Protein:L3MBTL1 |
Protein Summary |
 Gene summary |
| Gene name: L3MBTL1 | ASpdb.0 ID: 26013 | Gene | Gene symbol | L3MBTL1 | Gene ID | 26013 |
| Gene name | L3MBTL histone methyl-lysine binding protein 1 |
| Synonyms | H-L(3)MBT|L3MBTL|ZC2HC3|dJ138B7.3 |
| Cytomap | 20q13.12 |
| Type of gene | protein-coding |
| Description | lethal(3)malignant brain tumor-like protein 1L3MBTL1, histone methyl-lysine binding proteinl(3)mbt protein homologl(3)mbt-like 1lethal (3) malignant brain tumor l(3) |
| Modification date | 20240305 |
| UniProtAcc | Q9Y468 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | L3MBTL1 | GO:0000785 | chromatin | 18408754 |
| Gene | L3MBTL1 | GO:0000793 | condensed chromosome | 10445843 |
| Gene | L3MBTL1 | GO:0003682 | chromatin binding | 18408754 |
| Gene | L3MBTL1 | GO:0005634 | nucleus | 10445843|17540172|18408754 |
| Gene | L3MBTL1 | GO:0005654 | nucleoplasm | 10445843 |
| Gene | L3MBTL1 | GO:0005730 | nucleolus | 10445843 |
| Gene | L3MBTL1 | GO:0006325 | chromatin organization | 17540172 |
| Gene | L3MBTL1 | GO:0031491 | nucleosome binding | 17540172 |
| Gene | L3MBTL1 | GO:0031507 | heterochromatin formation | 17540172 |
| Gene | L3MBTL1 | GO:0035064 | methylated histone binding | 19144645|20622853|22120668 |
| Gene | L3MBTL1 | GO:0045652 | regulation of megakaryocyte differentiation | 18474616 |
| Gene | L3MBTL1 | GO:0045892 | negative regulation of DNA-templated transcription | 17540172|18408754|18474616 |
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 |
| Q9Y468-5 | Q9Y468-5_2rjd_A.pdb | 2RJD | X-ray | 1.65 | A | 272 | 596 |
| 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 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-1 | 840 | 772 | 1 | 98 | Substitution | MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLR | MRRREGHGTDSEMGQGPVRESQSSDPPALQ | 1 | 30 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-2 | 840 | 738 | 1 | 98 | Substitution | MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLR | MRRREGHGTDSEMGQGPVRESQSSDPPALQ | 1 | 30 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-2 | 840 | 738 | 777 | 840 | Substitution | ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY | VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC | 709 | 738 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-3 | 840 | 390 | 1 | 416 | Deletion | none | none | 0 | 0 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-3 | 840 | 390 | 777 | 840 | Substitution | ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY | VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC | 361 | 390 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-4 | 840 | 752 | 1 | 98 | Substitution | MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLR | MRRREGHGTDSEMGQGPVRESQSSDPPALQ | 1 | 30 |
| Q9Y468 | L3MBTL1 | Q9Y468-5 | Q9Y468-4 | 840 | 752 | 777 | 840 | Substitution | ARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY | MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADDTLK | 709 | 752 |
| Multiple sequence alignment of our canonical and alternatively spliced L3MBTL1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of L3MBTL1 |
| UniProt-id | ENSG | ENST | ENSP |
| Q9Y468-5 | ENSG00000185513.18 | ENST00000427442.8 | ENSP00000402107.4 |
| Q9Y468-1 | ENSG00000185513.18 | ENST00000373135.8 | ENSP00000362227.3 |
| Q9Y468-4 | ENSG00000185513.18 | ENST00000422861.3 | ENSP00000410139.2 |
| UniProt-id | NM ID | NP ID |
| Q9Y468-5 | NM_032107.4 | NP_115479.4 |
| Q9Y468-1 | NM_015478.6 | NP_056293.4 |
| Amino acid sequences of our canonical and alternatively spliced L3MBTL1 |
| accession_id | Protein sequence |
| Q9Y468-5 | MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAA PPPGGGLRFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQDPPEDDSTCQCQACGPHQAAGP DLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEGQPTASTPESEEWSSSQPATGEK KECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHP AGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNW DDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVE DVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLPHTRTSKYSFHHRKCPTPGCDGS GHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSA HPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGK |
| Q9Y468-1 | MRRREGHGTDSEMGQGPVRESQSSDPPALQFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQ DPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEG QPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRL HFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPS LVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFL VNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLP HTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQ EDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGK |
| Q9Y468-2 | MRRREGHGTDSEMGQGPVRESQSSDPPALQFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQ DPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEG QPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRL HFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPS LVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFL VNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLP HTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQ EDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEVRCKCRVGDRAG |
| Q9Y468-3 | MKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPT WAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASP GGCPPLSYRSLPHTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGR IGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDE |
| Q9Y468-4 | MRRREGHGTDSEMGQGPVRESQSSDPPALQFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQ DPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEG QPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRL HFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPS LVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFL VNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLP HTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQ EDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEMIDGEAFLLLTQ |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| L3MBTL1 (go to UniProt):Q9Y468 |
| 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 |
| Q9Y468 | Repeat | 274 | 374 | Note=MBT 1 | Type=Deletion;Start=1;End=416 |
| Q9Y468 | Repeat | 382 | 481 | Note=MBT 2 | Type=Deletion;Start=1;End=416 |
| Q9Y468 | Region | 127 | 269 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=416 |
| Q9Y468 | Compositional bias | 187 | 211 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=416 |
| Q9Y468 | Compositional bias | 213 | 246 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=416 |
| Q9Y468 | Compositional bias | 250 | 269 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=416 |
Gene Isoform Structures and Expression Levels for L3MBTL1 |
| Gene structures of our canonical and alternative spliced genes of L3MBTL1 * 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 Q9Y468-5 |
| 3D view using mol* of Q9Y468-1 |
| 3D view using mol* of Q9Y468-2 |
| 3D view using mol* of Q9Y468-3 |
| 3D view using mol* of Q9Y468-4 |
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 Q9Y468-5 |
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| pLDDT distribution across the protein length of Q9Y468-1 |
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| pLDDT distribution across the protein length of Q9Y468-2 |
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| pLDDT distribution across the protein length of Q9Y468-3 |
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| pLDDT distribution across the protein length of Q9Y468-4 |
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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 Q9Y468-5 |
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| Ramachandran plot of Q9Y468-2 |
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| Ramachandran plot of Q9Y468-3 |
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| Ramachandran plot of Q9Y468-4 |
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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 |
| Q9Y468-5 | 1.014 | 209 | 1.067 | 740.537 | 0.669 | 0.651 | 0.843 | 0.825 | 0.808 | 1.02 | 1.234 | 423,425,426,429,431,432,447,450,454,479,480,481,48 2,483,484,487,737,738,739,751,753,759,762,763,764, 765,766,767,768,769,772,773,776,777,780,785,787,78 9,790,793,796,797,800,801,812,813,814,815,816,817, 818,819,820,821,822,823,824 |
| Q9Y468-1 | 1.068 | 135 | 1.15 | 362.208 | 0.574 | 0.669 | 0.845 | 1.158 | 0.586 | 1.975 | 1.222 | 355,357,358,359,360,361,363,379,382,386,411,723,72 4,725,726,742,745,746,747,749,750,751,753,754,761, 766,767,768,769 |
| Q9Y468-2 | 1.043 | 211 | 1.064 | 939.477 | 0.598 | 0.749 | 0.936 | 0.556 | 0.998 | 0.557 | 0.914 | 226,227,228,229,231,247,248,249,250,251,252,256,26 7,272,275,278,279,281,282,283,284,286,287,288,289, 291,334,335,356,357,371,372,373,374,379,385,386,38 7,388,389,390,391,394,395,396,444,447,458,460,463, 477,495,496,497,498,499,500,592 |
