Primary Information |
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BoMiProt ID | Bomi10189 |
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Protein Name | U6 snRNA-associated Sm-like protein LSm8 |
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Organism | Bos taurus |
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Uniprot Id | Q3ZCE0 |
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Milk Fraction | whey |
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Ref Sequence Id | NP_001029912.1 |
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Aminoacid Length | 96 |
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Molecular Weight | 10403 |
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Fasta Sequence | https://www.uniprot.org/uniprot/Q3ZCE0.fasta |
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Gene Name | LSM8 |
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Gene Id | 613630 |
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Protein Existence Status | Reviewed |
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Secondary Information |
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Protein Function | The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.LSm proteins may play a role in U4/U6 snRNP formation. |
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Biochemical Properties | Conserved "Sm motif".The Sm motif is relatively degenerate and consists of two parts, termed Sm1 and Sm2 domains, which are often separated by a large loop region.form seven-member ring structures that interact with RNA. |
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PTMs | Acetylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| na |
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Predicted Disorder Regions | 1-4, 80-84, 86-96 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Bibliography | Achsel T, Brahms H, Kastner B, Bachi A, Wilm M, Lührmann R. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J. 1999 Oct 15;18(20):5789-802. doi: 10.1093/emboj/18.20.5789. PMID: 10523320; PMCID: PMC1171645. |