	Dlg4	physical	15883194
GRP78_MOUSE	Hspa5	physical	15883194
AGAP2_MOUSE	Agap2	physical	21847098

Drug and Disease Associations

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

Regulatory Network of GRIA2_MOUSE

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"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-610 AND CYS-836.	16129400 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of serine-880 in GluR2 by protein kinase C preventsits C terminus from binding with glutamate receptor-interactingprotein."; Matsuda S., Mikawa S., Hirai H.; J. Neurochem. 73:1765-1768(1999). Cited for: PHOSPHORYLATION AT SER-880.	10501226 [Abstract]
"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-869 AND TYR-876, ANDMASS SPECTROMETRY.	18034455 [Abstract]
"Tyrosine phosphorylation and regulation of the AMPA receptor by SRCfamily tyrosine kinases."; Hayashi T., Huganir R.L.; J. Neurosci. 24:6152-6160(2004). Cited for: PHOSPHORYLATION AT TYR-876, MUTAGENESIS OF TYR-869; TYR-873 ANDTYR-876, SUBCELLULAR LOCATION, INTERACTION WITH GRIP1; GRIP2 ANDPICK1, AND TISSUE SPECIFICITY.	15240807 [Abstract]

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