Q12879 (NMDE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor ionotropic, NMDA 2A
Short name=GluN2A

Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name=NMDAR2A
Short name=NR2A
Short name=hNR2A

Gene names

Name:	GRIN2A
Synonyms:	NMDAR2A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits.
Subunit structure	Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of AIP1, INADL and DLG4. Interacts with HIP1 and NETO1 By similarity. Interacts with LRFN2 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein.
Involvement in disease	Epilepsy with neurodevelopmental defects (EPND) [MIM:613971]: A neurologic disorder of variable severity characterized by epilepsy and neurodevelopmental defects, manifested as mental retardation, learning difficulties and behavioral problems. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 A chromosomal aberration involving GRIN2A has been found in a family with epilepsy and neurodevelopmental defects. Translocation t(16;17)(p13.2;q11.2). GRIN2A somatic mutations have been frequently found in cutaneous malignant melanoma, suggesting that the glutamate signaling pathway may play a role in the pathogenesis of melanoma (Ref.6).
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2A/GRIN2A subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Epilepsy
Domain	Signal Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding Zinc
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	directional locomotion Inferred from electronic annotation. Source: Compara dopamine metabolic process Inferred from electronic annotation. Source: Compara learning or memory Traceable author statement PubMed 7816096. Source: ProtInc memory Inferred from electronic annotation. Source: Compara negative regulation of protein catabolic process Inferred from electronic annotation. Source: Compara neurogenesis Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara protein localization Inferred from electronic annotation. Source: Compara regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara regulation of sensory perception of pain Inferred from electronic annotation. Source: Compara regulation of synaptic plasticity Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from direct assay PubMed 18445116. Source: UniProtKB response to wounding Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara serotonin metabolic process Inferred from electronic annotation. Source: Compara sleep Inferred from electronic annotation. Source: Compara startle response Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement. Source: Reactome visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	N-methyl-D-aspartate selective glutamate receptor complex Inferred from direct assay PubMed 10480938. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from sequence or structural similarity. Source: BHF-UCL outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro postsynaptic density Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell presynaptic membrane Inferred from electronic annotation. Source: Compara
Molecular_function	N-methyl-D-aspartate selective glutamate receptor activity Traceable author statement Ref.2. Source: ProtInc calcium channel activity Inferred from electronic annotation. Source: Compara extracellular-glutamate-gated ion channel activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12879-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q12879-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1464: NPATGEQVYQ...KKMPSIESDV → MTNAWLLGDAPRTLTNTRCHPRR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 1464

1442

Glutamate receptor ionotropic, NMDA 2A

PRO_0000011573

Regions

Topological domain

23 – 555

533

Extracellular Potential

Transmembrane

556 – 576

21

Helical; Potential

Topological domain

577 – 633

57

Cytoplasmic Potential

Transmembrane

634 – 654

21

Helical; Potential

Topological domain

655 – 816

162

Extracellular Potential

Transmembrane

817 – 837

21

Helical; Potential

Topological domain

838 – 1464

627

Cytoplasmic Potential

Region

511 – 513

3

Glutamate binding By similarity

Region

689 – 690

2

Glutamate binding By similarity

Motif

1462 – 1464

3

PDZ-binding By similarity

Sites

Metal binding

128

1

Zinc By similarity

Metal binding

283

1

Zinc By similarity

Binding site

518

1

Glutamate By similarity

Binding site

731

1

Glutamate; via amide nitrogen By similarity

Site

614

1

Functional determinant of NMDA receptors By similarity

Amino acid modifications

Modified residue

888

1

Phosphothreonine By similarity

Modified residue

917

1

Phosphoserine By similarity

Modified residue

929

1

Phosphoserine By similarity

Modified residue

943

1

Phosphotyrosine By similarity

Modified residue

1025

1

Phosphoserine By similarity

Modified residue

1459

1

Phosphoserine By similarity

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

340

1

N-linked (GlcNAc...) Potential

Glycosylation

380

1

N-linked (GlcNAc...) Potential

Glycosylation

443

1

N-linked (GlcNAc...) Potential

Glycosylation

444

1

N-linked (GlcNAc...) Potential

Glycosylation

541

1

N-linked (GlcNAc...) Potential

Disulfide bond

87 ↔ 320

By similarity

Natural variations

Alternative sequence

1259 – 1464

206

NPATG…IESDV → MTNAWLLGDAPRTLTNTRCH PRR in isoform 2.

