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Q13002 (GRIK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GRIK2
Synonyms:GLUR6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein.

Tissue specificity

Expression is higher in cerebellum than in cerebral cortex.

Post-translational modification

Sumoylation mediates kainate receptor-mediated endocytosis and regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and desumoylated by SENP1 By similarity. Ref.11

Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome By similarity.

Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation. Ref.11

Involvement in disease

Mental retardation, autosomal recessive 6 (MRT6) [MIM:611092]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

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.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK2 subfamily. [View classification]

RNA editing

Edited at positions 567, 571 and 621.
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). Ref.8 Ref.9

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
RNA editing
   DiseaseMental retardation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

glutamate receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

intracellular protein transport

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 15537878. Source: UniProtKB

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of inhibitory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of short-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 15537878. Source: UniProtKB

regulation of synaptic transmission

Inferred from direct assay PubMed 15537878. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

transport

Non-traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

kainate selective glutamate receptor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionextracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

kainate selective glutamate receptor activity

Inferred from direct assay PubMed 15537878. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13002-1)

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.
Isoform 2 (identifier: Q13002-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     855-908: RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA → ESSIWLVPPYHPDTV
Isoform 3 (identifier: Q13002-3)

The sequence of this isoform differs from the canonical sequence as follows:
     585-908: Missing.
Isoform 4 (identifier: Q13002-4)

The sequence of this isoform differs from the canonical sequence as follows:
     547-622: Missing.
Isoform 5 (identifier: Q13002-5)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     856-908: SFCSAMVEEL...RRLPGKETMA → AKTKLPQDYV...PSSSSLSSCS
Isoform 6 (identifier: Q13002-6)

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.
Isoform 7 (identifier: Q13002-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 908877Glutamate receptor ionotropic, kainate 2
PRO_0000011544

Regions

Topological domain32 – 561530Extracellular Potential
Transmembrane562 – 58221Helical; Potential
Topological domain583 – 63553Cytoplasmic Potential
Transmembrane636 – 65621Helical; Potential
Topological domain657 – 819163Extracellular Potential
Transmembrane820 – 84021Helical; Potential
Topological domain841 – 90868Cytoplasmic Potential
Region516 – 5183Glutamate binding By similarity
Region689 – 6902Glutamate binding By similarity

Sites

Binding site5231Glutamate By similarity
Binding site7381Glutamate By similarity

Amino acid modifications

Modified residue8461Phosphoserine; by PKC Ref.11
Modified residue8681Phosphoserine; by PKC Ref.11
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 347 By similarity
Cross-link886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.11

Natural variations

Alternative sequence509 – 695187Missing in isoform 6.
VSP_044388
Alternative sequence510 – 714205Missing in isoform 7.
VSP_044389
Alternative sequence547 – 62276Missing in isoform 4.
VSP_022334
Alternative sequence585 – 908324Missing in isoform 3.
VSP_022337
Alternative sequence855 – 90854RSFCS…KETMA → ESSIWLVPPYHPDTV in isoform 2 and isoform 6.
VSP_022335
Alternative sequence856 – 90853SFCSA…KETMA → AKTKLPQDYVFLPILESVSI STVLSSSPSSSSLSSCS in isoform 5 and isoform 7.
VSP_022336
Natural variant1871E → Q in a breast cancer sample; somatic mutation. Ref.13
VAR_035694
Natural variant5671I → V in RNA edited version.
VAR_000305
Natural variant5711Y → C in RNA edited version.
VAR_000306
Natural variant6211Q → R in RNA edited version.
VAR_000307
Natural variant7661V → I.
Corresponds to variant rs3213608 [ dbSNP | Ensembl ].
VAR_049186
Natural variant8671M → I.
Corresponds to variant rs2235076 [ dbSNP | Ensembl ].
VAR_037633

Experimental info

Sequence conflict201L → P in CAC81020. Ref.3
Sequence conflict201L → P in ADH93570. Ref.5
Sequence conflict201L → P in ADH93571. Ref.5
Sequence conflict201L → P in ADH93572. Ref.5
Sequence conflict201L → P in ADH93573. Ref.5
Sequence conflict7891G → S Ref.2

