NMDE3_HUMAN
ID NMDE3_HUMAN Reviewed; 1233 AA.
AC Q14957; B2RTT1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2C;
DE Short=GluN2C;
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-3;
DE AltName: Full=N-methyl D-aspartate receptor subtype 2C;
DE Short=NMDAR2C;
DE Short=NR2C;
DE Flags: Precursor;
GN Name=GRIN2C; Synonyms=NMDAR2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9037519; DOI=10.1016/s0169-328x(96)00146-5;
RA Lin Y.J., Bovetto S., Carver J.M., Giordano T.;
RT "Cloning of the cDNA for the human NMDA receptor NR2C subunit and its
RT expression in the central nervous system and periphery.";
RL Brain Res. Mol. Brain Res. 43:57-64(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH SNX27.
RX PubMed=21300787; DOI=10.1128/mcb.01044-10;
RA Cai L., Loo L.S., Atlashkin V., Hanson B.J., Hong W.;
RT "Deficiency of sorting nexin 27 (SNX27) leads to growth retardation and
RT elevated levels of N-methyl-D-aspartate receptor 2C (NR2C).";
RL Mol. Cell. Biol. 31:1734-1747(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26875626; DOI=10.1016/j.neuron.2016.01.016;
RA Hackos D.H., Lupardus P.J., Grand T., Chen Y., Wang T.M., Reynen P.,
RA Gustafson A., Wallweber H.J., Volgraf M., Sellers B.D., Schwarz J.B.,
RA Paoletti P., Sheng M., Zhou Q., Hanson J.E.;
RT "Positive Allosteric Modulators of GluN2A-Containing NMDARs with Distinct
RT Modes of Action and Impacts on Circuit Function.";
RL Neuron 89:983-999(2016).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF PRO-550.
RX PubMed=28095420; DOI=10.1371/journal.pgen.1006536;
RA Ogden K.K., Chen W., Swanger S.A., McDaniel M.J., Fan L.Z., Hu C.,
RA Tankovic A., Kusumoto H., Kosobucki G.J., Schulien A.J., Su Z., Pecha J.,
RA Bhattacharya S., Petrovski S., Cohen A.E., Aizenman E., Traynelis S.F.,
RA Yuan H.;
RT "Molecular mechanism of disease-associated mutations in the pre-M1 helix of
RT NMDA receptors and potential rescue pharmacology.";
RL PLoS Genet. 13:E1006536-E1006536(2017).
RN [7]
RP VARIANTS 18-TRP--VAL-1233 DEL; ILE-90; VAL-166; THR-573; THR-641; CYS-679;
RP THR-863; ARG-871; SER-877; ILE-911; ALA-982; PRO-989; LEU-995; TYR-1079;
RP ALA-1141; ARG-1180 AND ILE-1196.
RX PubMed=22833210; DOI=10.1038/tp.2011.52;
RG S2D team;
RA Tarabeux J., Kebir O., Gauthier J., Hamdan F.F., Xiong L., Piton A.,
RA Spiegelman D., Henrion E., Millet B., Fathalli F., Joober R.,
RA Rapoport J.L., DeLisi L.E., Fombonne E., Mottron L., Forget-Dubois N.,
RA Boivin M., Michaud J.L., Drapeau P., Lafreniere R.G., Rouleau G.A.,
RA Krebs M.O.;
RT "Rare mutations in N-methyl-D-aspartate glutamate receptors in autism
RT spectrum disorders and schizophrenia.";
RL Transl. Psychiatry 1:E55-E55(2011).
