GRIN1

Protein-coding gene in the species Homo sapiens

GRIN1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2HQW, 2NR1, 3BYA, 5H8N, 5H8H, 5H8Q, 5H8F, 5I2N, 5I2K, 5KCJ, 5KDT

Identifiers

Aliases

GRIN1, GluN1, MRD8, NMDA1, NMDAR1, NR1, NMD-R1, glutamate ionotropic receptor NMDA type subunit 1, NDHMSR, NDHMSD, DEE101

External IDs

OMIM: 138249 MGI: 95819 HomoloGene: 7187 GeneCards: GRIN1

Gene location (Human)

Chr.	Chromosome 9 (human)^[1]

Band	9q34.3	Start	137,139,154 bp^[1]
Band	9q34.3	End	137,168,756 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2 A3\|2 17.14 cM	Start	25,181,193 bp^[2]
Band	2 A3\|2 17.14 cM	End	25,209,199 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

nucleus accumbens

prefrontal cortex

Brodmann area 9

putamen

amygdala

caudate nucleus

Brodmann area 10

frontal pole

middle frontal gyrus

hypothalamus

Top expressed in

entorhinal cortex

superior frontal gyrus

cerebellar cortex

superior colliculus

primary motor cortex

subiculum

prefrontal cortex

hippocampus proper

inferior colliculus

nucleus accumbens

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	calcium ion binding signaling receptor binding glycine binding calmodulin binding protein binding cation channel activity extracellularly glutamate-gated ion channel activity glutamate binding calcium channel activity NMDA glutamate receptor activity ion channel activity ionotropic glutamate receptor activity neurotransmitter binding transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential amyloid-beta binding glutamate-gated calcium ion channel activity signaling receptor activity protein-containing complex binding
Cellular component	cytoplasm postsynaptic membrane membrane synapse NMDA selective glutamate receptor complex neuron projection synaptic vesicle dendritic spine cell surface endoplasmic reticulum integral component of membrane plasma membrane postsynaptic density integral component of plasma membrane excitatory synapse cell junction dendrite synaptic cleft terminal bouton postsynaptic density membrane synaptic membrane glutamatergic synapse integral component of postsynaptic density membrane
Biological process	negative regulation of neuron apoptotic process pons maturation synaptic transmission, glutamatergic regulation of respiratory gaseous exchange response to amphetamine regulation of membrane potential regulation of synapse assembly learning positive regulation of excitatory postsynaptic potential response to ethanol calcium ion transport suckling behavior prepulse inhibition male mating behavior regulation of long-term neuronal synaptic plasticity adult locomotory behavior regulation of neuron apoptotic process ion transport memory regulation of axonogenesis neuromuscular process ionotropic glutamate receptor signaling pathway excitatory postsynaptic potential learning or memory social behavior regulation of neuronal synaptic plasticity associative learning startle response calcium ion homeostasis cation transport cellular calcium ion homeostasis cation transmembrane transport respiratory gaseous exchange by respiratory system regulation of synaptic plasticity response to morphine propylene metabolic process conditioned taste aversion cerebral cortex development transport sensory perception of pain olfactory learning regulation of cell communication visual learning ephrin receptor signaling pathway MAPK cascade regulation of dendrite morphogenesis ion transmembrane transport long-term memory positive regulation of apoptotic process positive regulation of transcription by RNA polymerase II positive regulation of GTPase activity calcium ion transmembrane transport regulation of ion transmembrane transport brain development positive regulation of calcium ion transport into cytosol calcium-mediated signaling protein heterotetramerization calcium ion transmembrane import into cytosol excitatory chemical synaptic transmission positive regulation of reactive oxygen species biosynthetic process protein localization to postsynaptic membrane cellular response to amyloid-beta response to glycine positive regulation of cysteine-type endopeptidase activity regulation of NMDA receptor activity
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2902


14810

Ensembl


ENSG00000176884


ENSMUSG00000026959

UniProt


Q05586


P35438

RefSeq (mRNA)


