dbPTM

GRIA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA1_MOUSE
UniProt AC	P23818
Protein Name	Glutamate receptor 1
Gene Name	Gria1
Organism	Mus musculus (Mouse).
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	MPYIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQEALISIIDHYKWQTFVYIYDADRGLSVLQRVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPARIMQQWRTSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRGPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSGSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASGGSGSGENGRVVSQDFPKSMQSIPCMSHSSGMPLGATGL

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	-
226	Phosphorylation	LEKNGIGYHYILANL HHHCCCCHHHHHHCC	6.91	-
228	Phosphorylation	KNGIGYHYILANLGF HCCCCHHHHHHCCCC	6.80	-
249	N-linked_Glycosylation	KFKESGANVTGFQLV HHHHCCCCCCCEEEE	35.09	-
257	N-linked_Glycosylation	VTGFQLVNYTDTIPA CCCEEEEECCCCCCH	42.45	-
358	Ubiquitination	GNVQFNEKGRRTNYT CCEEECCCCCCCEEE	59.84	-
363	N-linked_Glycosylation	NEKGRRTNYTLHVIE CCCCCCCEEEEEEEE	26.44	-
393	Phosphorylation	DKFVPAATDAQAGGD CCCCCHHHCCCCCCC	33.69	-
401	N-linked_Glycosylation	DAQAGGDNSSVQNRT CCCCCCCCCCCCCCE	39.19	-
406	N-linked_Glycosylation	GDNSSVQNRTYIVTT CCCCCCCCCEEEEEE	35.79	-
438	Phosphorylation	GNDRYEGYCVELAAE CCCCCCCHHHHHHHH	4.95	-
577	Phosphorylation	FEEGRDQTTSDQSNE HHCCCCCCCCCCCCC	32.34	-
578	Phosphorylation	EEGRDQTTSDQSNEF HCCCCCCCCCCCCCC	25.36	-
579	Phosphorylation	EGRDQTTSDQSNEFG CCCCCCCCCCCCCCH	36.72	-
582	Phosphorylation	DQTTSDQSNEFGIFN CCCCCCCCCCCHHHH	43.23	-
603	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	16129400
645	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	-
690	Phosphorylation	KMWTYMKSAEPSVFV HHHHHHHHCCCCEEE	22.72	22871156
694	Phosphorylation	YMKSAEPSVFVRTTE HHHHCCCCEEEEECC	21.49	-
699	Phosphorylation	EPSVFVRTTEEGMIR CCCEEEEECCCCEEE	33.00	22871156
700	Phosphorylation	PSVFVRTTEEGMIRV CCEEEEECCCCEEEE	22.83	22871156
710	Phosphorylation	GMIRVRKSKGKYAYL CEEEEEECCCCEEEE	35.76	-
714	Phosphorylation	VRKSKGKYAYLLEST EEECCCCEEEEEHHH	14.78	25293948
716	Phosphorylation	KSKGKYAYLLESTMN ECCCCEEEEEHHHHH	14.55	25293948
720	Phosphorylation	KYAYLLESTMNEYIE CEEEEEHHHHHHHHH	32.69	25293948
721	Phosphorylation	YAYLLESTMNEYIEQ EEEEEHHHHHHHHHH	18.03	25293948
725	Phosphorylation	LESTMNEYIEQRKPC EHHHHHHHHHHCCCC	12.54	25293948
829	S-palmitoylation	LVALIEFCYKSRSES HHHHHHHHHHCCCCH	2.44	16129400
836	Phosphorylation	CYKSRSESKRMKGFC HHHCCCCHHCCCCEE	27.15	19004011
849	Phosphorylation	FCLIPQQSINEAIRT EEEECHHHHHHHHHH	23.33	12198546
856	Phosphorylation	SINEAIRTSTLPRNS HHHHHHHHCCCCCCC	21.68	22817900
857	Phosphorylation	INEAIRTSTLPRNSG HHHHHHHCCCCCCCC	20.35	22817900
858	Phosphorylation	NEAIRTSTLPRNSGA HHHHHHCCCCCCCCC	39.92	22817900
863	Phosphorylation	TSTLPRNSGAGASGG HCCCCCCCCCCCCCC	31.16	18455244
871	Phosphorylation	GAGASGGSGSGENGR CCCCCCCCCCCCCCC	33.05	29899451
873	Phosphorylation	GASGGSGSGENGRVV CCCCCCCCCCCCCEE	44.63	27708245
881	Phosphorylation	GENGRVVSQDFPKSM CCCCCEECCCCCHHH	22.60	-

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
849	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
849	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
849	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
849	S	Phosphorylation	Kinase	PKCA	P20444	PSP
849	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
858	T	Phosphorylation	Kinase	CAMK2A	P11798	PSP
858	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
858	T	Phosphorylation	Kinase	PKCA	P20444	PSP
858	T	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
858	T	Phosphorylation	Kinase	P70S6K	Q8BSK8	PSP
858	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PKACA	P17612	PSP
863	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
863	S	Phosphorylation	Kinase	PRKG2	Q61410	GPS
863	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
863	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Nedd4l	Q8CFI0	PMID:28212375

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
603	C	Palmitoylation	16129400
ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to Golgi retention and decreased cell surface expression.
645	S	Phosphorylation	23676497
Phosphorylated at Ser-645.
710	S	Phosphorylation	23676497
Phosphorylated at Ser-710 by PKC.
829	C	Palmitoylation	16129400
In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis.
849	S	Phosphorylation	23676497
Phosphorylated at Ser-849 by PKC, PKA and CAMK2.
863	S	Phosphorylation	23676497
Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (By similarity).
863	S	Phosphorylation	23676497
Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_MOUSE	Sqstm1	physical	19004011
NMDZ1_MOUSE	Grin1	physical	17018287
NMDE1_MOUSE	Grin2a	physical	17018287
EPS8_MOUSE	Eps8	physical	17018287
NMDE3_MOUSE	Grin2c	physical	17018287
LRP1_MOUSE	Lrp1	physical	23760271

Drug and Disease Associations

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

Regulatory Network of GRIA1_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-603 AND CYS-829.	16129400 [Abstract]

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