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+)
CC (PubMed:26875626). Sensitivity to glutamate and channel kinetics depend
CC on the subunit composition (Probable). Plays a role in regulating the
CC balance between excitatory and inhibitory activity of pyramidal neurons
CC in the prefrontal cortex. Contributes to the slow phase of excitatory
CC postsynaptic current, long-term synaptic potentiation, and learning (By
CC similarity). {ECO:0000250|UniProtKB:Q01098,
CC ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:28095420, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of
CC two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B,
CC GRIN2C or GRIN2D) (in vitro) (PubMed:26875626). In vivo, the subunit
CC composition may depend on the expression levels of the different
CC subunits (Probable). Interacts with PDZ domains of PATJ and DLG4 (By
CC similarity). Interacts (via PDZ-binding motif) with SNX27 (via PDZ
CC domain); the interaction is required for recycling to the plasma
CC membrane when endocytosed and prevent degradation in lysosomes
CC (PubMed:21300787). {ECO:0000250|UniProtKB:Q00961,
CC ECO:0000269|PubMed:21300787, ECO:0000269|PubMed:26875626, ECO:0000305}.
CC -!- INTERACTION:
CC Q14957; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-8285963, EBI-10173507;
CC Q14957; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-8285963, EBI-5280499;
CC Q14957; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-8285963, EBI-9089489;
CC Q14957; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-8285963, EBI-2548012;
CC Q14957; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-8285963, EBI-5666615;
CC Q14957; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-8285963, EBI-23662416;
CC Q14957; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-8285963, EBI-10693038;
CC Q14957; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-8285963, EBI-18036948;
CC Q14957; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-8285963, EBI-751596;
CC Q14957; Q5M9N0-2: CCDC158; NbExp=3; IntAct=EBI-8285963, EBI-21796846;
CC Q14957; P24941: CDK2; NbExp=3; IntAct=EBI-8285963, EBI-375096;
CC Q14957; O95674: CDS2; NbExp=3; IntAct=EBI-8285963, EBI-3913685;
CC Q14957; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-8285963, EBI-749253;
CC Q14957; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-8285963, EBI-744045;
CC Q14957; P02458-1: COL2A1; NbExp=3; IntAct=EBI-8285963, EBI-12375799;
CC Q14957; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-8285963, EBI-751783;
CC Q14957; Q6ZN54-2: DEF8; NbExp=3; IntAct=EBI-8285963, EBI-12346463;
CC Q14957; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-8285963, EBI-25842538;
CC Q14957; Q12959: DLG1; NbExp=2; IntAct=EBI-8285963, EBI-357481;
CC Q14957; P78352: DLG4; NbExp=4; IntAct=EBI-8285963, EBI-80389;
CC Q14957; Q7Z7J5: DPPA2; NbExp=3; IntAct=EBI-8285963, EBI-741400;
CC Q14957; Q14117: DPYS; NbExp=3; IntAct=EBI-8285963, EBI-12275416;
CC Q14957; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-8285963, EBI-724653;
CC Q14957; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-8285963, EBI-3443946;
CC Q14957; A0AVK6: E2F8; NbExp=3; IntAct=EBI-8285963, EBI-7779316;
CC Q14957; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-8285963, EBI-10248874;
CC Q14957; O00472: ELL2; NbExp=3; IntAct=EBI-8285963, EBI-395274;
CC Q14957; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-8285963, EBI-11793142;
CC Q14957; P15407: FOSL1; NbExp=3; IntAct=EBI-8285963, EBI-744510;
CC Q14957; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-8285963, EBI-618189;
CC Q14957; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-8285963, EBI-12143817;
CC Q14957; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-8285963, EBI-2514791;
CC Q14957; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-8285963, EBI-2558143;
