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Protein

Glutamate receptor 2

Gene

Gria2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (PubMed:16037816).15 Publications

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei471Glutamate1 Publication1
Binding sitei501Kainate; via amide nitrogen1 Publication1
Binding sitei506Glutamate1 Publication1
Binding sitei506Kainate1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei654Crucial to convey clamshell closure to channel opening1 Publication1
Binding sitei675Kainate; via amide nitrogen1 Publication1
Binding sitei676Kainate; via amide nitrogen1 Publication1
Binding sitei726Glutamate1 Publication1
Binding sitei726Kainate1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamate receptor 2Curated
Short name:
GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name:
GluA21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gria2Imported
Synonyms:Glur2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
61862 Gria2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 543ExtracellularAdd BLAST522
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei544 – 564HelicalAdd BLAST21
Topological domaini565 – 591CytoplasmicAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei592 – 607Helical; Pore-formingAdd BLAST16
Intramembranei608 – 6103
Topological domaini611 – 616Cytoplasmic6
Transmembranei617 – 637HelicalAdd BLAST21
Topological domaini638 – 812ExtracellularAdd BLAST175
Transmembranei813 – 833Helical; Name=M4Add BLAST21
Topological domaini834 – 883CytoplasmicAdd BLAST50

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi504L → Y: Promotes dimerization. Strongly reduced desensitization. 1 Publication1
Mutagenesisi775N → D: Increases rate of desensitization. 1 Publication1
Mutagenesisi851 – 852NP → AA: Strongly reduces interaction with NSF. 1 Publication2

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3503

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
445

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001153522 – 883Glutamate receptor 2Add BLAST862

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi78 ↔ 330
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi256N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi370N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi610S-palmitoyl cysteineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei683Phosphoserine; by PKC1 Publication1
Modified residuei717Phosphoserine; by PKG1 Publication1
Disulfide bondi739 ↔ 794
Lipidationi836S-palmitoyl cysteineBy similarity1
Modified residuei860PhosphoserineBy similarity1
Modified residuei863PhosphoserineBy similarity1
Modified residuei876Phosphotyrosine1 Publication1
Modified residuei880PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P19491

PRoteomics IDEntifications database

More...
PRIDEi
P19491

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19491

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P19491

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P19491

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in forebrain. Detected in dendrites of neuronal cells.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 8 to 14 day old animals. Detected at intermediate levels at day 42 (at protein level).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (By similarity). 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. Interacts with NSF via its C-terminus. Interacts with CACNG2, PRKCABP and GRIP2 (PubMed:27756895). Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ domain) (By similarity). Interacts with GRIA1 and SYNDIG1. 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). Interacts with LRFN1. Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5. Interacts with OLFM2 (By similarity). Interacts with AP4B1, AP4E1 and AP4M1; probably indirect it mediates the somatodendritic localization of GRIA2 in neurons (By similarity). Forms a complex with NSG1, GRIA2 and STX12; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (PubMed:16037816).By similarity18 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei474Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei681Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei773Interaction with the cone snail toxin Con-ikot-ikot1 Publication1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248250, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P19491

Database of interacting proteins

More...
DIPi
DIP-30952N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P19491

Protein interaction database and analysis system

More...
IntActi
P19491, 27 interactors

Molecular INTeraction database

More...
MINTi
P19491

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000062152

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P19491

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1883
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P19491

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P19491

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19491

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni499 – 501Glutamate binding3
Regioni675 – 676Glutamate binding2

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1054 Eukaryota
ENOG410XPSH LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234372

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051839

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P19491

KEGG Orthology (KO)

More...
KOi
K05198

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P19491

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00177 NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53822 SSF53822, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Flop (identifier: P19491-1) [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 TYRSLFQDLE
210 220 230 240 250
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI
260 270 280 290 300
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
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 SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD
810 820 830 840 850
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK
860 870 880
NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI
Length:883
Mass (Da):98,688
Last modified:July 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDEFA817027C1CCD1
GO
Isoform Flip (identifier: P19491-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     765-766: NA → TP
     775-775: N → S
     779-779: L → V
     796-800: SGGGD → AKDSG

