NMDE2_HUMAN - dbPTM
NMDE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDE2_HUMAN
UniProt AC Q13224
Protein Name Glutamate receptor ionotropic, NMDA 2B
Gene Name GRIN2B
Organism Homo sapiens (Human).
Sequence Length 1484
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 MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKNLTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPARFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV
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
31PhosphorylationSRARSQKSPPSIGIA
HHHHHCCCCCCCEEE		34.11-
34PhosphorylationRSQKSPPSIGIAVIL
HHCCCCCCCEEEEEE		36.51-
63PhosphorylationKDDFHHLSVVPRVEL
CCCCCCCCCCCCEEE		19.4023663014
74N-linked_GlycosylationRVELVAMNETDPKSI
CEEEEECCCCCHHHH		39.00UniProtKB CARBOHYD
80PhosphorylationMNETDPKSIITRICD
CCCCCHHHHHHHHHH		25.3124719451
239PhosphorylationCTKEEATYIFEVANS
ECHHHHHHHEECCCC		15.63-
255PhosphorylationGLTGYGYTWIVPSLV
CCCCCCEEEEEECHH		12.3526074081
260PhosphorylationGYTWIVPSLVAGDTD
CEEEEEECHHCCCCC		25.2826074081
266PhosphorylationPSLVAGDTDTVPAEF
ECHHCCCCCCCCCCC		32.4326074081
268PhosphorylationLVAGDTDTVPAEFPT
HHCCCCCCCCCCCCC		30.4026074081
338PhosphorylationQSNMLNRYLINVTFE
HHCCCCCEEEEEEEE		15.7430631047
341N-linked_GlycosylationMLNRYLINVTFEGRN
CCCCEEEEEEEECCC		24.96UniProtKB CARBOHYD
341N-linked_GlycosylationMLNRYLINVTFEGRN
CCCCEEEEEEEECCC		24.961350383
348N-linked_GlycosylationNVTFEGRNLSFSEDG
EEEEECCCCCCCCCC		51.39UniProtKB CARBOHYD
383PhosphorylationVGKWKDKSLQMKYYV
CCCCCCCCHHCEEEE		33.698940188
444N-linked_GlycosylationQKRIVTENKTDEEPG
CEEEECCCCCCCCCC		43.06UniProtKB CARBOHYD
475PhosphorylationISKSVKFTYDLYLVT
HCCCCCEEEEEEEEE		15.48-
491N-linked_GlycosylationGKHGKKINGTWNGMI
CCCCCEECCCCCCHH		51.20UniProtKB CARBOHYD
493PhosphorylationHGKKINGTWNGMIGE
CCCEECCCCCCHHHH		15.98-
495N-linked_GlycosylationKKINGTWNGMIGEVV
CEECCCCCCHHHHHH		29.961350383
495N-linked_GlycosylationKKINGTWNGMIGEVV
CEECCCCCCHHHHHH		29.96-
514PhosphorylationYMAVGSLTINEERSE
HHHHCCEEECCHHHC		24.37-
516N-linked_GlycosylationAVGSLTINEERSEVV
HHCCEEECCHHHCCE		39.581350383
516N-linked_GlycosylationAVGSLTINEERSEVV
HHCCEEECCHHHCCE		39.58-
542N-linked_GlycosylationSVMVSRSNGTVSPSA
EEEEECCCCCCCHHH		49.39UniProtKB CARBOHYD
688N-linked_GlycosylationFRFGTVPNGSTERNI
CCCCCCCCCCCHHHH		53.35UniProtKB CARBOHYD
699PhosphorylationERNIRNNYAEMHAYM
HHHHHHCHHHHHHHH		13.9029978859
705PhosphorylationNYAEMHAYMGKFNQR
CHHHHHHHHHHCHHC		7.5429978859
720PhosphorylationGVDDALLSLKTGKLD
CHHHHHHHCCCCCCC		28.7729978859
731PhosphorylationGKLDAFIYDAAVLNY
CCCCEEEEHHHHHHH		7.9624275569
759PhosphorylationGSGKVFASTGYGIAI
CCCCEEEECCEEEEE		15.76-
760PhosphorylationSGKVFASTGYGIAIQ
CCCEEEECCEEEEEE		30.87-
762PhosphorylationKVFASTGYGIAIQKD
CEEEECCEEEEEECC		12.87-
770PhosphorylationGIAIQKDSGWKRQVD
EEEEECCCCHHHHEE		54.30-
865PhosphorylationPGMVFSISRGIYSCI
CCCEEEECCCHHHHH		24.21-
882PhosphorylationVAIEERQSVMNSPTA
CHHHHHHHHHCCCCH		29.5629978859
886PhosphorylationERQSVMNSPTATMNN
HHHHHHCCCCHHHCC		12.9224076635
888PhosphorylationQSVMNSPTATMNNTH
HHHHCCCCHHHCCHH		34.2829978859
890PhosphorylationVMNSPTATMNNTHSN
HHCCCCHHHCCHHHH		23.9429978859
894PhosphorylationPTATMNNTHSNILRL
CCHHHCCHHHHHHHH		22.9829978859
896PhosphorylationATMNNTHSNILRLLR
HHHCCHHHHHHHHHH		24.4329978859
912PhosphorylationAKNMANLSGVNGSPQ
HHHHHHHCCCCCCHH		40.2724076635
917PhosphorylationNLSGVNGSPQSALDF
HHCCCCCCHHHHHHH		17.9824076635
920PhosphorylationGVNGSPQSALDFIRR
CCCCCHHHHHHHHHH		33.9025307156
930PhosphorylationDFIRRESSVYDISEH
HHHHHCCCCCCHHHH		21.6827196784
932PhosphorylationIRRESSVYDISEHRR
HHHCCCCCCHHHHHC		14.9811024032
962PhosphorylationEENLFSDYISEVERT
HHCCCHHHHHHHHHH		12.7327196784
1039PhosphorylationHSQLSDLYGKFSFKS
CHHHHHHHCCCCCCC		24.2227196784
1043PhosphorylationSDLYGKFSFKSDRYS
HHHHCCCCCCCCCCC		34.9429496963
1058PhosphorylationGHDDLIRSDVSDIST
CCHHHHHCCCCCCCC		35.06-
1061PhosphorylationDLIRSDVSDISTHTV
HHHHCCCCCCCCCEE		33.93-
1064PhosphorylationRSDVSDISTHTVTYG
HCCCCCCCCCEEECC		21.08-
1070PhosphorylationISTHTVTYGNIEGNA
CCCCEEECCCCCCHH		12.1127196784
1109PhosphorylationFDEIELAYRRRPPRS
HHHHHHHHHCCCCCC		19.7824043423
1133PhosphorylationKEGLRDFYLDQFRTK
CCCCCHHHHHHHCCC		17.41-
1143PhosphorylationQFRTKENSPHWEHVD
HHCCCCCCCCCCCCC		21.1625307156
1155PhosphorylationHVDLTDIYKERSDDF
CCCHHHHHHHCCCCC		15.0327196784
1166PhosphorylationSDDFKRDSVSGGGPC
CCCCCCCCCCCCCCC		23.4029978859
1168PhosphorylationDFKRDSVSGGGPCTN
CCCCCCCCCCCCCCC		35.3529978859
1183PhosphorylationRSHIKHGTGDKHGVV
HHHHCCCCCCCCCEE		41.76-
1191PhosphorylationGDKHGVVSGVPAPWE
CCCCCEECCCCCCCC		31.50-
1252PhosphorylationCKKAGNLYDISEDNS
HHHHCCEECCCCCCC		18.4111024032
1255PhosphorylationAGNLYDISEDNSLQE
HCCEECCCCCCCCCC		35.68-
1259PhosphorylationYDISEDNSLQELDQP
ECCCCCCCCCCCCCC		43.69-
1280AcetylationTSNASTTKYPQSPTN
ECCCCCCCCCCCCCC		55.8320167786
1284PhosphorylationSTTKYPQSPTNSKAQ
CCCCCCCCCCCCHHH		29.2325307156
1289AcetylationPQSPTNSKAQKKNRN
CCCCCCCHHHHHHHH		57.8320167786
1303PhosphorylationNKLRRQHSYDTFVDL
HHHHHHHCHHHHHHH		19.1619453375
1304PhosphorylationKLRRQHSYDTFVDLQ
HHHHHHCHHHHHHHH		19.5127196784
1306PhosphorylationRRQHSYDTFVDLQKE
HHHHCHHHHHHHHHH		19.82-
1323PhosphorylationALAPRSVSLKDKGRF
HHCCCCCCCCCCCCC		30.8311306676
1336PhosphorylationRFMDGSPYAHMFEMS
CCCCCCCCCEEEEEC		15.7311024032
1378PhosphorylationYMLSKSLYPDRVTQN
CCCCCCCCCCCCCCC		15.3527196784
1410PhosphorylationSYFFRQPTVAGASKA
EEECCCCCCCCCCCC		18.04-
1432PhosphorylationVTNKPVVSALHGAVP
HCCCCHHHHCCCCCC		25.91-
1452PhosphorylationDICIGNQSNPCVPNN
CEEECCCCCCCCCCC		46.9028348404
1469PhosphorylationPRAFNGSSNGHVYEK
CCCCCCCCCCCHHHH		48.51-
1474PhosphorylationGSSNGHVYEKLSSIE
CCCCCCHHHHHHCCC		11.1520427654
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
1166SPhosphorylationKinasePKACAP17612
PSP
1303SPhosphorylationKinaseDAPK1P53355
Uniprot
1303SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1303SPhosphorylationKinaseKPCAP17252
PhosphoELM
1303SPhosphorylationKinasePRKCAP05696
GPS
1323SPhosphorylationKinaseKPCAP17252
PhosphoELM
1323SPhosphorylationKinasePRKCAP05696
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1303SPhosphorylation