CC Q14957; Q5T447-2: HECTD3; NbExp=3; IntAct=EBI-8285963, EBI-25854793;
CC Q14957; P10809: HSPD1; NbExp=3; IntAct=EBI-8285963, EBI-352528;
CC Q14957; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-8285963, EBI-12141931;
CC Q14957; Q9NZH6: IL37; NbExp=3; IntAct=EBI-8285963, EBI-3862125;
CC Q14957; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-8285963, EBI-9089060;
CC Q14957; A0A0C4DGV4: LAMTOR5; NbExp=3; IntAct=EBI-8285963, EBI-10173304;
CC Q14957; Q14847-2: LASP1; NbExp=3; IntAct=EBI-8285963, EBI-9088686;
CC Q14957; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-8285963, EBI-25835523;
CC Q14957; Q68G74: LHX8; NbExp=3; IntAct=EBI-8285963, EBI-8474075;
CC Q14957; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-8285963, EBI-10264791;
CC Q14957; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-8285963, EBI-2510853;
CC Q14957; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-8285963, EBI-749562;
CC Q14957; Q96LR2: LURAP1; NbExp=3; IntAct=EBI-8285963, EBI-741355;
CC Q14957; D3DX41: MGC16703; NbExp=3; IntAct=EBI-8285963, EBI-25850974;
CC Q14957; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-8285963, EBI-25835557;
CC Q14957; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-8285963, EBI-25835707;
CC Q14957; Q96H12: MSANTD3; NbExp=3; IntAct=EBI-8285963, EBI-8466227;
CC Q14957; Q9NPC6: MYOZ2; NbExp=3; IntAct=EBI-8285963, EBI-746712;
CC Q14957; P41271-2: NBL1; NbExp=3; IntAct=EBI-8285963, EBI-12135485;
CC Q14957; Q99743: NPAS2; NbExp=3; IntAct=EBI-8285963, EBI-3932727;
CC Q14957; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-8285963, EBI-2802743;
CC Q14957; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-8285963, EBI-9090919;
CC Q14957; O43482: OIP5; NbExp=3; IntAct=EBI-8285963, EBI-536879;
CC Q14957; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-8285963, EBI-25830200;
CC Q14957; Q495U3: PANX2; NbExp=3; IntAct=EBI-8285963, EBI-17242559;
CC Q14957; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-8285963, EBI-17159452;
CC Q14957; O15534: PER1; NbExp=3; IntAct=EBI-8285963, EBI-2557276;
CC Q14957; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-8285963, EBI-12891828;
CC Q14957; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-8285963, EBI-26412802;
CC Q14957; P19388: POLR2E; NbExp=3; IntAct=EBI-8285963, EBI-395189;
CC Q14957; Q07869: PPARA; NbExp=3; IntAct=EBI-8285963, EBI-78615;
CC Q14957; O60237-2: PPP1R12B; NbExp=3; IntAct=EBI-8285963, EBI-10700351;
CC Q14957; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-8285963, EBI-25835994;
CC Q14957; O43741: PRKAB2; NbExp=3; IntAct=EBI-8285963, EBI-1053424;
CC Q14957; P62333: PSMC6; NbExp=3; IntAct=EBI-8285963, EBI-357669;
CC Q14957; Q06323: PSME1; NbExp=3; IntAct=EBI-8285963, EBI-712149;
CC Q14957; P06454-2: PTMA; NbExp=3; IntAct=EBI-8285963, EBI-10194874;
CC Q14957; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-8285963, EBI-25835884;
CC Q14957; P47804-3: RGR; NbExp=3; IntAct=EBI-8285963, EBI-25834767;
CC Q14957; Q15382: RHEB; NbExp=3; IntAct=EBI-8285963, EBI-1055287;
CC Q14957; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-8285963, EBI-749039;
CC Q14957; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-8285963, EBI-751555;
CC Q14957; P62701: RPS4X; NbExp=3; IntAct=EBI-8285963, EBI-354303;
CC Q14957; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-8285963, EBI-9089805;
CC Q14957; O60902-3: SHOX2; NbExp=3; IntAct=EBI-8285963, EBI-9092164;
CC Q14957; Q13573: SNW1; NbExp=3; IntAct=EBI-8285963, EBI-632715;
CC Q14957; Q496A3: SPATS1; NbExp=3; IntAct=EBI-8285963, EBI-3923692;
CC Q14957; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-8285963, EBI-12408727;
CC Q14957; Q13586: STIM1; NbExp=3; IntAct=EBI-8285963, EBI-448878;
CC Q14957; O15273: TCAP; NbExp=3; IntAct=EBI-8285963, EBI-954089;
CC Q14957; Q86WV5: TEN1; NbExp=3; IntAct=EBI-8285963, EBI-2562799;
CC Q14957; P54274-2: TERF1; NbExp=3; IntAct=EBI-8285963, EBI-711018;
