NMDE1_HUMAN - dbPTM
NMDE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDE1_HUMAN
UniProt AC Q12879
Protein Name Glutamate receptor ionotropic, NMDA 2A
Gene Name GRIN2A
Organism Homo sapiens (Human).
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+). [PubMed: 8768735]
Protein Sequence MGRVGYWTLLVLPALLVWRGPAPSAAAEKGPPALNIAVMLGHSHDVTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNSSRMDSPKRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEVAVSTESKANSRPRQLWKKSVDSIRQDSLSQNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPDNSKNHKTKDNFKRSVASKYPKDCSEVERTYLKTKSSSPRDKIYTIDGEKEPGFHLDPPQFVENVTLPENVDFPDPYQDPSENFRKGDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKGSPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATGEQVYQQDWAQNNALQLQKNKLRISRQHSYDNIVDKPRELDLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESDV
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		43.60UniProtKB CARBOHYD
87S-nitrosylationKSLITHVCDLMSGAR
HHHHHHHHHHHCCCE		2.3022178444
87S-nitrosocysteineKSLITHVCDLMSGAR
HHHHHHHHHHHCCCE		2.30-
104PhosphorylationGLVFGDDTDQEAVAQ
EEEECCCCCHHHHHH		44.3028348404
117PhosphorylationAQMLDFISSHTFVPI
HHHHHHHHHCCCCEE		18.9628348404
120PhosphorylationLDFISSHTFVPILGI
HHHHHHCCCCEEEEE		28.4227251275
132PhosphorylationLGIHGGASMIMADKD
EEEECCEEEEECCCC		16.4728348404
225PhosphorylationQLKKIHSSVILLYCS
HHHHHCCEEEEEEEC		10.0627762562
232PhosphorylationSVILLYCSKDEAVLI
EEEEEEECCCCEEEE		29.5923403867
274PhosphorylationLIPKEFPSGLISVSY
CCCCCCCCCCEEEEC		52.10-
278PhosphorylationEFPSGLISVSYDDWD
CCCCCCEEEECCCCC		15.28-
280PhosphorylationPSGLISVSYDDWDYS
CCCCEEEECCCCCCE		18.96-
281PhosphorylationSGLISVSYDDWDYSL
CCCEEEECCCCCCEE		18.76-
320S-nitrosocysteineIPEAKASCYGQMERP
CHHHHHHHCCCCCCC		5.45-
320S-nitrosylationIPEAKASCYGQMERP
CHHHHHHHCCCCCCC		5.4522178444
340N-linked_GlycosylationTLHPFMVNVTWDGKD
CCCCEEEEEEECCCC		17.451350383
340N-linked_GlycosylationTLHPFMVNVTWDGKD
CCCCEEEEEEECCCC		17.45UniProtKB CARBOHYD
380N-linked_GlycosylationEKVGKWENHTLSLRH
HCCCCEECCCCHHHH		32.12UniProtKB CARBOHYD
384PhosphorylationKWENHTLSLRHAVWP
CEECCCCHHHHCHHH		25.2224719451
393PhosphorylationRHAVWPRYKSFSDCE
HHCHHHCCCCCCCCC		13.60-
399S-nitrosocysteineRYKSFSDCEPDDNHL
CCCCCCCCCCCCCCE		8.72-
399S-nitrosylationRYKSFSDCEPDDNHL
CCCCCCCCCCCCCCE		8.7210571239
443N-linked_GlycosylationCRKFVKINNSTNEGM
CCCEEEECCCCCCCC		30.59UniProtKB CARBOHYD
444N-linked_GlycosylationRKFVKINNSTNEGMN
CCEEEECCCCCCCCC		54.40UniProtKB CARBOHYD
470PhosphorylationILKKLSRTVKFTYDL
HHHHHCCCEEEEEEE		25.36-
