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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:GRIN1

Protein Summary

check button Gene summary
Gene name: GRIN1
ASpdb.0 ID: 2902
Gene
Gene symbol

GRIN1

Gene ID

2902

Gene nameglutamate ionotropic receptor NMDA type subunit 1
SynonymsDEE101|GluN1|MRD8|NDHMSD|NDHMSR|NMD-R1|NMDA1|NMDAR1|NR1
Cytomap

9q34.3

Type of geneprotein-coding
Descriptionglutamate receptor ionotropic, NMDA 1N-methyl-D-aspartate receptor channel, subunit zeta-1N-methyl-D-aspartate receptor subunit NR1glutamate [NMDA] receptor subunit zeta-1glutamate receptor, ionotropic, N-methyl D-aspartate 1putative NMDtranscript(al
Modification date20240407
UniProtAcc

Q05586


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneGRIN1

GO:0004972

NMDA glutamate receptor activity

7679115|7685113

GeneGRIN1

GO:0004972

NMDA glutamate receptor activity

26919761|28105280

GeneGRIN1

GO:0005262

calcium channel activity

7685113

GeneGRIN1

GO:0005886

plasma membrane

7685113|26875626|26919761|28105280|28228639

GeneGRIN1

GO:0006812

monoatomic cation transport

7685113

GeneGRIN1

GO:0016594

glycine binding

7685113|28105280

GeneGRIN1

GO:0016595

glutamate binding

7685113

GeneGRIN1

GO:0017146

NMDA selective glutamate receptor complex

7679115|10480938|17047094|26875626|26919761|28105280

GeneGRIN1

GO:0022849

glutamate-gated calcium ion channel activity

26875626

GeneGRIN1

GO:0030425

dendrite

10749211

GeneGRIN1

GO:0042391

regulation of membrane potential

7679115|7685113|17047094

GeneGRIN1

GO:0045471

response to ethanol

18445116

GeneGRIN1

GO:0097553

calcium ion transmembrane import into cytosol

26875626

GeneGRIN1

GO:1905429

response to glycine

28105280



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
Q05586-1Q05586-1_6ira_A.pdb6IRAEM4.5A25844

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
Q05586GRIN1Q05586-1Q05586-2938885864885SubstitutionDRKSGRAEPDPKKKATFRAITSQYHPTDITGPLNLSDPSVSTVV864885
Q05586GRIN1Q05586-1Q05586-2938885886938Deletionnonenone885885
Q05586GRIN1Q05586-1Q05586-3938901864900Deletionnonenone863863
Q05586GRIN1Q05586-1Q05586-4938922901922SubstitutionSTGGGRGALQNQKDTVLPRRAIQYHPTDITGPLNLSDPSVSTVV901922
Q05586GRIN1Q05586-1Q05586-4938922923938Deletionnonenone922922
Q05586GRIN1Q05586-1Q05586-5938959190190SubstitutionKKSKKRNYENLDQLSYDNKRGPK190211
Q05586GRIN1Q05586-1Q05586-6938943190190SubstitutionKKSKKRNYENLDQLSYDNKRGPK190211
Q05586GRIN1Q05586-1Q05586-6938943901922SubstitutionSTGGGRGALQNQKDTVLPRRAIQYHPTDITGPLNLSDPSVSTVV922943
Q05586GRIN1Q05586-1Q05586-6938943923938Deletionnonenone943943
Q05586GRIN1Q05586-1Q05586-7938906190190SubstitutionKKSKKRNYENLDQLSYDNKRGPK190211
Q05586GRIN1Q05586-1Q05586-7938906864938SubstitutionDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRESQYHPTDITGPLNLSDPSVSTVV885906

check buttonMultiple sequence alignment of our canonical and alternatively spliced GRIN1

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of GRIN1
UniProt-idENSGENSTENSP
Q05586-1ENSG00000176884.17ENST00000371561.8ENSP00000360616.3
Q05586-2ENSG00000176884.17ENST00000371559.8ENSP00000360614.4
Q05586-3ENSG00000176884.17ENST00000371550.8ENSP00000360605.4
Q05586-5ENSG00000176884.17ENST00000371546.8ENSP00000360601.4
Q05586-6ENSG00000176884.17ENST00000371553.8ENSP00000360608.3
Q05586-7ENSG00000176884.17ENST00000371560.5ENSP00000360615.3

