dbPTM

GRIA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIA4_HUMAN
UniProt AC	P48058
Protein Name	Glutamate receptor 4
Gene Name	GRIA4
Organism	Homo sapiens (Human).
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..
Protein Sequence	MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP

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	UniProtKB CARBOHYD
258	N-linked_Glycosylation	RFIHGGANVTGFQLV HEEECCCCCCCEEEE	34.85	UniProtKB CARBOHYD
258	N-linked_Glycosylation	RFIHGGANVTGFQLV HEEECCCCCCCEEEE	34.85	12603841
292	Phosphorylation	REYPGSETPPKYTSA CCCCCCCCCCCCCCC	46.73	24719451
314	Phosphorylation	VMAETFRSLRRQKID EEHHHHHHHHHHCCC	23.26	20058876
371	N-linked_Glycosylation	DHYGRRVNYTMDVFE CCCCCEEEEEEEEEE	25.42	UniProtKB CARBOHYD
371	N-linked_Glycosylation	DHYGRRVNYTMDVFE CCCCCEEEEEEEEEE	25.42	12603841
372	Phosphorylation	HYGRRVNYTMDVFEL CCCCEEEEEEEEEEE	10.69	30266825
373	Phosphorylation	YGRRVNYTMDVFELK CCCEEEEEEEEEEEC	11.16	30266825
404 (in isoform 2)	Phosphorylation	-	47.33	22210691
407	N-linked_Glycosylation	QDVPTLGNDTAAIEN ECCCCCCCCCHHHCC	46.72	12603841
407	N-linked_Glycosylation	QDVPTLGNDTAAIEN ECCCCCCCCCHHHCC	46.72	UniProtKB CARBOHYD
414	N-linked_Glycosylation	NDTAAIENRTVVVTT CCCHHHCCCEEEEEE	38.52	12603841
414	N-linked_Glycosylation	NDTAAIENRTVVVTT CCCHHHCCCEEEEEE	38.52	UniProtKB CARBOHYD
416	Phosphorylation	TAAIENRTVVVTTIM CHHHCCCEEEEEEEE	29.27	23663014
416 (in isoform 2)	Phosphorylation	-	29.27	22210691
420 (in isoform 2)	Phosphorylation	-	10.05	21712546
420	Phosphorylation	ENRTVVVTTIMESPY CCCEEEEEEEECCCE	10.05	23663014
421 (in isoform 2)	Phosphorylation	-	13.50	21712546
421	Phosphorylation	NRTVVVTTIMESPYV CCEEEEEEEECCCEE	13.50	23663014
425	Phosphorylation	VVTTIMESPYVMYKK EEEEEECCCEEEEEC	12.26	23663014
427	Phosphorylation	TTIMESPYVMYKKNH EEEECCCEEEEECCC	13.71	23663014
430	Phosphorylation	MESPYVMYKKNHEMF ECCCEEEEECCCCCC	14.57	23663014
442	Acetylation	EMFEGNDKYEGYCVD CCCCCCCCCCCCHHH	49.56	7428207
514	Phosphorylation	REEVIDFSKPFMSLG EHHHHCCCCCCCCCC	35.35	-
519	Phosphorylation	DFSKPFMSLGISIMI CCCCCCCCCCEEEEE	24.67	24719451
523	Phosphorylation	PFMSLGISIMIKKPQ CCCCCCEEEEEECCC	12.33	20860994
559	Phosphorylation	VFAYIGVSVVLFLVS HHHHHHHHHHHHHHH	10.99	22210691
611	S-palmitoylation	GAFMQQGCDISPRSL HHHHHCCCCCCCCCC	3.50	-
653	Phosphorylation	LTVERMVSPIESAED HCHHHCCCCCCCHHH	15.71	7877986
684	Phosphorylation	TKEFFRRSKIAVYEK CHHHHHHHHHHHHHH	24.94	24719451
694	Phosphorylation	AVYEKMWTYMRSAEP HHHHHHHHHHHCCCC	12.16	24719451
695	Phosphorylation	VYEKMWTYMRSAEPS HHHHHHHHHHCCCCC	3.81	24719451
751	Phosphorylation	KVGGNLDSKGYGVAT EECCCCCCCCCCCCC	31.01	22210691
760	Ubiquitination	GYGVATPKGSSLRTP CCCCCCCCCCCCCCC	68.05	-
766	Phosphorylation	PKGSSLRTPVNLAVL CCCCCCCCCCEEEEE	36.56	-
837	S-palmitoylation	LVALIEFCYKSRAEA HHHHHHHHHHCHHHH	2.44	-
838	Phosphorylation	VALIEFCYKSRAEAK HHHHHHHHHCHHHHH	19.81	-
850	Phosphorylation	EAKRMKLTFSEAIRN HHHHCCCCHHHHHHH	21.43	10366608
862	Phosphorylation	IRNKARLSITGSVGE HHHHCCEEEEECCCC	16.73	22817900

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
850	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
850	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
862	S	Phosphorylation	Kinase	PRKCG	P05129	Uniprot
862	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
862	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
862	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
862	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
862	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

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	-
In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).
862	S	Phosphorylation	-
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PICK1_HUMAN	PICK1	physical	11891216
GRIP1_HUMAN	GRIP1	physical	11891216
SDCB1_HUMAN	SDCBP	physical	11891216
KPCG_HUMAN	PRKCG	physical	12471040
GRIA1_HUMAN	GRIA1	physical	9466455

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 GRIA4_HUMAN

Related Literatures of Post-Translational Modification

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