494N-linked_GlycosylationKKVNNVWNGMIGEVV
CEECCCCCHHHHHHH		26.351350383
494N-linked_GlycosylationKKVNNVWNGMIGEVV
CEECCCCCHHHHHHH		26.35-
515N-linked_GlycosylationAVGSLTINEERSEVV
HHCCEEECCHHHCCC		39.581350383
515N-linked_GlycosylationAVGSLTINEERSEVV
HHCCEEECCHHHCCC		39.58-
541N-linked_GlycosylationSVMVSRSNGTVSPSA
EEEEECCCCCCCHHH		49.39UniProtKB CARBOHYD
687N-linked_GlycosylationFRFGTVPNGSTERNI
CCCCCCCCCCCCCCC		53.35-
698PhosphorylationERNIRNNYPYMHQYM
CCCCHHCCHHHHHHH		10.1729052541
700PhosphorylationNIRNNYPYMHQYMTK
CCHHCCHHHHHHHHH		9.2529052541
704PhosphorylationNYPYMHQYMTKFNQK
CCHHHHHHHHHCHHC		7.6529052541
706PhosphorylationPYMHQYMTKFNQKGV
HHHHHHHHHCHHCCH		27.7929052541
719PhosphorylationGVEDALVSLKTGKLD
CHHHHHHHHHCCCCC		25.6224719451
730PhosphorylationGKLDAFIYDAAVLNY
CCCCEEEEEHHHHCC		7.9620736484
737PhosphorylationYDAAVLNYKAGRDEG
EEHHHHCCCCCCCCC		9.6922817900
749PhosphorylationDEGCKLVTIGSGYIF
CCCCEEEEECCCEEE		30.01-
880MethylationGVHIEEKKKSPDFNL
CEECCHHCCCCCCCC		62.8623644510
882PhosphorylationHIEEKKKSPDFNLTG
ECCHHCCCCCCCCCC		38.2824076635
890PhosphorylationPDFNLTGSQSNMLKL
CCCCCCCCHHHHHHH		25.7925307156
892PhosphorylationFNLTGSQSNMLKLLR
CCCCCCHHHHHHHHH		26.3825332170
900PhosphorylationNMLKLLRSAKNISSM
HHHHHHHHCCCHHHH		43.49-
905PhosphorylationLRSAKNISSMSNMNS
HHHCCCHHHHHCCCC		29.4020393185
906PhosphorylationRSAKNISSMSNMNSS
HHCCCHHHHHCCCCC		23.5620393185
908PhosphorylationAKNISSMSNMNSSRM
CCCHHHHHCCCCCCC		34.5720393185
912PhosphorylationSSMSNMNSSRMDSPK
HHHHCCCCCCCCCHH		14.4622817900
913PhosphorylationSMSNMNSSRMDSPKR
HHHCCCCCCCCCHHH		26.9820393185
917PhosphorylationMNSSRMDSPKRAADF
CCCCCCCCHHHHHHH		23.9922817900
929PhosphorylationADFIQRGSLIMDMVS
HHHHHHCCHHHHCCC		19.5324719451
938UbiquitinationIMDMVSDKGNLMYSD
HHHCCCCCCCEECCC		42.0421906983
943PhosphorylationSDKGNLMYSDNRSFQ
CCCCCEECCCCCCCC		18.9522817900
944PhosphorylationDKGNLMYSDNRSFQG
CCCCEECCCCCCCCC		17.9125247763
991PhosphorylationHPLTLNESNPNTVEV
CCCCCCCCCCCCEEE		57.4219845377
1025PhosphorylationVDSIRQDSLSQNPVS
HHHHHHHCCCCCCCC		22.91-
1048PhosphorylationNRTHSLKSPRYLPEE
HHCCCCCCCCCCCHH		21.65-
1059PhosphorylationLPEEMAHSDISETSN
CCHHHCCCCCCCCCC		27.40-
1062PhosphorylationEMAHSDISETSNRAT
HHCCCCCCCCCCCCC		39.55-
1105PhosphorylationCSEVERTYLKTKSSS
CHHHHHHHCCCCCCC		16.6622817900
1118PhosphorylationSSPRDKIYTIDGEKE
CCCCCEEEEECCCCC		11.9022817900
1163PhosphorylationENFRKGDSTLPMNRN
CCCCCCCCCCCCCCC		40.28-
1164PhosphorylationNFRKGDSTLPMNRNP
CCCCCCCCCCCCCCC		39.35-
1179PhosphorylationLHNEEGLSNNDQYKL
CCCCCCCCCCHHHEE		44.43-
