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P42262

- GRIA2_HUMAN

UniProt

P42262 - GRIA2_HUMAN

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Protein

Glutamate receptor 2

Gene

GRIA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei471 – 4711Glutamate2 Publications
Binding sitei506 – 5061Glutamate2 Publications
Binding sitei726 – 7261Glutamate2 Publications

GO - Molecular functioni

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
  2. extracellular-glutamate-gated ion channel activity Source: RefGenome
  3. ionotropic glutamate receptor activity Source: UniProtKB

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: UniProtKB
  2. ion transmembrane transport Source: GOC
  3. signal transduction Source: ProtInc
  4. synaptic transmission Source: Reactome
  5. synaptic transmission, glutamatergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinkiP42262.

Protein family/group databases

TCDBi1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 2
Short name:
GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name:
GluA2
Gene namesi
Name:GRIA2
Synonyms:GLUR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4572. GRIA2.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 543519ExtracellularBy similarityAdd
BLAST
Transmembranei544 – 56421HelicalBy similarityAdd
BLAST
Topological domaini565 – 59127CytoplasmicBy similarityAdd
BLAST
Intramembranei592 – 60716Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei608 – 6103By similarity
Topological domaini611 – 6166CytoplasmicBy similarity
Transmembranei617 – 63721HelicalBy similarityAdd
BLAST
Topological domaini638 – 812175ExtracellularBy similarityAdd
BLAST
Transmembranei813 – 83321Helical; Name=M4Add
BLAST
Topological domaini834 – 88350CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: RefGenome
  4. endocytic vesicle membrane Source: Reactome
  5. endoplasmic reticulum Source: UniProtKB-KW
  6. integral component of plasma membrane Source: UniProtKB
  7. plasma membrane Source: Reactome
  8. postsynaptic membrane Source: RefGenome
  9. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 883859Glutamate receptor 2PRO_0000011532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi78 ↔ 330
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)1 Publication
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
Lipidationi610 – 6101S-palmitoyl cysteineBy similarity
Modified residuei683 – 6831Phosphoserine; by PKCBy similarity
Modified residuei717 – 7171Phosphoserine; by PKGBy similarity
Disulfide bondi739 ↔ 794
Lipidationi836 – 8361S-palmitoyl cysteineBy similarity
Modified residuei876 – 8761PhosphotyrosineBy similarity
Modified residuei880 – 8801PhosphoserineBy similarity

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP42262.
PRIDEiP42262.

PTM databases

PhosphoSiteiP42262.

Expressioni

Gene expression databases

BgeeiP42262.
CleanExiHS_GRIA2.
ExpressionAtlasiP42262. baseline and differential.
GenevestigatoriP42262.

Organism-specific databases

HPAiCAB006830.
CAB007812.
CAB012981.
HPA008441.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly (By similarity). Interacts with PICK1 (via PDZ domain). Interacts with PRKCABP and GRIP2 (By similarity). Interacts with GRIA1 and SYNDIG1 (By similarity). Interacts with LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity). Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NSFP464592EBI-3909876,EBI-712251

Protein-protein interaction databases

BioGridi109148. 21 interactions.
DIPiDIP-42852N.
IntActiP42262. 2 interactions.
MINTiMINT-2791741.
STRINGi9606.ENSP00000264426.

