dbPTM

GRIA2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA2_RAT
UniProt AC	P19491
Protein Name	Glutamate receptor 2 {ECO:0000305}
Gene Name	Gria2 {ECO:0000312\|RGD:61862}
Organism	Rattus norvegicus (Rat).
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 surfa
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. 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. [PubMed: 16037816]
Protein Sequence	MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
256	N-linked_Glycosylation	KIQFGGANVSGFQIV EEEECCCCCCCEEEE	31.59	21317873
370	N-linked_Glycosylation	DQNGKRINYTINIME CCCCCEEEEEEEEEE	31.74	25103405
406	N-linked_Glycosylation	LTELPSGNDTSGLEN EEECCCCCCCCCCCC	54.44	-
413	N-linked_Glycosylation	NDTSGLENKTVVVTT CCCCCCCCCEEEEEE	50.79	-
610	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	19508696
652	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
661	Phosphorylation	IESAEDLSKQTEIAY CCCHHHHHHCCEEEE	34.73	8848293
683	Phosphorylation	TKEFFRRSKIAVFDK CHHHHHHHCCCHHHH	24.94	8848293
697	Phosphorylation	KMWTYMRSAEPSVFV HHHHHHHCCCCCEEE	22.06	8848293
717	Phosphorylation	GVARVRKSKGKYAYL HHHHHHHCCCCEEEE	35.76	8848293
836	S-palmitoylation	LVALIEFCYKSRAEA HHHHHHHHHHHHHHH	2.44	-
850	Ubiquitination	AKRMKVAKNPQNINP HHHHHHCCCCCCCCC	72.63	-
858	Phosphorylation	NPQNINPSSSQNSQN CCCCCCCCCCCCCCC	37.83	27097102
859	Phosphorylation	PQNINPSSSQNSQNF CCCCCCCCCCCCCCC	36.88	27097102
860	Phosphorylation	QNINPSSSQNSQNFA CCCCCCCCCCCCCCE	37.41	27097102
863	Phosphorylation	NPSSSQNSQNFATYK CCCCCCCCCCCEEEC	20.90	27097102
868	Phosphorylation	QNSQNFATYKEGYNV CCCCCCEEECCCCEE	30.87	27097102
869	Phosphorylation	NSQNFATYKEGYNVY CCCCCEEECCCCEEE	12.01	27097102
870	Ubiquitination	SQNFATYKEGYNVYG CCCCEEECCCCEEEC	40.07	-
873	Phosphorylation	FATYKEGYNVYGIES CEEECCCCEEECEEE	11.53	25403869
876	Phosphorylation	YKEGYNVYGIESVKI ECCCCEEECEEEEEC	14.56	20547133
880	Phosphorylation	YNVYGIESVKI---- CEEECEEEEEC----	27.13	17337442
882	Ubiquitination	VYGIESVKI------ EECEEEEEC------	52.56	-

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
661	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
683	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
683	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
683	S	Phosphorylation	Kinase	PKC	-	Uniprot
697	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
697	S	Phosphorylation	Kinase	PRKG1	P00516	GPS
717	S	Phosphorylation	Kinase	PKG/CGK_GROUP	-	PhosphoELM
717	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
717	S	Phosphorylation	Kinase	PKG	-	Uniprot
717	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
717	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
869	Y	Phosphorylation	Kinase	SRC	P12931	PSP
873	Y	Phosphorylation	Kinase	SRC	P12931	PSP
876	Y	Phosphorylation	Kinase	SRC	P12931	PSP
876	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
880	S	Phosphorylation	Kinase	PKCA	P05696	PSP
880	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
880	S	Phosphorylation	Kinase	PKCA	P17252	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
610	C	Palmitoylation	-
Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression.
836	C	Palmitoylation	-
In contrast, Cys-836 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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of GRIA2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GIPC1_RAT	Gipc1	physical	15458844
GRIP1_RAT	Grip1	physical	15458844
RGS3_RAT	Rgs3	physical	15458844
SDCB1_RAT	Sdcbp	physical	15458844
PICK1_RAT	Pick1	physical	15458844
NSF_RAT	Nsf	physical	15858065
P85A_RAT	Pik3r1	physical	15858065
GRIP1_RAT	Grip1	physical	21847098

Drug and Disease Associations

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

Regulatory Network of GRIA2_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Subunit-selective N-terminal domain associations organize theformation of AMPA receptor heteromers."; Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M.,Greger I.H.; EMBO J. 30:959-971(2011). Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT,DISULFIDE BOND, AND GLYCOSYLATION AT ASN-256 AND ASN-370.	21317873 [Abstract]
"X-ray structure, symmetry and mechanism of an AMPA-subtype glutamatereceptor."; Sobolevsky A.I., Rosconi M.P., Gouaux E.; Nature 462:745-756(2009). Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITHGLUTAMATE ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796,FUNCTION, SUBUNIT, MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-370.	19946266 [Abstract]
Phosphorylation
Reference	PubMed
"Antibody specific for phosphorylated AMPA-type glutamate receptors atGluR2 Ser-696."; Nakazawa K., Tadakuma T., Nokihara K., Ito M.; Neurosci. Res. 24:75-86(1995). Cited for: PHOSPHORYLATION AT SER-683 AND SER-717.	8848293 [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, AND TISSUE SPECIFICITY.	15240807 [Abstract]

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