Protein:GRM1 |
Protein Summary |
 Gene summary |
| Gene name: GRM1 | ASpdb.0 ID: 2911 | Gene | Gene symbol | GRM1 | Gene ID | 2911 |
| Gene name | glutamate metabotropic receptor 1 |
| Synonyms | GPRC1A|MGLU1|MGLUR1|PPP1R85|SCA44|SCAR13 |
| Cytomap | 6q24.3 |
| Type of gene | protein-coding |
| Description | metabotropic glutamate receptor 1glutamate receptor, metabotropic 1protein phosphatase 1, regulatory subunit 85 |
| Modification date | 20240411 |
| UniProtAcc | Q13255 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | GRM1 | GO:0008066 | glutamate receptor activity | 10945991|24603153 |
| Gene | GRM1 | GO:0038037 | G protein-coupled receptor dimeric complex | 24603153 |
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 |
| Q13255-1 | Q13255-1_3ks9_A.pdb | 3KS9 | X-ray | 1.9 | A | 35 | 512 |
| 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 |
| Q13255 | GRM1 | Q13255-1 | Q13255-2 | 1194 | 906 | 887 | 906 | Substitution | NSNGKSVSWSEPGGGQVPKG | KKRQPEFSPTSQCPSAHVQL | 887 | 906 |
| Q13255 | GRM1 | Q13255-1 | Q13255-2 | 1194 | 906 | 907 | 1194 | Deletion | none | none | 906 | 906 |
| Q13255 | GRM1 | Q13255-1 | Q13255-3 | 1194 | 908 | 887 | 908 | Substitution | NSNGKSVSWSEPGGGQVPKGQH | KWRTGAQGTAYVAPPLCAREDQ | 887 | 908 |
| Q13255 | GRM1 | Q13255-1 | Q13255-3 | 1194 | 908 | 909 | 1194 | Deletion | none | none | 908 | 908 |
| Multiple sequence alignment of our canonical and alternatively spliced GRM1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of GRM1 |
| UniProt-id | ENSG | ENST | ENSP |
| Q13255-1 | ENSG00000152822.15 | ENST00000282753.6 | ENSP00000282753.1 |
| Q13255-1 | ENSG00000152822.15 | ENST00000361719.6 | ENSP00000354896.2 |
| Q13255-1 | ENSG00000152822.15 | ENST00000706833.1 | ENSP00000516579.1 |
| Q13255-1 | ENSG00000152822.15 | ENST00000706835.1 | ENSP00000516581.1 |
| Q13255-2 | ENSG00000152822.15 | ENST00000492807.6 | ENSP00000424095.1 |
| Q13255-2 | ENSG00000152822.15 | ENST00000507907.1 | ENSP00000425599.1 |
| Q13255-2 | ENSG00000152822.15 | ENST00000706834.1 | ENSP00000516580.1 |
| Q13255-2 | ENSG00000152822.15 | ENST00000706836.1 | ENSP00000516582.1 |
| Q13255-3 | ENSG00000152822.15 | ENST00000355289.8 | ENSP00000347437.4 |
| UniProt-id | NM ID | NP ID |
| Q13255-1 | NM_001278064.1 | NP_001264993.1 |
| Q13255-1 | XM_011535782.1 | XP_011534084.1 |
| Q13255-1 | XM_017010783.1 | XP_016866272.1 |
| Q13255-1 | XM_017010784.1 | XP_016866273.1 |
| Q13255-2 | NM_001278065.1 | NP_001264994.1 |
| Q13255-2 | NM_001278066.1 | NP_001264995.1 |
| Q13255-3 | NM_001278067.1 | NP_001264996.1 |
| Amino acid sequences of our canonical and alternatively spliced GRM1 |
| accession_id | Protein sequence |
| Q13255-1 | MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKIN ADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDI PQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSF DRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLD TNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKL LDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGE VSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSREL CYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTL VVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNY KIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGG GQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEEEDAQPIRFSPPGSPSMVVHRRVPSAATTPP LPSHLTAEETPLFLAEPALPKGLPPPLQQQQQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPL QLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPDDSPALTPPSPFRDSVASGSSVPSSPVSESV |
| Q13255-2 | MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKIN ADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDI PQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSF DRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLD TNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKL LDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGE VSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSREL CYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTL VVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNY KIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNAKKRQPEFSPTSQCP |
| Q13255-3 | MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKIN ADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDI PQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSF DRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLD TNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKL LDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGE VSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSREL CYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTL VVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNY KIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNAKWRTGAQGTAYVAP |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| GRM1 (go to UniProt):Q13255 |
| 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 |
| Q13255 | Topological domain | 841 | 1194 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24603153;Dbxref=PMID:24603153 | Type=Substitution;Start=887;End=906 |
| Q13255 | Topological domain | 841 | 1194 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24603153;Dbxref=PMID:24603153 | Type=Deletion;Start=907;End=1194 |
| Q13255 | Topological domain | 841 | 1194 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24603153;Dbxref=PMID:24603153 | Type=Substitution;Start=887;End=908 |
| Q13255 | Topological domain | 841 | 1194 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24603153;Dbxref=PMID:24603153 | Type=Deletion;Start=909;End=1194 |
| Q13255 | Region | 883 | 905 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=887;End=906 |
| Q13255 | Region | 883 | 905 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=887;End=908 |
| Q13255 | Region | 1007 | 1030 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=907;End=1194 |
| Q13255 | Region | 1007 | 1030 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=909;End=1194 |
