UniProtKB - P19490 (GRIA1_RAT)
Glutamate receptor 1
Gria1
Functioni
Miscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 464 | GlutamateBy similarity | 1 | |
Binding sitei | 499 | GlutamateBy similarity | 1 | |
Binding sitei | 719 | GlutamateBy similarity | 1 |
GO - Molecular functioni
- adenylate cyclase binding Source: RGD
- AMPA glutamate receptor activity Source: UniProtKB
- amyloid-beta binding Source: ARUK-UCL
- beta-2 adrenergic receptor binding Source: ARUK-UCL
- glutamate receptor binding Source: UniProtKB
- G-protein alpha-subunit binding Source: RGD
- G-protein beta-subunit binding Source: RGD
- identical protein binding Source: UniProtKB
- immunoglobulin binding Source: UniProtKB
- ionotropic glutamate receptor activity Source: RGD
- ligand-gated ion channel activity Source: GO_Central
- myosin V binding Source: RGD
- neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration Source: RGD
- PDZ domain binding Source: RGD
- protein C-terminus binding Source: ARUK-UCL
- protein domain specific binding Source: RGD
- protein kinase A binding Source: RGD
- protein kinase binding Source: RGD
- scaffold protein binding Source: SynGO-UCL
- signaling receptor activity Source: GO_Central
- small GTPase binding Source: RGD
- transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential Source: RGD
GO - Biological processi
- cellular response to amine stimulus Source: RGD
- cellular response to amino acid stimulus Source: RGD
- cellular response to dsRNA Source: RGD
- cellular response to growth factor stimulus Source: RGD
- cellular response to organic cyclic compound Source: RGD
- cellular response to peptide hormone stimulus Source: RGD
- chemical synaptic transmission Source: RGD
- long-term memory Source: RGD
- long-term synaptic depression Source: RGD
- modulation of chemical synaptic transmission Source: UniProtKB
- neuronal action potential Source: UniProtKB
- positive regulation of membrane potential Source: RGD
- positive regulation of synaptic transmission Source: UniProtKB
- receptor internalization Source: UniProtKB
- regulation of postsynaptic membrane potential Source: RGD
- regulation of receptor recycling Source: UniProtKB
- regulation of synaptic plasticity Source: UniProtKB
- response to arsenic-containing substance Source: RGD
- response to cocaine Source: RGD
- response to drug Source: RGD
- response to electrical stimulus Source: RGD
- response to estradiol Source: RGD
- response to fungicide Source: RGD
- response to lithium ion Source: UniProtKB
- response to organic cyclic compound Source: RGD
- response to peptide hormone Source: RGD
- response to toxic substance Source: RGD
- spinal cord development Source: RGD
- synaptic transmission, glutamatergic Source: UniProtKB
Keywordsi
Molecular function | Ion channel, Ligand-gated ion channel, Receptor |
Biological process | Ion transport, Transport |
Enzyme and pathway databases
Reactomei | R-RNO-204005, COPII-mediated vesicle transport R-RNO-399710, Activation of AMPA receptors R-RNO-399719, Trafficking of AMPA receptors R-RNO-416993, Trafficking of GluR2-containing AMPA receptors R-RNO-438066, Unblocking of NMDA receptors, glutamate binding and activation R-RNO-5694530, Cargo concentration in the ER R-RNO-8849932, Synaptic adhesion-like molecules |
Protein family/group databases
TCDBi | 1.A.10.1.1, the glutamate-gated ion channel (gic) family of neurotransmitter receptors |
Names & Taxonomyi
Protein namesi | Recommended name: Glutamate receptor 1Short name: GluR-1 Alternative name(s): AMPA-selective glutamate receptor 1 GluR-A GluR-K1 Glutamate receptor ionotropic, AMPA 1 Short name: GluA1 |
Gene namesi | Name:Gria1 Synonyms:Glur1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621531, Gria1 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Multi-pass membrane protein By similarity
- postsynaptic cell membrane By similarity; Multi-pass membrane protein By similarity
- postsynaptic density membrane By similarity; Multi-pass membrane protein Curated
Endosome
- Early endosome membrane 1 Publication; Multi-pass membrane protein Curated
- Recycling endosome membrane 1 Publication; Multi-pass membrane protein Curated
Endoplasmic reticulum
- Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein Curated
Other locations
- dendrite By similarity
- dendritic spine By similarity
Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (PubMed:19265014). Colocalizes with PDLIM4 in early endosomes (PubMed:15456832). Displays a somatodendritic localization and is excluded from axons in neurons (By similarity). Localized to cone photoreceptor pedicles (By similarity).By similarity2 Publications