VSP_044300

Natural variant

57

1

P → L Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067725

Natural variant

183

1

F → I Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067726

Natural variant

252

1

D → N Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067727

Natural variant

270

1

K → E. Ref.1

VAR_010938

Natural variant

278

1

S → F Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067728

Natural variant

371

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067729

Natural variant

373

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067730

Natural variant

449

1

G → E Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067731

Natural variant

459

1

F → S Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067732

Natural variant

595

1

H → R Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067733

Natural variant

598

1

S → F Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067734

Natural variant

615

1

N → K in EPND; the mutant receptor has decreased calcium permeability; shows a dominant-negative effect. Ref.5

VAR_065899

Natural variant

653

1

M → I Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067735

Natural variant

712

1

G → E Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067736

Natural variant

740

1

G → W Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067737

Natural variant

889

1

G → E Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067738

Natural variant

920

1

R → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067739

Natural variant

929

1

S → F Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067740

Natural variant

962

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067741

Natural variant

1073

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067742

Natural variant

1074

1

P → L Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067743

Natural variant

1153

1

D → N Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067744

Natural variant

1175

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067745

Natural variant

1276

1

A → G Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067746

Natural variant

1285

1

R → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067747

Natural variant

1318

1

R → W Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067748

Natural variant

1366

1

P → L Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067749

Natural variant

1421

1

D → N Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067750

Natural variant

1425

1

S → L Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067751

Natural variant

1426

1

E → K Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067752

Natural variant

1462

1

S → C Found in a cutaneous malignant melanoma sample; somatic mutation. Ref.6

VAR_067753

Secondary structure

1

.

.

1464

Helix Strand Turn

Details...