Show »
Length:883
Mass (Da):98,745
Checksum:i3B70561B4F9E1C61
GO
Isoform 3 (identifier: P19491-3) [UniParc]FASTAAdd to basket
Also known as: Long

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

Show »
Length:901
Mass (Da):100,409
Checksum:i13CE9B51B120A799
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V914G3V914_RAT
Glutamate receptor 2
Gria2
883Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1LNE4F1LNE4_RAT
Glutamate receptor 2
Gria2
883Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section provides information relevant to all types of RNA editing events (conversion, insertion, deletion of nucleotides) that lead to one or more amino acid changes compared to the translation of the non-edited RNA version.<p><a href='/help/rna_editing' target='_top'>More...</a></p>RNA editingi

Edited at position 607.1 Publication
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 (By similarity).By similarity

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti607Q → R in RNA edited version. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000111765 – 766NA → TP in isoform Flip. 3 Publications2
Alternative sequenceiVSP_000112775N → S in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000113779L → V in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000114796 – 800SGGGD → AKDSG in isoform Flip. 3 Publications5
Alternative sequenceiVSP_029310848 – 883VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedAdd BLAST36

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M36419 mRNA Translation: AAA41244.1
M38061 mRNA Translation: AAC37652.1
M85035 mRNA Translation: AAA41240.1
X54655 mRNA Translation: CAA38465.1
AF164344 mRNA Translation: AAD51284.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S13677

NCBI Reference Sequences

More...
RefSeqi
NP_001077280.1, NM_001083811.1
NP_058957.1, NM_017261.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.91361

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29627

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29627

UCSC genome browser

More...
UCSCi
RGD:61862 rat [P19491-1]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36419 mRNA Translation: AAA41244.1
M38061 mRNA Translation: AAC37652.1
M85035 mRNA Translation: AAA41240.1
X54655 mRNA Translation: CAA38465.1
AF164344 mRNA Translation: AAD51284.1
PIRiS13677
RefSeqiNP_001077280.1, NM_001083811.1
NP_058957.1, NM_017261.2
UniGeneiRn.91361