Cytosol
- cytosol Source: RGD
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
- endoplasmic reticulum membrane Source: UniProtKB
Endosome
- early endosome Source: UniProtKB
- early endosome membrane Source: UniProtKB
- recycling endosome Source: RGD
- recycling endosome membrane Source: UniProtKB
Extracellular region or secreted
- perisynaptic space Source: RGD
Plasma Membrane
- AMPA glutamate receptor complex Source: UniProtKB
- dendrite membrane Source: RGD
- dendritic spine membrane Source: RGD
- integral component of postsynaptic density membrane Source: SynGO
- integral component of postsynaptic membrane Source: SynGO
- integral component of presynaptic membrane Source: SynGO
- ionotropic glutamate receptor complex Source: RGD
- plasma membrane Source: ARUK-UCL
- postsynaptic density membrane Source: RGD
- postsynaptic membrane Source: RGD
- synaptic membrane Source: ARUK-UCL
Other locations
- asymmetric synapse Source: RGD
- axonal spine Source: RGD
- cell surface Source: RGD
- cell-cell junction Source: UniProtKB
- dendrite Source: ARUK-UCL
- dendritic shaft Source: UniProtKB
- dendritic spine Source: ARUK-UCL
- excitatory synapse Source: BHF-UCL
- glutamatergic synapse Source: SynGO
- membrane Source: RGD
- neuromuscular junction Source: RGD
- neuron projection Source: RGD
- neuron spine Source: RGD
- neuronal cell body Source: UniProtKB
- postsynapse Source: RGD
- postsynaptic density Source: RGD
- protein-containing complex Source: RGD
- somatodendritic compartment Source: RGD
- synapse Source: SynGO-UCL
- synaptic vesicle Source: RGD
- synaptic vesicle membrane Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 19 – 536 | ExtracellularBy similarityAdd BLAST | 518 | |
Transmembranei | 537 – 557 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 558 – 584 | CytoplasmicBy similarityAdd BLAST | 27 | |
Intramembranei | 585 – 600 | Helical; Pore-formingBy similarityAdd BLAST | 16 | |
Intramembranei | 601 – 603 | By similarity | 3 | |
Topological domaini | 604 – 609 | CytoplasmicBy similarity | 6 | |
Transmembranei | 610 – 630 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 631 – 805 | ExtracellularBy similarityAdd BLAST | 175 | |
Transmembranei | 806 – 826 | Helical; Name=M4By similarityAdd BLAST | 21 | |
Topological domaini | 827 – 907 | CytoplasmicBy similarityAdd BLAST | 81 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Endosome, Membrane, Postsynaptic cell membrane, SynapsePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 645 | S → A: No effect on phosphorylation by CaMK2. 1 Publication | 1 | |
Mutagenesisi | 849 | S → A: Abolishes phosphorylation by CaMK2. 1 Publication | 1 | |
Mutagenesisi | 855 | R → A: Decreases binding efficiency to PRKG2. | 1 | |
Mutagenesisi | 855 | R → E: Abolishes binding to PRKG2. 1 Publication | 1 | |
Mutagenesisi | 863 | S → A: Decreases synaptic insertion during chemical-induced long term potentiation. 1 Publication | 1 | |
Mutagenesisi | 905 | T → A: Loss of interaction with DLG1. 1 Publication | 1 | |
Mutagenesisi | 907 | L → A: Loss of interaction with DLG1. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3753 |
DrugCentrali | P19490 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
ChainiPRO_0000011531 | 19 – 907 | Glutamate receptor 1Add BLAST | 889 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 63 | N-linked (GlcNAc...) asparagine | 1 | |
Disulfide bondi | 75 ↔ 323 | 1 Publication | ||
Glycosylationi | 249 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 257 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 363 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 401 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 406 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 603 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 645 | Phosphoserine1 Publication | 1 | |
Modified residuei | 710 | Phosphoserine; by PKC1 Publication | 1 | |
Disulfide bondi | 732 ↔ 787 | By similarity | ||
Lipidationi | 829 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 849 | Phosphoserine; by PKC, PKA and CAMK22 Publications | 1 | |
Modified residuei | 863 | Phosphoserine; by PKC, PKA and PKG/PRKG22 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
PRIDEi | P19490 |
PTM databases
GlyGeni | P19490, 6 sites |
iPTMneti | P19490 |
PhosphoSitePlusi | P19490 |
SwissPalmi | P19490 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (PubMed:21639859). Tetramers may be formed by the dimerization of dimers (By similarity).
