P42263 (GRIA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor 3
Short name=GluR-3

Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name=GluA3

Gene names

Name:	GRIA3
Synonyms:	GLUR3, GLURC

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	894 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	Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Ref.6
Subunit structure	Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 By similarity. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression By similarity.
Post-translational modification	Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-621 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-847 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.
Involvement in disease	Mental retardation, X-linked 94 (MRX94) [MIM:300699]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX94 patients have moderate mental retardation. Other variable features are macrocephaly, seizures, myoclonic jerks, autistic behavior, asthenic body habitus, distal muscle weakness and hyporeflexia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7
Miscellaneous	The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA3 subfamily. [View classification]
Caution	It is uncertain whether Met-1 or Met-7 is the initiator.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Inferred from sequence or structural similarity. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW endocytic vesicle membrane Traceable author statement. Source: Reactome postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from direct assay Ref.6. Source: UniProtKB extracellular-glutamate-gated ion channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform Flop (identifier: P42263-1)

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 Flip (identifier: P42263-2)

The sequence of this isoform differs from the canonical sequence as follows:
     776-777: NA → TP
     786-786: N → S
     790-790: L → I
     807-811: SGGGD → AKDSG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 894	866	Glutamate receptor 3		PRO_0000011536
Regions
	Topological domain	29 – 552	524	Extracellular By similarity
	Transmembrane	553 – 573	21	Helical; By similarity
	Topological domain	574 – 602	29	Cytoplasmic By similarity
	Intramembrane	603 – 618	16	Helical; Pore-forming; By similarity
	Intramembrane	619 – 621	3	By similarity
	Topological domain	622 – 627	6	Cytoplasmic By similarity
	Transmembrane	628 – 648	21	Helical; By similarity
	Topological domain	649 – 823	175	Extracellular By similarity
	Transmembrane	824 – 844	21	Helical; By similarity
	Topological domain	845 – 894	50	Cytoplasmic By similarity
	Region	508 – 510	3	Glutamate binding By similarity
	Region	686 – 687	2	Glutamate binding By similarity
Sites
	Binding site	480	1	Glutamate By similarity
	Binding site	515	1	Glutamate By similarity
	Binding site	737	1	Glutamate By similarity
Amino acid modifications
	Modified residue	877	1	Phosphotyrosine By similarity
	Modified residue	887	1	Phosphotyrosine By similarity
	Lipidation	621	1	S-palmitoyl cysteine By similarity
	Lipidation	847	1	S-palmitoyl cysteine By similarity
	Glycosylation	63	1	N-linked (GlcNAc...) Potential
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	380	1	N-linked (GlcNAc...) Potential
	Glycosylation	415	1	N-linked (GlcNAc...) Potential
	Glycosylation	422	1	N-linked (GlcNAc...) Potential
	Disulfide bond	91 ↔ 340		By similarity
	Disulfide bond	750 ↔ 805		By similarity
Natural variations
	Alternative sequence	776 – 777	2	NA → TP in isoform Flip.		VSP_000115
	Alternative sequence	786	1	N → S in isoform Flip.		VSP_000116
	Alternative sequence	790	1	L → I in isoform Flip.		VSP_000117
	Alternative sequence	807 – 811	5	SGGGD → AKDSG in isoform Flip.		VSP_000118
	Natural variant	450	1	R → Q in MRX94. Ref.7		VAR_043484
	Natural variant	525	1	F → L. Ref.1 Ref.3 Corresponds to variant rs1052538 [ dbSNP | Ensembl ].		VAR_023579
	Natural variant	631	1	R → S in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. Ref.7		VAR_043485
	Natural variant	706	1	M → T in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. Ref.7		VAR_043486
	Natural variant	833	1	G → R in MRX94; reduced receptor expression possibly due to rapid degradation. Ref.7		VAR_043487
Experimental info
	Sequence conflict	775	1	R → G Ref.1
	Sequence conflict	775	1	R → G Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Flop [UniParc]. Last modified October 11, 2005. Version 2. Checksum: 178589A870E0D102	FASTA	894	101,157
	10 20 30 40 50 60 MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT 70 80 90 100 110 120 NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL 130 140 150 160 170 180 HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA 190 200 210 220 230 240 AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS 250 260 270 280 290 300 RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN 310 320 330 340 350 360 APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM 370 380 390 400 410 420 VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS 430 440 450 460 470 480 ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY 490 500 510 520 530 540 GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS 550 560 570 580 590 600 KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP 610 620 630 640 650 660 NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 670 680 690 700 710 720 MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD 730 740 750 760 770 780 GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRNAVNL 790 800 810 820 830 840 AVLKLNEQGL LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM 850 860 870 880 890 VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI
	Isoform Flip [UniParc]. Checksum: EB3ED4EBBA353021	FASTA	894	101,228