NM_000832 NM_001185090 NM_001185091 NM_007327 NM_021569

NM_001177656 NM_001177657 NM_008169 NM_001372558 NM_001372559
NM_001372560 NM_001372561 NM_001372562

RefSeq (protein)


NP_000823 NP_001172019 NP_001172020 NP_015566 NP_067544

NP_001171127 NP_001171128 NP_032195 NP_001359487 NP_001359488
NP_001359489 NP_001359490 NP_001359491

Location (UCSC)

Chr 9: 137.14 – 137.17 Mb

Chr 2: 25.18 – 25.21 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Glutamate [NMDA] receptor subunit zeta-1 is a protein that in humans is encoded by the GRIN1 gene.^[5]^[6]

The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. The gene consists of 21 exons and is alternatively spliced, producing transcript variants differing in the C-terminus. The sequence of exon 5 is identical in vertebrates, with exon 5 splicing demonstrated in human, mouse and rat.^[7]^[8]^[9]^[10] Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000176884 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026959 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Monyer H, Sprengel R, Schoepfer R, Herb A, Higuchi M, Lomeli H, et al. (May 1992). "Heteromeric NMDA receptors: molecular and functional distinction of subtypes". Science. 256 (5060): 1217–1221. Bibcode:1992Sci...256.1217M. doi:10.1126/science.256.5060.1217. PMID 1350383. S2CID 989677.
^ ^a ^b "Entrez Gene: GRIN1 glutamate receptor, ionotropic, N-methyl D-aspartate 1".
^ Sengar AS, Li H, Zhang W, Leung C, Ramani AK, Saw NM, et al. (December 2019). "Control of Long-Term Synaptic Potentiation and Learning by Alternative Splicing of the NMDA Receptor Subunit GluN1". Cell Reports. 29 (13): 4285–4294.e5. doi:10.1016/j.celrep.2019.11.087. PMID 31875540. S2CID 209482250.
^ Liu H, Wang H, Peterson M, Zhang W, Hou G, Zhang ZW (October 2019). "N-terminal alternative splicing of GluN1 regulates the maturation of excitatory synapses and seizure susceptibility". Proceedings of the National Academy of Sciences of the United States of America. 116 (42): 21207–21212. Bibcode:2019PNAS..11621207L. doi:10.1073/pnas.1905721116. PMC 6800312. PMID 31570583.
^ Herbrechter R, Hube N, Buchholz R, Reiner A (July 2021). "Splicing and editing of ionotropic glutamate receptors: a comprehensive analysis based on human RNA-Seq data". Cellular and Molecular Life Sciences. 78 (14): 5605–5630. doi:10.1007/s00018-021-03865-z. PMC 8257547. PMID 34100982.
^ Manta G, Spathis AD, Taraviras S, Kouvelas ED, Mitsacos A (August 2011). "Age and visual experience-dependent expression of NMDAR1 splice variants in rat retina". Neurochemical Research. 36 (8): 1417–1425. doi:10.1007/s11064-011-0467-5. PMID 21499738. S2CID 11853676.