Structurei

Secondary structure

1
883
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 348Combined sources
Helixi38 – 5114Combined sources
Beta strandi58 – 658Combined sources
Helixi70 – 8314Combined sources
Beta strandi88 – 903Combined sources
Turni94 – 963Combined sources
Helixi97 – 10711Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi125 – 1273Combined sources
Helixi133 – 14210Combined sources
Beta strandi147 – 1526Combined sources
Helixi159 – 17113Combined sources
Beta strandi174 – 1796Combined sources
Helixi188 – 1914Combined sources
Helixi193 – 2019Combined sources
Beta strandi206 – 2116Combined sources
Helixi213 – 22513Combined sources
Helixi230 – 2323Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi239 – 2413Combined sources
Helixi247 – 2493Combined sources
Beta strandi256 – 2627Combined sources
Helixi268 – 27710Combined sources
Turni282 – 2843Combined sources
Beta strandi289 – 2913Combined sources
Helixi295 – 31622Combined sources
Helixi341 – 3499Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi382 – 3909Combined sources
Turni391 – 3933Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi416 – 4205Combined sources
Turni424 – 4263Combined sources
Beta strandi427 – 4293Combined sources
Helixi433 – 4353Combined sources
Helixi438 – 4414Combined sources
Beta strandi442 – 4443Combined sources
Helixi445 – 45713Combined sources
Beta strandi461 – 4655Combined sources
Turni476 – 4783Combined sources
Helixi483 – 4897Combined sources
Beta strandi494 – 4963Combined sources
Helixi504 – 5074Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi516 – 5194Combined sources
Beta strandi521 – 5266Combined sources
Helixi657 – 6615Combined sources
Beta strandi664 – 6718Combined sources
Helixi675 – 6828Combined sources
Helixi686 – 69712Combined sources
Beta strandi704 – 7063Combined sources
Helixi707 – 71610Combined sources
Turni717 – 7193Combined sources
Beta strandi720 – 7267Combined sources
Helixi727 – 7348Combined sources
Beta strandi741 – 7455Combined sources
Beta strandi751 – 7533Combined sources
Beta strandi756 – 7583Combined sources
Helixi764 – 77613Combined sources
Helixi779 – 78810Combined sources
Turni789 – 7913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WJWX-ray1.80A25-412[»]
2WJXX-ray4.10A/B/C25-412[»]
2XHDX-ray1.80A/B413-527[»]
A/B653-796[»]
3R7XX-ray2.10A/B413-527[»]
A/B653-796[»]
3RN8X-ray1.70A/B/C413-527[»]
A/B/C653-812[»]
3RNNX-ray1.75A/B/C413-527[»]
A/B/C653-812[»]
3UA8X-ray1.90A413-527[»]
A653-796[»]
ProteinModelPortaliP42262.
SMRiP42262. Positions 25-838.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42262.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni499 – 5013Glutamate binding
Regioni675 – 6762Glutamate binding

Domaini

The M4 transmembrane segment mediates tetramerization and is required for cell surface expression.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP42262.
KOiK05198.
OMAiHAVPYVS.
OrthoDBiEOG7C2R0J.
PhylomeDBiP42262.
TreeFamiTF315232.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Flop (identifier: P42262-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ
60 70 80 90 100
FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI
110 120 130 140 150
TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY
160 170 180 190 200
LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE MYRSLFQDLE
210 220 230 240 250
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI
260 270 280 290 300
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT
310 320 330 340 350
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ
360 370 380 390 400
VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT
410 420 430 440 450
ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA
460 470 480 490 500
AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL
510 520 530 540 550
TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI
560 570 580 590 600
VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
610 620 630 640 650
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM
660 670 680 690 700
VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP
710 720 730 740 750
SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS
760 770 780 790 800
KGYGIATPKG SSLRNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD
810 820 830 840 850
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK
860 870 880
NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
Length:883
Mass (Da):98,821
Last modified:October 10, 2002 - v3
Checksum:i6DAB96C76D1D8448
GO
Isoform Flip (identifier: P42262-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     765-800: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG

Show »
Length:883
Mass (Da):98,878
Checksum:i882141AC054254F8
GO
Isoform 3 (identifier: P42262-3) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     848-883: VAKNAQNINP...NVYGIESVKI → MTLNDAMRNK...GMNVSVTDLS

Show »
Length:901
Mass (Da):100,594
Checksum:i6E668073D621EFBB
GO
Isoform 4 (identifier: P42262-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.
     765-800: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG

Note: No experimental confirmation available.