UniProt-idNM IDNP ID
Q05586-1NM_007327.3NP_015566.1
Q05586-2NM_000832.6NP_000823.4
Q05586-3NM_021569.3NP_067544.1
Q05586-4XM_005266071.3XP_005266128.1
Q05586-5XM_005266073.4XP_005266130.1
Q05586-6NM_001185090.1NP_001172019.1
Q05586-7NM_001185091.1NP_001172020.1

check buttonAmino acid sequences of our canonical and alternatively spliced GRIN1
accession_idProtein sequence
Q05586-1MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ
LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT
VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR
ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF
ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT
Q05586-2MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ
LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT
VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR
ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF
Q05586-3MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ
LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT
VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR
ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF
ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRE
Q05586-4MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ
LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT
VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR
ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF
ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT
Q05586-5MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV
GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE
FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD
PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI
NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF
SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL
STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD
KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKAT
Q05586-6MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV
GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE
FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD
PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI
NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF
SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL
STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD
KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKAT
Q05586-7MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI
LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV
GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE
FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD
PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI
NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF
SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL
STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD
KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQQYHPTDITGPLNLSDP

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
GRIN1 (go to UniProt):Q05586

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q05586Topological domain19559Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=190;End=190
Q05586Topological domain19559Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=190;End=190
Q05586Topological domain19559Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=190;End=190
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=864;End=885
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Deletion;Start=886;End=938
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Deletion;Start=864;End=900
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=901;End=922
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Deletion;Start=923;End=938
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=901;End=922
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Deletion;Start=923;End=938
Q05586Topological domain834938Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439Type=Substitution;Start=864;End=938
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=886;End=938
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=864;End=900
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=901;End=922
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=923;End=938
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=901;End=922
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=923;End=938
Q05586Region889938Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=864;End=938
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=886;End=938
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=901;End=922
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=923;End=938
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=901;End=922
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=923;End=938
Q05586Compositional bias917938Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=864;End=938


Gene Isoform Structures and Expression Levels for GRIN1

check buttonGene structures of our canonical and alternative spliced genes of GRIN1
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of GRIN1

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of Q05586-1
3D view using mol* of Q05586-2
3D view using mol* of Q05586-3
3D view using mol* of Q05586-4
3D view using mol* of Q05586-5
3D view using mol* of Q05586-6
3D view using mol* of Q05586-7


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of Q05586-1
all structure
pLDDT distribution across the protein length of Q05586-2
all structure
pLDDT distribution across the protein length of Q05586-3
all structure
pLDDT distribution across the protein length of Q05586-4
all structure
pLDDT distribution across the protein length of Q05586-5
all structure
pLDDT distribution across the protein length of Q05586-6
all structure
pLDDT distribution across the protein length of Q05586-7
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of Q05586-1
all structure
Ramachandran plot of Q05586-3
all structure
Ramachandran plot of Q05586-4
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
Q05586-11.0212070.882485.6880.4730.7291.0010.0541.5190.0360.84403,404,405,406,411,413,414,438,439,440,441,443,44
4,445,446,448,451,452,453,478,479,480,481,482,483,
484,523,684,685,686,687,688,712,713,714,715,718,71
9,722,731,735,738,739,742,743
Q05586-20.9931950.94447.9580.5380.6870.920.1231.2640.0971.11403,404,405,406,411,439,440,441,442,443,444,445,44
6,447,448,449,451,453,478,479,480,481,482,483,484,
684,685,686,712,713,714,715,718,731,735,739,742,74
3
Q05586-31.011151.022346.7730.5940.7130.8820.4091.0590.3861.167155,161,162,163,165,180,181,184,185,188,189,190,19
1,192,193,194,214,215,506,508,526,527,763,764,765,
766
Q05586-41.0041750.926455.5040.5380.7030.9590.0981.3380.0730.941403,404,405,406,411,413,439,440,441,442,443,444,44
5,446,447,448,449,451,453,478,479,480,481,482,483,
484,684,685,686,687,712,713,714,715,718,719,722,73
1,735,739,742,743
Q05586-51.0291001.079459.9630.6770.6780.790.520.820.6340.73734,93,94,95,96,98,99,100,102,103,122,124,125,126,1
27,144,170,171,172,245,246,272,273,276,292,295,296
,297,298,299
Q05586-61.0341061.076324.1350.5780.70.9351.030.8721.1810.723126,129,130,142,143,145,146,149,150,152,153,171,17
4,175,178,179,182,183,362,363,364,366,367,368,369,
370,372,388,390,391
Q05586-70.9992221.036688.0580.6260.6630.8170.4330.9260.4681.166555,563,564,565,566,567,568,569,570,571,574,577,67
5,676,679,680,681,682,683,684,758,759,761,762,765,
767,768,770,814,815,816,817,818,819,820,822,823,82
4,825,826,827,828,829,830,833

