dbPTM

GRIK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIK2_HUMAN
UniProt AC	Q13002
Protein Name	Glutamate receptor ionotropic, kainate 2
Gene Name	GRIK2
Organism	Homo sapiens (Human).
Sequence Length	908
Subcellular Localization	Cell membrane Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein.
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. [PubMed: 28180184 May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity]
Protein Sequence	MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	N-linked_Glycosylation	AVNTINRNRTLLPNT HHHHCCCCCCCCCCC	36.48	UniProtKB CARBOHYD
73	N-linked_Glycosylation	RNRTLLPNTTLTYDT CCCCCCCCCEEEECC	45.74	UniProtKB CARBOHYD
171	Phosphorylation	VQFFKWKTVTVVYDD HHHHCCCEEEEEEEC	21.94	-
173	Phosphorylation	FFKWKTVTVVYDDST HHCCCEEEEEEECCC	14.97	-
193	Phosphorylation	QELIKAPSRYNLRLK HHHHHCCCCCCCEEE	52.86	24719451
195	Phosphorylation	LIKAPSRYNLRLKIR HHHCCCCCCCEEEEE	23.92	24719451
209	Acetylation	RQLPADTKDAKPLLK EECCCCCCCCHHHHH	57.12	7971985
212	Acetylation	PADTKDAKPLLKEMK CCCCCCCHHHHHHHH	46.46	7632029
275	N-linked_Glycosylation	PYRYSGVNMTGFRIL CCCCCCCCCCCEEEE	26.31	UniProtKB CARBOHYD
361	Phosphorylation	RFGTRFMSLIKEAHW CCHHHHHHHHHHHCC	25.00	24719451
372	Phosphorylation	EAHWEGLTGRITFNK HHCCCCCCCEEEEEC	34.96	26074081
376	Phosphorylation	EGLTGRITFNKTNGL CCCCCEEEEECCCCC	21.57	26074081
378	N-linked_Glycosylation	LTGRITFNKTNGLRT CCCEEEEECCCCCCC	41.41	UniProtKB CARBOHYD
380	Phosphorylation	GRITFNKTNGLRTDF CEEEEECCCCCCCCC	35.31	26074081
385	Phosphorylation	NKTNGLRTDFDLDVI ECCCCCCCCCEEEEE	46.17	26074081
393	Phosphorylation	DFDLDVISLKEEGLE CCEEEEEEECHHHHH	32.98	24719451
395	Ubiquitination	DLDVISLKEEGLEKI EEEEEEECHHHHHHC	47.10	-
404	Phosphorylation	EGLEKIGTWDPASGL HHHHHCCCCCCCCCC	30.12	23663014
409	Phosphorylation	IGTWDPASGLNMTES CCCCCCCCCCCCCHH	49.56	23663014
412	N-linked_Glycosylation	WDPASGLNMTESQKG CCCCCCCCCCHHHCC	38.56	UniProtKB CARBOHYD
414	Phosphorylation	PASGLNMTESQKGKP CCCCCCCCHHHCCCC	31.26	23663014
416	Phosphorylation	SGLNMTESQKGKPAN CCCCCCHHHCCCCCC	28.20	23663014
423	N-linked_Glycosylation	SQKGKPANITDSLSN HHCCCCCCCCHHCCC	46.34	UniProtKB CARBOHYD
425	Phosphorylation	KGKPANITDSLSNRS CCCCCCCCHHCCCCC	21.24	-
429	Phosphorylation	ANITDSLSNRSLIVT CCCCHHCCCCCEEEE	33.86	-
430	N-linked_Glycosylation	NITDSLSNRSLIVTT CCCHHCCCCCEEEEE	42.74	UniProtKB CARBOHYD
437	Phosphorylation	NRSLIVTTILEEPYV CCCEEEEEECCCCEE	16.81	-
546	N-linked_Glycosylation	SILYRKPNGTNPGVF EEEEECCCCCCCCHH	73.32	8188697
546	N-linked_Glycosylation	SILYRKPNGTNPGVF EEEEECCCCCCCCHH	73.32	UniProtKB CARBOHYD
590	Phosphorylation	RFSPYEWYNPHPCNP CCCCCCCCCCCCCCC	13.58	-
666	Phosphorylation	LTVERMESPIDSADD HCHHCCCCCCCCHHH	20.15	-
670	Phosphorylation	RMESPIDSADDLAKQ CCCCCCCCHHHHHHH	34.03	-
682	Phosphorylation	AKQTKIEYGAVEDGA HHHHCCEEECCCCCC	17.54	-
697	Phosphorylation	TMTFFKKSKISTYDK EEEEEEHHCCCHHHH	35.49	8382377
700	Phosphorylation	FFKKSKISTYDKMWA EEEHHCCCHHHHHHH	25.34	-
702	Phosphorylation	KKSKISTYDKMWAFM EHHCCCHHHHHHHHH	13.53	-
715	Phosphorylation	FMSSRRQSVLVKSNE HHHHCCCEEEEECCH	18.66	8094892
751	N-linked_Glycosylation	FVTQRNCNLTQIGGL EECCCCCCEEEECCE	50.07	-
751	N-linked_Glycosylation	FVTQRNCNLTQIGGL EECCCCCCEEEECCE	50.07	8163463
834	Phosphorylation	LAAGLVLSVFVAVGE HHHHHHHHHHHHHHH	13.16	-
846	Phosphorylation	VGEFLYKSKKNAQLE HHHHHHHCCCCHHHH	34.99	22808340
847	Acetylation	GEFLYKSKKNAQLEK HHHHHHCCCCHHHHH	45.99	26210075
848	Acetylation	EFLYKSKKNAQLEKR HHHHHCCCCHHHHHH	65.68	26210075
859	Phosphorylation	LEKRSFCSAMVEELR HHHHHHHHHHHHHHH	19.86	28555341
868	Phosphorylation	MVEELRMSLKCQRRL HHHHHHHHHHHHHHH	20.45	22808340
886	Sumoylation	PQAPVIVKTEEVINM CCCCEEEECHHEEEC	38.81	22808340
886	Sumoylation	PQAPVIVKTEEVINM CCCCEEEECHHEEEC	38.81	-