Show »
Length:836
Mass (Da):93,775
Checksum:i1B3F13BC745D4A45
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401I → V in AAH10574. (PubMed:15489334)Curated
Sequence conflicti241 – 2411G → E in AAA58631. (PubMed:8003671)Curated
Sequence conflicti415 – 4151T → I in AAH28736. (PubMed:15489334)Curated
Sequence conflicti764 – 7641R → G in AAA58631. (PubMed:8003671)Curated

RNA editingi

Partially edited. Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti607 – 6071Q → R in RNA edited version. 2 Publications
Corresponds to variant rs17850674 [ dbSNP | Ensembl ].
VAR_000303
Natural varianti608 – 6081Q → R.1 Publication
Corresponds to variant rs17850675 [ dbSNP | Ensembl ].
VAR_037055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 4. 1 PublicationVSP_055920Add
BLAST
Alternative sequencei765 – 80036NAVNL…SGGGD → TPVNLAVLKLSEQGVLDKLK NKWWYDKGECGAKDSG in isoform Flip and isoform 4. 2 PublicationsVSP_053350Add
BLAST
Alternative sequencei848 – 88336VAKNA…ESVKI → MTLNDAMRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedVSP_029309Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20814 mRNA. Translation: AAA58631.1.
AC079233 Genomic DNA. No translation available.
AC112240 Genomic DNA. No translation available.
BC010574 mRNA. Translation: AAH10574.1.
BC028736 mRNA. Translation: AAH28736.2.
CCDSiCCDS3797.1. [P42262-2]
CCDS43274.1. [P42262-1]
PIRiI58181.
RefSeqiNP_000817.2. NM_000826.3.
NP_001077088.1. NM_001083619.1.
NP_001077089.1. NM_001083620.1.
UniGeneiHs.32763.

Genome annotation databases

EnsembliENST00000264426; ENSP00000264426; ENSG00000120251. [P42262-1]
ENST00000296526; ENSP00000296526; ENSG00000120251. [P42262-2]
ENST00000393815; ENSP00000377403; ENSG00000120251. [P42262-4]
ENST00000507898; ENSP00000426845; ENSG00000120251. [P42262-4]
GeneIDi2891.
KEGGihsa:2891.
UCSCiuc003ipm.4. human. [P42262-1]

Polymorphism databases

DMDMi23831146.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20814 mRNA. Translation: AAA58631.1 .
AC079233 Genomic DNA. No translation available.
AC112240 Genomic DNA. No translation available.
BC010574 mRNA. Translation: AAH10574.1 .
BC028736 mRNA. Translation: AAH28736.2 .
CCDSi CCDS3797.1. [P42262-2 ]
CCDS43274.1. [P42262-1 ]
PIRi I58181.
RefSeqi NP_000817.2. NM_000826.3.
NP_001077088.1. NM_001083619.1.
NP_001077089.1. NM_001083620.1.
UniGenei Hs.32763.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WJW X-ray 1.80 A 25-412 [» ]
2WJX X-ray 4.10 A/B/C 25-412 [» ]
2XHD X-ray 1.80 A/B 413-527 [» ]
A/B 653-796 [» ]
3R7X X-ray 2.10 A/B 413-527 [» ]
A/B 653-796 [» ]
3RN8 X-ray 1.70 A/B/C 413-527 [» ]
A/B/C 653-812 [» ]
3RNN X-ray 1.75 A/B/C 413-527 [» ]
A/B/C 653-812 [» ]
3UA8 X-ray 1.90 A 413-527 [» ]
A 653-796 [» ]
ProteinModelPortali P42262.
SMRi P42262. Positions 25-838.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109148. 21 interactions.
DIPi DIP-42852N.
IntActi P42262. 2 interactions.
MINTi MINT-2791741.
STRINGi 9606.ENSP00000264426.

Chemistry

BindingDBi P42262.
ChEMBLi CHEMBL2096670.
DrugBanki DB01351. Amobarbital.
DB01352. Aprobarbital.
DB00237. Butabarbital.
DB00241. Butalbital.
DB01353. Butethal.
DB01354. Heptabarbital.
DB01355. Hexobarbital.
DB00849. Methylphenobarbital.
DB00312. Pentobarbital.
DB01174. Phenobarbital.
DB00794. Primidone.
DB01346. Quinidine barbiturate.
DB00418. Secobarbital.
DB00306. Talbutal.
DB00599. Thiopental.
GuidetoPHARMACOLOGYi 445.

Protein family/group databases

TCDBi 1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P42262.

Polymorphism databases

DMDMi 23831146.