| Q9Y468-3 | 1.021 | 124 | 1 | 310.415 | 0.585 | 0.73 | 0.952 | 0.322 | 1.159 | 0.278 | 0.779 | 111,113,114,115,116,117,119,136,138,142,167,168,16 9,170,171,174,210,211,212,214,215,216,217,219,221, 222,224,231,232,240 |
| Q9Y468-4 | 1.002 | 760 | 1.018 | 2713.816 | 0.6 | 0.701 | 0.889 | 0.434 | 1.052 | 0.412 | 0.853 | 226,228,229,247,248,249,250,251,252,256,262,264,26 7,269,272,275,277,278,279,280,281,282,283,284,286, 287,288,289,334,335,336,337,338,339,354,355,356,35 7,358,359,361,363,371,372,373,374,379,382,383,385, 386,387,388,389,390,391,394,395,396,398,411,414,44 4,458,460,461,462,463,464,465,466,475,476,477,478, 480,488,489,491,492,493,494,495,497,498,499,500,51 2,513,515,562,563,564,567,569,570,579,586,587,588, 589,590,591,592,593,594,595,596,646,647,648,649,65 0,651,652,653,654,656,657,658,659,660,661,662,663, 665,666,672,673,674,675,719,720,731,732,735,738,74 2,743,746,747,750 |
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 Q9Y468-5_Q9Y468-5_2rjd_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 Q9Y468-5_2rjd_A_Q9Y468-1.pdb |
| 3D view using mol* of Q9Y468-5_2rjd_A_Q9Y468-2.pdb |
| 3D view using mol* of Q9Y468-5_2rjd_A_Q9Y468-3.pdb |
| 3D view using mol* of Q9Y468-5_2rjd_A_Q9Y468-4.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q9Y468-5_Q9Y468-1.pdb |
| 3D view using mol* of Q9Y468-5_Q9Y468-2.pdb |
| 3D view using mol* of Q9Y468-5_Q9Y468-3.pdb |
| 3D view using mol* of Q9Y468-5_Q9Y468-4.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q9Y468-5_vs_Q9Y468-1.png |
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| ./stats/secondary_structure/figure/Q9Y468-5_vs_Q9Y468-2.png |
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| ./stats/secondary_structure/figure/Q9Y468-5_vs_Q9Y468-3.png |
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| ./stats/secondary_structure/figure/Q9Y468-5_vs_Q9Y468-4.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q9Y468-5_vs_Q9Y468-1.png |
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| ./stats/relative_asa/Q9Y468-5_vs_Q9Y468-2.png |
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| ./stats/relative_asa/Q9Y468-5_vs_Q9Y468-3.png |
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| ./stats/relative_asa/Q9Y468-5_vs_Q9Y468-4.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 L3MBTL1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q9Y468 | L3MBTL1 | DB03814 | 2-(N-morpholino)ethanesulfonic acid | experimental |
Related Diseases to L3MBTL1 |
| Previous studies relating to the alternative splicing of L3MBTL1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| L3MBTL1 | 15566354 | Characterization of the imprinted polycomb gene L3MBTL, a candidate 20q tumour suppressor gene, in patients with myeloid malignancies. | Chromosome 20q deletion is a recurrent chromosomal abnormality associated with myeloid malignancies. L3MBTL represents a strong candidate tumour suppressor gene since it lies within the common deleted region, is a member of the Polycomb-like family, encodes the human homologue of a Drosophila tumour suppressor and is expressed within haematopoietic progenitor cells. We describe the structure of L3MBTL, identify two putative promoters each associated with two CpG islands and characterize a complex pattern of alternative splicing events. Mutation analysis of the gene in patients with and without a 20q deletion identified several polymorphisms but no acquired mutations. The two CpG islands spanning promoter 2 undergo monoallelic methylation in normal haematopoietic cells consistent with imprinting of L3MBTL. Samples from patients with a 20q deletion retained either the methylated or unmethylated allele but retention of the methylated allele did not correlate with reduction in L3MBTL mRNA levels. The absence of a correlation between L3MBTL methylation and transcription could be shown to reflect loss of imprinting in one patient. In addition, our results demonstrate that inactivation of L3MBTL is not a common occurrence in patients with a 20q deletion or in cytogenetically normal patients with polycythaemia vera. | D001855 | Bone Marrow Diseases |
| L3MBTL1 | 15566354 | Characterization of the imprinted polycomb gene L3MBTL, a candidate 20q tumour suppressor gene, in patients with myeloid malignancies. | Chromosome 20q deletion is a recurrent chromosomal abnormality associated with myeloid malignancies. L3MBTL represents a strong candidate tumour suppressor gene since it lies within the common deleted region, is a member of the Polycomb-like family, encodes the human homologue of a Drosophila tumour suppressor and is expressed within haematopoietic progenitor cells. We describe the structure of L3MBTL, identify two putative promoters each associated with two CpG islands and characterize a complex pattern of alternative splicing events. Mutation analysis of the gene in patients with and without a 20q deletion identified several polymorphisms but no acquired mutations. The two CpG islands spanning promoter 2 undergo monoallelic methylation in normal haematopoietic cells consistent with imprinting of L3MBTL. Samples from patients with a 20q deletion retained either the methylated or unmethylated allele but retention of the methylated allele did not correlate with reduction in L3MBTL mRNA levels. The absence of a correlation between L3MBTL methylation and transcription could be shown to reflect loss of imprinting in one patient. In addition, our results demonstrate that inactivation of L3MBTL is not a common occurrence in patients with a 20q deletion or in cytogenetically normal patients with polycythaemia vera. | D002872 | Chromosome Deletion |
| L3MBTL1 | 15566354 | Characterization of the imprinted polycomb gene L3MBTL, a candidate 20q tumour suppressor gene, in patients with myeloid malignancies. | Chromosome 20q deletion is a recurrent chromosomal abnormality associated with myeloid malignancies. L3MBTL represents a strong candidate tumour suppressor gene since it lies within the common deleted region, is a member of the Polycomb-like family, encodes the human homologue of a Drosophila tumour suppressor and is expressed within haematopoietic progenitor cells. We describe the structure of L3MBTL, identify two putative promoters each associated with two CpG islands and characterize a complex pattern of alternative splicing events. Mutation analysis of the gene in patients with and without a 20q deletion identified several polymorphisms but no acquired mutations. The two CpG islands spanning promoter 2 undergo monoallelic methylation in normal haematopoietic cells consistent with imprinting of L3MBTL. Samples from patients with a 20q deletion retained either the methylated or unmethylated allele but retention of the methylated allele did not correlate with reduction in L3MBTL mRNA levels. The absence of a correlation between L3MBTL methylation and transcription could be shown to reflect loss of imprinting in one patient. In addition, our results demonstrate that inactivation of L3MBTL is not a common occurrence in patients with a 20q deletion or in cytogenetically normal patients with polycythaemia vera. | D009190 | Myelodysplastic Syndromes |
| L3MBTL1 | 15566354 | Characterization of the imprinted polycomb gene L3MBTL, a candidate 20q tumour suppressor gene, in patients with myeloid malignancies. | Chromosome 20q deletion is a recurrent chromosomal abnormality associated with myeloid malignancies. L3MBTL represents a strong candidate tumour suppressor gene since it lies within the common deleted region, is a member of the Polycomb-like family, encodes the human homologue of a Drosophila tumour suppressor and is expressed within haematopoietic progenitor cells. We describe the structure of L3MBTL, identify two putative promoters each associated with two CpG islands and characterize a complex pattern of alternative splicing events. Mutation analysis of the gene in patients with and without a 20q deletion identified several polymorphisms but no acquired mutations. The two CpG islands spanning promoter 2 undergo monoallelic methylation in normal haematopoietic cells consistent with imprinting of L3MBTL. Samples from patients with a 20q deletion retained either the methylated or unmethylated allele but retention of the methylated allele did not correlate with reduction in L3MBTL mRNA levels. The absence of a correlation between L3MBTL methylation and transcription could be shown to reflect loss of imprinting in one patient. In addition, our results demonstrate that inactivation of L3MBTL is not a common occurrence in patients with a 20q deletion or in cytogenetically normal patients with polycythaemia vera. | D009196 | Myeloproliferative Disorders |
Clinically important variants in L3MBTL1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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