GRID2_HUMAN - dbPTM
GRID2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRID2_HUMAN
UniProt AC O43424
Protein Name Glutamate receptor ionotropic, delta-2
Gene Name GRID2
Organism Homo sapiens (Human).
Sequence Length 1007
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein.
Protein Description Receptor for glutamate. 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. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex. [PubMed: 27418511]
Protein Sequence MEVFPFLLVLSVWWSRTWDSANADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLHDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQCDLYSSVDTKQKGGALDIKSFAGVFCILAAGIVLSCFIAMLETWWNKRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGNVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI
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
17PhosphorylationLSVWWSRTWDSANAD
HHHHHHCCCCCCCCC
28.2722210691
20PhosphorylationWWSRTWDSANADSII
HHHCCCCCCCCCCEE
18.2522210691
36PhosphorylationIGAIFDESAKKDDEV
EEECCCHHHCCCCHH
47.4322210691
223PhosphorylationRIEELNRYRDTLRRA
CHHHHHHHHHHHHHH
16.2728555341
238PhosphorylationILVMNPATAKSFITE
HHHCCHHHHHHHHHH
35.5627251275
293N-linked_GlycosylationQTFPVPQNISQRCFR
ECCCCCCCHHHHHCC
29.79UniProtKB CARBOHYD
349PhosphorylationLEDRKWHSMASLSCI
HHHCCCCCCCCHHHH
18.2222210691
352PhosphorylationRKWHSMASLSCIRKN
CCCCCCCCHHHHHCC
16.5122210691
354PhosphorylationWHSMASLSCIRKNSK
CCCCCCHHHHHCCCC
12.6624719451
368PhosphorylationKPWQGGRSMLETIKK
CCCCCCHHHHHHHHH
30.8722210691
382PhosphorylationKGGVSGLTGELEFGE
HCCCCCCEEEEEECC
31.9422210691
426N-linked_GlycosylationWNPVTGLNGSLTDKK
CCCCCCCCCCCCHHH
39.08UniProtKB CARBOHYD
525PhosphorylationDIGISALTITPDREN
CCEEEEEEECCCCHH
23.63-
543PhosphorylationFTTRYMDYSVGVLLR
HHHHHHCHHHHHHHH
6.69-
663PhosphorylationLTITRIESSIQSLQD
HHHHHHHHHHHHHHH
30.3025850435
664PhosphorylationTITRIESSIQSLQDL
HHHHHHHHHHHHHHH
16.3225850435
667PhosphorylationRIESSIQSLQDLSKQ
HHHHHHHHHHHHHHC
26.7427794612
672PhosphorylationIQSLQDLSKQTEIPY
HHHHHHHHHCCCCCC
30.8927794612
713N-linked_GlycosylationSQMWRMINRSNGSEN
HHHHHHHHCCCCCCC
31.80-
716N-linked_GlycosylationWRMINRSNGSENNVL
HHHHHCCCCCCCCCC
55.56-
880MethylationDLEHLHRRVNSLCTD
CHHHHHHHHHHHCCC
22.63-
883PhosphorylationHLHRRVNSLCTDDDS
HHHHHHHHHCCCCCC
23.20-
886PhosphorylationRRVNSLCTDDDSPHK
HHHHHHCCCCCCCCC
47.99-
890PhosphorylationSLCTDDDSPHKQFST
HHCCCCCCCCCCCCC
35.58-
903PhosphorylationSTSSIDLTPLDIDTL
CCCCCCCCCCCCCCC
20.32-
912PhosphorylationLDIDTLPTRQALEQI
CCCCCCCHHHHHHHH
38.23-
913MethylationDIDTLPTRQALEQIS
CCCCCCHHHHHHHHH
20.17-
1006PhosphorylationNDPDRGTSI------
CCCCCCCCC------
29.17-

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 GRID2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRID2_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 GRID2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRD2I_HUMANGRID2IPphysical
11826110
GRIA1_HUMANGRIA1physical
12573530
GRIK2_HUMANGRIK2physical
12573530
GOPC_HUMANGOPCphysical
12372286
PTN4_HUMANPTPN4physical
10748123

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRID2_HUMAN

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Related Literatures of Post-Translational Modification

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