dbPTM

GRIA4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA4_MOUSE
UniProt AC	Q9Z2W8
Protein Name	Glutamate receptor 4
Gene Name	Gria4
Organism	Mus musculus (Mouse).
Sequence Length	902
Subcellular Localization	Cell membrane Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein. Cell projection, dendrite. Interaction with CNIH2, CNIH3 and PRKCG promotes cell surface expression..
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 (By similarity)..
Protein Sequence	MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDAPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	N-linked_Glycosylation	RLAIFLHNTSPNASE EEEHHHHCCCCCCCC	44.38	-
56	N-linked_Glycosylation	FLHNTSPNASEAPFN HHHCCCCCCCCCCCC	56.73	-
248	Phosphorylation	NLGFKDISLERFIHG CCCCCCEEEEHEEEC	34.02	25159016
258	N-linked_Glycosylation	RFIHGGANVTGFQLV HEEECCCCCCCEEEE	34.85	-
371	N-linked_Glycosylation	DHYGRRVNYTMDVFE CCCCCEEEEEEEEEE	25.42	-
407	N-linked_Glycosylation	QDAPTLGNDTAAIEN ECCCCCCCCCHHHCC	46.72	-
414	N-linked_Glycosylation	NDTAAIENRTVVVTT CCCHHHCCCEEEEEE	38.52	-
420	Phosphorylation	ENRTVVVTTIMESPY CCCEEEEEEEECCCE	10.05	23140645
421	Phosphorylation	NRTVVVTTIMESPYV CCEEEEEEEECCCEE	13.50	23140645
425	Phosphorylation	VVTTIMESPYVMYKK EEEEEECCCEEEEEC	12.26	23140645
430	Phosphorylation	MESPYVMYKKNHEMF ECCCEEEEECCCCCC	14.57	23140645
611	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	-
684	Phosphorylation	TKEFFRRSKIAVYEK CHHHHHHHHHHHHHH	24.94	-
694	Phosphorylation	AVYEKMWTYMRSAEP HHHHHHHHHHHCCCC	12.16	-
695	Phosphorylation	VYEKMWTYMRSAEPS HHHHHHHHHHCCCCC	3.81	-
754	Phosphorylation	GNLDSKGYGVATPKG CCCCCCCCCCCCCCC	16.50	-
763	Phosphorylation	VATPKGSSLRTPVNL CCCCCCCCCCCCCEE	30.45	25367039
837	S-palmitoylation	LVALIEFCYKSRAEA HHHHHHHHHHCHHHH	2.44	16129400
850	Phosphorylation	EAKRMKLTFSEAIRN HHHHCCCCHHHHHHH	21.43	29899451
862	Phosphorylation	IRNKARLSITGSVGE HHHHCCEEEEECCCC	16.73	25521595
864	Phosphorylation	NKARLSITGSVGENG HHCCEEEEECCCCCC	21.74	22817900
866	Phosphorylation	ARLSITGSVGENGRV CCEEEEECCCCCCEE	20.49	25521595
875	Phosphorylation	GENGRVLTPDCPKAV CCCCEEECCCCCCCC	17.77	22817900
880	Ubiquitination	VLTPDCPKAVHTGTA EECCCCCCCCCCCCH	70.17	-

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
Oops, there are no upstream regulatory protein records of GRIA4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
611	C	Palmitoylation	-
Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression.
837	C	Palmitoylation	16129400
In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).
862	S	Phosphorylation	21183079
Phosphorylated at Ser-862 by PRKCG; phosphorylation increases plasma membrane-associated GRI4 expression.

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 GRIA4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of GRIA4_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of GRIA4_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-837.	16129400 [Abstract]

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