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P39086

- GRIK1_HUMAN

UniProt

P39086 - GRIK1_HUMAN

Protein

Glutamate receptor ionotropic, kainate 1

Gene

GRIK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei538 – 5381GlutamateBy similarity
    Binding sitei753 – 7531GlutamateBy similarity

    GO - Molecular functioni

    1. extracellular-glutamate-gated ion channel activity Source: RefGenome
    2. kainate selective glutamate receptor activity Source: UniProtKB

    GO - Biological processi

    1. adult behavior Source: Ensembl
    2. behavioral response to pain Source: Ensembl
    3. central nervous system development Source: ProtInc
    4. glutamate receptor signaling pathway Source: ProtInc
    5. ionotropic glutamate receptor signaling pathway Source: GOC
    6. ion transmembrane transport Source: GOC
    7. negative regulation of synaptic transmission, glutamatergic Source: Ensembl
    8. nervous system development Source: ProtInc
    9. positive regulation of gamma-aminobutyric acid secretion Source: Ensembl
    10. positive regulation of synaptic transmission, GABAergic Source: Ensembl
    11. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    12. regulation of inhibitory postsynaptic membrane potential Source: Ensembl
    13. regulation of synaptic transmission, glutamatergic Source: UniProtKB
    14. synaptic transmission Source: Reactome
    15. synaptic transmission, glutamatergic Source: RefGenome
    16. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_21343. Activation of Na-permeable Kainate Receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    SignaLinkiP39086.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, kainate 1
    Short name:
    GluK1
    Alternative name(s):
    Excitatory amino acid receptor 3
    Short name:
    EAA3
    Glutamate receptor 5
    Short name:
    GluR-5
    Short name:
    GluR5
    Gene namesi
    Name:GRIK1
    Synonyms:GLUR5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:4579. GRIK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dendrite Source: RefGenome
    3. integral component of plasma membrane Source: ProtInc
    4. kainate selective glutamate receptor complex Source: RefGenome
    5. plasma membrane Source: Reactome
    6. postsynaptic membrane Source: RefGenome
    7. presynaptic membrane Source: RefGenome

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28973.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 918888Glutamate receptor ionotropic, kainate 1PRO_0000011541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
    Modified residuei725 – 7251Phosphoserine; by PKCSequence Analysis
    Modified residuei761 – 7611Phosphothreonine; by PKCSequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP39086.
    PRIDEiP39086.

    PTM databases

    PhosphoSiteiP39086.

    Expressioni

    Tissue specificityi

    Most abundant in the cerebellum and the suprachiasmatic nuclei (SCN) of the hypothalamus.

    Gene expression databases

    ArrayExpressiP39086.
    BgeeiP39086.
    CleanExiHS_GRIK1.
    GenevestigatoriP39086.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers Probable. The unedited version (Q) assembles into a functional kainate-gated homomeric channel, whereas the edited version (R) is unable to produce channel activity when expressed alone. Both edited and unedited versions can form functional channels with GRIK4 and GRIK5. Interacts with KLHL17 By similarity.By similarityCurated

    Protein-protein interaction databases

    BioGridi109154. 6 interactions.
    STRINGi9606.ENSP00000382791.

    Structurei

    Secondary structure

    1
    918
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi449 – 4535
    Turni457 – 4593
    Beta strandi460 – 4623
    Helixi471 – 4744
    Beta strandi475 – 4773
    Helixi478 – 49013
    Beta strandi494 – 4985
    Helixi515 – 5217
    Beta strandi526 – 5283
    Helixi536 – 5394
    Beta strandi542 – 5443
    Beta strandi548 – 5514
    Beta strandi553 – 5597
    Helixi686 – 6916
    Beta strandi693 – 6986
    Helixi704 – 7118
    Helixi715 – 72612
    Helixi728 – 7314
    Beta strandi732 – 7354
    Helixi736 – 74510
    Beta strandi746 – 7538
    Helixi754 – 7618
    Beta strandi767 – 7715
    Beta strandi777 – 7793
    Beta strandi782 – 7843
    Helixi790 – 80213
    Helixi805 – 81410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZNSX-ray2.00A445-559[»]
    A682-820[»]
    2ZNTX-ray1.60A445-559[»]
    A682-820[»]
    2ZNUX-ray1.80A445-559[»]
    A682-820[»]
    3FUZX-ray1.65A/B445-559[»]
    A/B682-820[»]
    3FV1X-ray1.50A/B445-559[»]
    A/B682-820[»]
    3FV2X-ray1.50A/B445-559[»]
    A/B682-820[»]
    3FVGX-ray1.50A/B445-559[»]
    A/B682-820[»]
    3FVKX-ray1.50A/B445-559[»]
    A/B682-820[»]
    3FVNX-ray1.50A/B445-559[»]
    A/B682-820[»]
    3FVOX-ray1.50A/B445-559[»]
    A/B682-820[»]
    4MF3X-ray3.00A/B443-822[»]
    ProteinModelPortaliP39086.
    SMRiP39086. Positions 35-860.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39086.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 576546ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini598 – 65356CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini675 – 834160ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini856 – 91863CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei577 – 59721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei654 – 67421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei835 – 85521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni531 – 5333Glutamate bindingBy similarity
    Regioni704 – 7052Glutamate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    HOGENOMiHOG000234371.
    HOVERGENiHBG051839.
    KOiK05201.
    PhylomeDBiP39086.
    TreeFamiTF334668.