Secondary structure

................................................... 908
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5F34630524401E84

FASTA908102,583
        10         20         30         40         50         60 
MKIIFPILSN PVFRRTVKLL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM GAEELAFRFA 

        70         80         90        100        110        120 
VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS LGVAAIFGPS HSSSANAVQS 

       130        140        150        160        170        180 
ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST 

       190        200        210        220        230        240 
GLIRLQELIK APSRYNLRLK IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK 

       250        260        270        280        290        300 
QALAMGMMTE YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER 

       310        320        330        340        350        360 
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH KPWRFGTRFM 

       370        380        390        400        410        420 
SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE KIGTWDPASG LNMTESQKGK 

       430        440        450        460        470        480 
PANITDSLSN RSLIVTTILE EPYVLFKKSD KPLYGNDRFE GYCIDLLREL STILGFTYEI 

       490        500        510        520        530        540 
RLVEDGKYGA QDDANGQWNG MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI 

       550        560        570        580        590        600 
LYRKPNGTNP GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD 

       610        620        630        640        650        660 
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT 

       670        680        690        700        710        720 
VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS TYDKMWAFMS SRRQSVLVKS 

       730        740        750        760        770        780 
NEEGIQRVLT SDYAFLMEST TIEFVTQRNC NLTQIGGLID SKGYGVGTPM GSPYRDKITI 

       790        800        810        820        830        840 
AILQLQEEGK LHMMKEKWWR GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG 

       850        860        870        880        890        900 
EFLYKSKKNA QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR 


LPGKETMA 

« Hide

Isoform 2 (B) [UniParc].

Checksum: D85D8A5CB2B0C1FA
Show »

FASTA86997,981
Isoform 3 [UniParc].

Checksum: E0E9EC92339921A1
Show »

FASTA58466,108
Isoform 4 [UniParc].

Checksum: C0E9B91AC6AD6012
Show »

FASTA83293,966
Isoform 5 (C) [UniParc].

Checksum: 50A477CB1265AF26
Show »

FASTA892100,243
Isoform 6 (D) [UniParc].

Checksum: B08053B65BE3087F
Show »

FASTA68277,054
Isoform 7 (E) [UniParc].

Checksum: 5BBD1224CA1A5FCC
Show »

FASTA68777,112

References

« Hide 'large scale' references
[1]"Functional expression and pharmacological characterization of the human EAA4 (GluR6) glutamate receptor: a kainate selective channel subunit."
Hoo K.H., Nutt S.L., Fletcher E.J., Elliott C.E., Korczak B., Deverill R.M., Rampersad V., Fantaske R.P., Kamboj R.K.
Recept. Channels 2:327-337(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[2]"Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment."
Paschen W., Blackstone C.D., Huganir R.L., Ross C.A.
Genomics 20:435-440(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Myeloid progenitor cell growth and apoptosis involves know and cell-specific ionotropic glutamate receptor."
Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]"Genomic organization of the human GRIK2 gene and characterization of multiple splicing variants."
Barbon A., Vallini I., Barlati S.
Gene 274:187-197(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), GENE ORGANIZATION.
[5]"Novel spliced variants of ionotropic glutamate receptor GluR6 in normal human fibroblast and brain cells are transcribed by tissue specific promoters."
Zhawar V.K., Kaur G., deRiel J.K., Kaur G.P., Kandpal R.P., Athwal R.S.
Gene 459:1-10(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7), ALTERNATIVE SPLICING.
Tissue: Brain.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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].
[8]"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 621.
[9]"RNA editing of human kainate receptor subunits."
Nutt S.L., Kamboj R.K.
NeuroReport 5:2625-2629(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITIONS 567; 571 AND 621.
Tissue: Brain.
[10]"The PDZ1 domain of SAP90. Characterization of structure and binding."
Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P., Marshall J., Mierke D.F.
J. Biol. Chem. 277:6967-6973(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG4.
[11]"Modification and movement: Phosphorylation and SUMOylation regulate endocytosis of GluK2-containing kainate receptors."
Wilkinson K.A., Konopacki F., Henley J.M.
Commun. Integr. Biol. 5:223-226(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-846 AND SER-868, SUMOYLATION AT LYS-886.
[12]"Binding and selectivity of the marine toxin neodysiherbaine A and its synthetic analogues to GluK1 and GluK2 kainate receptors."
Unno M., Shinohara M., Takayama K., Tanaka H., Teruya K., Doh-ura K., Sakai R., Sasaki M., Ikeda-Saito M.
J. Mol. Biol. 413:667-683(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEX WITH AGONIST.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-187.
[14]"A defect in the ionotropic glutamate receptor 6 gene (GRIK2) is associated with autosomal recessive mental retardation."
Motazacker M.M., Rost B.R., Hucho T., Garshasbi M., Kahrizi K., Ullmann R., Abedini S.S., Nieh S.E., Amini S.H., Goswami C., Tzschach A., Jensen L.R., Schmitz D., Ropers H.H., Najmabadi H., Kuss A.W.
Am. J. Hum. Genet. 81:792-798(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRT6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5048.1. [Q13002-1]
CCDS5049.1. [Q13002-2]
CCDS55045.1. [Q13002-5]
PIRA54260.
RefSeqNP_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_005266945.1. [Q13002-1]
XP_006715528.1. XM_006715465.1. [Q13002-5]
UniGeneHs.98262.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QXMX-ray1.65A/B429-544[»]
A/B667-806[»]
ProteinModelPortalQ13002.
SMRQ13002. Positions 33-415, 430-805.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109155. 12 interactions.
IntActQ13002. 2 interactions.
STRING9606.ENSP00000397026.

