NMDE1_RAT - dbPTM
NMDE1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDE1_RAT
UniProt AC Q00959
Protein Name Glutamate receptor ionotropic, NMDA 2A
Gene Name Grin2a
Organism Rattus norvegicus (Rat).
Sequence Length 1464
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein .
Protein Description Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B. [PubMed: 28384476 Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity]
Protein Sequence MGRLGYWTLLVLPALLVWRDPAQNAAAEKGPPALNIAVLLGHSHDVTERELRNLWGPEQATGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSQTFIPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYRDFISFIKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGLGILTTAASSMLEKFSYIPEAKASCYGQAEKPETPLHTLHQFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENQTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTRFNQRGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFASTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISNMSNMNSSRMDSPKRATDFIQRGSLIVDMVSDKGNLIYSDNRSFQGKDSIFGDNMNELQTFVANRHKDNLSNYVFQGQHPLTLNESNPNTVEVAVSTESKGNSRPRQLWKKSMESLRQDSLNQNPVSQRDEKTAENRTHSLKSPRYLPEEVAHSDISETSSRATCHREPDNNKNHKTKDNFKRSMASKYPKDCSDVDRTYMKTKASSPRDKIYTIDGEKEPSFHLDPPQFVENITLPENVGFPDTYQDHNENFRKGDSTLPMNRNPLHNEDGLPNNDQYKLYAKHFTLKDKGSPHSEGSDRYRQNSTHCRSCLSNLPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATREEVYQQDWSQNNALQFQKNKLRINRQHSYDNILDKPREIDLSRPSRSISLKDRERLLEGNLYGSLFSVPSSKLLGNKSSLFPQGLEDSKRSKSLLPDHASDNPFLHTYGDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHSDVYISEHVMPYAANKNTMYSTPRVLNSCSNRRVYKKMPSIESDV
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
75N-linked_GlycosylationNVVALLMNRTDPKSL
HHHHHHCCCCCHHHH
43.60-
340N-linked_GlycosylationTLHQFMVNVTWDGKD
EEEEEEEEEEECCCC
17.45-
443N-linked_GlycosylationCRKFVKINNSTNEGM
CCCEEEECCCCCCCC
30.59-
444N-linked_GlycosylationRKFVKINNSTNEGMN
CCEEEECCCCCCCCC
54.40-
511PhosphorylationRAVMAVGSLTINEER
HHHHHHCCEEECCHH
18.7522335236
541N-linked_GlycosylationSVMVSRSNGTVSPSA
EEEEECCCCCCCHHH
49.39-
687N-linked_GlycosylationFRFGTVPNGSTERNI
CCCCCCCCCCCCCCC
53.35-
848S-palmitoylationFYWKLRFCFTGVCSD
HHHHHHHHHHHHCCC
2.1119874789
853S-palmitoylationRFCFTGVCSDRPGLL
HHHHHHHCCCCCCEE
3.5619874789
870S-palmitoylationISRGIYSCIHGVHIE
EHHHHHHHHHCEECC
1.1719874789
882PhosphorylationHIEEKKKSPDFNLTG
ECCHHCCCCCCCCCC
38.2825403869
888PhosphorylationKSPDFNLTGSQSNML
CCCCCCCCCCHHHHH
35.5722673903
890PhosphorylationPDFNLTGSQSNMLKL
CCCCCCCCHHHHHHH
25.7925403869
892PhosphorylationFNLTGSQSNMLKLLR
CCCCCCHHHHHHHHH
26.3822673903
929PhosphorylationTDFIQRGSLIVDMVS
HHHHHHCCEEEEEEC
19.6725403869
943PhosphorylationSDKGNLIYSDNRSFQ
CCCCCEEECCCCCCC
17.0927097102
944PhosphorylationDKGNLIYSDNRSFQG
CCCCEEECCCCCCCC
22.7827097102
948PhosphorylationLIYSDNRSFQGKDSI
EEECCCCCCCCCCCC
28.3325403869
976PhosphorylationNRHKDNLSNYVFQGQ
HCCCCCHHHHCCCCC
32.16-
978PhosphorylationHKDNLSNYVFQGQHP
CCCCHHHHCCCCCCC
10.16-
1025PhosphorylationMESLRQDSLNQNPVS
HHHHHHHHCCCCCCC
22.3827097102
1059PhosphorylationLPEEVAHSDISETSS
CCHHHHCCCCCCCCC
27.2325403869
1062PhosphorylationEVAHSDISETSSRAT
HHHCCCCCCCCCCCC
39.5525403869
1064PhosphorylationAHSDISETSSRATCH