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Adriani W, Felici A, Sargolini F, Roullet P, Usiello A, Oliverio A, Mele A (November 1998). "N-methyl-D-aspartate and dopamine receptor involvement in the modulation of locomotor activity and memory processes". Experimental Brain Research. 123 (1–2): 52–59. doi:10.1007/s002210050544. PMID 9835392. S2CID 8388670.
Dingledine R, Borges K, Bowie D, Traynelis SF (March 1999). "The glutamate receptor ion channels". Pharmacological Reviews. 51 (1): 7–61. PMID 10049997.
King JE, Eugenin EA, Buckner CM, Berman JW (April 2006). "HIV tat and neurotoxicity". Microbes and Infection. 8 (5): 1347–1357. doi:10.1016/j.micinf.2005.11.014. PMID 16697675.
Zimmer M, Fink TM, Franke Y, Lichter P, Spiess J (July 1995). "Cloning and structure of the gene encoding the human N-methyl-D-aspartate receptor (NMDAR1)". Gene. 159 (2): 219–223. doi:10.1016/0378-1119(95)00044-7. PMID 7622053.
Karp SJ, Masu M, Eki T, Ozawa K, Nakanishi S (February 1993). "Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor". The Journal of Biological Chemistry. 268 (5): 3728–3733. doi:10.1016/S0021-9258(18)53754-6. PMID 7679115.
Younkin DP, Tang CM, Hardy M, Reddy UR, Shi QY, Pleasure SJ, et al. (March 1993). "Inducible expression of neuronal glutamate receptor channels in the NT2 human cell line". Proceedings of the National Academy of Sciences of the United States of America. 90 (6): 2174–2178. Bibcode:1993PNAS...90.2174Y. doi:10.1073/pnas.90.6.2174. PMC 46048. PMID 7681588.
Planells-Cases R, Sun W, Ferrer-Montiel AV, Montal M (June 1993). "Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain". Proceedings of the National Academy of Sciences of the United States of America. 90 (11): 5057–5061. Bibcode:1993PNAS...90.5057P. doi:10.1073/pnas.90.11.5057. PMC 46653. PMID 7685113.
Magnuson DS, Knudsen BE, Geiger JD, Brownstone RM, Nath A (March 1995). "Human immunodeficiency virus type 1 tat activates non-N-methyl-D-aspartate excitatory amino acid receptors and causes neurotoxicity". Annals of Neurology. 37 (3): 373–380. doi:10.1002/ana.410370314. PMID 7695237. S2CID 24405132.
Foldes RL, Rampersad V, Kamboj RK (September 1994). "Cloning and sequence analysis of additional splice variants encoding human N-methyl-D-aspartate receptor (hNR1) subunits". Gene. 147 (2): 303–304. doi:10.1016/0378-1119(94)90089-2. PMID 7926821.
Sheng M, Cummings J, Roldan LA, Jan YN, Jan LY (March 1994). "Changing subunit composition of heteromeric NMDA receptors during development of rat cortex". Nature. 368 (6467): 144–147. Bibcode:1994Natur.368..144S. doi:10.1038/368144a0. PMID 8139656. S2CID 4332025.
Tingley WG, Roche KW, Thompson AK, Huganir RL (July 1993). "Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain". Nature. 364 (6432): 70–73. Bibcode:1993Natur.364...70T. doi:10.1038/364070a0. PMID 8316301. S2CID 4322831.
Foldes RL, Rampersad V, Kamboj RK (September 1993). "Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing". Gene. 131 (2): 293–298. doi:10.1016/0378-1119(93)90309-Q. PMID 8406025.
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Lannuzel A, Lledo PM, Lamghitnia HO, Vincent JD, Tardieu M (November 1995). "HIV-1 envelope proteins gp120 and gp160 potentiate NMDA-induced [Ca2+]i increase, alter [Ca2+]i homeostasis and induce neurotoxicity in human embryonic neurons". The European Journal of Neuroscience. 7 (11): 2285–2293. doi:10.1111/j.1460-9568.1995.tb00649.x. PMID 8563977. S2CID 27201873.
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Ion channel, cell surface receptor: ligand-gated ion channels

Cys-loop receptors

5-HT/serotonin	5-HT₃ A B C D E
GABA	GABA_A α₁ α₂ α₃ α₄ α₅ α₆ β₁ β₂ β₃ γ₁ γ₂ γ₃ δ ε π θ GABA_A-ρ ρ₁ ρ₂ ρ₃
Glycine	α₁ α₂ α₃ α₄ β
Nicotinic acetylcholine	monomers: α1 α2 α3 α4 α5 α6 α7 α9 α10 β1 β2 β3 β4 δ ε pentamers: (α3)₂(β4)₃ (α4)₂(β2)₃ (α7)₅ (α1)₂(β4)₃ - Ganglion type (α1)₂β1δε - Muscle type
Zinc	Zinc-activated

Ionotropic glutamates

Ligand-gated only	AMPA (1 2 3 4) Kainate 1 2 3 4 5
Voltage- and ligand-gated	NMDA 1 2A 2B 2C 2D 3A 3B L1A L1B
‘Orphan’	GluD δ₁ δ₂