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Protein

Glutamate receptor ionotropic, kainate 2

Gene

GRIK2

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

Functioni

Ionotropic glutamate receptor. 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. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei523GlutamateBy similarity1
Binding sitei738GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-451307. Activation of Na-permeable Kainate Receptors.
R-HSA-451308. Activation of Ca-permeable Kainate Receptor.
SignaLinkiQ13002.
SIGNORiQ13002.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, kainate 2
Short name:
GluK2
Alternative name(s):
Excitatory amino acid receptor 4
Short name:
EAA4
Glutamate receptor 6
Short name:
GluR-6
Short name:
GluR6
Gene namesi
Name:GRIK2
Synonyms:GLUR6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4580. GRIK2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 561ExtracellularSequence analysisAdd BLAST530
Transmembranei562 – 582HelicalSequence analysisAdd BLAST21
Topological domaini583 – 635CytoplasmicSequence analysisAdd BLAST53
Transmembranei636 – 656HelicalSequence analysisAdd BLAST21
Topological domaini657 – 819ExtracellularSequence analysisAdd BLAST163
Transmembranei820 – 840HelicalSequence analysisAdd BLAST21
Topological domaini841 – 908CytoplasmicSequence analysisAdd BLAST68

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 6 (MRT6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic mental retardation. MRT6 patients display mild to severe mental retardation and psychomotor development delay in early childhood. Patients do not have neurologic problems, congenital malformations, or facial dysmorphism. Body height, weight, and head circumference are normal.
See also OMIM:611092

Keywords - Diseasei

Mental retardation

Organism-specific databases

DisGeNETi2898.
MalaCardsiGRIK2.
MIMi611092. phenotype.
OpenTargetsiENSG00000164418.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA164741600.

Chemistry databases

ChEMBLiCHEMBL3683.
DrugBankiDB01351. Amobarbital.
DB01352. Aprobarbital.
DB00237. Butabarbital.
DB00241. Butalbital.
DB01353. Butethal.
DB01354. Heptabarbital.
DB01355. Hexobarbital.
DB00849. Methylphenobarbital.
DB00312. Pentobarbital.
DB01174. Phenobarbital.
DB00794. Primidone.
DB00418. Secobarbital.
DB00306. Talbutal.
DB00599. Thiopental.
GuidetoPHARMACOLOGYi451.

Polymorphism and mutation databases

BioMutaiGRIK2.
DMDMi2492627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000001154432 – 908Glutamate receptor ionotropic, kainate 2Add BLAST877

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...)Sequence analysis1
Glycosylationi73N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi96 ↔ 347By similarity
Glycosylationi275N-linked (GlcNAc...)Sequence analysis1
Glycosylationi378N-linked (GlcNAc...)Sequence analysis1
Glycosylationi412N-linked (GlcNAc...)Sequence analysis1
Glycosylationi423N-linked (GlcNAc...)Sequence analysis1
Glycosylationi430N-linked (GlcNAc...)Sequence analysis1
Glycosylationi546N-linked (GlcNAc...)Sequence analysis1
Modified residuei846Phosphoserine; by PKC1 Publication1
Modified residuei868Phosphoserine; by PKC1 Publication1
Cross-linki886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication

Post-translational modificationi

Sumoylation mediates kainate receptor-mediated endocytosis and regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and desumoylated by SENP1 (By similarity).By similarity
Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome (By similarity).By similarity
Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13002.
PaxDbiQ13002.
PeptideAtlasiQ13002.
PRIDEiQ13002.

PTM databases

iPTMnetiQ13002.
PhosphoSitePlusiQ13002.
SwissPalmiQ13002.

Expressioni

Tissue specificityi

Expression is higher in cerebellum than in cerebral cortex.

Gene expression databases

BgeeiENSG00000164418.
CleanExiHS_GRIK2.
ExpressionAtlasiQ13002. baseline and differential.
GenevisibleiQ13002. HS.

Organism-specific databases

HPAiCAB022463.
HPA014395.
HPA014623.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers (Probable). Assembles into a kainate-gated homomeric channel that does not bind AMPA. GRIK2 associated to GRIK5 forms functional channels that can be gated by AMPA (By similarity). Interacts with DLG4. Interacts with NETO2 (By similarity). Interacts (via C-terminus) with KLHL17 (via kelch repeats); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi109155. 13 interactors.
IntActiQ13002. 2 interactors.
STRINGi9606.ENSP00000397026.

Chemistry databases

BindingDBiQ13002.

Structurei

Secondary structure

1908
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi433 – 437Combined sources5
Turni441 – 443Combined sources3
Beta strandi444 – 446Combined sources3
Helixi455 – 458Combined sources4
Beta strandi459 – 461Combined sources3
Helixi462 – 474Combined sources13
Beta strandi478 – 482Combined sources5
Turni493 – 495Combined sources3
Helixi500 – 506Combined sources7
Beta strandi511 – 513Combined sources3
Helixi521 – 524Combined sources4
Beta strandi527 – 529Combined sources3
Beta strandi533 – 536Combined sources4
Beta strandi538 – 544Combined sources7
Helixi671 – 675Combined sources5
Beta strandi678 – 683Combined sources6
Helixi689 – 696Combined sources8
Helixi700 – 711Combined sources12
Helixi713 – 716Combined sources4
Beta strandi717 – 720Combined sources4
Helixi721 – 730Combined sources10
Beta strandi731 – 738Combined sources8
Helixi739 – 748Combined sources10
Beta strandi752 – 756Combined sources5
Beta strandi762 – 764Combined sources3
Beta strandi767 – 769Combined sources3
Helixi774 – 787Combined sources14
Helixi790 – 799Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QXMX-ray1.65A/B429-544[»]
A/B667-806[»]
5CMMX-ray1.27A667-806[»]
ProteinModelPortaliQ13002.
SMRiQ13002.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni516 – 518Glutamate bindingBy similarity3
Regioni689 – 690Glutamate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiQ13002.
KOiK05202.
OMAiVFRCTIR.
OrthoDBiEOG091G02LN.
PhylomeDBiQ13002.
TreeFamiTF334668.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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 (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13002-1) [UniParc]FASTAAdd to basket
Also known as: A

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
MKIIFPILSN PVFRRTVKLL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM
60 70 80 90 100
GAEELAFRFA VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS
110 120 130 140 150
LGVAAIFGPS HSSSANAVQS ICNALGVPHI QTRWKHQVSD NKDSFYVSLY
160 170 180 190 200
PDFSSLSRAI LDLVQFFKWK TVTVVYDDST GLIRLQELIK APSRYNLRLK
210 220 230 240 250
IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK QALAMGMMTE
260 270 280 290 300
YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER
310 320 330 340 350
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH
360 370 380 390 400
KPWRFGTRFM SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE
410 420 430 440 450
KIGTWDPASG LNMTESQKGK PANITDSLSN RSLIVTTILE EPYVLFKKSD
460 470 480 490 500
KPLYGNDRFE GYCIDLLREL STILGFTYEI RLVEDGKYGA QDDANGQWNG
510 520 530 540 550
MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI LYRKPNGTNP
560 570 580 590 600
GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
610 620 630 640 650
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS
660 670 680 690 700
YTANLAAFLT VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS
710 720 730 740 750
TYDKMWAFMS SRRQSVLVKS NEEGIQRVLT SDYAFLMEST TIEFVTQRNC
760 770 780 790 800
NLTQIGGLID SKGYGVGTPM GSPYRDKITI AILQLQEEGK LHMMKEKWWR
810 820 830 840 850
GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG EFLYKSKKNA
860 870 880 890 900
QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR

LPGKETMA
Length:908
Mass (Da):102,583
Last modified:November 1, 1996 - v1
Checksum:i5F34630524401E84
GO
Isoform 2 (identifier: Q13002-2) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     855-908: RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA → ESSIWLVPPYHPDTV

Show »
Length:869
Mass (Da):97,981
Checksum:iD85D8A5CB2B0C1FA
GO
Isoform 3 (identifier: Q13002-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     585-908: Missing.

Show »
Length:584
Mass (Da):66,108
Checksum:iE0E9EC92339921A1
GO
Isoform 4 (identifier: Q13002-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     547-622: Missing.

Show »
Length:832
Mass (Da):93,966
Checksum:iC0E9B91AC6AD6012
GO
Isoform 5 (identifier: Q13002-5) [UniParc]FASTAAdd to basket
Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     856-908: SFCSAMVEEL...RRLPGKETMA → AKTKLPQDYV...PSSSSLSSCS

Show »
Length:892
Mass (Da):100,243
Checksum:i50A477CB1265AF26
GO
Isoform 6 (identifier: Q13002-6) [UniParc]FASTAAdd to basket
Also known as: D

The sequence of this isoform differs from the canonical sequence as follows:
     509-695: Missing.
     855-908: RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA → ESSIWLVPPYHPDTV

Note: Seems to be specific for non-neuronal cells. May not function as active channel.
Show »
Length:682
Mass (Da):77,054
Checksum:iB08053B65BE3087F
GO
Isoform 7 (identifier: Q13002-7) [UniParc]FASTAAdd to basket
Also known as: E