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of Q05586-1_Q05586-1_6ira_A.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q05586-1_6ira_A_Q05586-2.pdb
3D view using mol* of Q05586-1_6ira_A_Q05586-3.pdb
3D view using mol* of Q05586-1_6ira_A_Q05586-4.pdb
3D view using mol* of Q05586-1_6ira_A_Q05586-5.pdb
3D view using mol* of Q05586-1_6ira_A_Q05586-6.pdb
3D view using mol* of Q05586-1_6ira_A_Q05586-7.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q05586-1_Q05586-2.pdb
3D view using mol* of Q05586-1_Q05586-3.pdb
3D view using mol* of Q05586-1_Q05586-4.pdb
3D view using mol* of Q05586-1_Q05586-5.pdb
3D view using mol* of Q05586-1_Q05586-6.pdb
3D view using mol* of Q05586-1_Q05586-7.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/Q05586-1_vs_Q05586-2.png
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./stats/secondary_structure/figure/Q05586-1_vs_Q05586-3.png
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./stats/secondary_structure/figure/Q05586-1_vs_Q05586-4.png
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./stats/secondary_structure/figure/Q05586-1_vs_Q05586-5.png
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./stats/secondary_structure/figure/Q05586-1_vs_Q05586-6.png
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./stats/secondary_structure/figure/Q05586-1_vs_Q05586-7.png
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check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/Q05586-1_vs_Q05586-2.png
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./stats/relative_asa/Q05586-1_vs_Q05586-3.png
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./stats/relative_asa/Q05586-1_vs_Q05586-4.png
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./stats/relative_asa/Q05586-1_vs_Q05586-5.png
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./stats/relative_asa/Q05586-1_vs_Q05586-6.png
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./stats/relative_asa/Q05586-1_vs_Q05586-7.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to GRIN1


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions
Q05586GRIN1DB00659Acamprosateapproved, investigationalantagonist
Q05586GRIN1DB06741Gavestinelinvestigationalantagonist
Q05586GRIN1DB06151Acetylcysteineapproved, investigationalactivator
Q05586GRIN1DB06738Ketobemidoneinvestigationalantagonist
Q05586GRIN1DB01238Aripiprazoleapproved, investigationalligand
Q05586GRIN1DB03929D-Serineapproved, experimental
Q05586GRIN1DB01173Orphenadrineapprovedantagonist
Q05586GRIN1DB09481Magnesium carbonateapproved, investigationalblocker
Q05586GRIN1DB01043Memantineapproved, investigationalbinder
Q05586GRIN1DB09409Magnesium acetate tetrahydrateapprovedligand
Q05586GRIN1DB04896Milnacipranapproved, investigationalinhibitor
Q05586GRIN1DB00142Glutamic acidapproved, nutraceutical
Q05586GRIN1DB04620Cycloleucineexperimental
Q05586GRIN1DB01174Phenobarbitalapproved, investigationalantagonist
Q05586GRIN1DB08838Agmatineexperimentalantagonist
Q05586GRIN1DB00647Dextropropoxypheneapproved, illicit, investigational, withdrawnantagonist
Q05586GRIN1DB00418Secobarbitalapproved, vet_approvedantagonist
Q05586GRIN1DB01043Memantineapproved, investigationalantagonist
Q05586GRIN1DB00454Meperidineapprovedantagonist
Q05586GRIN1DB00312Pentobarbitalapproved, investigational, vet_approvedantagonist
Q05586GRIN1DB05824CNS-5161investigational
Q05586GRIN1DB019315,7-Dichlorokynurenic acidexperimental
Q05586GRIN1DB00228Enfluraneapproved, investigational, vet_approvedantagonist
Q05586GRIN1DB00874Guaifenesinapproved, investigational, vet_approvedantagonist
Q05586GRIN1DB00193Tramadolapproved, investigationalinhibitor
Q05586GRIN1DB00333Methadoneapprovedantagonist
Q05586GRIN1DB01708Prasteroneapproved, investigational, nutraceuticalagonist
Q05586GRIN1DB00843Donepezilapproveddownregulator
Q05586GRIN1DB00289Atomoxetineapprovedblocker
Q05586GRIN1DB13146Fluciclovine (18F)approvedinhibitor
Q05586GRIN1DB11823Esketamineapproved, investigationalantagonist
Q05586GRIN1DB08954Ifenprodilinvestigational, withdrawnantagonist