    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P39086-1) [UniParc]FASTAAdd to Basket

    Also known as: GluR5-1D

    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

    MEHGTLLAQP GLWTRDTSWA LLYFLCYILP QTAPQVLRIG GIFETVENEP    50
    VNVEELAFKF AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL 100
    ALGVAALFGP SHSSSVSAVQ SICNALEVPH IQTRWKHPSV DNKDLFYINL 150
    YPDYAAISRA ILDLVLYYNW KTVTVVYEDS TGLIRLQELI KAPSRYNIKI 200
    KIRQLPSGNK DAKPLLKEMK KGKEFYVIFD CSHETAAEIL KQILFMGMMT 250
    EYYHYFFTTL DLFALDLELY RYSGVNMTGF RLLNIDNPHV SSIIEKWSME 300
    RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR 350
    HKPWRLGPRF MNLIKEARWD GLTGHITFNK TNGLRKDFDL DIISLKEEGT 400
    EKAAGEVSKH LYKVWKKIGI WNSNSGLNMT DSNKDKSSNI TDSLANRTLI 450
    VTTILEEPYV MYRKSDKPLY GNDRFEGYCL DLLKELSNIL GFIYDVKLVP 500
    DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK VIDFSKPFMT 550
    LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 600
    PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI 650
    VGGIWWFFTL IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV 700
    RDGSTMTFFK KSKISTYEKM WAFMSSRQQT ALVRNSDEGI QRVLTTDYAL 750
    LMESTSIEYV TQRNCNLTQI GGLIDSKGYG VGTPIGSPYR DKITIAILQL 800
    QEEGKLHMMK EKWWRGNGCP EEDNKEASAL GVENIGGIFI VLAAGLVLSV 850
    FVAIGEFIYK SRKNNDIEQA FCFFYGLQCK QTHPTNSTSG TTLSTDLECG 900
    KLIREERGIR KQSSVHTV 918
    Length:918
    Mass (Da):103,981
    Last modified:February 1, 1995 - v1
    Checksum:i0EB8DB6356599002
    GO
    Isoform 2 (identifier: P39086-2) [UniParc]FASTAAdd to Basket

    Also known as: EAA3A

    The sequence of this isoform differs from the canonical sequence as follows:
         402-416: Missing.
         870-918: AFCFFYGLQC...IRKQSSVHTV → CLSFNAIMEE...RRTQRKETVA

    Show »
    Length:905
    Mass (Da):102,631
    Checksum:i6D9350206E5A2E9C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811R → G in AAA95961. (PubMed:8589992)Curated

    RNA editingi

    Partially edited.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti332 – 3321A → V.1 Publication
    Corresponds to variant rs143252117 [ dbSNP | Ensembl ].
    VAR_012751
    Natural varianti636 – 6361Q → R in RNA edited version.
    VAR_000304
    Natural varianti757 – 7571I → V.
    Corresponds to variant rs363494 [ dbSNP | Ensembl ].
    VAR_012041
    Natural varianti862 – 8621R → Q.1 Publication
    VAR_012752
    Natural varianti870 – 8701A → V.
    Corresponds to variant rs363503 [ dbSNP | Ensembl ].
    VAR_012042
    Natural varianti902 – 9021L → S.1 Publication
    Corresponds to variant rs363504 [ dbSNP | Ensembl ].
    VAR_012043

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei402 – 41615Missing in isoform 2. 2 PublicationsVSP_000127Add
    BLAST
    Alternative sequencei870 – 91849AFCFF…SVHTV → CLSFNAIMEELGISLKNQKK IKKKSRTKGKSSFTSILTCH QRRTQRKETVA in isoform 2. 2 PublicationsVSP_000128Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19058 mRNA. Translation: AAA52568.1.
    U16125 mRNA. Translation: AAA95961.1.
    AJ249208 mRNA. Translation: CAC80546.1.
    CCDSiCCDS33530.1. [P39086-2]
    CCDS42913.1. [P39086-1]
    PIRiI58178.
    RefSeqiNP_000821.1. NM_000830.3. [P39086-1]
    NP_783300.1. NM_175611.2. [P39086-2]
    UniGeneiHs.664641.

