NMDZ1_HUMAN - dbPTM
NMDZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDZ1_HUMAN
UniProt AC Q05586
Protein Name Glutamate receptor ionotropic, NMDA 1
Gene Name GRIN1
Organism Homo sapiens (Human).
Sequence Length 938
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Enriched in postsynaptic plasma membrane and postsynaptic densities..
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: 7685113]
Protein Sequence MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES
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
2Phosphorylation------MSTMRLLTL
------CCHHHHHHH		30.8024043423
3Phosphorylation-----MSTMRLLTLA
-----CCHHHHHHHH		12.6624043423
8PhosphorylationMSTMRLLTLALLFSC
CCHHHHHHHHHHHHH		17.9924043423
14PhosphorylationLTLALLFSCSVARAA
HHHHHHHHHHHHHHH		12.8824043423
16PhosphorylationLALLFSCSVARAACD
HHHHHHHHHHHHHCC		20.0124043423
51AcetylationEAVNQANKRHGSWKI
HHHHHHHHHCCCEEE		49.1130590787
61N-linked_GlycosylationGSWKIQLNATSVTHK
CCEEEEEECEECCCC		25.46UniProtKB CARBOHYD
122PhosphorylationRIPVLGLTTRMSIYS
EEEECEEEECEEECC		15.5723403867
123PhosphorylationIPVLGLTTRMSIYSD
EEECEEEECEEECCC		29.4423403867
126PhosphorylationLGLTTRMSIYSDKSI
CEEEECEEECCCCEE		18.3230206219
128PhosphorylationLTTRMSIYSDKSIHL
EEECEEECCCCEEEE		11.9630206219
129PhosphorylationTTRMSIYSDKSIHLS
EECEEECCCCEEEEE		36.5730206219
196 (in isoform 7)Phosphorylation-43.6229083192
196 (in isoform 6)Phosphorylation-43.6229083192
196 (in isoform 5)Phosphorylation-43.6229083192
203N-linked_GlycosylationQFDPGTKNVTALLME
CCCCCCCCHHHHHHH		35.89UniProtKB CARBOHYD
203 (in isoform 7)Phosphorylation-35.8929083192
203 (in isoform 6)Phosphorylation-35.8929083192
203 (in isoform 5)Phosphorylation-35.8929083192
204 (in isoform 5)Phosphorylation-3.3629083192
204 (in isoform 6)Phosphorylation-3.3629083192
204 (in isoform 7)Phosphorylation-3.3629083192
205O-linked_GlycosylationDPGTKNVTALLMEAK
CCCCCCHHHHHHHHH		22.4528657654
232PhosphorylationEDDAATVYRAAAMLN
CCHHHHHHHHHHHHH		7.0925332170
239N-linked_GlycosylationYRAAAMLNMTGSGYV
HHHHHHHHCCCCCEE		16.94UniProtKB CARBOHYD
245PhosphorylationLNMTGSGYVWLVGER
HHCCCCCEEEEEEEE		7.0825332170
276N-linked_GlycosylationLQLINGKNESAHISD
EEEECCCCCCCCHHH		50.26UniProtKB CARBOHYD
300N-linked_GlycosylationHELLEKENITDPPRG
HHHHHHCCCCCCCCC		54.23UniProtKB CARBOHYD
350N-linked_GlycosylationDGDRKFANYSIMNLQ
CCCCCEEEEEEEECC		33.93UniProtKB CARBOHYD
368N-linked_GlycosylationLVQVGIYNGTHVIPN
EEEEEEECCCEECCC		47.14UniProtKB CARBOHYD
440N-linked_GlycosylationKVICTGPNDTSPGSP
EEEECCCCCCCCCCC		67.54UniProtKB CARBOHYD
442PhosphorylationICTGPNDTSPGSPRH
EECCCCCCCCCCCCC		43.3830266825
443PhosphorylationCTGPNDTSPGSPRHT
ECCCCCCCCCCCCCC		30.0830266825
446PhosphorylationPNDTSPGSPRHTVPQ
CCCCCCCCCCCCCCC		23.3430266825
471N-linked_GlycosylationIKLARTMNFTYEVHL
HHHHHHCCCEEEEEE		26.04UniProtKB CARBOHYD
491N-linked_GlycosylationFGTQERVNNSNKKEW
CCCHHCCCCCCHHHH		53.05UniProtKB CARBOHYD