HCCCCCCCCCCCCCC
25.8022673903
1099PhosphorylationSKYPKDCSDVDRTYM
HHCCCCCCCCHHHHC
51.29-
1104PhosphorylationDCSDVDRTYMKTKAS
CCCCCHHHHCCCCCC
24.41-
1105PhosphorylationCSDVDRTYMKTKASS
CCCCHHHHCCCCCCC
9.48-
1118PhosphorylationSSPRDKIYTIDGEKE
CCCCCEEEEECCCCC
11.90-
1119PhosphorylationSPRDKIYTIDGEKEP
CCCCEEEEECCCCCC
18.96-
1127PhosphorylationIDGEKEPSFHLDPPQ
ECCCCCCCCCCCCHH
26.79-
1184PhosphorylationGLPNNDQYKLYAKHF
CCCCCHHHEEEEEEE
13.06-
1187PhosphorylationNNDQYKLYAKHFTLK
CCHHHEEEEEEEEEC
14.95-
1198PhosphorylationFTLKDKGSPHSEGSD
EEECCCCCCCCCCCH
25.7725403869
1201PhosphorylationKDKGSPHSEGSDRYR
CCCCCCCCCCCHHHH
47.2225403869
1204PhosphorylationGSPHSEGSDRYRQNS
CCCCCCCCHHHHCCC
18.1825403869
1223PhosphorylationSCLSNLPTYSGHFTM
HHHHCCCCCCCCEEC
33.2225403869
1224PhosphorylationCLSNLPTYSGHFTMR
HHHCCCCCCCCEECC
15.6625403869
1225PhosphorylationLSNLPTYSGHFTMRS
HHCCCCCCCCEECCC
28.4125403869
1229PhosphorylationPTYSGHFTMRSPFKC
CCCCCCEECCCCCCC
13.1525403869
1232PhosphorylationSGHFTMRSPFKCDAC
CCCEECCCCCCCCEE
24.7025403869
1235UbiquitinationFTMRSPFKCDACLRM
EECCCCCCCCEEEEC
34.29-
1246PhosphorylationCLRMGNLYDIDEDQM
EEECCCEECCCHHHH
18.17-
1262PhosphorylationQETGNPATREEVYQQ
HHHCCCCCHHHHHHH
39.61-
1267PhosphorylationPATREEVYQQDWSQN
CCCHHHHHHHCCCCC
12.07-
1291PhosphorylationLRINRQHSYDNILDK
HHHCCCCCCCCCCCC
26.3323625947
1292PhosphorylationRINRQHSYDNILDKP
HHCCCCCCCCCCCCC
15.75-
1325PhosphorylationRLLEGNLYGSLFSVP
HHHCCCCHHHCCCCC
14.52-
1327PhosphorylationLEGNLYGSLFSVPSS
HCCCCHHHCCCCCHH
16.82-
1370PhosphorylationSDNPFLHTYGDDQRL
CCCCCCCCCCCCCEE
31.20-
1371PhosphorylationDNPFLHTYGDDQRLV
CCCCCCCCCCCCEEE
14.07-
1384PhosphorylationLVIGRCPSDPYKHSL
EEEEECCCCCCCCCC
55.64-
1387PhosphorylationGRCPSDPYKHSLPSQ
EECCCCCCCCCCCHH
26.7315748156
1390PhosphorylationPSDPYKHSLPSQAVN
CCCCCCCCCCHHHCC
37.51-
1399PhosphorylationPSQAVNDSYLRSSLR
CHHHCCHHHHHHHHH
22.36-
1400PhosphorylationSQAVNDSYLRSSLRS
HHHCCHHHHHHHHHH
14.70-
1416PhosphorylationASYCSRDSRGHSDVY
HHHHCCCCCCCCCEE
38.7722817900
1423PhosphorylationSRGHSDVYISEHVMP
CCCCCCEEEECCCHH
12.06-
1425PhosphorylationGHSDVYISEHVMPYA
CCCCEEEECCCHHCC
12.17-
1431PhosphorylationISEHVMPYAANKNTM
EECCCHHCCCCCCCC
10.55-
1437PhosphorylationPYAANKNTMYSTPRV
HCCCCCCCCCCCHHH
21.06-
1439PhosphorylationAANKNTMYSTPRVLN
CCCCCCCCCCHHHHH
13.83-
1440PhosphorylationANKNTMYSTPRVLNS
CCCCCCCCCHHHHHH
22.55-
1459PhosphorylationRVYKKMPSIESDV--
CHHHCCCCCCCCC--
35.1722673903
1462PhosphorylationKKMPSIESDV-----
HCCCCCCCCC-----
41.8422673903

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
1048SPhosphorylationKinaseDYRK1AQ13627
PSP
1232SPhosphorylationKinaseCDK5Q03114
PSP
1416SPhosphorylationKinasePRKCAP05696
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMDE1_RAT !!

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 NMDE1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG4_RATDlg4physical
8601796
DLG1_RATDlg1physical
8601796

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NMDE1_RAT

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Related Literatures of Post-Translational Modification

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