Chemistry

BindingDBQ13002.
ChEMBLCHEMBL3683.
DrugBankDB00142. L-Glutamic Acid.
GuidetoPHARMACOLOGY451.

PTM databases

PhosphoSiteQ13002.

Polymorphism databases

DMDM2492627.

Proteomic databases

MaxQBQ13002.
PaxDbQ13002.
PRIDEQ13002.

Protocols and materials databases

DNASU2898.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318991; ENSP00000313276; ENSG00000164418. [Q13002-2]
ENST00000369137; ENSP00000358133; ENSG00000164418. [Q13002-4]
ENST00000369138; ENSP00000358134; ENSG00000164418. [Q13002-5]
ENST00000413795; ENSP00000405596; ENSG00000164418. [Q13002-2]
ENST00000421544; ENSP00000397026; ENSG00000164418. [Q13002-1]
GeneID2898.
KEGGhsa:2898.
UCSCuc003pqn.3. human. [Q13002-1]
uc003pqo.4. human. [Q13002-2]
uc010kcw.3. human. [Q13002-5]
uc021zdk.1. human. [Q13002-6]

Organism-specific databases

CTD2898.
GeneCardsGC06P101846.
H-InvDBHIX0006094.
HGNCHGNC:4580. GRIK2.
HPACAB022463.
HPA014395.
HPA014623.
MIM138244. gene.
611092. phenotype.
neXtProtNX_Q13002.
Orphanet88616. Autosomal recessive nonsyndromic intellectual disability.
PharmGKBPA164741600.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316680.
HOVERGENHBG051839.
InParanoidQ13002.
KOK05202.
OMAVNGQWNG.
OrthoDBEOG71G9W6.
PhylomeDBQ13002.
TreeFamTF334668.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ13002.

Gene expression databases

ArrayExpressQ13002.
BgeeQ13002.
CleanExHS_GRIK2.
GenevestigatorQ13002.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

GeneWikiGRIK2.
GenomeRNAi2898.
NextBio11469.
PROQ13002.
SOURCESearch...

Entry information

Entry nameGRIK2_HUMAN
AccessionPrimary (citable) accession number: Q13002
Secondary accession number(s): A6NMY9 expand/collapse secondary AC list , B5MCV0, D7RWZ3, D7RWZ4, D7RWZ5, D7RWZ6, D7RWZ7, Q8WWS1, Q96KS6, Q96KS7, Q96KS8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM