NMDE3_HUMAN - dbPTM
NMDE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMDE3_HUMAN
UniProt AC Q14957
Protein Name Glutamate receptor ionotropic, NMDA 2C
Gene Name GRIN2C
Organism Homo sapiens (Human).
Sequence Length 1233
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: 26875626 Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable Plays a role in regulating the balance between excitatory and inhibitory activity of pyramidal neurons in the prefrontal cortex. Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity]
Protein Sequence MGGALGPALLLTSLFGAWAGLGPGQGEQGMTVAVVFSSSGPPQAQFRARLTPQSFLDLPLEIQPLTVGVNTTNPSSLLTQICGLLGAAHVHGIVFEDNVDTEAVAQILDFISSQTHVPILSISGGSAVVLTPKEPGSAFLQLGVSLEQQLQVLFKVLEEYDWSAFAVITSLHPGHALFLEGVRAVADASHVSWRLLDVVTLELGPGGPRARTQRLLRQLDAPVFVAYCSREEAEVLFAEAAQAGLVGPGHVWLVPNLALGSTDAPPATFPVGLISVVTESWRLSLRQKVRDGVAILALGAHSYWRQHGTLPAPAGDCRVHPGPVSPAREAFYRHLLNVTWEGRDFSFSPGGYLVQPTMVVIALNRHRLWEMVGRWEHGVLYMKYPVWPRYSASLQPVVDSRHLTVATLEERPFVIVESPDPGTGGCVPNTVPCRRQSNHTFSSGDVAPYTKLCCKGFCIDILKKLARVVKFSYDLYLVTNGKHGKRVRGVWNGMIGEVYYKRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAITVFMFEYFSPVSYNQNLTRGKKSGGPAFTIGKSVWLLWALVFNNSVPIENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEQYIDTVSGLSDKKFQRPQDQYPPFRFGTVPNGSTERNIRSNYRDMHTHMVKFNQRSVEDALTSLKMGKLDAFIYDAAVLNYMAGKDEGCKLVTIGSGKVFATTGYGIAMQKDSHWKRAIDLALLQFLGDGETQKLETVWLSGICQNEKNEVMSSKLDIDNMAGVFYMLLVAMGLALLVFAWEHLVYWKLRHSVPNSSQLDFLLAFSRGIYSCFSGVQSLASPPRQASPDLTASSAQASVLKMLQAARDMVTTAGVSSSLDRATRTIENWGGGRRAPPPSPCPTPRSGPSPCLPTPDPPPEPSPTGWGPPDGGRAALVRRAPQPPGRPPTPGPPLSDVSRVSRRPAWEARWPVRTGHCGRHLSASERPLSPARCHYSSFPRADRSGRPFLPLFPELEDLPLLGPEQLARREALLHAAWARGSRPRHASLPSSVAEAFARPSSLPAGCTGPACARPDGHSACRRLAQAQSMCLPIYREACQEGEQAGAPAWQHRQHVCLHAHAHLPFCWGAVCPHLPPCASHGSWLSGAWGPLGHRGRTLGLGTGYRDSGGLDEISRVARGTQGFPGPCTWRRISSLESEV
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
70N-linked_GlycosylationQPLTVGVNTTNPSSL
EEEEEECCCCCHHHH		34.94UniProtKB CARBOHYD
73N-linked_GlycosylationTVGVNTTNPSSLLTQ
EEECCCCCHHHHHHH		32.20-
212PhosphorylationPGGPRARTQRLLRQL
CCCHHHHHHHHHHHC		19.63-
227PhosphorylationDAPVFVAYCSREEAE
CCCEEEEEECHHHHH		5.90-
229PhosphorylationPVFVAYCSREEAEVL
CEEEEEECHHHHHHH		30.01-
284PhosphorylationVTESWRLSLRQKVRD
HCHHHHHHHHHHHHH		16.9723532336
337N-linked_GlycosylationAFYRHLLNVTWEGRD
HHHHHHHCCEECCCC		35.22UniProtKB CARBOHYD
337N-linked_GlycosylationAFYRHLLNVTWEGRD
HHHHHHHCCEECCCC		35.221350383
384PhosphorylationHGVLYMKYPVWPRYS
CCEEEEECCCCCCCC		6.1127642862
390PhosphorylationKYPVWPRYSASLQPV
ECCCCCCCCCCCCCC		12.4322817900
393PhosphorylationVWPRYSASLQPVVDS
CCCCCCCCCCCCCCC		22.92-
400PhosphorylationSLQPVVDSRHLTVAT
CCCCCCCCCCEEEEE		15.25-
438N-linked_GlycosylationVPCRRQSNHTFSSGD
CCCCCCCCCCCCCCC		29.85UniProtKB CARBOHYD
492N-linked_GlycosylationKRVRGVWNGMIGEVY
CEEECHHCCCCCEEE		27.961350383
492N-linked_GlycosylationKRVRGVWNGMIGEVY
CEEECHHCCCCCEEE		27.96-
513N-linked_GlycosylationAIGSLTINEERSEIV
EECEEEECCHHHHCC		39.581350383
513N-linked_GlycosylationAIGSLTINEERSEIV
EECEEEECCHHHHCC		39.58-
539N-linked_GlycosylationSVMVARSNGTVSPSA
EEEEEECCCCCCHHH		44.60UniProtKB CARBOHYD
551PhosphorylationPSAFLEPYSPAVWVM
HHHHCCCCCHHHHHH		20.22-
685N-linked_GlycosylationFRFGTVPNGSTERNI
CCCCCCCCCCCCCCH		53.35-
716PhosphorylationRSVEDALTSLKMGKL
HCHHHHHHHHHCCCC		33.46-
728PhosphorylationGKLDAFIYDAAVLNY
CCCCEEHHHHHHHHH		7.9624275569
735PhosphorylationYDAAVLNYMAGKDEG
HHHHHHHHHCCCCCC		5.56-
875PhosphorylationSGVQSLASPPRQASP
CCHHHHCCCCCCCCC		40.5026437602
881PhosphorylationASPPRQASPDLTASS
CCCCCCCCCCCCCCH		15.60-
885PhosphorylationRQASPDLTASSAQAS
CCCCCCCCCCHHHHH		31.6924114839
887PhosphorylationASPDLTASSAQASVL
CCCCCCCCHHHHHHH		22.4424114839
888PhosphorylationSPDLTASSAQASVLK
CCCCCCCHHHHHHHH		23.1824114839
912PhosphorylationTTAGVSSSLDRATRT
HHHCCCHHHHHHHCC		27.12-
917PhosphorylationSSSLDRATRTIENWG
CHHHHHHHCCCHHCC		29.2824719451
919PhosphorylationSLDRATRTIENWGGG
HHHHHHCCCHHCCCC		28.4324719451
1075PhosphorylationHAAWARGSRPRHASL
HHHHHCCCCCCCCCC		33.2922798277
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

Oops, there are no upstream regulatory protein records of NMDE3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMDE3_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 NMDE3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NMDE3_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00711 Ketamine hydrochloride (JP16/USP); Ketalar (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)
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
DB00659Acamprosate
DB00289Atomoxetine
DB00996Gabapentin
DB00145Glycine
DB06738Ketobemidone
DB04896Milnacipran
DB00312Pentobarbital
DB00454Pethidine
DB01174Phenobarbital
DB00418Secobarbital
Regulatory Network of NMDE3_HUMAN

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Related Literatures of Post-Translational Modification

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