Protein:GRIN1 |
Protein Summary |
Gene summary |
| Gene name: GRIN1 | ASpdb.0 ID: 2902 | Gene | Gene symbol | GRIN1 | Gene ID | 2902 |
| Gene name | glutamate ionotropic receptor NMDA type subunit 1 |
| Synonyms | DEE101|GluN1|MRD8|NDHMSD|NDHMSR|NMD-R1|NMDA1|NMDAR1|NR1 |
| Cytomap | 9q34.3 |
| Type of gene | protein-coding |
| Description | glutamate 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 date | 20240407 |
| UniProtAcc | Q05586 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | GRIN1 | GO:0004972 | NMDA glutamate receptor activity | 7679115|7685113 |
| Gene | GRIN1 | GO:0004972 | NMDA glutamate receptor activity | 26919761|28105280 |
| Gene | GRIN1 | GO:0005262 | calcium channel activity | 7685113 |
| Gene | GRIN1 | GO:0005886 | plasma membrane | 7685113|26875626|26919761|28105280|28228639 |
| Gene | GRIN1 | GO:0006812 | monoatomic cation transport | 7685113 |
| Gene | GRIN1 | GO:0016594 | glycine binding | 7685113|28105280 |
| Gene | GRIN1 | GO:0016595 | glutamate binding | 7685113 |
| Gene | GRIN1 | GO:0017146 | NMDA selective glutamate receptor complex | 7679115|10480938|17047094|26875626|26919761|28105280 |
| Gene | GRIN1 | GO:0022849 | glutamate-gated calcium ion channel activity | 26875626 |
| Gene | GRIN1 | GO:0030425 | dendrite | 10749211 |
| Gene | GRIN1 | GO:0042391 | regulation of membrane potential | 7679115|7685113|17047094 |
| Gene | GRIN1 | GO:0045471 | response to ethanol | 18445116 |
| Gene | GRIN1 | GO:0097553 | calcium ion transmembrane import into cytosol | 26875626 |
| Gene | GRIN1 | GO:1905429 | response to glycine | 28105280 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q05586-1 | Q05586-1_6ira_A.pdb | 6IRA | EM | 4.5 | A | 25 | 844 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q05586 | GRIN1 | Q05586-1 | Q05586-2 | 938 | 885 | 864 | 885 | Substitution | DRKSGRAEPDPKKKATFRAITS | QYHPTDITGPLNLSDPSVSTVV | 864 | 885 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-2 | 938 | 885 | 886 | 938 | Deletion | none | none | 885 | 885 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-3 | 938 | 901 | 864 | 900 | Deletion | none | none | 863 | 863 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-4 | 938 | 922 | 901 | 922 | Substitution | STGGGRGALQNQKDTVLPRRAI | QYHPTDITGPLNLSDPSVSTVV | 901 | 922 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-4 | 938 | 922 | 923 | 938 | Deletion | none | none | 922 | 922 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-5 | 938 | 959 | 190 | 190 | Substitution | K | KSKKRNYENLDQLSYDNKRGPK | 190 | 211 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-6 | 938 | 943 | 190 | 190 | Substitution | K | KSKKRNYENLDQLSYDNKRGPK | 190 | 211 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-6 | 938 | 943 | 901 | 922 | Substitution | STGGGRGALQNQKDTVLPRRAI | QYHPTDITGPLNLSDPSVSTVV | 922 | 943 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-6 | 938 | 943 | 923 | 938 | Deletion | none | none | 943 | 943 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-7 | 938 | 906 | 190 | 190 | Substitution | K | KSKKRNYENLDQLSYDNKRGPK | 190 | 211 |
| Q05586 | GRIN1 | Q05586-1 | Q05586-7 | 938 | 906 | 864 | 938 | Substitution | DRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES | QYHPTDITGPLNLSDPSVSTVV | 885 | 906 |
Multiple sequence alignment of our canonical and alternatively spliced GRIN1 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of GRIN1 |
| UniProt-id | ENSG | ENST | ENSP |
| Q05586-1 | ENSG00000176884.17 | ENST00000371561.8 | ENSP00000360616.3 |
| Q05586-2 | ENSG00000176884.17 | ENST00000371559.8 | ENSP00000360614.4 |
| Q05586-3 | ENSG00000176884.17 | ENST00000371550.8 | ENSP00000360605.4 |
| Q05586-5 | ENSG00000176884.17 | ENST00000371546.8 | ENSP00000360601.4 |
| Q05586-6 | ENSG00000176884.17 | ENST00000371553.8 | ENSP00000360608.3 |
| Q05586-7 | ENSG00000176884.17 | ENST00000371560.5 | ENSP00000360615.3 |
| UniProt-id | NM ID | NP ID |
| Q05586-1 | NM_007327.3 | NP_015566.1 |
| Q05586-2 | NM_000832.6 | NP_000823.4 |
| Q05586-3 | NM_021569.3 | NP_067544.1 |
| Q05586-4 | XM_005266071.3 | XP_005266128.1 |
| Q05586-5 | XM_005266073.4 | XP_005266130.1 |
| Q05586-6 | NM_001185090.1 | NP_001172019.1 |
| Q05586-7 | NM_001185091.1 | NP_001172020.1 |
Amino acid sequences of our canonical and alternatively spliced GRIN1 |
| accession_id | Protein sequence |
| Q05586-1 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT |
| Q05586-2 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF |
| Q05586-3 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRE |
| Q05586-4 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQ LINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHT VPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSAR ILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTF ENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT |
| Q05586-5 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKAT |
| Q05586-6 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKAT |
| Q05586-7 | MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAI LVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL ETLLEERESKSKKRNYENLDQLSYDNKRGPKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV GEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVE FNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGD PVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTI NNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWF SWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVEL STMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD KTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQQYHPTDITGPLNLSDP |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| GRIN1 (go to UniProt):Q05586 |
Retention 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 * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q05586 | Topological domain | 19 | 559 | Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=190;End=190 |
| Q05586 | Topological domain | 19 | 559 | Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=190;End=190 |
| Q05586 | Topological domain | 19 | 559 | Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=190;End=190 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=864;End=885 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Deletion;Start=886;End=938 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Deletion;Start=864;End=900 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=901;End=922 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Deletion;Start=923;End=938 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=901;End=922 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Deletion;Start=923;End=938 |
| Q05586 | Topological domain | 834 | 938 | Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35439 | Type=Substitution;Start=864;End=938 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=886;End=938 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=864;End=900 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=901;End=922 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=923;End=938 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=901;End=922 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=923;End=938 |
| Q05586 | Region | 889 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=864;End=938 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=886;End=938 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=901;End=922 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=923;End=938 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=901;End=922 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=923;End=938 |
| Q05586 | Compositional bias | 917 | 938 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=864;End=938 |
Gene Isoform Structures and Expression Levels for GRIN1 |
Gene 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. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
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 |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
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 |
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| Ramachandran plot of Q05586-3 |
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| Ramachandran plot of Q05586-4 |
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Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q05586-1 | 1.021 | 207 | 0.882 | 485.688 | 0.473 | 0.729 | 1.001 | 0.054 | 1.519 | 0.036 | 0.84 | 403,404,405,406,411,413,414,438,439,440,441,443,44 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 |
| Q05586-2 | 0.993 | 195 | 0.94 | 447.958 | 0.538 | 0.687 | 0.92 | 0.123 | 1.264 | 0.097 | 1.11 | 403,404,405,406,411,439,440,441,442,443,444,445,44 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 |
| Q05586-3 | 1.01 | 115 | 1.022 | 346.773 | 0.594 | 0.713 | 0.882 | 0.409 | 1.059 | 0.386 | 1.167 | 155,161,162,163,165,180,181,184,185,188,189,190,19 1,192,193,194,214,215,506,508,526,527,763,764,765, 766 |