Interacts with HIP1 and RASGRF2.
Interacts with SYNDIG1 and GRIA2 (By similarity).
Interacts with DLG1 (via C-terminus) (PubMed:12070168, PubMed:17069616, PubMed:9677374).
Interacts with LRFN1 (PubMed:16630835).
Interacts with PRKG2 (PubMed:18031684).
Interacts with CNIH2 and CACNG2 (PubMed:20805473).
Interacts with CACNG5 (PubMed:18817736, PubMed:19234459).
Interacts (via C-terminus) with PDLIM4 (via LIM domain); this interaction as well as the interaction of PDLIM4 with alpha-actinin is required for their colocalization in early endosomes (PubMed:15456832).
Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (PubMed:16793768, PubMed:19265014).
Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes.
Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain) (By similarity).
Interacts with CACNG3; associates GRIA1 with the adaptor protein complex 4 (AP-4) to target GRIA1 to the somatodendritic compartment of neurons (By similarity).
By similarity12 PublicationsBinary interactionsi
Hide detailsP19490
GO - Molecular functioni
- adenylate cyclase binding Source: RGD
- beta-2 adrenergic receptor binding Source: ARUK-UCL
- glutamate receptor binding Source: UniProtKB
- G-protein alpha-subunit binding Source: RGD
- G-protein beta-subunit binding Source: RGD
- identical protein binding Source: UniProtKB
- myosin V binding Source: RGD
- PDZ domain binding Source: RGD
- protein C-terminus binding Source: ARUK-UCL
- protein domain specific binding Source: RGD
- protein kinase A binding Source: RGD
- protein kinase binding Source: RGD
- scaffold protein binding Source: SynGO-UCL
- small GTPase binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 248399, 13 interactors |
CORUMi | P19490 |
DIPi | DIP-30929N |
ELMi | P19490 |
IntActi | P19490, 25 interactors |
MINTi | P19490 |
STRINGi | 10116.ENSRNOP00000064722 |
Chemistry databases
BindingDBi | P19490 |
Structurei
Secondary structure
3D structure databases
SMRi | P19490 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19490 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 492 – 494 | Glutamate bindingBy similarity | 3 | |
Regioni | 668 – 669 | Glutamate bindingBy similarity | 2 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 904 – 907 | PDZ-binding | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1054, Eukaryota |
InParanoidi | P19490 |
OrthoDBi | 188544at2759 |
PhylomeDBi | P19490 |
Family and domain databases
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 |
Pfami | View protein in Pfam PF01094, ANF_receptor, 1 hit PF00060, Lig_chan, 1 hit PF10613, Lig_chan-Glu_bd, 1 hit |
PRINTSi | PR00177, NMDARECEPTOR |
SMARTi | View protein in SMART SM00918, Lig_chan-Glu_bd, 1 hit SM00079, PBPe, 1 hit |
SUPFAMi | SSF53822, SSF53822, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT
60 70 80 90 100
EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF
110 120 130 140 150
CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ EALISIIDHY KWQTFVYIYD
160 170 180 190 200
ADRGLSVLQR VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV
210 220 230 240 250
VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV
260 270 280 290 300
TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM
310 320 330 340 350
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT
360 370 380 390 400
GNVQFNEKGR RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD
410 420 430 440 450
NSSVQNRTYI VTTILEDPYV MLKKNANQFE GNDRYEGYCV ELAAEIAKHV
460 470 480 490 500
GYSYRLEIVS DGKYGARDPD TKAWNGMVGE LVYGRADVAV APLTITLVRE
510 520 530 540 550
EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV
560 570 580 590 600
SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
610 620 630 640 650
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA
660 670 680 690 700
EDLAKQTEIA YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT
710 720 730 740 750
EEGMIRVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT
760 770 780 790 800
PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKDKTSA
810 820 830 840 850
LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI
860 870 880 890 900
NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM
PLGATGL
The sequence of this isoform differs from the canonical sequence as follows:
758-758: N → G