CC Q14957; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-8285963, EBI-12090309;
CC Q14957; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-8285963, EBI-12833746;
CC Q14957; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-8285963, EBI-17438286;
CC Q14957; O60830: TIMM17B; NbExp=3; IntAct=EBI-8285963, EBI-2372529;
CC Q14957; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-8285963, EBI-25830583;
CC Q14957; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-8285963, EBI-9089156;
CC Q14957; P36406: TRIM23; NbExp=3; IntAct=EBI-8285963, EBI-740098;
CC Q14957; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-8285963, EBI-17716262;
CC Q14957; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-8285963, EBI-8656864;
CC Q14957; P49459: UBE2A; NbExp=3; IntAct=EBI-8285963, EBI-2339348;
CC Q14957; Q13404: UBE2V1; NbExp=3; IntAct=EBI-8285963, EBI-1050671;
CC Q14957; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-8285963, EBI-25835297;
CC Q14957; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-8285963, EBI-10316321;
CC Q14957; O43829: ZBTB14; NbExp=3; IntAct=EBI-8285963, EBI-10176632;
CC Q14957; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-8285963, EBI-14104088;
CC Q14957; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-8285963, EBI-746345;
CC Q14957; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-8285963, EBI-25835852;
CC Q14957; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-8285963, EBI-18036029;
CC Q14957; B7Z3E8; NbExp=3; IntAct=EBI-8285963, EBI-25831617;
CC Q14957; Q62936: Dlg3; Xeno; NbExp=6; IntAct=EBI-8285963, EBI-349596;
CC Q14957; P31016: Dlg4; Xeno; NbExp=2; IntAct=EBI-8285963, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626};
CC Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane;
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain with predominant
CC expression is in the cerebellum, also present in the hippocampus,
CC amygdala, caudate nucleus, corpus callosum, subthalamic nuclei and
CC thalamus. Detected in the heart, skeletal muscle and pancreas.
CC {ECO:0000269|PubMed:9037519}.
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000250|UniProtKB:Q00960}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2C/GRIN2C subfamily. {ECO:0000305}.
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DR EMBL; L76224; AAA88096.1; -; mRNA.
DR EMBL; AC068874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140801; AAI40802.1; -; mRNA.
DR CCDS; CCDS32724.1; -.
DR RefSeq; NP_000826.2; NM_000835.4.
DR AlphaFoldDB; Q14957; -.
DR SMR; Q14957; -.
DR BioGRID; 109162; 13.
DR ComplexPortal; CPX-286; NMDA receptor complex, GluN1-GluN2C.
DR IntAct; Q14957; 108.
DR MINT; Q14957; -.
DR STRING; 9606.ENSP00000293190; -.
DR BindingDB; Q14957; -.
DR ChEMBL; CHEMBL4109; -.
DR DrugBank; DB00659; Acamprosate.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB00843; Donepezil.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB11823; Esketamine.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB06741; Gavestinel.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00874; Guaifenesin.
DR DrugBank; DB06738; Ketobemidone.
DR DrugBank; DB09409; Magnesium acetate tetrahydrate.
DR DrugBank; DB09481; Magnesium carbonate.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB04896; Milnacipran.
DR DrugBank; DB00312; Pentobarbital.
DR DrugBank; DB01174; Phenobarbital.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB00418; Secobarbital.
DR DrugBank; DB01520; Tenocyclidine.
DR DrugBank; DB00193; Tramadol.
DR DrugCentral; Q14957; -.
DR GuidetoPHARMACOLOGY; 458; -.
DR TCDB; 1.A.10.1.3; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q14957; 6 sites.
DR iPTMnet; Q14957; -.
DR PhosphoSitePlus; Q14957; -.
DR BioMuta; GRIN2C; -.
DR DMDM; 313104210; -.
DR jPOST; Q14957; -.
DR MassIVE; Q14957; -.
DR PaxDb; Q14957; -.