The sequence of this isoform differs from the canonical sequence as follows:
     510-714: Missing.
     856-908: SFCSAMVEEL...RRLPGKETMA → AKTKLPQDYV...PSSSSLSSCS

Note: Seems to be specific for non-neuronal cells. May not function as active channel.
Show »
Length:687
Mass (Da):77,112
Checksum:i5BBD1224CA1A5FCC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20L → P in CAC81020 (Ref. 3) Curated1
Sequence conflicti20L → P in ADH93570 (PubMed:20230879).Curated1
Sequence conflicti20L → P in ADH93571 (PubMed:20230879).Curated1
Sequence conflicti20L → P in ADH93572 (PubMed:20230879).Curated1
Sequence conflicti20L → P in ADH93573 (PubMed:20230879).Curated1
Sequence conflicti789G → S (PubMed:8034316).Curated1

RNA editingi

Edited at positions 567, 571 and 621.1 Publication
Partially edited. The presence of Gln at position 621 (non-edited) determines channels with low calcium permeability, whereas Arg (edited) determines a higher calcium permeability especially if the preceding sites are fully edited. This receptor is nearly completely edited in all gray matter structures (90% of the receptors), whereas much less edited in the white matter (10% of the receptors).

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035694187E → Q in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_000305567I → V in RNA edited version. 1
Natural variantiVAR_000306571Y → C in RNA edited version. 1
Natural variantiVAR_000307621Q → R in RNA edited version. 1
Natural variantiVAR_049186766V → I.Corresponds to variant rs3213608dbSNPEnsembl.1
Natural variantiVAR_037633867M → I.Corresponds to variant rs2235076dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044388509 – 695Missing in isoform 6. 1 PublicationAdd BLAST187
Alternative sequenceiVSP_044389510 – 714Missing in isoform 7. 1 PublicationAdd BLAST205
Alternative sequenceiVSP_022334547 – 622Missing in isoform 4. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_022337585 – 908Missing in isoform 3. 1 PublicationAdd BLAST324
Alternative sequenceiVSP_022335855 – 908RSFCS…KETMA → ESSIWLVPPYHPDTV in isoform 2 and isoform 6. 2 PublicationsAdd BLAST54
Alternative sequenceiVSP_022336856 – 908SFCSA…KETMA → AKTKLPQDYVFLPILESVSI STVLSSSPSSSSLSSCS in isoform 5 and isoform 7. 2 PublicationsAdd BLAST53

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16126 mRNA. Translation: AAC50420.1.
AJ252246 mRNA. Translation: CAC81020.1.
AJ301608 mRNA. Translation: CAC67485.1.
AJ301609 mRNA. Translation: CAC67486.1.
AJ301610 mRNA. Translation: CAC67487.1.
HM149335 mRNA. Translation: ADH93569.1.
HM149336 mRNA. Translation: ADH93570.1.
HM149337 mRNA. Translation: ADH93571.1.
HM149338 mRNA. Translation: ADH93572.1.
HM149339 mRNA. Translation: ADH93573.1.
AL109919 Genomic DNA. No translation available.
AP002528 Genomic DNA. No translation available.
AP002529 Genomic DNA. No translation available.
AP002530 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48448.1.
CCDSiCCDS5048.1. [Q13002-1]
CCDS5049.1. [Q13002-2]
CCDS55045.1. [Q13002-5]
PIRiA54260.
RefSeqiNP_001159719.1. NM_001166247.1. [Q13002-5]
NP_068775.1. NM_021956.4. [Q13002-1]
NP_786944.1. NM_175768.3. [Q13002-2]
XP_005267002.1. XM_005266945.2. [Q13002-1]
XP_011534079.1. XM_011535777.2. [Q13002-5]
XP_011534080.1. XM_011535778.2. [Q13002-2]
UniGeneiHs.98262.