	10 20 30 40 50 60 MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT 70 80 90 100 110 120 NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL 130 140 150 160 170 180 HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA 190 200 210 220 230 240 AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS 250 260 270 280 290 300 RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN 310 320 330 340 350 360 APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM 370 380 390 400 410 420 VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS 430 440 450 460 470 480 ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY 490 500 510 520 530 540 GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS 550 560 570 580 590 600 KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP 610 620 630 640 650 660 NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 670 680 690 700 710 720 MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD 730 740 750 760 770 780 GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRTPVNL 790 800 810 820 830 840 AVLKLSEQGI LDKLKNKWWY DKGECGAKDS GSKDKTSALS LSNVAGVFYI LVGGLGLAMM 850 860 870 880 890 VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human glutamate receptor hGluR3 flip and flop isoforms: cloning and sequencing of the cDNAs and primary structure of the proteins." Rampersad V., Elliott C.E., Nutt S.L., Foldes R.L., Kamboj R.K. Biochim. Biophys. Acta 1219:563-566(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP), VARIANT LEU-525. Tissue: Hippocampus.
[2]	McLaughlin D.P., Kerwin R.W. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq." Amir R., Dahle E.J., Toriolo D., Zoghbi H.Y. Am. J. Med. Genet. 90:69-71(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-525.
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins." Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S. Neuron 68:1082-1096(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Mutations in ionotropic AMPA receptor 3 alter channel properties and are associated with moderate cognitive impairment in humans." Wu Y., Arai A.C., Rumbaugh G., Srivastava A.K., Turner G., Hayashi T., Suzuki E., Jiang Y., Zhang L., Rodriguez J., Boyle J., Tarpey P., Raymond F.L., Nevelsteen J., Froyen G., Stratton M., Futreal A., Gecz J. , Stevenson R., Schwartz C.E., Valle D., Huganir R.L., Wang T. Proc. Natl. Acad. Sci. U.S.A. 104:18163-18168(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MRX94 GLN-450; SER-631; THR-706 AND ARG-833, CHARACTERIZATION OF VARIANTS MRX94 SER-631; THR-706 AND ARG-833.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10302 mRNA. Translation: AAA67923.1. U10301 mRNA. Translation: AAA67922.1. X82068 mRNA. Translation: CAA57567.1. AF166365 , AF166362, AF166363, AF166364 Genomic DNA. Translation: AAF97857.1. AF167332 , AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166375 Genomic DNA. Translation: AAF97858.1. AF167332 , AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166374 Genomic DNA. Translation: AAF97859.1. AL356213 , AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95643.1. AL356213 , AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95644.1. AL590139 , AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95164.1. AL590139 , AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95165.1. Z83848 , AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95709.1. Z83848 , AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95710.1. Z82899 , Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95664.1. Z82899 , Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95665.1. AL035426 , Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95683.1. AL035426 , Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95684.1. CH471107 Genomic DNA. Translation: EAX11865.1. CH471107 Genomic DNA. Translation: EAX11867.1.
IPI	IPI00219315. IPI00298700.
PIR	S49460. S50128. S53696.
RefSeq	NP_000819.3. NM_000828.4. NP_015564.4. NM_007325.4.
UniGene	Hs.377070.
3D structure databases
ProteinModelPortal	P42263.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46195N.
STRING	9606.ENSP00000360302.
Protein family/group databases
TCDB	1.A.10.1.4. glutamate-gated ion channel (GIC) family of neurotransmitter receptors.
PTM databases
PhosphoSite	P42263.
Polymorphism databases
DMDM	77416864.
Proteomic databases
PaxDb	P42263.
PRIDE	P42263.
Protocols and materials databases
DNASU	2892.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264357; ENSP00000264357; ENSG00000125675. ENST00000371251; ENSP00000360297; ENSG00000125675. ENST00000371256; ENSP00000360302; ENSG00000125675.
GeneID	2892.
KEGG	hsa:2892.
UCSC	uc004etq.4. human. uc004etr.4. human.
Organism-specific databases
CTD	2892.
GeneCards	GC0XP122318.
HGNC	HGNC:4573. GRIA3.
HPA	CAB007799.
MIM	300699. phenotype. 305915. gene.
neXtProt	NX_P42263.
Orphanet	777. X-linked nonsyndromic intellectual deficit.
PharmGKB	PA28968.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG316680.
HOVERGEN	HBG051839.
InParanoid	P42263.
KO	K05199.
OMA	MVQQFLQ.
OrthoDB	EOG4XKV68.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	P42263.
Bgee	P42263.
CleanEx	HS_GRIA3.
Genevestigator	P42263.
GermOnline	ENSG00000125675. 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. [Graphical view]
Pfam	PF01094. ANF_receptor. 1 hit. PF00060. Lig_chan. 1 hit. PF10613. Lig_chan-Glu_bd. 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	P42263.
ChEMBL	CHEMBL3595.
ChiTaRS	GRIA3. human.
DrugBank	DB00142. L-Glutamic Acid.
GenomeRNAi	2892.
NextBio	11437.
SOURCE	Search...

Entry information

Entry name

GRIA3_HUMAN

Accession

Primary (citable) accession number: P42263
Secondary accession number(s): D3DTF1 , Q4VXD5, Q4VXD6, Q9HDA0, Q9HDA1, Q9HDA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 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.