GRIK3_HUMAN - dbPTM
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 Orthologous
Protein Cluster
2Phosphorylation------MTAPWRRLR
------CCCCHHHHH
41.2317192257
70N-linked_GlycosylationSANIINRNRTLLPNT
HHHHHCCCCCCCCCC
36.48UniProtKB CARBOHYD
76N-linked_GlycosylationRNRTLLPNTTLTYDI
CCCCCCCCCEEEEEE
45.74UniProtKB CARBOHYD
234PhosphorylationFRIIFDCSHTMAAQI
EEEEEECCHHHHHHH
24.68-
236PhosphorylationIIFDCSHTMAAQILK
EEEECCHHHHHHHHH
7.69-
278N-linked_GlycosylationPYRYSGVNLTGFRIL
CCCCCCCCCCCEEEE
35.10UniProtKB CARBOHYD
280PhosphorylationRYSGVNLTGFRILNV
CCCCCCCCCEEEEEC
29.1324719451
293PhosphorylationNVDNPHVSAIVEKWS
ECCCCCHHHHHHHCC
14.8322496350
300PhosphorylationSAIVEKWSMERLQAA
HHHHHHCCHHHHHCC
23.1022496350
381N-linked_GlycosylationLTGRIVFNKTSGLRT
CCEEEEEECCCCCCC
35.48UniProtKB CARBOHYD
396PhosphorylationDFDLDIISLKEDGLE
CCEEEEEEECCCCCE
33.4524719451
415N-linked_GlycosylationWSPADGLNITEVAKG
ECCCCCCCHHHHHCC
44.67UniProtKB CARBOHYD
426N-linked_GlycosylationVAKGRGPNVTDSLTN
HHCCCCCCCHHHCCC
52.74UniProtKB CARBOHYD
433N-linked_GlycosylationNVTDSLTNRSLIVTT
CCHHHCCCCCEEEEE
36.52UniProtKB CARBOHYD
435PhosphorylationTDSLTNRSLIVTTVL
HHHCCCCCEEEEEEE
25.2327762562
439PhosphorylationTNRSLIVTTVLEEPF
CCCCEEEEEEECCCE
12.2827762562
440PhosphorylationNRSLIVTTVLEEPFV
CCCEEEEEEECCCEE
16.5227762562
544PhosphorylationTLGVSILYRKPNGTN
EEEEEEEEECCCCCC
18.2117053785
548N-linked_GlycosylationSILYRKPNGTNPSVF
EEEEECCCCCCCHHH
73.32UniProtKB CARBOHYD
551N-linked_GlycosylationYRKPNGTNPSVFSFL
EECCCCCCCHHHHHC
28.40-
668PhosphorylationLTVERMESPIDSADD
HCHHCCCCCCCCHHH
20.15-
672PhosphorylationRMESPIDSADDLAKQ
CCCCCCCCHHHHHHH
34.03-
702PhosphorylationFFKKSKISTFEKMWA
EEEHHCCCHHHHHHH
30.6829970186
703PhosphorylationFKKSKISTFEKMWAF
EEHHCCCHHHHHHHH
39.0122210691
752N-linked_GlycosylationYVTQRNCNLTQIGGL
HHHCCCCCCEEECCE
50.07-
803PhosphorylationKEKWWRGSGCPEEEN
CHHHCCCCCCCHHHC
28.7528258704
814PhosphorylationEEENKEASALGIQKI
HHHCHHHHHHCCCHH
25.7228258704
869PhosphorylationVADEIRFSLTCQRRV
HHHHHHHHHCCCCCC
16.9629978859
871PhosphorylationDEIRFSLTCQRRVKH
HHHHHHHCCCCCCCC
12.8529978859

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

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

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

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRIK5_HUMANGRIK5physical
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.
Regulatory Network of GRIK3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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