-
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 NMDE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG32_HUMANARHGAP32physical
12857875
DLG4_HUMANDLG4physical
12738960
DLG3_HUMANDLG3physical
12738960
EXOC4_HUMANEXOC4physical
12738960
EXOC3_HUMANEXOC3physical
12738960
DLG4_HUMANDLG4physical
11997254
DLG2_HUMANDLG2physical
11997254
DLG1_HUMANDLG1physical
11997254
DLG3_HUMANDLG3physical
11997254
DLG4_HUMANDLG4physical
9278515
DLG3_HUMANDLG3physical
9278515
DLG2_HUMANDLG2physical
9278515
DLG4_HUMANDLG4physical
9581762
FYN_HUMANFYNphysical
10458595
LIN7A_HUMANLIN7Aphysical
10341223
LIN7B_HUMANLIN7Bphysical
10341223
DLGP2_RATDlgap2physical
7569905
DLG4_HUMANDLG4physical
7569905
MIB2_HUMANMIB2physical
17962190
DLG1_HUMANDLG1physical
8601796
DLG4_HUMANDLG4physical
8601796
SPTN1_HUMANSPTAN1physical
9670010
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
OMIM Disease
613970Mental retardation, autosomal dominant 6 (MRD6)
616139Epileptic encephalopathy, early infantile, 27 (EIEE27)
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)
D03100 Besonprodil (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)
D06204 Traxoprodil mesylate (USAN); Traxoprodil mesylate hydrate
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 NMDE2_HUMAN

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Related Literatures of Post-Translational Modification

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