dbPTM

GRIA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA1_HUMAN
UniProt AC	P42261
Protein Name	Glutamate receptor 1
Gene Name	GRIA1
Organism	Homo sapiens (Human).
Sequence Length	906
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	MQHIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASSGGSGENGRVVSHDFPKSMQSIPCMSHSSGMPLGATGL

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	UniProtKB CARBOHYD
63	N-linked_Glycosylation	LPQIDIVNISDSFEM CCCCCEEECCCCCHH	28.51	12603841
72	Phosphorylation	SDSFEMTYRFCSQFS CCCCHHHHHHHHHHH	10.61	29759185
79	Phosphorylation	YRFCSQFSKGVYAIF HHHHHHHHCCCEEEE	22.36	29759185
164	Phosphorylation	VLQKVLDTAAEKNWQ HHHHHHHHHHHHCCE	24.49	20860994
181	Phosphorylation	AVNILTTTEEGYRML EEEEEEECHHHHHHH	27.14	20860994
226	Phosphorylation	LEKNGIGYHYILANL HHHCCCCHHHHHHCC	6.91	-
228	Phosphorylation	KNGIGYHYILANLGF HCCCCHHHHHHCCCC	6.80	-
249	N-linked_Glycosylation	KFKESGANVTGFQLV HHHHCCCCCCCEEEE	35.09	UniProtKB CARBOHYD
249	N-linked_Glycosylation	KFKESGANVTGFQLV HHHHCCCCCCCEEEE	35.09	12603841
257	N-linked_Glycosylation	VTGFQLVNYTDTIPA CCCEEEEEECCCCCH	42.45	12603841
257	N-linked_Glycosylation	VTGFQLVNYTDTIPA CCCEEEEEECCCCCH	42.45	12603841
265	Acetylation	YTDTIPAKIMQQWKN ECCCCCHHHHHHHHC	33.10	19825611
294	Phosphorylation	KYTSALTYDGVKVMA CCCCCEECCHHHHHH	16.14	-
306	Phosphorylation	VMAEAFQSLRRQRID HHHHHHHHHHHCCCC	19.86	24719451
350	Phosphorylation	QVRFEGLTGNVQFNE HHCCCCCCCCEEECC	37.25	-
362	O-linked_Glycosylation	FNEKGRRTNYTLHVI ECCCCCCCEEEEEEE	31.08	OGP
363	N-linked_Glycosylation	NEKGRRTNYTLHVIE CCCCCCCEEEEEEEE	26.44	12603841
363	N-linked_Glycosylation	NEKGRRTNYTLHVIE CCCCCCCEEEEEEEE	26.44	12603841
393	Phosphorylation	DKFVPAATDAQAGGD CCCCCHHHCCCCCCC	33.69	18452278
401	N-linked_Glycosylation	DAQAGGDNSSVQNRT CCCCCCCCCCCCCCE	39.19	12603841
401	N-linked_Glycosylation	DAQAGGDNSSVQNRT CCCCCCCCCCCCCCE	39.19	UniProtKB CARBOHYD
406	N-linked_Glycosylation	GDNSSVQNRTYIVTT CCCCCCCCCEEEEEE	35.79	12603841
406	N-linked_Glycosylation	GDNSSVQNRTYIVTT CCCCCCCCCEEEEEE	35.79	UniProtKB CARBOHYD
453	Phosphorylation	IAKHVGYSYRLEIVS HHHHHCCEEEEEEEE	9.61	24719451
460	Phosphorylation	SYRLEIVSDGKYGAR EEEEEEEECCCCCCC	46.43	28152594
464	Phosphorylation	EIVSDGKYGARDPDT EEEECCCCCCCCCCC	22.88	28152594
506	Phosphorylation	REEVIDFSKPFMSLG EHHHHCCCCCCHHCC	35.35	-
511	Phosphorylation	DFSKPFMSLGISIMI CCCCCCHHCCEEEEE	24.67	24719451
515	Phosphorylation	PFMSLGISIMIKKPQ CCHHCCEEEEEECCC	12.33	20860994
551	Phosphorylation	VFAYIGVSVVLFLVS HHHHHHHHHHHHHHH	10.99	22210691
567	Phosphorylation	FSPYEWHSEEFEEGR CCCCCCCCHHHHCCC	39.64	21135237
603	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	-
645	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
710	Phosphorylation	GMIRVRKSKGKYAYL CEEEEEECCCCEEEE	35.76	-
754	Phosphorylation	GIATPKGSALRNPVN CCCCCCCCCCCCCCE	30.20	-
768 (in isoform 2)	Phosphorylation	-	37.65	-
778 (in isoform 6)	Phosphorylation	-	56.47	-
789 (in isoform 2)	Phosphorylation	-	46.02	22468782
798 (in isoform 2)	Phosphorylation	-	29.39	22210691
799 (in isoform 6)	Phosphorylation	-	32.71	22468782
808 (in isoform 6)	Phosphorylation	-	13.04	22210691
829	S-palmitoylation	LVALIEFCYKSRSES HHHHHHHHHHCCCCH	2.44	-
830 (in isoform 2)	Phosphorylation	-	19.81	22210691
832	Phosphorylation	LIEFCYKSRSESKRM HHHHHHHCCCCHHCC	17.98	-
832 (in isoform 2)	Phosphorylation	-	17.98	22210691
834	Phosphorylation	EFCYKSRSESKRMKG HHHHHCCCCHHCCCC	54.00	19503082
836	Phosphorylation	CYKSRSESKRMKGFC HHHCCCCHHCCCCEE	27.15	19503082
840 (in isoform 6)	Phosphorylation	-	53.52	22210691
842 (in isoform 6)	Phosphorylation	-	2.27	22210691
849	O-linked_Glycosylation	FCLIPQQSINEAIRT EEEECHHHHHHHHHH	23.33	28657654
849	Phosphorylation	FCLIPQQSINEAIRT EEEECHHHHHHHHHH	23.33	18305116
858	Phosphorylation	NEAIRTSTLPRNSGA HHHHHHCCCCCCCCC	39.92	25954137
863	Phosphorylation	TSTLPRNSGAGASSG HCCCCCCCCCCCCCC	31.16	18305116
868	Phosphorylation	RNSGAGASSGGSGEN CCCCCCCCCCCCCCC	28.70	20860994
885	Ubiquitination	VVSHDFPKSMQSIPC EEECCCCHHHCCCCC	59.56	-

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
567	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
567	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
834	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
836	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
849	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
849	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
849	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
849	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
863	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
863	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:21148011

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
603	C	Palmitoylation	-
Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression.
645	S	Phosphorylation	-
Phosphorylated at Ser-645.
710	S	Phosphorylation	-
Phosphorylated at Ser-710 by PKC.
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.
863	S	Phosphorylation	-
Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (By similarity).
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).

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 GRIA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E41L2_HUMAN	EPB41L2	physical	11050113
GRID2_HUMAN	GRID2	physical	12573530
GRIA2_HUMAN	GRIA2	physical	10358037
PICK1_HUMAN	PICK1	physical	11891216
GRIP1_HUMAN	GRIP1	physical	11891216
SDCB1_HUMAN	SDCBP	physical	11891216
E41L1_HUMAN	EPB41L1	physical	11050113
DLG1_HUMAN	DLG1	physical	9677374
DLG1_HUMAN	DLG1	physical	11567040
MYO5A_HUMAN	MYO5A	physical	18311135
RB11A_HUMAN	RAB11A	physical	18311135

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 GRIA1_HUMAN

Related Literatures of Post-Translational Modification

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