768-768: N → S
772-772: L → V
778-778: N → S
790-793: GGGD → KDSG
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2K798 | A0A0G2K798_RAT | Glutamate receptor | Gria1 | 831 | Annotation score: | ||
M0R9A7 | M0R9A7_RAT | Glutamate receptor | Gria1 | 812 | Annotation score: | ||
M0R5P7 | M0R5P7_RAT | Glutamate receptor | Gria1 | 754 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 67 | S → T in AAA63479 (PubMed:1699275).Curated | 1 | |
Sequence conflicti | 248 | A → R in AAA63479 (PubMed:1699275).Curated | 1 | |
Sequence conflicti | 698 | R → L in AAA63479 (PubMed:1699275).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 710 | S → T2 Publications | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000097 | 758 | N → G in isoform Flip. 1 Publication | 1 | |
Alternative sequenceiVSP_000098 | 768 | N → S in isoform Flip. 1 Publication | 1 | |
Alternative sequenceiVSP_000099 | 772 | L → V in isoform Flip. 1 Publication | 1 | |
Alternative sequenceiVSP_000100 | 778 | N → S in isoform Flip. 1 Publication | 1 | |
Alternative sequenceiVSP_000101 | 790 – 793 | GGGD → KDSG in isoform Flip. 1 Publication | 4 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X17184 mRNA Translation: CAA35050.1 M36418 mRNA Translation: AAA41243.2 M38060 mRNA Translation: AAA63479.1 |
PIRi | A40170 S07059, ACRTK1 |
RefSeqi | NP_113796.1, NM_031608.1 [P19490-1] |
Genome annotation databases
GeneIDi | 50592 |
KEGGi | rno:50592 |
UCSCi | RGD:621531, rat [P19490-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X17184 mRNA Translation: CAA35050.1 M36418 mRNA Translation: AAA41243.2 M38060 mRNA Translation: AAA63479.1 |
PIRi | A40170 S07059, ACRTK1 |
RefSeqi | NP_113796.1, NM_031608.1 [P19490-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2AWW | X-ray | 2.21 | C | 890-907 | [»] | |
2G2L | X-ray | 2.35 | C/D | 890-907 | [»] | |
3SAJ | X-ray | 2.50 | A/B/C/D | 22-392 | [»] | |
6NJL | electron microscopy | 6.70 | A/C | 1-907 | [»] | |
6NJN | electron microscopy | 6.50 | A | 1-907 | [»] | |
6QKC | electron microscopy | 4.10 | A/C | 1-907 | [»] | |
6QKZ | electron microscopy | 6.30 | A/C | 20-907 | [»] | |
SMRi | P19490 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 248399, 13 interactors |
CORUMi | P19490 |
DIPi | DIP-30929N |
ELMi | P19490 |
IntActi | P19490, 25 interactors |
MINTi | P19490 |
STRINGi | 10116.ENSRNOP00000064722 |
Chemistry databases
BindingDBi | P19490 |
ChEMBLi | CHEMBL3753 |
DrugCentrali | P19490 |
Protein family/group databases
TCDBi | 1.A.10.1.1, the glutamate-gated ion channel (gic) family of neurotransmitter receptors |
PTM databases
GlyGeni | P19490, 6 sites |
iPTMneti | P19490 |
PhosphoSitePlusi | P19490 |
SwissPalmi | P19490 |
Proteomic databases
PRIDEi | P19490 |
Protocols and materials databases
ABCDi | P19490, 2 sequenced antibodies |
Genome annotation databases
GeneIDi | 50592 |
KEGGi | rno:50592 |
UCSCi | RGD:621531, rat [P19490-1] |
Organism-specific databases
CTDi | 2890 |
RGDi | 621531, Gria1 |
Phylogenomic databases
eggNOGi | KOG1054, Eukaryota |
InParanoidi | P19490 |
OrthoDBi | 188544at2759 |
PhylomeDBi | P19490 |
Enzyme and pathway databases
Reactomei | R-RNO-204005, COPII-mediated vesicle transport R-RNO-399710, Activation of AMPA receptors R-RNO-399719, Trafficking of AMPA receptors R-RNO-416993, Trafficking of GluR2-containing AMPA receptors R-RNO-438066, Unblocking of NMDA receptors, glutamate binding and activation R-RNO-5694530, Cargo concentration in the ER R-RNO-8849932, Synaptic adhesion-like molecules |
Miscellaneous databases
EvolutionaryTracei | P19490 |
PROi | PR:P19490 |
Family and domain databases
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 |
Pfami | View protein in Pfam PF01094, ANF_receptor, 1 hit PF00060, Lig_chan, 1 hit PF10613, Lig_chan-Glu_bd, 1 hit |
PRINTSi | PR00177, NMDARECEPTOR |
SMARTi | View protein in SMART SM00918, Lig_chan-Glu_bd, 1 hit SM00079, PBPe, 1 hit |
SUPFAMi | SSF53822, SSF53822, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GRIA1_RAT | |
Accessioni | P19490Primary (citable) accession number: P19490 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | May 16, 2006 | |
Last modified: | February 10, 2021 | |
This is version 206 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families