Beta strand

1461 – 1464

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: AF5EDD599EC0B1E3	FASTA	1,464	165,283
	10 20 30 40 50 60 MGRVGYWTLL VLPALLVWRG PAPSAAAEKG PPALNIAVML GHSHDVTERE LRTLWGPEQA 70 80 90 100 110 120 AGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSHT 130 140 150 160 170 180 FVPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY 190 200 210 220 230 240 REFISFVKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL 250 260 270 280 290 300 SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGIGILT 310 320 330 340 350 360 TAASSMLEKF SYIPEAKASC YGQMERPEVP MHTLHPFMVN VTWDGKDLSF TEEGYQVHPR 370 380 390 400 410 420 LVVIVLNKDR EWEKVGKWEN HTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE 430 440 450 460 470 480 DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV 490 500 510 520 530 540 TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS 550 560 570 580 590 600 NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT 610 620 630 640 650 660 IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD 670 680 690 700 710 720 QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTKFNQ KGVEDALVSL 730 740 750 760 770 780 KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL 790 800 810 820 830 840 QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL 850 860 870 880 890 900 FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS 910 920 930 940 950 960 AKNISSMSNM NSSRMDSPKR AADFIQRGSL IMDMVSDKGN LMYSDNRSFQ GKESIFGDNM 970 980 990 1000 1010 1020 NELQTFVANR QKDNLNNYVF QGQHPLTLNE SNPNTVEVAV STESKANSRP RQLWKKSVDS 1030 1040 1050 1060 1070 1080 IRQDSLSQNP VSQRDEATAE NRTHSLKSPR YLPEEMAHSD ISETSNRATC HREPDNSKNH 1090 1100 1110 1120 1130 1140 KTKDNFKRSV ASKYPKDCSE VERTYLKTKS SSPRDKIYTI DGEKEPGFHL DPPQFVENVT 1150 1160 1170 1180 1190 1200 LPENVDFPDP YQDPSENFRK GDSTLPMNRN PLHNEEGLSN NDQYKLYSKH FTLKDKGSPH 1210 1220 1230 1240 1250 1260 SETSERYRQN STHCRSCLSN MPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP 1270 1280 1290 1300 1310 1320 ATGEQVYQQD WAQNNALQLQ KNKLRISRQH SYDNIVDKPR ELDLSRPSRS ISLKDRERLL 1330 1340 1350 1360 1370 1380 EGNFYGSLFS VPSSKLSGKK SSLFPQGLED SKRSKSLLPD HTSDNPFLHS HRDDQRLVIG 1390 1400 1410 1420 1430 1440 RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHN DVYISEHVMP YAANKNNMYS 1450 1460 TPRVLNSCSN RRVYKKMPSI ESDV
	Isoform 2 [UniParc]. Checksum: 7454CF24F5BE8373	FASTA	1,281	144,431
	10 20 30 40 50 60 MGRVGYWTLL VLPALLVWRG PAPSAAAEKG PPALNIAVML GHSHDVTERE LRTLWGPEQA 70 80 90 100 110 120 AGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSHT 130 140 150 160 170 180 FVPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY 190 200 210 220 230 240 REFISFVKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL 250 260 270 280 290 300 SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGIGILT 310 320 330 340 350 360 TAASSMLEKF SYIPEAKASC YGQMERPEVP MHTLHPFMVN VTWDGKDLSF TEEGYQVHPR 370 380 390 400 410 420 LVVIVLNKDR EWEKVGKWEN HTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE 430 440 450 460 470 480 DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV 490 500 510 520 530 540 TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS 550 560 570 580 590 600 NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT 610 620 630 640 650 660 IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD 670 680 690 700 710 720 QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTKFNQ KGVEDALVSL 730 740 750 760 770 780 KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL 790 800 810 820 830 840 QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL 850 860 870 880 890 900 FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS 910 920 930 940 950 960 AKNISSMSNM NSSRMDSPKR AADFIQRGSL IMDMVSDKGN LMYSDNRSFQ GKESIFGDNM 970 980 990 1000 1010 1020 NELQTFVANR QKDNLNNYVF QGQHPLTLNE SNPNTVEVAV STESKANSRP RQLWKKSVDS 1030 1040 1050 1060 1070 1080 IRQDSLSQNP VSQRDEATAE NRTHSLKSPR YLPEEMAHSD ISETSNRATC HREPDNSKNH 1090 1100 1110 1120 1130 1140 KTKDNFKRSV ASKYPKDCSE VERTYLKTKS SSPRDKIYTI DGEKEPGFHL DPPQFVENVT 1150 1160 1170 1180 1190 1200 LPENVDFPDP YQDPSENFRK GDSTLPMNRN PLHNEEGLSN NDQYKLYSKH FTLKDKGSPH 1210 1220 1230 1240 1250 1260 SETSERYRQN STHCRSCLSN MPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGMT 1270 1280 NAWLLGDAPR TLTNTRCHPR R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning and sequencing of the cDNA and primary structure of the protein." Foldes R.L., Adams S.L., Fantaske R.P., Kamboj R.K. Biochim. Biophys. Acta 1223:155-159(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-270.
[2]	"Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors." Hess S.D., Daggett L.P., Crona J., Deal C., Lu C.-C., Urrutia A., Chavez-Noriega L., Ellis S.B., Johnson E.C., Velicelebi G. J. Pharmacol. Exp. Ther. 278:808-816(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cerebellum.
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[5]	"Mutations in GRIN2A and GRIN2B encoding regulatory subunits of NMDA receptors cause variable neurodevelopmental phenotypes." Endele S., Rosenberger G., Geider K., Popp B., Tamer C., Stefanova I., Milh M., Kortum F., Fritsch A., Pientka F.K., Hellenbroich Y., Kalscheuer V.M., Kohlhase J., Moog U., Rappold G., Rauch A., Ropers H.H., von Spiczak S. , Tonnies H., Villeneuve N., Villard L., Zabel B., Zenker M., Laube B., Reis A., Wieczorek D., Van Maldergem L., Kutsche K. Nat. Genet. 42:1021-1026(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION, VARIANT EPND LYS-615, CHARACTERIZATION OF VARIANT EPND LYS-615.
[6]	"Exome sequencing identifies GRIN2A as frequently mutated in melanoma." Wei X., Walia V., Lin J.C., Teer J.K., Prickett T.D., Gartner J., Davis S., Stemke-Hale K., Davies M.A., Gershenwald J.E., Robinson W., Robinson S., Rosenberg S.A., Samuels Y. Nat. Genet. 43:442-446(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PROBABLE INVOLVEMENT IN MELANOMA, VARIANTS LEU-57; ILE-183; ASN-252; PHE-278; LYS-371; LYS-373; GLU-449; SER-459; ARG-595; PHE-598; ILE-653; GLU-712; TRP-740; GLU-889; LYS-920; PHE-929; LYS-962; LYS-1073; LEU-1074; ASN-1153; LYS-1175; GLY-1276; LYS-1285; TRP-1318; LEU-1366; ASN-1421; LEU-1425; LYS-1426 AND CYS-1462.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U09002 mRNA. Translation: AAB60343.1.
U90277 mRNA. Translation: AAB49992.1.
AC006531 Genomic DNA. No translation available.
AC007218 Genomic DNA. No translation available.
AC022168 Genomic DNA. No translation available.
AC026423 Genomic DNA. No translation available.
AC133565 Genomic DNA. No translation available.
BC117131 mRNA. Translation: AAI17132.1.
BC143273 mRNA. Translation: AAI43274.1.