    Genome annotation databases

    EnsembliENST00000389125; ENSP00000373777; ENSG00000171189. [P39086-2]
    ENST00000399907; ENSP00000382791; ENSG00000171189. [P39086-1]
    GeneIDi2897.
    KEGGihsa:2897.
    UCSCiuc002ynn.3. human. [P39086-2]
    uc002yno.1. human. [P39086-1]

    Polymorphism databases

    DMDMi729597.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19058 mRNA. Translation: AAA52568.1 .
    U16125 mRNA. Translation: AAA95961.1 .
    AJ249208 mRNA. Translation: CAC80546.1 .
    CCDSi CCDS33530.1. [P39086-2 ]
    CCDS42913.1. [P39086-1 ]
    PIRi I58178.
    RefSeqi NP_000821.1. NM_000830.3. [P39086-1 ]
    NP_783300.1. NM_175611.2. [P39086-2 ]
    UniGenei Hs.664641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZNS X-ray 2.00 A 445-559 [» ]
    A 682-820 [» ]
    2ZNT X-ray 1.60 A 445-559 [» ]
    A 682-820 [» ]
    2ZNU X-ray 1.80 A 445-559 [» ]
    A 682-820 [» ]
    3FUZ X-ray 1.65 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FV1 X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FV2 X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FVG X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FVK X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FVN X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3FVO X-ray 1.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    4MF3 X-ray 3.00 A/B 443-822 [» ]
    ProteinModelPortali P39086.
    SMRi P39086. Positions 35-860.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109154. 6 interactions.
    STRINGi 9606.ENSP00000382791.

    Chemistry

    BindingDBi P39086.
    ChEMBLi CHEMBL2109241.
    DrugBanki DB00142. L-Glutamic Acid.
    DB00273. Topiramate.
    GuidetoPHARMACOLOGYi 450.

    PTM databases

    PhosphoSitei P39086.

    Polymorphism databases

    DMDMi 729597.

    Proteomic databases

    PaxDbi P39086.
    PRIDEi P39086.

    Protocols and materials databases

    DNASUi 2897.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389125 ; ENSP00000373777 ; ENSG00000171189 . [P39086-2 ]
    ENST00000399907 ; ENSP00000382791 ; ENSG00000171189 . [P39086-1 ]
    GeneIDi 2897.
    KEGGi hsa:2897.
    UCSCi uc002ynn.3. human. [P39086-2 ]
    uc002yno.1. human. [P39086-1 ]

    Organism-specific databases

    CTDi 2897.
    GeneCardsi GC21M030909.
    HGNCi HGNC:4579. GRIK1.
    MIMi 138245. gene.
    neXtProti NX_P39086.
    PharmGKBi PA28973.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316680.
    HOGENOMi HOG000234371.
    HOVERGENi HBG051839.
    KOi K05201.
    PhylomeDBi P39086.
    TreeFami TF334668.

    Enzyme and pathway databases

    Reactomei REACT_21343. Activation of Na-permeable Kainate Receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    SignaLinki P39086.

    Miscellaneous databases

    EvolutionaryTracei P39086.
    GeneWikii GRIK1.
    GenomeRNAii 2897.
    NextBioi 11463.
    PROi P39086.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39086.
    Bgeei P39086.
    CleanExi HS_GRIK1.
    Genevestigatori P39086.

    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

    1. "Expression and novel subunit isoforms of glutamate receptor genes GluR5 and GluR6."
      Gregor P., O'Hara B.F., Yang X., Uhl G.R.
      NeuroReport 4:1343-1346(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    2. "cDNA cloning and functional properties of human glutamate receptor EAA3 (GluR5) in homomeric and heteromeric configuration."
      Korczak B., Nutt S.L., Fletcher E.J., Hoo K.H., Elliott C.E., Rampersad V., McWhinnie E.A., Kamboj R.K.
      Recept. Channels 3:41-49(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    3. "Myeloid progenitor cell growth and apoptosis involves known and cell-specific ionotropic glutamate receptors."
      Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Erythroleukemia.
    4. "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 POSITION 636.
      Tissue: Brain.
    5. "Association study of polymorphisms in the GluR5 kainate receptor gene (GRIK1) with schizophrenia."
      Shibata H., Joo A., Fujii Y., Tani A., Makino C., Hirata N., Kikuta R., Ninomiya H., Tashiro N., Fukumaki Y.
      Psychiatr. Genet. 11:139-144(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-332; GLN-862 AND SER-902.

    Entry informationi

    Entry nameiGRIK1_HUMAN
    AccessioniPrimary (citable) accession number: P39086
    Secondary accession number(s): Q13001, Q86SU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 147 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 > L-glutamate = quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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