| Q13255 | Region | 1113 | 1173 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=907;End=1194 |
| Q13255 | Region | 1113 | 1173 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=909;End=1194 |
| Q13255 | Compositional bias | 1008 | 1022 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=907;End=1194 |
| Q13255 | Compositional bias | 1008 | 1022 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=909;End=1194 |
| Q13255 | Compositional bias | 1152 | 1173 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=907;End=1194 |
| Q13255 | Compositional bias | 1152 | 1173 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=909;End=1194 |
Gene Isoform Structures and Expression Levels for GRM1 |
| Gene structures of our canonical and alternative spliced genes of GRM1 * 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. |
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| Expression levels of gene isoforms across TCGA. |
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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 Q13255-1 |
| 3D view using mol* of Q13255-2 |
| 3D view using mol* of Q13255-3 |
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. |
| pLDDT distribution across the protein length of Q13255-1 |
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| pLDDT distribution across the protein length of Q13255-2 |
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| pLDDT distribution across the protein length of Q13255-3 |
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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 Q13255-1 |
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| Ramachandran plot of Q13255-2 |
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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 |
| Q13255-1 | 1.13 | 258 | 1.18 | 539.539 | 0.394 | 0.809 | 1.052 | 1.527 | 0.752 | 2.03 | 0.682 | 584,585,586,587,590,592,648,649,650,651,652,660,66 1,664,665,668,721,724,735,737,743,744,745,746,747, 748,750,752,753,756,757,760,798,801,805,809,810,81 1,812,813,815 |
| Q13255-2 | 1.116 | 267 | 1.159 | 538.853 | 0.393 | 0.804 | 1.052 | 1.522 | 0.808 | 1.883 | 0.753 | 584,585,586,587,590,648,649,650,651,652,660,661,66 4,665,668,721,733,735,737,743,744,745,746,747,748, 749,750,753,756,757,760,764,798,801,802,805,806,80 8,809,810,811,812,813,815 |
| Q13255-3 | 1.119 | 265 | 1.158 | 512.785 | 0.382 | 0.817 | 1.059 | 1.384 | 0.835 | 1.657 | 0.63 | 584,585,586,587,590,648,649,650,651,652,660,661,66 4,665,668,721,724,725,733,737,743,744,745,746,747, 748,749,750,752,753,756,757,760,798,801,802,805,80 6,809,810,811,812,813,815 |
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 Q13255-1_Q13255-1_3ks9_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 Q13255-1_3ks9_A_Q13255-2.pdb |
| 3D view using mol* of Q13255-1_3ks9_A_Q13255-3.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13255-1_Q13255-2.pdb |
| 3D view using mol* of Q13255-1_Q13255-3.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q13255-1_vs_Q13255-2.png |
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| ./stats/secondary_structure/figure/Q13255-1_vs_Q13255-3.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q13255-1_vs_Q13255-2.png |
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| ./stats/relative_asa/Q13255-1_vs_Q13255-3.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to GRM1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q13255 | GRM1 | DB00142 | Glutamic acid | approved, nutraceutical | |
| Q13255 | GRM1 | DB04256 | (S)-alpha-methyl-4-carboxyphenylglycine | experimental |
Related Diseases to GRM1 |
| Previous studies relating to the alternative splicing of GRM1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| GRM1 | 22901947 | Autosomal-recessive congenital cerebellar ataxia is caused by mutations in metabotropic glutamate receptor 1. | Autosomal-recessive congenital cerebellar ataxia was identified in Roma patients originating from a small subisolate with a known strong founder effect. Patients presented with global developmental delay, moderate to severe stance and gait ataxia, dysarthria, mild dysdiadochokinesia, dysmetria and tremors, intellectual deficit, and mild pyramidal signs. Brain imaging revealed progressive generalized cerebellar atrophy, and inferior vermian hypoplasia and/or a constitutionally small brain were observed in some patients. Exome sequencing, used for linkage analysis on extracted SNP genotypes and for mutation detection, identified two novel (i.e., not found in any database) variants located 7 bp apart within a unique 6q24 linkage region. Both mutations cosegregated with the disease in five affected families, in which all ten patients were homozygous. The mutated gene, GRM1, encodes metabotropic glutamate receptor mGluR1, which is highly expressed in cerebellar Purkinje cells and plays an important role in cerebellar development and synaptic plasticity. The two mutations affect a gene region critical for alternative splicing and the generation of receptor isoforms; they are a 3 bp exon 8 deletion and an intron 8 splicing mutation (c.2652_2654del and c.2660+2T>G, respectively [RefSeq accession number NM_000838.3]). The functional impact of the deletion is unclear and is overshadowed by the splicing defect. Although ataxia lymphoblastoid cell lines expressed GRM1 at levels comparable to those of control cells, the aberrant transcripts skipped exon 8 or ended in intron 8 and encoded various species of nonfunctional receptors either lacking the transmembrane domain and containing abnormal intracellular tails or completely missing the tail. The study implicates mGluR1 in human hereditary ataxia. It also illustrates the potential of the Roma founder populations for mutation identification by exome sequencing. | D002524 | Cerebellar Ataxia |
Clinically important variants in GRM1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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