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FTJX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1FTKX-ray1.60A404-528[»]
A653-796[»]
1FTLX-ray1.80A/B413-527[»]
A/B653-796[»]
1FTMX-ray1.70A/B/C413-527[»]
A/B/C653-796[»]
1FTOX-ray2.00A/B413-527[»]
A/B653-796[»]
1FW0X-ray1.90A413-527[»]
A653-796[»]
1GR2X-ray1.90A404-528[»]
A652-796[»]
1LB8X-ray2.30A/B413-527[»]
A/B653-796[»]
1LB9X-ray2.30A/B413-527[»]
A/B653-796[»]
1LBBX-ray2.10A413-527[»]
A653-796[»]
1LBCX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1M5BX-ray1.85A/B/C413-527[»]
A/B/C653-796[»]
1M5CX-ray1.65A413-527[»]
A653-796[»]
1M5DX-ray1.73A413-527[»]
A653-796[»]
1M5EX-ray1.46A/B/C413-527[»]
A/B/C653-796[»]
1M5FX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MM6X-ray2.15A/B413-527[»]
A/B653-796[»]
1MM7X-ray1.65A/B/C413-527[»]
A/B/C653-796[»]
1MQDX-ray1.46A/B/C/D413-527[»]
A/B/C/D653-794[»]
1MQGX-ray2.15A/B413-527[»]
A/B653-796[»]
1MQHX-ray1.80A413-527[»]
A653-796[»]
1MQIX-ray1.35A413-527[»]
A653-796[»]
1MQJX-ray1.65A413-527[»]
A653-796[»]
1MS7X-ray1.97A/B/C413-527[»]
A/B/C653-796[»]
1MXUX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1MXVX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MXWX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MXXX-ray2.00A/B/C413-527[»]
A/B/C653-796[»]
1MXYX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MXZX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY0X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY1X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY2X-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1MY3X-ray1.75A/B/C413-527[»]
A/B/C653-796[»]
1MY4X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1N0TX-ray2.10A/B/C/D413-527[»]
A/B/C/D653-796[»]
1NNKX-ray1.85A413-527[»]
A653-796[»]
1NNPX-ray1.90A/B413-527[»]
A/B653-796[»]
1P1NX-ray1.60A413-527[»]
A653-796[»]
1P1OX-ray1.60A413-527[»]
A653-796[»]
1P1QX-ray2.00A/B/C413-527[»]
A/B/C653-796[»]
1P1UX-ray2.00A/B413-527[»]
A/B653-796[»]
1P1WX-ray1.80A/B413-527[»]
A/B653-796[»]
1SYHX-ray1.80A413-527[»]
A653-796[»]
1SYIX-ray2.10A/B413-527[»]
A/B653-796[»]
1WVJX-ray1.75A413-527[»]
A653-796[»]
1XHYX-ray1.85A413-527[»]
A653-796[»]
2AIXX-ray2.17A413-527[»]
A653-796[»]
2AL4X-ray1.70A/B/C/D/E/F413-527[»]
A/B/C/D/E/F653-796[»]
2AL5X-ray1.65A/B413-527[»]
A/B653-796[»]
2ANJX-ray2.10A413-527[»]
A653-796[»]
2CMOX-ray2.65A/B413-527[»]
A/B653-796[»]
2GFEX-ray1.54A/B/C413-527[»]
A/B/C653-795[»]
2I3VX-ray2.40A/B/C/D413-527[»]
A/B/C/D655-794[»]
2I3WX-ray2.30A/B413-527[»]
A/B653-794[»]
2P2AX-ray2.26A/B413-527[»]
A/B653-796[»]
2UXAX-ray2.38A/B/C412-795[»]
2XX7X-ray2.20A/B/C413-527[»]
A/B/C653-795[»]
2XX8X-ray1.55A/B/C413-527[»]
A/B/C653-796[»]
2XX9X-ray1.97A/B/C413-527[»]
A/B/C653-796[»]
2XXHX-ray1.50A/B/C413-527[»]
A/B/C653-796[»]
2XXIX-ray1.60A/B/C413-527[»]
A/B/C653-796[»]
3B6QX-ray2.00A413-527[»]
A653-796[»]
3B6TX-ray2.10A413-527[»]
A653-796[»]
3B6WX-ray1.70A/B/C/D413-527[»]
A/B/C/D653-796[»]
3B7DX-ray2.50A/B/C/D/E/F/G/H413-527[»]
A/B/C/D/E/F/G/H653-794[»]
3BBRX-ray2.25A/B413-527[»]
A/B653-796[»]
3BFTX-ray2.27A/B/C413-527[»]
A/B/C653-796[»]
3BFUX-ray1.95A/B/C/D413-527[»]
A/B/C/D653-796[»]
3BKIX-ray1.87B/C/D/P413-527[»]
B/C/D/P653-796[»]
3DP6X-ray1.55A/B/C413-527[»]
A/B/C653-794[»]
3H03X-ray1.90A/B/D/G414-527[»]
A/B/D/G653-794[»]
3H06X-ray2.80B/E/G/H/J/L/N/P414-527[»]
B/E/G/H/J/L/N/P653-794[»]
3H5VX-ray2.33A/B/C21-404[»]
3H5WX-ray2.69A/B21-404[»]
3H6TX-ray2.25A/B/C413-527[»]
A/B/C653-796[»]
3H6UX-ray1.85A413-527[»]
A653-796[»]
3H6VX-ray2.10A/B413-527[»]