Proteomic databases

PaxDbi P42262.
PRIDEi P42262.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264426 ; ENSP00000264426 ; ENSG00000120251 . [P42262-1 ]
ENST00000296526 ; ENSP00000296526 ; ENSG00000120251 . [P42262-2 ]
ENST00000393815 ; ENSP00000377403 ; ENSG00000120251 . [P42262-4 ]
ENST00000507898 ; ENSP00000426845 ; ENSG00000120251 . [P42262-4 ]
GeneIDi 2891.
KEGGi hsa:2891.
UCSCi uc003ipm.4. human. [P42262-1 ]

Organism-specific databases

CTDi 2891.
GeneCardsi GC04P158141.
HGNCi HGNC:4572. GRIA2.
HPAi CAB006830.
CAB007812.
CAB012981.
HPA008441.
MIMi 138247. gene.
neXtProti NX_P42262.
PharmGKBi PA28967.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316680.
GeneTreei ENSGT00760000118920.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
InParanoidi P42262.
KOi K05198.
OMAi HAVPYVS.
OrthoDBi EOG7C2R0J.
PhylomeDBi P42262.
TreeFami TF315232.

Enzyme and pathway databases

Reactomei REACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinki P42262.

Miscellaneous databases

ChiTaRSi GRIA2. human.
EvolutionaryTracei P42262.
GeneWikii GRIA2.
GenomeRNAii 2891.
NextBioi 11429.
PROi P42262.
SOURCEi Search...

Gene expression databases

Bgeei P42262.
CleanExi HS_GRIA2.
ExpressionAtlasi P42262. baseline and differential.
Genevestigatori P42262.

Family and domain databases

InterProi IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view ]
PRINTSi PR00177. NMDARECEPTOR.
SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and functional expression of the AMPA/kainate receptor subunit 2 from human brain."
    Sun W., Ferrer-Montiel A.V., Montal M.
    NeuroReport 5:441-444(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), VARIANT ARG-607.
    Tissue: Brain.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS FLOP AND 4), VARIANTS ARG-607 AND ARG-608.
    Tissue: Brain.
  4. "RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue."
    Paschen W., Hedreen J.C., Ross C.A.
    J. Neurochem. 63:1596-1602(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 607.
  5. "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors."
    Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P.
    Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 3).
  6. "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands."
    Dev K.K., Nakanishi S., Henley J.M.
    J. Biol. Chem. 279:41393-41397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PICK1.
  7. "A eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptors."
    Salussolia C.L., Gan Q., Kazi R., Singh P., Allopenna J., Furukawa H., Wollmuth L.P.
    J. Neurosci. 33:9840-9845(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  8. "Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors."
    Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K., McIlhinney R.A., Jones E.Y., Aricescu A.R.
    J. Mol. Biol. 392:1125-1132(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-370.
  9. "Discovery of N-[(2S)-5-(6-fluoro-3-pyridinyl)-2,3-dihydro-1H-inden-2-yl]-2-propanesulfonamide, a novel clinical AMPA receptor positive modulator."
    Ward S.E., Harries M., Aldegheri L., Andreotti D., Ballantine S., Bax B.D., Harris A.J., Harker A.J., Lund J., Melarange R., Mingardi A., Mookherjee C., Mosley J., Neve M., Oliosi B., Profeta R., Smith K.J., Smith P.W.
    , Spada S., Thewlis K.M., Yusaf S.P.
    J. Med. Chem. 53:5801-5812(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-795 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, FUNCTION.
  10. "Quinazolinedione sulfonamides: a novel class of competitive AMPA receptor antagonists with oral activity."
    Koller M., Lingenhoehl K., Schmutz M., Vranesic I.T., Kallen J., Auberson Y.P., Carcache D.A., Mattes H., Ofner S., Orain D., Urwyler S.
    Bioorg. Med. Chem. Lett. 21:3358-3361(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, DISULFIDE BOND.

Entry informationi

Entry nameiGRIA2_HUMAN
AccessioniPrimary (citable) accession number: P42262
Secondary accession number(s): A8MT92, I6L997, Q96FP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 10, 2002
Last modified: November 26, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3