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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
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 |
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 GRIK3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GRIK3_HUMAN !! |
* 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 GRIK3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GRIK5_HUMAN | GRIK5 | physical | 9466455 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. | |
"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. |