A/B653-796[»]
3H6WX-ray1.49A/B413-527[»]
A/B653-796[»]
3HSYX-ray1.75A/B25-400[»]
3IJOX-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3IJXX-ray2.88B/D/H414-527[»]
B/D/H653-794[»]
3IK6X-ray2.10B/E/H414-527[»]
B/E/H653-794[»]
3IL1X-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3ILTX-ray2.11B/E/H414-527[»]
B/E/H653-794[»]
3ILUX-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3KG2X-ray3.60A/B/C/D25-412[»]
A/B/C/D414-847[»]
3KGCX-ray1.55A/B414-527[»]
A/B654-795[»]
3LSFX-ray1.85B/E/H414-527[»]
B/E/H653-794[»]
3LSLX-ray2.12A/D/G414-527[»]
A/D/G653-794[»]
3M3LX-ray1.85A/D/G414-794[»]
3N6VX-ray3.20A/B/C/D/E/F27-400[»]
3O28X-ray2.00A413-527[»]
A653-795[»]
3O29X-ray2.02A413-527[»]
A653-795[»]
3O2AX-ray1.90A413-527[»]
A653-795[»]
3O2JX-ray1.95A/B22-400[»]
3O6GX-ray1.80A413-527[»]
A653-795[»]
3O6HX-ray2.10A413-527[»]
A653-795[»]
3O6IX-ray1.80A413-527[»]
A653-795[»]
3PD8X-ray2.48A/B/C413-527[»]
A/B/C653-795[»]
3PD9X-ray2.10A/B413-527[»]
A/B653-795[»]
3PMVX-ray1.80A413-527[»]
A653-795[»]
3PMWX-ray2.20A413-527[»]
A653-795[»]
3PMXX-ray1.87A413-527[»]
A653-795[»]
3RTFX-ray1.70B/D/F414-527[»]
B/D/F653-794[»]
3RTWX-ray2.10B/D/F414-527[»]
B/D/F653-794[»]
3T93X-ray1.91B/D/F414-527[»]
B/D/F653-794[»]
3T96X-ray1.87B/D/F414-527[»]
B/D/F653-794[»]
3T9HX-ray2.02B/D/F414-527[»]
B/D/F653-794[»]
3T9UX-ray1.97A/B/C414-527[»]
A/B/C653-794[»]
3T9VX-ray1.98A/B414-527[»]
A/B653-794[»]
3T9XX-ray1.82B/D/F414-527[»]
B/D/F653-794[»]
3TDJX-ray1.95A/B413-527[»]
A/B653-796[»]
3TKDX-ray1.45A/B413-527[»]
A/B653-795[»]
3TZAX-ray1.90A/B413-527[»]
A/B653-796[»]
4FATX-ray1.40A413-527[»]
A653-796[»]
4G8MX-ray2.05A/B413-527[»]
A/B653-796[»]
4GXSX-ray1.96B/D414-527[»]
B/D653-794[»]
4H8JX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
4IGTX-ray1.24A413-527[»]
A653-796[»]
4ISUX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-796[»]
4IY5X-ray2.00A/B413-527[»]
A/B653-796[»]
4IY6X-ray1.72A413-527[»]
A653-796[»]
4L17X-ray2.80A/C/E/G413-527[»]
A/C/E/G653-796[»]
4LZ5X-ray1.50A/B/C404-527[»]
A/B/C653-796[»]
4LZ7X-ray2.10A/B/C404-527[»]
A/B/C653-796[»]
4LZ8X-ray1.85A/B/C404-527[»]
A/B/C653-796[»]
4N07X-ray1.87A/B/C413-527[»]
A/B/C653-796[»]
4O3AX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
4O3BX-ray1.91A/B413-527[»]
A/B653-796[»]
4O3CX-ray1.50A413-527[»]
A653-796[»]
4Q30X-ray2.03B/D/F414-527[»]
B/D/F653-794[»]
4U1OX-ray1.85A413-527[»]
A653-796[»]
4U1WX-ray3.25A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U1XX-ray3.30A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1YX-ray3.90A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1ZX-ray1.94A413-527[»]
A653-796[»]
4U21X-ray1.39A/B413-527[»]
A/B654-796[»]
4U22X-ray1.44A413-527[»]
A653-796[»]
4U23X-ray1.67A413-527[»]
A653-796[»]
4U2PX-ray3.24A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2QX-ray3.52A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2RX-ray1.41A/B/C/D413-527[»]
A/B/C/D653-796[»]
4U4FX-ray4.79A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4GX-ray4.49A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4SX-ray1.90A/B413-527[»]
A/B653-796[»]
4U4XX-ray1.56A/B413-527[»]
A/B653-796[»]
4U5BX-ray3.50A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5CX-ray3.69A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5DX-ray3.58A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5EX-ray3.51A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5FX-ray3.70A/B/C/D25-412[»]
A/B/C/D414-850[»]
4UQ6electron microscopy12.80A/B/C/D22-847[»]
4UQJelectron microscopy10.40A/B/C/D22-847[»]
