GRIA1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRIA1_RAT
• UniProt AC: P19490
• Protein Name: Glutamate receptor 1
• Gene Name: Gria1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 907
• 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 . Cell junction, synapse, postsynaptic cell membrane, postsynapti
• Protein Description: Ionotropic glutamate receptor. 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..
• Protein Sequence: MPYIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQEALISIIDHYKWQTFVYIYDADRGLSVLQRVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPARIMQQWRTSDSRDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASGGGGSGENGRVVSQDFPKSMQSIPCMSHSSGMPLGATGL

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
63	N-linked_Glycosylation	LPQIDIVNISDSFEM CCCCCEEECCCCCHH	28.51	-
249	N-linked_Glycosylation	KFKESGANVTGFQLV HHHHCCCCCCCEEEE	35.09	21639859
257	N-linked_Glycosylation	VTGFQLVNYTDTIPA CCCEEEEECCCCCCH	42.45	21639859
363	N-linked_Glycosylation	NEKGRRTNYTLHVIE CCCCCCCEEEEEEEE	26.44	21639859
401	N-linked_Glycosylation	DAQAGGDNSSVQNRT CCCCCCCCCCCCCCE	39.19	-
406	N-linked_Glycosylation	GDNSSVQNRTYIVTT CCCCCCCCCEEEEEE	35.79	-
567	Phosphorylation	FSPYEWHSEEFEEGR CCCCCCCCHHHHCCC	39.64	21135237
603	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	25698923
645	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
710	Phosphorylation	GMIRVRKSKGKYAYL CEEEEEECCCCEEEE	35.76	8848293
829	S-palmitoylation	LVALIEFCYKSRSES HHHHHHHHHHCCCCH	2.44	-
831	Acetylation	ALIEFCYKSRSESKR HHHHHHHHCCCCHHC	40.34	412439297
836	Phosphorylation	CYKSRSESKRMKGFC HHHCCCCHHCCCCEE	27.15	16846856
837	Acetylation	YKSRSESKRMKGFCL HHCCCCHHCCCCEEE	53.08	412439295
840	Acetylation	RSESKRMKGFCLIPQ CCCHHCCCCEEEECH	53.52	412439291
849	Phosphorylation	FCLIPQQSINEAIRT EEEECHHHHHHHHHH	23.33	16029214
855	Methylation	QSINEAIRTSTLPRN HHHHHHHHHCCCCCC	29.67	-
863	Phosphorylation	TSTLPRNSGAGASGG HCCCCCCCCCCCCCC	31.16	11943807
886	Ubiquitination	VVSQDFPKSMQSIPC EECCCCCHHHCCCCC	59.56	-
886	Acetylation	VVSQDFPKSMQSIPC EECCCCCHHHCCCCC	59.56	412439293

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
645	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
645	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
645	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
710	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
710	S	Phosphorylation	Kinase	PKC	-	Uniprot
710	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
832	S	Phosphorylation	Kinase	CAMK2A	P11275	GPS
836	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
836	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
836	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
849	S	Phosphorylation	Kinase	PKA	-	Uniprot
849	S	Phosphorylation	Kinase	PKC	-	Uniprot
849	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
849	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
849	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
863	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PKACA	P17612	PSP
863	S	Phosphorylation	Kinase	PAK3	Q62829	PSP
863	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PAK3	O75914	PSP
863	S	Phosphorylation	Kinase	PRKG2	Q64595	Uniprot
863	S	Phosphorylation	Kinase	PKC	-	Uniprot
863	S	Phosphorylation	Kinase	PKA	-	Uniprot
863	S	Phosphorylation	Kinase	PRKACA	P27791	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
603	C	Palmitoylation	Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression.	-
645	S	Phosphorylation	Phosphorylated at Ser-645.	7877986
710	S	Phosphorylation	Phosphorylated at Ser-710 by PKC.	8848293
829	C	Palmitoylation	In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).	-
849	S	Phosphorylation	Phosphorylated at Ser-849 by PKC, PKA and CAMK2.	9405465
863	S	Phosphorylation	Phosphorylated at Ser-863 by PKC, PKA and PRKG2.	9405465
863	S	Phosphorylation	Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation (By similarity).	9405465

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GRIA1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	22405206
DLG1_RAT	Dlg1	physical	12050163

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Crystal structure of the glutamate receptor GluA1 N-terminaldomain.";
Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.;
Biochem. J. 438:255-263(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT,GLYCOSYLATION AT ASN-249; ASN-257 AND ASN-363, AND DISULFIDE BOND.
PubMed: 21639859

Phosphorylation

"Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependentkinase II.";
Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.;
J. Biol. Chem. 272:32528-32533(1997).
Cited for: PHOSPHORYLATION AT SER-849 AND SER-863, AND MUTAGENESIS OF SER-645 ANDSER-849.
PubMed: 9405465

"Identification of a Ca2+/calmodulin-dependent protein kinase IIregulatory phosphorylation site in non-N-methyl-D-aspartate glutamatereceptors.";
Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A.,Soderling T.R.;
Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995).
Cited for: PHOSPHORYLATION AT SER-645.
PubMed: 7877986