dbPTM

GRIA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA2_HUMAN
UniProt AC	P42262
Protein Name	Glutamate receptor 2
Gene Name	GRIA2
Organism	Homo sapiens (Human).
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 (By similarity)..
Protein Sequence	MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
101	Phosphorylation	KKSVNTITSFCGTLH CCCCHHHHHHCCEEE	17.45	22210691
118	Phosphorylation	FITPSFPTDGTHPFV EECCCCCCCCCCCEE	45.08	22210691
256	N-linked_Glycosylation	KIQFGGANVSGFQIV EEEECCCCCCCEEEE	31.59	UniProtKB CARBOHYD
279	Phosphorylation	KFIERWSTLEEKEYP HHHHHHHCCCCCCCC	31.09	-
285	Phosphorylation	STLEEKEYPGAHTTT HCCCCCCCCCCCCCC	20.31	-
291	Phosphorylation	EYPGAHTTTIKYTSA CCCCCCCCCEEEEEC	19.36	-
292	Phosphorylation	YPGAHTTTIKYTSAL CCCCCCCCEEEEECC	19.34	-
370	N-linked_Glycosylation	DQNGKRINYTINIME CCCCCEEEEEEEEEE	31.74	19651138
406	N-linked_Glycosylation	LTELPSGNDTSGLEN EEECCCCCCCCCCCC	54.44	UniProtKB CARBOHYD
413	N-linked_Glycosylation	NDTSGLENKTVVVTT CCCCCCCCCEEEEEE	50.79	UniProtKB CARBOHYD
442	Phosphorylation	MLEGNERYEGYCVDL HCCCCCCCCCHHHHH	13.92	22817900
513	Phosphorylation	REEVIDFSKPFMSLG EHHHHCCCCCCCCCC	35.35	-
518	Phosphorylation	DFSKPFMSLGISIMI CCCCCCCCCCEEEEE	24.67	24719451
522	Phosphorylation	PFMSLGISIMIKKPQ CCCCCCEEEEEECCC	12.33	20860994
558	Phosphorylation	VFAYIGVSVVLFLVS HHHHHHHHHHHHHHH	10.99	22210691
610	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	-
652	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
683	Phosphorylation	TKEFFRRSKIAVFDK CHHHHHHHCCCHHHH	24.94	8848293
717	Phosphorylation	GVARVRKSKGKYAYL HHHHHHHCCCCEEEE	35.76	8848293
728 (in isoform 4)	Phosphorylation	-	18.03	-
775 (in isoform 2)	Phosphorylation	-	37.65	-
803	Ubiquitination	SGGGDSKEKTSALSL CCCCCCHHHHCHHHH	66.57	30230243
836	S-palmitoylation	LVALIEFCYKSRAEA HHHHHHHHHHHHHHH	2.44	-
837	Phosphorylation	VALIEFCYKSRAEAK HHHHHHHHHHHHHHH	19.81	-
850	Ubiquitination	AKRMKVAKNAQNINP HHHHHHHHHHCCCCC	56.66	30230243
860	Phosphorylation	QNINPSSSQNSQNFA CCCCCCCCCCCCCCC	37.41	-
863	Phosphorylation	NPSSSQNSQNFATYK CCCCCCCCCCCCEEC	20.90	-
876	Phosphorylation	YKEGYNVYGIESVKI ECCCCEEECEEEEEC	14.56	24927040
880	Phosphorylation	YNVYGIESVKI---- CEEECEEEEEC----	27.13	12058067

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
863	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
880	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRID2_HUMAN	GRID2	physical	12573530
PICK1_HUMAN	PICK1	physical	11891216
GRIP1_HUMAN	GRIP1	physical	11891216
SDCB1_HUMAN	SDCBP	physical	11891216
SPTN1_HUMAN	SPTAN1	physical	10576550
MYO5A_HUMAN	MYO5A	physical	18311135
RB11A_HUMAN	RAB11A	physical	18311135
GRIP1_HUMAN	GRIP1	physical	18311135
GRIA1_HUMAN	GRIA1	physical	18311135
GRIP1_RAT	Grip1	physical	14730302
TF3C2_HUMAN	GTF3C2	physical	21988832
PICK1_HUMAN	PICK1	physical	24749734
PICK1_RAT	Pick1	physical	24749734
AT5F1_HUMAN	ATP5F1	physical	26496610
NDUV3_HUMAN	NDUFV3	physical	26496610
NCOA4_HUMAN	NCOA4	physical	26496610
KCAB2_HUMAN	KCNAB2	physical	26496610
P121A_HUMAN	POM121	physical	26496610
TXN4A_HUMAN	TXNL4A	physical	26496610
ECD_HUMAN	ECD	physical	26496610
TRM6_HUMAN	TRMT6	physical	26496610
TSYL2_HUMAN	TSPYL2	physical	26496610
DPP9_HUMAN	DPP9	physical	26496610
GRIP1_HUMAN	GRIP1	physical	21847098
AGAP2_HUMAN	AGAP2	physical	21847098
G3P_HUMAN	GAPDH	physical	22537872

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00537	Topiramate (JAN/USAN/INN); Topamax (TN); Trokendi xr (TN)
D02696	Talampanel (INN)
D04131	Farampator (USAN/INN); Org 24448
D06656	Tezampanel (USAN); Tezampanel hydrate
D08964	Perampanel (USAN); Fycompa (TN)
D09035	Zonampanel (INN/USAN)
D09931	Mibampator (USAN/INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GRIA2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of the GluR2 amino-terminal domain providesinsights into the architecture and assembly of ionotropic glutamatereceptors."; Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K.,McIlhinney R.A., Jones E.Y., Aricescu A.R.; J. Mol. Biol. 392:1125-1132(2009). Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDEBOND, AND GLYCOSYLATION AT ASN-370.	19651138 [Abstract]

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