IPI

IPI00029768.

PIR

S47555.

RefSeq

NP_000824.1. NM_000833.3.
NP_001127879.1. NM_001134407.1.
NP_001127880.1. NM_001134408.1.

UniGene

Hs.411472.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NFL	X-ray	1.91	E/F/G/H	1449-1464	[»]

ProteinModelPortal

Q12879.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-414776.

STRING

9606.ENSP00000332549.

PTM databases

PhosphoSite

Q12879.

Polymorphism databases

DMDM

14285603.

Proteomic databases

PaxDb

Q12879.

PRIDE

Q12879.

Protocols and materials databases

DNASU

2903.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330684; ENSP00000332549; ENSG00000183454.
ENST00000396573; ENSP00000379818; ENSG00000183454.
ENST00000396575; ENSP00000379820; ENSG00000183454.
ENST00000404927; ENSP00000385872; ENSG00000183454.
ENST00000562109; ENSP00000454998; ENSG00000183454.

GeneID

2903.

KEGG

hsa:2903.

UCSC

uc002czo.4. human.

Organism-specific databases

CTD

2903.

GeneCards

GC16M009762.

HGNC

HGNC:4585. GRIN2A.

HPA

CAB022725.

MIM

138253. gene.
613971. phenotype.

neXtProt

NX_Q12879.

Orphanet

289266. Early-onset epileptic encephalopathy and intellectual deficit due to GRIN2A mutation.

PharmGKB

PA28979.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282132.

HOVERGEN

HBG052635.

InParanoid

Q12879.

KO

K05209.

OMA

CRSCLSN.

OrthoDB

EOG4X0MRG.

PhylomeDB

Q12879.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q12879.

Bgee

Q12879.

CleanEx

HS_GRIN2A.

Genevestigator

Q12879.

GermOnline

ENSG00000183454. Homo sapiens.

Family and domain databases

InterPro

IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR018884. NMDAR2_C.
IPR001638. SBP_bac_3.
[Graphical view]

Pfam

PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]

PRINTS

PR00177. NMDARECEPTOR.

SMART

SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q12879.

ChEMBL

CHEMBL1972.

DrugBank

DB00949. Felbamate.
DB00145. Glycine.
DB00142. L-Glutamic Acid.
DB00836. Loperamide.
DB01043. Memantine.

EvolutionaryTrace

Q12879.

GenomeRNAi

2903.

NextBio

11495.

SOURCE

Search...

Entry information

Entry name

NMDE1_HUMAN

Accession

Primary (citable) accession number: Q12879
Secondary accession number(s): O00669, Q17RZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.