NMDE1_MOUSE - dbPTM
NMDE1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDE1_MOUSE
UniProt AC P35436
Protein Name Glutamate receptor ionotropic, NMDA 2A
Gene Name Grin2a
Organism Mus musculus (Mouse).
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. [PubMed: 1374164 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 (By similarity Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning]
Protein Sequence MGRLGYWTLLVLPALLVWHGPAQNAAAEKGTPALNIAVLLGHSHDVTERELRNLWGPEQATGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSQTFIPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYRDFISFIKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGLGILTTAASSMLEKFSYIPEAKASCYGQTEKPETPLHTLHQFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENQTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQRGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISNMSNMNSSRMDSPKRAADFIQRGSLIVDMVSDKGNLIYSDNRSFQGKDSIFGENMNELQTFVANRHKDSLSNYVFQGQHPLTLNESNPNTVEVAVSTESKGNSRPRQLWKKSMESLRQDSLNQNPVSQRDEKTAENRTHSLKSPRYLPEEVAHSDISETSSRATCHREPDNNKNHKTKDNFKRSMASKYPKDCSEVERTYVKTKASSPRDKIYTIDGEKEPSFHLDPPQFIENIVLPENVDFPDTYQDHNENFRKGDSTLPMNRNPLHNEDGLPNNDQYKLYAKHFTLKDKGSPHSEGSDRYRQNSTHCRSCLSNLPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATREEAYQQDWSQNNALQFQKNKLKINRQHSYDNILDKPREIDLSRPSRSISLKDRERLLEGNLYGSLFSVPSSKLLGNKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHTYGDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHSDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESDV
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-
380N-linked_GlycosylationEKVGKWENQTLSLRH
HHCCCCCCCCHHHHH		38.74-
438AcetylationRNTVPCRKFVKINNS
HCCCCCCCEEEECCC		62.317712657
443N-linked_GlycosylationCRKFVKINNSTNEGM
CCCEEEECCCCCCCC		30.59-
444N-linked_GlycosylationRKFVKINNSTNEGMN
CCEEEECCCCCCCCC		54.40-
445PhosphorylationKFVKINNSTNEGMNV
CEEEECCCCCCCCCH		28.2820415495
446PhosphorylationFVKINNSTNEGMNVK
EEEECCCCCCCCCHH		39.1420415495
453AcetylationTNEGMNVKKCCKGFC
CCCCCCHHHHHHHHH		34.787712669
502PhosphorylationGMIGEVVYQRAVMAV
HHHHHHHHHHHHHHH		9.47-
511PhosphorylationRAVMAVGSLTINEER
HHHHHHCCEEECCHH		18.7526824392
541N-linked_GlycosylationSVMVSRSNGTVSPSA
EEEEECCCCCCCHHH		49.39-
687N-linked_GlycosylationFRFGTVPNGSTERNI
CCCCCCCCCCCCCCC		53.35-
870S-palmitoylationISRGIYSCIHGVHIE
EHHHHHHHHHCEECC		1.1728680068
882PhosphorylationHIEEKKKSPDFNLTG
ECCHHCCCCCCCCCC		38.2825521595
888PhosphorylationKSPDFNLTGSQSNML
CCCCCCCCCCHHHHH		35.5725521595
890PhosphorylationPDFNLTGSQSNMLKL
CCCCCCCCHHHHHHH		25.7925521595
892PhosphorylationFNLTGSQSNMLKLLR