DR PeptideAtlas; Q14957; -.
DR PRIDE; Q14957; -.
DR ProteomicsDB; 60260; -.
DR ABCD; Q14957; 3 sequenced antibodies.
DR Antibodypedia; 19474; 286 antibodies from 35 providers.
DR DNASU; 2905; -.
DR Ensembl; ENST00000293190.10; ENSP00000293190.5; ENSG00000161509.14.
DR GeneID; 2905; -.
DR KEGG; hsa:2905; -.
DR MANE-Select; ENST00000293190.10; ENSP00000293190.5; NM_000835.6; NP_000826.2.
DR UCSC; uc002jlt.3; human.
DR CTD; 2905; -.
DR DisGeNET; 2905; -.
DR GeneCards; GRIN2C; -.
DR HGNC; HGNC:4587; GRIN2C.
DR HPA; ENSG00000161509; Tissue enhanced (brain, thyroid gland).
DR MIM; 138254; gene.
DR neXtProt; NX_Q14957; -.
DR OpenTargets; ENSG00000161509; -.
DR PharmGKB; PA28981; -.
DR VEuPathDB; HostDB:ENSG00000161509; -.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000156964; -.
DR HOGENOM; CLU_002039_1_0_1; -.
DR InParanoid; Q14957; -.
DR OMA; VENQARH; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q14957; -.
DR TreeFam; TF314731; -.
DR PathwayCommons; Q14957; -.
DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; Q14957; -.
DR SIGNOR; Q14957; -.
DR BioGRID-ORCS; 2905; 10 hits in 1071 CRISPR screens.
DR GeneWiki; GRIN2C; -.
DR GenomeRNAi; 2905; -.
DR Pharos; Q14957; Tclin.
DR PRO; PR:Q14957; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14957; protein.
DR Bgee; ENSG00000161509; Expressed in right hemisphere of cerebellum and 104 other tissues.
DR ExpressionAtlas; Q14957; baseline and differential.
DR Genevisible; Q14957; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IC:ComplexPortal.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; NAS:ARUK-UCL.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IDA:UniProtKB.
DR GO; GO:0098655; P:cation transmembrane transport; IC:ComplexPortal.
DR GO; GO:0033058; P:directional locomotion; IEA:Ensembl.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; NAS:ARUK-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IC:ComplexPortal.
DR GO; GO:0048167; P:regulation of synaptic plasticity; NAS:ARUK-UCL.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR Pfam; PF10565; NMDAR2_C; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1233
FT /note="Glutamate receptor ionotropic, NMDA 2C"
FT /id="PRO_0000011580"
FT TOPO_DOM 20..554
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 555..573
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 574..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT INTRAMEM 601..620
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 621..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 628..643
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 644..814
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 815..834
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 835..1233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT REGION 601..620
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT REGION 920..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1231..1233
FT /note="PDZ-binding"
FT COMPBIAS 929..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..511
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 511
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 516
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 687..688
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 729
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT SITE 612
FT /note="Functional determinant of NMDA receptors"
FT /evidence="ECO:0000250"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01098"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01098"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00961"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..317
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 426..453
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 433..454
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 743..798
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT VARIANT 18..1233
FT /note="Missing (found in a patient with autism spectrum
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079958"