1184PhosphorylationGLSNNDQYKLYSKHF
CCCCCHHHEEEEECE		13.0620448061
1187PhosphorylationNNDQYKLYSKHFTLK
CCHHHEEEEECEECC		16.1222817900
1198PhosphorylationFTLKDKGSPHSETSE
EECCCCCCCCCHHHH		25.77-
1211PhosphorylationSERYRQNSTHCRSCL
HHHHHHCCHHHHHHH		15.9322210691
1212PhosphorylationERYRQNSTHCRSCLS
HHHHHCCHHHHHHHH		32.3222210691
1223PhosphorylationSCLSNMPTYSGHFTM
HHHHCCCCCCCCEEE		21.3922210691
1232PhosphorylationSGHFTMRSPFKCDAC
CCCEEECCCCCCCEE		24.7011675505
1246PhosphorylationCLRMGNLYDIDEDQM
EEECCCEECCCHHHH		18.1722817900
1267PhosphorylationPATGEQVYQQDWAQN
CCCCHHHHHHHHHHC		10.5122817900
1287PhosphorylationQKNKLRISRQHSYDN
HHHHHHHHHHCCCCC		21.3219053533
1291PhosphorylationLRISRQHSYDNIVDK
HHHHHHCCCCCCCCC		26.3312147342
1292PhosphorylationRISRQHSYDNIVDKP
HHHHHCCCCCCCCCC		15.7519053533
1305PhosphorylationKPRELDLSRPSRSIS
CCHHHCCCCCCCCCC		41.6429449344
1308PhosphorylationELDLSRPSRSISLKD
HHCCCCCCCCCCHHH		37.2329449344
1310PhosphorylationDLSRPSRSISLKDRE
CCCCCCCCCCHHHHH		22.3724719451
1312PhosphorylationSRPSRSISLKDRERL
CCCCCCCCHHHHHHH		30.5224719451
1325PhosphorylationRLLEGNFYGSLFSVP
HHHCCCCCHHCCCCC		15.1420448061
1337PhosphorylationSVPSSKLSGKKSSLF
CCCHHHCCCCCCCCC		52.9117081983
1387PhosphorylationGRCPSDPYKHSLPSQ
EECCCCCCCCCCCHH		26.7322817900
1403PhosphorylationVNDSYLRSSLRSTAS
CCHHHHHHHHHHHHH		31.0023927012
1404PhosphorylationNDSYLRSSLRSTASY
CHHHHHHHHHHHHHH		22.7420068231
1416PhosphorylationASYCSRDSRGHNDVY
HHHHCCCCCCCCCEE		38.7711104776
1423PhosphorylationSRGHNDVYISEHVMP
CCCCCCEEEECCHHH		11.1220448061
1439PhosphorylationAANKNNMYSTPRVLN
CCCCCCCCCCHHHHH		16.1227251275
1440PhosphorylationANKNNMYSTPRVLNS
CCCCCCCCCHHHHHC		22.5927251275
1441PhosphorylationNKNNMYSTPRVLNSC
CCCCCCCCHHHHHCC		9.5327251275
1459PhosphorylationRVYKKMPSIESDV--
CHHHCCCCCCCCC--		35.1725307156
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
943YPhosphorylationKinaseFYNP06241
PSP
1105YPhosphorylationKinaseFYNP06241
PSP
1118YPhosphorylationKinaseFYNP06241
PSP
1184YPhosphorylationKinaseSRCP12931
PSP
1187YPhosphorylationKinaseFYNP06241
PSP
1232SPhosphorylationKinaseCDK-FAMILY-GPS
1232SPhosphorylationKinaseCDK_GROUP-PhosphoELM
1246YPhosphorylationKinaseFYNP06241
PSP
1267YPhosphorylationKinaseFYNP06241
PSP
1267YPhosphorylationKinaseSRCP12931
PSP
1325YPhosphorylationKinaseFYNP06241
PSP
1325YPhosphorylationKinaseSRCP12931
PSP
1423YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMDE1_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 NMDE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG1_HUMANDLG1physical
12933808
FAK2_HUMANPTK2Bphysical
12576483
FYN_HUMANFYNphysical
12419528
DLG4_HUMANDLG4physical
12419528
DLG4_HUMANDLG4physical
9278515
DLG3_HUMANDLG3physical
9278515
DLG2_HUMANDLG2physical
9278515
DLG4_HUMANDLG4physical
10648730
SRC_HUMANSRCphysical
10458595
FYN_HUMANFYNphysical
10458595
FAK2_HUMANPTK2Bphysical
11478920
DLGP2_RATDlgap2physical
7569905
DLG1_HUMANDLG1physical
8601796
DLG4_HUMANDLG4physical
8601796
SPTN1_HUMANSPTAN1physical
9670010
NMDZ1_HUMANGRIN1physical
14732708
DLG4_HUMANDLG4physical
14732708
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
OMIM Disease
245570Epilepsy, focal, with speech disorder and with or without mental retardation (FESD)
Kegg Drug
D00711 Ketamine hydrochloride (JP16/USP); Ketalar (TN)
D00777 Amantadine hydrochloride (JP16/USP); Symmetrel (TN)
D00848 Dextromethorphan hydrobromide hydrate (JP16); Dextromethorphan hydrobromide (USP); Benylin DM (TN)
D01445 Ifenprodil tartrate (JP16); Cerocral (TN)
D02102 Methadone hydrochloride (JAN/USP); Dolophine hydrochloride (TN)
D02410 Selfotel (USAN/INN)
D02780 Acamprosate calcium (JAN/USAN); Campral (TN); Regtect (TN)
D02973 Aptiganel hydrochloride (USAN)
D03679 Delucemine hydrochloride (USAN)
D03742 Dextromethorphan (USP)
D03744 Dextromethorphan polistirex (USAN); Delsym (TN)
D03746 Dextrorphan hydrochloride (USAN)
D03878 Dizocilpine maleate (USAN)
D04226 Flupirtine maleate (USAN)
D04308 Gavestinel (USAN/INN)
D04728 Licostinel (USAN/INN)
D04905 Memantine hydrochloride (JAN/USAN); Namenda (TN); Memary (TN)
D05145 Neramexane mesylate (USAN)
D05447 Perzinfotel (USAN/INN)
D05453 Phencyclidine hydrochloride (USAN); PCP
D05714 Remacemide hydrochloride (USAN)
D06146 Tiletamine hydrochloride (USP)
D07058 Acamprosate (INN); Aotal (TN)
D07283 Esketamine (INN)
D07441 Amantadine (INN)
D07978 Flupirtine (INN)
D07979 Flupirtine D-gluconate; Katadolon (TN)
D08064 Ifenprodil (INN)
D08098 Ketamine (INN); Tekam (TN)
D08100 Ketobemidone (INN)
D08101 Ketobemidone hydrochloride; Ketogan (TN)
D08121 Levomethadone (INN)
D08122 Levomethadone hydrochloride; L-polamidon (TN)
D08174 Memantine (INN); Exiba (TN)
D08195 Methadone (BAN)
D08596 Tiletamine (INN)
D09917 Latrepirdine (USAN/INN)
D09918 Latrepirdine dihydrochloride (USAN); Dimebolin; Dimebon
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NMDE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912 AND SER-917, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1337, AND MASSSPECTROMETRY.

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