CCCCCCHHHHHHHHH		26.3825521595
900PhosphorylationNMLKLLRSAKNISNM
HHHHHHHHHHCHHHH		43.4922817900
902UbiquitinationLKLLRSAKNISNMSN
HHHHHHHHCHHHHHC		56.9422790023
908PhosphorylationAKNISNMSNMNSSRM
HHCHHHHHCCCCCCC		36.86-
912PhosphorylationSNMSNMNSSRMDSPK
HHHHCCCCCCCCCHH		14.4622324799
913PhosphorylationNMSNMNSSRMDSPKR
HHHCCCCCCCCCHHH		26.9822324799
917PhosphorylationMNSSRMDSPKRAADF
CCCCCCCCHHHHHHH		23.9922817900
929PhosphorylationADFIQRGSLIVDMVS
HHHHHHCCEEEEEEC		19.6725521595
936PhosphorylationSLIVDMVSDKGNLIY
CEEEEEECCCCCEEE		27.2825521595
943PhosphorylationSDKGNLIYSDNRSFQ
CCCCCEEECCCCCCC		17.0922324799
944PhosphorylationDKGNLIYSDNRSFQG
CCCCEEECCCCCCCC		22.7822817900
948PhosphorylationLIYSDNRSFQGKDSI
EEECCCCCCCCCCCC		28.3325521595
952UbiquitinationDNRSFQGKDSIFGEN
CCCCCCCCCCCCCCC		37.2022790023
954PhosphorylationRSFQGKDSIFGENMN
CCCCCCCCCCCCCHH		24.2529899451
974PhosphorylationVANRHKDSLSNYVFQ
HHHCCHHHHHHHCCC		38.2029899451
976PhosphorylationNRHKDSLSNYVFQGQ
HCCHHHHHHHCCCCC		30.0229899451
978PhosphorylationHKDSLSNYVFQGQHP
CHHHHHHHCCCCCCC		10.1629899451
1017PhosphorylationPRQLWKKSMESLRQD
CHHHHHHHHHHHHHH		24.8529899451
1020PhosphorylationLWKKSMESLRQDSLN
HHHHHHHHHHHHHCC		21.8829899451
1025PhosphorylationMESLRQDSLNQNPVS
HHHHHHHHCCCCCCC		22.3828382018
1032PhosphorylationSLNQNPVSQRDEKTA
HCCCCCCCHHHHHHH		22.2829899451
1059PhosphorylationLPEEVAHSDISETSS
CCHHHHCCCCCCCCC		27.2325521595
1062PhosphorylationEVAHSDISETSSRAT
HHHCCCCCCCCCCCC		39.5525521595
1064PhosphorylationAHSDISETSSRATCH
HCCCCCCCCCCCCCC		25.8029899451
1065PhosphorylationHSDISETSSRATCHR
CCCCCCCCCCCCCCC		17.4920415495
1066PhosphorylationSDISETSSRATCHRE
CCCCCCCCCCCCCCC		33.1020415495
1069PhosphorylationSETSSRATCHREPDN
CCCCCCCCCCCCCCC		14.0329899451
1105PhosphorylationCSEVERTYVKTKASS
CHHCHHHEEECCCCC		13.2329899451
1118PhosphorylationSSPRDKIYTIDGEKE
CCCCCEEEEECCCCC		11.9022324799
1119PhosphorylationSPRDKIYTIDGEKEP
CCCCEEEEECCCCCC		18.9629899451
1187PhosphorylationNNDQYKLYAKHFTLK
CCHHHEEEEEEEEEC		14.95-
1198PhosphorylationFTLKDKGSPHSEGSD
EEECCCCCCCCCCCH		25.7725521595
1201PhosphorylationKDKGSPHSEGSDRYR
CCCCCCCCCCCHHHH		47.2220415495
1204PhosphorylationGSPHSEGSDRYRQNS
CCCCCCCCHHHHCCC		18.1825521595
1207PhosphorylationHSEGSDRYRQNSTHC
CCCCCHHHHCCCHHH		22.8829899451
1211PhosphorylationSDRYRQNSTHCRSCL
CHHHHCCCHHHHHHH		15.9329899451
1212PhosphorylationDRYRQNSTHCRSCLS
HHHHCCCHHHHHHHH		32.3229899451
1223PhosphorylationSCLSNLPTYSGHFTM
HHHHCCCCCCCCEEC		33.22-
1229PhosphorylationPTYSGHFTMRSPFKC
CCCCCCEECCCCCCC		13.1529899451
1232PhosphorylationSGHFTMRSPFKCDAC
CCCEECCCCCCCCEE		24.7016337919