507PhosphorylationGMMGELLSGQADMIV
HHHHHHHHCCCCEEE		41.2924719451
665PhosphorylationDRPEERITGINDPRL
CCCHHHCCCCCCHHH		37.9322210691
674N-linked_GlycosylationINDPRLRNPSDKFIY
CCCHHHCCCCCCEEE		45.05-
683PhosphorylationSDKFIYATVKQSSVD
CCCEEEEEECHHHCE		15.9718452278
744S-nitrosocysteineEFEASQKCDLVTTGE
EEHHHCCCCEEEECC		3.66-
744S-nitrosylationEFEASQKCDLVTTGE
EEHHHCCCCEEEECC		3.669182795
771N-linked_GlycosylationKDSPWKQNVSLSILK
CCCCCCCCEEEEHHH		22.94-
775PhosphorylationWKQNVSLSILKSHEN
CCCCEEEEHHHHCCC		20.5424719451
798S-nitrosocysteineTWVRYQECDSRSNAP
HEEEHHHCCCCCCCC		3.21-
798S-nitrosylationTWVRYQECDSRSNAP
HEEEHHHCCCCCCCC		3.219182795
837PhosphorylationLIFIEIAYKRHKDAR
HHHHHHHHHHHHHHH		17.7621113815
867O-linked_GlycosylationKNLQDRKSGRAEPDP
HHHHHCCCCCCCCCH		34.1128657654
879PhosphorylationPDPKKKATFRAITST
CCHHHHHHHHHHHHH		23.6410049997
884PhosphorylationKATFRAITSTLASSF
HHHHHHHHHHHHHHH		18.0529759185
886PhosphorylationTFRAITSTLASSFKR
HHHHHHHHHHHHHCH		20.0729759185
889PhosphorylationAITSTLASSFKRRRS
HHHHHHHHHHCHHHC		39.158316301
890PhosphorylationITSTLASSFKRRRSS
HHHHHHHHHCHHHCC		29.2210049997
896PhosphorylationSSFKRRRSSKDTSTG
HHHCHHHCCCCCCCC		39.6710049997
897PhosphorylationSFKRRRSSKDTSTGG
HHCHHHCCCCCCCCC		32.519231706
897DephosphorylationSFKRRRSSKDTSTGG
HHCHHHCCCCCCCCC		32.5111588171
900PhosphorylationRRRSSKDTSTGGGRG
HHHCCCCCCCCCCCH		31.74-
901PhosphorylationRRSSKDTSTGGGRGA
HHCCCCCCCCCCCHH		34.8822210691
902PhosphorylationRSSKDTSTGGGRGAL
HCCCCCCCCCCCHHH		41.77-
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
837YPhosphorylationKinaseSRCP12931
PSP
889SPhosphorylationKinasePKC-FAMILY-GPS
889SPhosphorylationKinasePKC-Uniprot
889SPhosphorylationKinasePKC_GROUP-PhosphoELM
890SPhosphorylationKinaseNEK6Q9HC98
PSP
890SPhosphorylationKinasePKC-FAMILY-GPS
890SPhosphorylationKinasePKC-Uniprot
890SPhosphorylationKinasePKC_GROUP-PhosphoELM
896SPhosphorylationKinasePKC-FAMILY-GPS
896SPhosphorylationKinasePKC-Uniprot
896SPhosphorylationKinasePKC_GROUP-PhosphoELM
897SPhosphorylationKinasePKC-FAMILY-GPS
897SPhosphorylationKinasePKC-Uniprot
897SPhosphorylationKinasePKC_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseLNX1Q8TBB1
PMID:22889411
-KUbiquitinationE3 ubiquitin ligaseFBXO2Q9UK22
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
897SPhosphorylation

8316301
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 NMDZ1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMDE1_HUMANGRIN2Aphysical
12391275
NMDE2_HUMANGRIN2Bphysical
12391275
NMD3A_HUMANGRIN3Aphysical
12391275
SPTN1_HUMANSPTAN1physical
9670010
CALX_HUMANCANXphysical
14732708
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614254Mental retardation, autosomal dominant 8 (MRD8)
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 NMDZ1_HUMAN

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Related Literatures of Post-Translational Modification

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