| Q05586-4 | 1.004 | 175 | 0.926 | 455.504 | 0.538 | 0.703 | 0.959 | 0.098 | 1.338 | 0.073 | 0.941 | 403,404,405,406,411,413,439,440,441,442,443,444,44 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 |
| Q05586-5 | 1.029 | 100 | 1.079 | 459.963 | 0.677 | 0.678 | 0.79 | 0.52 | 0.82 | 0.634 | 0.737 | 34,93,94,95,96,98,99,100,102,103,122,124,125,126,1 27,144,170,171,172,245,246,272,273,276,292,295,296 ,297,298,299 |
| Q05586-6 | 1.034 | 106 | 1.076 | 324.135 | 0.578 | 0.7 | 0.935 | 1.03 | 0.872 | 1.181 | 0.723 | 126,129,130,142,143,145,146,149,150,152,153,171,17 4,175,178,179,182,183,362,363,364,366,367,368,369, 370,372,388,390,391 |
| Q05586-7 | 0.999 | 222 | 1.036 | 688.058 | 0.626 | 0.663 | 0.817 | 0.433 | 0.926 | 0.468 | 1.166 | 555,563,564,565,566,567,568,569,570,571,574,577,67 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 |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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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 |
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 |
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 |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to GRIN1 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q05586 | GRIN1 | DB00659 | Acamprosate | approved, investigational | antagonist |
| Q05586 | GRIN1 | DB06741 | Gavestinel | investigational | antagonist |
| Q05586 | GRIN1 | DB06151 | Acetylcysteine | approved, investigational | activator |
| Q05586 | GRIN1 | DB06738 | Ketobemidone | investigational | antagonist |
| Q05586 | GRIN1 | DB01238 | Aripiprazole | approved, investigational | ligand |
| Q05586 | GRIN1 | DB03929 | D-Serine | approved, experimental | |
| Q05586 | GRIN1 | DB01173 | Orphenadrine | approved | antagonist |
| Q05586 | GRIN1 | DB09481 | Magnesium carbonate | approved, investigational | blocker |
| Q05586 | GRIN1 | DB01043 | Memantine | approved, investigational | binder |
| Q05586 | GRIN1 | DB09409 | Magnesium acetate tetrahydrate | approved | ligand |
| Q05586 | GRIN1 | DB04896 | Milnacipran | approved, investigational | inhibitor |
| Q05586 | GRIN1 | DB00142 | Glutamic acid | approved, nutraceutical | |
| Q05586 | GRIN1 | DB04620 | Cycloleucine | experimental | |
| Q05586 | GRIN1 | DB01174 | Phenobarbital | approved, investigational | antagonist |
| Q05586 | GRIN1 | DB08838 | Agmatine | experimental | antagonist |
| Q05586 | GRIN1 | DB00647 | Dextropropoxyphene | approved, illicit, investigational, withdrawn | antagonist |
| Q05586 | GRIN1 | DB00418 | Secobarbital | approved, vet_approved | antagonist |
| Q05586 | GRIN1 | DB01043 | Memantine | approved, investigational | antagonist |
| Q05586 | GRIN1 | DB00454 | Meperidine | approved | antagonist |
| Q05586 | GRIN1 | DB00312 | Pentobarbital | approved, investigational, vet_approved | antagonist |
| Q05586 | GRIN1 | DB05824 | CNS-5161 | investigational | |
| Q05586 | GRIN1 | DB01931 | 5,7-Dichlorokynurenic acid | experimental | |
| Q05586 | GRIN1 | DB00228 | Enflurane | approved, investigational, vet_approved | antagonist |
| Q05586 | GRIN1 | DB00874 | Guaifenesin | approved, investigational, vet_approved | antagonist |
| Q05586 | GRIN1 | DB00193 | Tramadol | approved, investigational | inhibitor |
| Q05586 | GRIN1 | DB00333 | Methadone | approved | antagonist |
| Q05586 | GRIN1 | DB01708 | Prasterone | approved, investigational, nutraceutical | agonist |
| Q05586 | GRIN1 | DB00843 | Donepezil | approved | downregulator |
| Q05586 | GRIN1 | DB00289 | Atomoxetine | approved | blocker |
| Q05586 | GRIN1 | DB13146 | Fluciclovine (18F) | approved | inhibitor |
| Q05586 | GRIN1 | DB11823 | Esketamine | approved, investigational | antagonist |
| Q05586 | GRIN1 | DB08954 | Ifenprodil | investigational, withdrawn | antagonist |
Related Diseases to GRIN1 |
Previous studies relating to the alternative splicing of GRIN1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| GRIN1 | 15635650 | GRIN1 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. | D020270 | Alcohol Withdrawal Seizures |
| GRIN1 | 15635650 | GRIN1 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. | D019973 | Alcohol-Related Disorders |
| GRIN1 | 15635650 | GRIN1 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. | D020022 | Genetic Predisposition to Disease |
| GRIN1 | 15635650 | GRIN1 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. | D013375 | Substance Withdrawal Syndrome |
Clinically important variants in GRIN1 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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