1246PhosphorylationCLRMGNLYDIDEDQM
EEECCCEECCCHHHH		18.17-
1267PhosphorylationPATREEAYQQDWSQN
CCCHHHHHHHCCHHC		15.2427180971
1291PhosphorylationLKINRQHSYDNILDK
HCCCCCCCCCCCCCC		26.3328382018
1292PhosphorylationKINRQHSYDNILDKP
CCCCCCCCCCCCCCC		15.7529899451
1305PhosphorylationKPREIDLSRPSRSIS
CCCCCCCCCCCCCCC		38.1029899451
1308PhosphorylationEIDLSRPSRSISLKD
CCCCCCCCCCCCHHH		37.2329899451
1310PhosphorylationDLSRPSRSISLKDRE
CCCCCCCCCCHHHHH		22.3729899451
1312PhosphorylationSRPSRSISLKDRERL
CCCCCCCCHHHHHHH		30.52-
1325PhosphorylationRLLEGNLYGSLFSVP
HHHCCCCHHHCCCCC		14.5222817900
1327PhosphorylationLEGNLYGSLFSVPSS
HCCCCHHHCCCCCHH		16.8229899451
1333PhosphorylationGSLFSVPSSKLLGNK
HHCCCCCHHHHCCCC		37.64-
1334PhosphorylationSLFSVPSSKLLGNKS
HCCCCCHHHHCCCCH		22.66-
1340UbiquitinationSSKLLGNKSSLFPQG
HHHHCCCCHHCCCCC		39.3622790023
1352UbiquitinationPQGLEDSKRSKSLLP
CCCCCCCHHHHHCCC		73.3722790023
1384PhosphorylationLVIGRCPSDPYKHSL
EEEEECCCCCCCCCC		55.6425521595
1387PhosphorylationGRCPSDPYKHSLPSQ
EECCCCCCCCCCCHH		26.73-
1399PhosphorylationPSQAVNDSYLRSSLR
CHHHCCHHHHHHHHH		22.3629899451
1403PhosphorylationVNDSYLRSSLRSTAS
CCHHHHHHHHHHHHH		31.0029899451
1404PhosphorylationNDSYLRSSLRSTASY
CHHHHHHHHHHHHHH		22.7429899451
1416PhosphorylationASYCSRDSRGHSDVY
HHHHCCCCCCCCCEE		38.7729899451
1420PhosphorylationSRDSRGHSDVYISEH
CCCCCCCCCEEEECC		31.4329899451
1423PhosphorylationSRGHSDVYISEHVMP
CCCCCCEEEECCHHH		12.0629899451
1425PhosphorylationGHSDVYISEHVMPYA
CCCCEEEECCHHHCC		12.1729899451
1449PhosphorylationPRVLNSCSNRRVYKK
HHHHHCCCCCCHHHC		32.9422817900
1459PhosphorylationRVYKKMPSIESDV--
CHHHCCCCCCCCC--		35.1721082442
1462PhosphorylationKKMPSIESDV-----
HCCCCCCCCC-----		41.8421183079
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
-KUbiquitinationE3 ubiquitin ligaseFbxo2Q80UW2
PMID:25878288
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMDE1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMDZ1_MOUSEGrin1physical
16554481
NMDE2_MOUSEGrin2bphysical
16554481
CHIN_HUMANCHN1physical
16221859
NMDE2_MOUSEGrin2bphysical
14645471
NMDZ1_MOUSEGrin1physical
14645471
DLG4_MOUSEDlg4physical
15663482
NMDZ1_MOUSEGrin1physical
17018287
EPS8_MOUSEEps8physical
17018287
NMDE3_MOUSEGrin2cphysical
17018287
LRP1_MOUSELrp1physical
23760271
IL16_MOUSEIl16physical
10479680
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NMDE1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-888; SER-929; SER-1025AND SER-1459, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-943, AND MASSSPECTROMETRY.

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