4UQKelectron microscopy16.40A/B/C/D22-847[»]
4X48X-ray1.89A/B/C413-527[»]
A/B/C653-796[»]
4YMAX-ray1.90A/B413-527[»]
A/B653-797[»]
4YU0X-ray1.26A/B413-527[»]
A/B653-796[»]
4Z0IX-ray1.45A/B413-527[»]
A/B653-796[»]
5BUUX-ray2.07A/B413-527[»]
A/B653-796[»]
5CBRX-ray2.00A413-527[»]
A653-797[»]
5CBSX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
5ELVX-ray1.92A/B413-527[»]
A/B653-797[»]
5FHMX-ray1.55A/B413-527[»]
A/B653-797[»]
5FHNX-ray1.60A413-527[»]
A653-797[»]
5FHOX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-797[»]
5FTHX-ray2.90A/B/C404-527[»]
A/B/C653-795[»]
5FTIX-ray1.35A/B404-527[»]
A/B653-795[»]
5FWXX-ray2.50A/C25-400[»]
5FWYX-ray2.12A/C25-400[»]
5IDEelectron microscopy8.25A/C23-883[»]
5IDFelectron microscopy10.31A/C23-883[»]
5JEIX-ray1.23A413-527[»]
A653-797[»]
5KBSelectron microscopy8.70A/B/C/D25-847[»]
5KBTelectron microscopy6.40A/B/C/D25-847[»]
5KBUelectron microscopy7.80A/B/C/D25-847[»]
5KBVelectron microscopy6.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KK2electron microscopy7.30A/B/C/D1-883[»]
5L1BX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1EX-ray4.37A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1FX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1GX-ray4.51A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1HX-ray3.80A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5N6PX-ray2.80A25-400[»]
5NG9X-ray1.15A413-527[»]
A653-797[»]
5NIHX-ray1.30A/B413-527[»]
A/B653-797[»]
5NS9X-ray1.44A/B413-527[»]
A/B653-797[»]
5O9AX-ray1.78A/B/C/D413-527[»]
A/B/C/D653-797[»]
5OEWX-ray2.00A/B/C413-527[»]
A/B/C653-797[»]
5VHWelectron microscopy7.80A/B/C/D25-847[»]
5VHXelectron microscopy8.30A/B/C/D/E25-847[»]
5VHYelectron microscopy4.60A/B/C/D/E/F25-847[»]
5VHZelectron microscopy8.40A/B/C/D/E/F25-847[»]
5VOTelectron microscopy4.90A/B/C/D1-883[»]
5VOUelectron microscopy6.40A/B/C/D1-883[»]
5VOVelectron microscopy7.70A/B/C/D1-883[»]
5WEKelectron microscopy4.60A/B/C/D25-847[»]
5WELelectron microscopy4.40A/B/C/D25-847[»]
5WEMelectron microscopy6.10A/B/C/D25-847[»]
5WENelectron microscopy6.80A/B/C/D25-847[»]
5WEOelectron microscopy4.20A/B/C/D25-847[»]
6DLZelectron microscopy3.90A/B/C/D25-847[»]
6DM0electron microscopy4.40A/B/C/D25-847[»]
6DM1electron microscopy4.20A/B/C/D25-847[»]
6DM2electron microscopy4.60A/B/C/D25-847[»]
ProteinModelPortaliP19491
SMRiP19491
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248250, 9 interactors
CORUMiP19491
DIPiDIP-30952N
ELMiP19491
IntActiP19491, 27 interactors
MINTiP19491
STRINGi10116.ENSRNOP00000062152

Chemistry databases

BindingDBiP19491
ChEMBLiCHEMBL3503
GuidetoPHARMACOLOGYi445

PTM databases

iPTMnetiP19491
PhosphoSitePlusiP19491
SwissPalmiP19491

Proteomic databases

PaxDbiP19491
PRIDEiP19491

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29627
KEGGirno:29627
UCSCiRGD:61862 rat [P19491-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2891
RGDi61862 Gria2

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
HOGENOMiHOG000234372
HOVERGENiHBG051839
InParanoidiP19491
KOiK05198
PhylomeDBiP19491

Miscellaneous databases

EvolutionaryTraceiP19491

Protein Ontology

More...
PROi
PR:P19491

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGRIA2_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19491
Secondary accession number(s): Q9R174
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: November 7, 2018
This is version 212 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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