Genome annotation databases

EnsembliENST00000369138; ENSP00000358134; ENSG00000164418. [Q13002-5]
ENST00000413795; ENSP00000405596; ENSG00000164418. [Q13002-2]
ENST00000421544; ENSP00000397026; ENSG00000164418. [Q13002-1]
GeneIDi2898.
KEGGihsa:2898.
UCSCiuc003pqo.5. human. [Q13002-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16126 mRNA. Translation: AAC50420.1.
AJ252246 mRNA. Translation: CAC81020.1.
AJ301608 mRNA. Translation: CAC67485.1.
AJ301609 mRNA. Translation: CAC67486.1.
AJ301610 mRNA. Translation: CAC67487.1.
HM149335 mRNA. Translation: ADH93569.1.
HM149336 mRNA. Translation: ADH93570.1.
HM149337 mRNA. Translation: ADH93571.1.
HM149338 mRNA. Translation: ADH93572.1.
HM149339 mRNA. Translation: ADH93573.1.
AL109919 Genomic DNA. No translation available.
AP002528 Genomic DNA. No translation available.
AP002529 Genomic DNA. No translation available.
AP002530 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48448.1.
CCDSiCCDS5048.1. [Q13002-1]
CCDS5049.1. [Q13002-2]
CCDS55045.1. [Q13002-5]
PIRiA54260.
RefSeqiNP_001159719.1. NM_001166247.1. [Q13002-5]
NP_068775.1. NM_021956.4. [Q13002-1]
NP_786944.1. NM_175768.3. [Q13002-2]
XP_005267002.1. XM_005266945.2. [Q13002-1]
XP_011534079.1. XM_011535777.2. [Q13002-5]
XP_011534080.1. XM_011535778.2. [Q13002-2]
UniGeneiHs.98262.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QXMX-ray1.65A/B429-544[»]
A/B667-806[»]
5CMMX-ray1.27A667-806[»]
ProteinModelPortaliQ13002.
SMRiQ13002.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109155. 13 interactors.
IntActiQ13002. 2 interactors.
STRINGi9606.ENSP00000397026.

Chemistry databases

BindingDBiQ13002.
ChEMBLiCHEMBL3683.
DrugBankiDB01351. Amobarbital.
DB01352. Aprobarbital.
DB00237. Butabarbital.
DB00241. Butalbital.
DB01353. Butethal.
DB01354. Heptabarbital.
DB01355. Hexobarbital.
DB00849. Methylphenobarbital.
DB00312. Pentobarbital.
DB01174. Phenobarbital.
DB00794. Primidone.
DB00418. Secobarbital.
DB00306. Talbutal.
DB00599. Thiopental.
GuidetoPHARMACOLOGYi451.

PTM databases

iPTMnetiQ13002.
PhosphoSitePlusiQ13002.
SwissPalmiQ13002.

Polymorphism and mutation databases

BioMutaiGRIK2.
DMDMi2492627.

Proteomic databases

MaxQBiQ13002.
PaxDbiQ13002.
PeptideAtlasiQ13002.
PRIDEiQ13002.

Protocols and materials databases

DNASUi2898.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369138; ENSP00000358134; ENSG00000164418. [Q13002-5]
ENST00000413795; ENSP00000405596; ENSG00000164418. [Q13002-2]
ENST00000421544; ENSP00000397026; ENSG00000164418. [Q13002-1]
GeneIDi2898.
KEGGihsa:2898.
UCSCiuc003pqo.5. human. [Q13002-1]

Organism-specific databases

CTDi2898.
DisGeNETi2898.
GeneCardsiGRIK2.
H-InvDBHIX0006094.
HGNCiHGNC:4580. GRIK2.
HPAiCAB022463.
HPA014395.
HPA014623.
MalaCardsiGRIK2.
MIMi138244. gene.
611092. phenotype.
neXtProtiNX_Q13002.
OpenTargetsiENSG00000164418.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA164741600.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiQ13002.
KOiK05202.
OMAiVFRCTIR.
OrthoDBiEOG091G02LN.
PhylomeDBiQ13002.
TreeFamiTF334668.

Enzyme and pathway databases

ReactomeiR-HSA-451307. Activation of Na-permeable Kainate Receptors.
R-HSA-451308. Activation of Ca-permeable Kainate Receptor.
SignaLinkiQ13002.
SIGNORiQ13002.

Miscellaneous databases

GeneWikiiGRIK2.
GenomeRNAii2898.
PROiQ13002.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164418.
CleanExiHS_GRIK2.
ExpressionAtlasiQ13002. baseline and differential.
GenevisibleiQ13002. HS.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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.
ProtoNetiSearch...

Entry informationi

Entry nameiGRIK2_HUMAN
AccessioniPrimary (citable) accession number: Q13002
Secondary accession number(s): A6NMY9
, B5MCV0, D7RWZ3, D7RWZ4, D7RWZ5, D7RWZ6, D7RWZ7, Q8WWS1, Q96KS6, Q96KS7, Q96KS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 168 of the entry and version 1 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 domoate > kainate > quisqualate > 6-cyano-7-nitroquinoxaline-2,3-dione > L-glutamate = 6,7-dinitroquinoxaline-2,3-dione > dihydrokainate.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.