FT VARIANT 90
FT /note="V -> I (in dbSNP:rs192960268)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079959"
FT VARIANT 166
FT /note="A -> V (in dbSNP:rs201199917)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079960"
FT VARIANT 573
FT /note="M -> T"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079961"
FT VARIANT 641
FT /note="A -> T (in dbSNP:rs746610735)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079962"
FT VARIANT 679
FT /note="R -> C (found in a patient with schizophrenia;
FT unknown pathological significance; dbSNP:rs1381530257)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079963"
FT VARIANT 863
FT /note="I -> T (found in a patient with autism spectrum
FT disorder; unknown pathological significance;
FT dbSNP:rs1308468356)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079964"
FT VARIANT 871
FT /note="Q -> R (in dbSNP:rs765016248)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079965"
FT VARIANT 877
FT /note="P -> S (in dbSNP:rs139011774)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079966"
FT VARIANT 911
FT /note="S -> I (in dbSNP:rs370546831)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079967"
FT VARIANT 982
FT /note="P -> A (in dbSNP:rs960726960)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079968"
FT VARIANT 989
FT /note="S -> P (found in a patient with schizophrenia;
FT unknown pathological significance; dbSNP:rs552196496)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079969"
FT VARIANT 995
FT /note="S -> L (found in a patient with schizophrenia;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079970"
FT VARIANT 1079
FT /note="H -> Y (in dbSNP:rs889196426)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079971"
FT VARIANT 1141
FT /note="P -> A (in dbSNP:rs751640851)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079972"
FT VARIANT 1180
FT /note="G -> R (in dbSNP:rs115230539)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079973"
FT VARIANT 1196
FT /note="T -> I (in dbSNP:rs143282101)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079974"
FT VARIANT 1209
FT /note="R -> S (in dbSNP:rs3744215)"
FT /id="VAR_037634"
FT MUTAGEN 550
FT /note="P->R: Changed glutamate-gated calcium ion channel
FT activity characterized by increased glutamate and glycine
FT potency."
FT /evidence="ECO:0000269|PubMed:28095420"
FT CONFLICT 1048
FT /note="E -> EPPE (in Ref. 3; AAI40802)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="P -> K (in Ref. 1; AAA88096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1233 AA; 134209 MW; 7B1F2F7995C0D689 CRC64;
MGGALGPALL LTSLFGAWAG LGPGQGEQGM TVAVVFSSSG PPQAQFRARL TPQSFLDLPL
EIQPLTVGVN TTNPSSLLTQ ICGLLGAAHV HGIVFEDNVD TEAVAQILDF ISSQTHVPIL
SISGGSAVVL TPKEPGSAFL QLGVSLEQQL QVLFKVLEEY DWSAFAVITS LHPGHALFLE
GVRAVADASH VSWRLLDVVT LELGPGGPRA RTQRLLRQLD APVFVAYCSR EEAEVLFAEA
AQAGLVGPGH VWLVPNLALG STDAPPATFP VGLISVVTES WRLSLRQKVR DGVAILALGA
HSYWRQHGTL PAPAGDCRVH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG GYLVQPTMVV
IALNRHRLWE MVGRWEHGVL YMKYPVWPRY SASLQPVVDS RHLTVATLEE RPFVIVESPD
PGTGGCVPNT VPCRRQSNHT FSSGDVAPYT KLCCKGFCID ILKKLARVVK FSYDLYLVTN
GKHGKRVRGV WNGMIGEVYY KRADMAIGSL TINEERSEIV DFSVPFVETG ISVMVARSNG
TVSPSAFLEP YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTRGK KSGGPAFTIG
KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF MIQEQYIDTV
SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH THMVKFNQRS VEDALTSLKM
GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IAMQKDSHWK RAIDLALLQF
LGDGETQKLE TVWLSGICQN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY
WKLRHSVPNS SQLDFLLAFS RGIYSCFSGV QSLASPPRQA SPDLTASSAQ ASVLKMLQAA
RDMVTTAGVS SSLDRATRTI ENWGGGRRAP PPSPCPTPRS GPSPCLPTPD PPPEPSPTGW
GPPDGGRAAL VRRAPQPPGR PPTPGPPLSD VSRVSRRPAW EARWPVRTGH CGRHLSASER
PLSPARCHYS SFPRADRSGR PFLPLFPELE DLPLLGPEQL ARREALLHAA WARGSRPRHA
SLPSSVAEAF ARPSSLPAGC TGPACARPDG HSACRRLAQA QSMCLPIYRE ACQEGEQAGA
PAWQHRQHVC LHAHAHLPFC WGAVCPHLPP CASHGSWLSG AWGPLGHRGR TLGLGTGYRD
SGGLDEISRV ARGTQGFPGP CTWRRISSLE SEV
