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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Glutamate receptor ionotropic, NMDA 2A

UniprotKB/SwissProt ID: Q12879 (Q12879)

Gene Name: GRIN2A

Organism: Homo sapiens (Human)

Function: Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:20890276, PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:28242877, PubMed:36117210, PubMed:38538865, PubMed:8768735). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:27288002, PubMed:28095420, PubMed:28105280, PubMed:28126851, PubMed:28182669, PubMed:29644724, PubMed:38307912, PubMed:8768735). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:26919761). Participates in the synaptic plasticity regulation through activation by the L-glutamate releaseed by BEST1, into the synaptic cleft, upon F2R/PAR-1 activation in astrocyte (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell projection, dendritic spine. Cell membrane. Synapse. Postsynaptic cell membrane. Cytoplasmic vesicle membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_Glu_rcpt_met
IPR015683 Ionotropic_Glu_rcpt
IPR001320 Iontro_rcpt_C
IPR018884 NMDAR2_C
IPR028082 Peripla_BP_I

The S-nitrosylation sites of Q12879

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 320 FSYIPEAKAS C YGQMERPEVP  CCCCHHHHHH H HHHHHHHCCC  5.45% 22178444
17434127
17196530
12183209
2 399 VWPRYKSFSD C EPDDNHLSIV  CCCCHHHHHH H HHHHHHHCCC  8.72% 10571239
15688001
17434127
12183209
11092448
22178444
10607390
3 87 TDPKSLITHV C DLMSGARIHG  CCCCHHHHHH H HHHHHHHCCC  2.3% 22178444
17434127
17196530
12183209