dbPTM

GRIK2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRIK2_RAT
UniProt AC	P42260
Protein Name	Glutamate receptor ionotropic, kainate 2
Gene Name	Grik2
Organism	Rattus norvegicus (Rat).
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: 17115050]
Protein Sequence	MKIISPVLSNLVFSRSIKVLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	VLSNLVFSRSIKVLL HHHHHHHHHHHHHHH	20.03	29779826
16	Phosphorylation	SNLVFSRSIKVLLCL HHHHHHHHHHHHHHH	26.09	29779826
67	N-linked_Glycosylation	AVNTINRNRTLLPNT HHHHCCCCCCCCCCC	36.48	21791290
73	N-linked_Glycosylation	RNRTLLPNTTLTYDT CCCCCCCCCEEEECC	45.74	-
275	N-linked_Glycosylation	PYRYSGVNMTGFRIL CCCCCCCCCCCEEEE	26.31	-
378	N-linked_Glycosylation	LTGRITFNKTNGLRT CCCEEEEECCCCCCC	41.41	21791290
412	N-linked_Glycosylation	WDPASGLNMTESQKG CCCCCCCCCCHHHCC	38.56	21791290
423	N-linked_Glycosylation	SQKGKPANITDSLSN HHCCCCCCCCHHCCC	46.34	15677325
430	N-linked_Glycosylation	NITDSLSNRSLIVTT CCCHHCCCCCEEEEE	42.74	-
546	N-linked_Glycosylation	SILYRKPNGTNPGVF EEEEECCCCCCCCHH	73.32	-
715	Phosphorylation	FMSSRRQSVLVKSNE HHHHCCCEEEEECCH	18.66	8094892
751	N-linked_Glycosylation	FVTQRNCNLTQIGGL EECCCCCCEEEECCE	50.07	15677325
846	Phosphorylation	VGEFLYKSKKNAQLE HHHHHHHCCCCHHHH	34.99	22089239
856	Phosphorylation	NAQLEKRSFCSAMVE CHHHHHHHHHHHHHH	41.49	17379418
868	Phosphorylation	MVEELRMSLKCQRRL HHHHHHHHHHHHHHH	20.45	22089239
886	Sumoylation	PQAPVIVKTEEVINM CCCCEEEECHHEEEC	38.81	-
886	Sumoylation	PQAPVIVKTEEVINM CCCCEEEECHHEEEC	38.81	17486098

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
715	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
846	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
846	S	Phosphorylation	Kinase	PKC	-	Uniprot
856	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
868	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
868	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
868	S	Phosphorylation	Kinase	PKC	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Klhl17	Q8K430	PMID:22199232

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KLH17_RAT	Klhl17	physical	17062563
UBC_RAT	Ubc	physical	17062563
PICK1_RAT	Pick1	physical	15458844
PRKN_HUMAN	PARK2	physical	25316086
DLG4_RAT	Dlg4	physical	19449206
M3K11_RAT	Map3k11	physical	19449206

Drug and Disease Associations

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

Regulatory Network of GRIK2_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structure of the kainate receptor subunit GluR6 agonist-bindingdomain complexed with domoic acid."; Nanao M.H., Green T., Stern-Bach Y., Heinemann S.F., Choe S.; Proc. Natl. Acad. Sci. U.S.A. 102:1708-1713(2005). Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 419-819 IN COMPLEX WITHDOMOATE, SUBUNIT, AND GLYCOSYLATION AT ASN-423 AND ASN-751.	15677325 [Abstract]

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