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
590	Y	Phosphorylation	Kinase	SRC	P12931	PSP
697	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
697	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
715	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
715	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
846	S	Phosphorylation	Kinase	PKC	-	Uniprot
868	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
868	S	Phosphorylation	Kinase	PKC	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL17	Q6TDP4	PMID:17062563

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
868	S	Phosphorylation	22808340
Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.
868	S	Sumoylation	22808340
Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.

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 GRIK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SDCB1_HUMAN	SDCBP	physical	12597860
PICK1_HUMAN	PICK1	physical	12597860
DLG4_HUMAN	DLG4	physical	12597860
GRIP1_HUMAN	GRIP1	physical	12597860
GRID2_HUMAN	GRID2	physical	12573530
DLG4_HUMAN	DLG4	physical	9808460
DLG3_HUMAN	DLG3	physical	9808460
DLG1_HUMAN	DLG1	physical	9808460
GRIK5_HUMAN	GRIK5	physical	8288598
GRIA1_HUMAN	GRIA1	physical	8288598
GRIA2_HUMAN	GRIA2	physical	8288598
GRIK5_HUMAN	GRIK5	physical	9466455
PICK1_HUMAN	PICK1	physical	18692513
TRI25_HUMAN	TRIM25	physical	21988832
GRIK5_HUMAN	GRIK5	physical	15583001

Drug and Disease Associations

Kegg Disease
H00768	Nonsyndromic autosomal recessive mental retardation (NS-ARMR)
OMIM Disease
611092	Mental retardation, autosomal recessive 6 (MRT6)
Kegg Drug
D00537	Topiramate (JAN/USAN/INN); Topamax (TN); Trokendi xr (TN)
D02546	Kainic acid hydrate (JP16); Digenin (TN)
D06656	Tezampanel (USAN); Tezampanel hydrate
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GRIK2_HUMAN

Related Literatures of Post-Translational Modification

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