Related Diseases to GRIN1


check button Previous studies relating to the alternative splicing of GRIN1 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
GRIN115635650GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal.N-Methyl-D-aspartate (NMDA) receptors, members of the glutamate receptor channel superfamily, are generally inhibited by alcohol. The expression and alternative splicing of the obligatory NR1 subunit is altered by alcohol exposure, emphasizing the involvement of the NR1 subunit, which is coded by the GRIN1 gene, in alcohol-mediated effects. We performed an association study in patients with alcohol dependence with the GRIN1 locus. Two independent case control samples consisting of a total of 442 alcohol-dependent patients and 442 unrelated controls were included. There was no overall difference in allele or genotype frequency between patients and controls. However, the 2108A allele and A-containing genotypes were over-represented in the patients with a history of withdrawal-induced seizures when compared to healthy volunteers (allele: chi(2) = 5.412, df = 1, P = 0.020) or an independent sample of patients without a history of seizures (allele: chi(2) = 4.185, df = 1, P = 0.041). Age at onset, years of alcohol dependence, and a history of delirium tremens did not differ between genotype or allele groups. These findings support the hypothesis that the GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal. This novel finding warrants replication.D020270Alcohol Withdrawal Seizures
GRIN115635650GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal.N-Methyl-D-aspartate (NMDA) receptors, members of the glutamate receptor channel superfamily, are generally inhibited by alcohol. The expression and alternative splicing of the obligatory NR1 subunit is altered by alcohol exposure, emphasizing the involvement of the NR1 subunit, which is coded by the GRIN1 gene, in alcohol-mediated effects. We performed an association study in patients with alcohol dependence with the GRIN1 locus. Two independent case control samples consisting of a total of 442 alcohol-dependent patients and 442 unrelated controls were included. There was no overall difference in allele or genotype frequency between patients and controls. However, the 2108A allele and A-containing genotypes were over-represented in the patients with a history of withdrawal-induced seizures when compared to healthy volunteers (allele: chi(2) = 5.412, df = 1, P = 0.020) or an independent sample of patients without a history of seizures (allele: chi(2) = 4.185, df = 1, P = 0.041). Age at onset, years of alcohol dependence, and a history of delirium tremens did not differ between genotype or allele groups. These findings support the hypothesis that the GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal. This novel finding warrants replication.D019973Alcohol-Related Disorders
GRIN115635650GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal.N-Methyl-D-aspartate (NMDA) receptors, members of the glutamate receptor channel superfamily, are generally inhibited by alcohol. The expression and alternative splicing of the obligatory NR1 subunit is altered by alcohol exposure, emphasizing the involvement of the NR1 subunit, which is coded by the GRIN1 gene, in alcohol-mediated effects. We performed an association study in patients with alcohol dependence with the GRIN1 locus. Two independent case control samples consisting of a total of 442 alcohol-dependent patients and 442 unrelated controls were included. There was no overall difference in allele or genotype frequency between patients and controls. However, the 2108A allele and A-containing genotypes were over-represented in the patients with a history of withdrawal-induced seizures when compared to healthy volunteers (allele: chi(2) = 5.412, df = 1, P = 0.020) or an independent sample of patients without a history of seizures (allele: chi(2) = 4.185, df = 1, P = 0.041). Age at onset, years of alcohol dependence, and a history of delirium tremens did not differ between genotype or allele groups. These findings support the hypothesis that the GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal. This novel finding warrants replication.D020022Genetic Predisposition to Disease
GRIN115635650GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal.N-Methyl-D-aspartate (NMDA) receptors, members of the glutamate receptor channel superfamily, are generally inhibited by alcohol. The expression and alternative splicing of the obligatory NR1 subunit is altered by alcohol exposure, emphasizing the involvement of the NR1 subunit, which is coded by the GRIN1 gene, in alcohol-mediated effects. We performed an association study in patients with alcohol dependence with the GRIN1 locus. Two independent case control samples consisting of a total of 442 alcohol-dependent patients and 442 unrelated controls were included. There was no overall difference in allele or genotype frequency between patients and controls. However, the 2108A allele and A-containing genotypes were over-represented in the patients with a history of withdrawal-induced seizures when compared to healthy volunteers (allele: chi(2) = 5.412, df = 1, P = 0.020) or an independent sample of patients without a history of seizures (allele: chi(2) = 4.185, df = 1, P = 0.041). Age at onset, years of alcohol dependence, and a history of delirium tremens did not differ between genotype or allele groups. These findings support the hypothesis that the GRIN1 locus may modify the susceptibility to seizures during alcohol withdrawal. This novel finding warrants replication.D013375Substance Withdrawal Syndrome


Clinically important variants in GRIN1


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance