GRIK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRIK3_HUMAN
• UniProt AC: Q13003
• Protein Name: Glutamate receptor ionotropic, kainate 3
• Gene Name: GRIK3
• Organism: Homo sapiens (Human).
• Sequence Length: 919
• Subcellular Localization: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.
• 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. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA..
• Protein Sequence: MTAPWRRLRSLVWEYWAGLLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQYLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWSMERLQAAPRSESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFVYKLRKTAEREQRSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMACSTSLAPVFP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTAPWRRLR ------CCCCHHHHH	41.23	17192257
70	N-linked_Glycosylation	SANIINRNRTLLPNT HHHHHCCCCCCCCCC	36.48	UniProtKB CARBOHYD
76	N-linked_Glycosylation	RNRTLLPNTTLTYDI CCCCCCCCCEEEEEE	45.74	UniProtKB CARBOHYD
234	Phosphorylation	FRIIFDCSHTMAAQI EEEEEECCHHHHHHH	24.68	-
236	Phosphorylation	IIFDCSHTMAAQILK EEEECCHHHHHHHHH	7.69	-
278	N-linked_Glycosylation	PYRYSGVNLTGFRIL CCCCCCCCCCCEEEE	35.10	UniProtKB CARBOHYD
280	Phosphorylation	RYSGVNLTGFRILNV CCCCCCCCCEEEEEC	29.13	24719451
293	Phosphorylation	NVDNPHVSAIVEKWS ECCCCCHHHHHHHCC	14.83	22496350
300	Phosphorylation	SAIVEKWSMERLQAA HHHHHHCCHHHHHCC	23.10	22496350
381	N-linked_Glycosylation	LTGRIVFNKTSGLRT CCEEEEEECCCCCCC	35.48	UniProtKB CARBOHYD
396	Phosphorylation	DFDLDIISLKEDGLE CCEEEEEEECCCCCE	33.45	24719451
415	N-linked_Glycosylation	WSPADGLNITEVAKG ECCCCCCCHHHHHCC	44.67	UniProtKB CARBOHYD
426	N-linked_Glycosylation	VAKGRGPNVTDSLTN HHCCCCCCCHHHCCC	52.74	UniProtKB CARBOHYD
433	N-linked_Glycosylation	NVTDSLTNRSLIVTT CCHHHCCCCCEEEEE	36.52	UniProtKB CARBOHYD
435	Phosphorylation	TDSLTNRSLIVTTVL HHHCCCCCEEEEEEE	25.23	27762562
439	Phosphorylation	TNRSLIVTTVLEEPF CCCCEEEEEEECCCE	12.28	27762562
440	Phosphorylation	NRSLIVTTVLEEPFV CCCEEEEEEECCCEE	16.52	27762562
544	Phosphorylation	TLGVSILYRKPNGTN EEEEEEEEECCCCCC	18.21	17053785
548	N-linked_Glycosylation	SILYRKPNGTNPSVF EEEEECCCCCCCHHH	73.32	UniProtKB CARBOHYD
551	N-linked_Glycosylation	YRKPNGTNPSVFSFL EECCCCCCCHHHHHC	28.40	-
668	Phosphorylation	LTVERMESPIDSADD HCHHCCCCCCCCHHH	20.15	-
672	Phosphorylation	RMESPIDSADDLAKQ CCCCCCCCHHHHHHH	34.03	-
702	Phosphorylation	FFKKSKISTFEKMWA EEEHHCCCHHHHHHH	30.68	29970186
703	Phosphorylation	FKKSKISTFEKMWAF EEHHCCCHHHHHHHH	39.01	22210691
752	N-linked_Glycosylation	YVTQRNCNLTQIGGL HHHCCCCCCEEECCE	50.07	-
803	Phosphorylation	KEKWWRGSGCPEEEN CHHHCCCCCCCHHHC	28.75	28258704
814	Phosphorylation	EEENKEASALGIQKI HHHCHHHHHHCCCHH	25.72	28258704
869	Phosphorylation	VADEIRFSLTCQRRV HHHHHHHHHCCCCCC	16.96	29978859
871	Phosphorylation	DEIRFSLTCQRRVKH HHHHHHHCCCCCCCC	12.85	29978859

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of GRIK3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GRIK3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GRIK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRIK5_HUMAN	GRIK5	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)
• D02546: Kainic acid hydrate (JP16); Digenin (TN)
• D06656: Tezampanel (USAN); Tezampanel hydrate
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASSSPECTROMETRY.
PubMed: 18691976

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-544, AND MASSSPECTROMETRY.
PubMed: 17053785