Search Results
Overview
| Uniprot ID | Q9BWJ5 |
|---|---|
| Protein Name | Splicing factor 3B subunit 5 |
| Gene Name | SF3B5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 17 | QLEHLQSKYIGTGHA |
Function
Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:28781166, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B4 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0071011 | precatalytic spliceosome |
| Cellular Component | GO:0005689 | U12-type spliceosomal complex |
| Cellular Component | GO:0005686 | U2 snRNP |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Cellular Component | GO:0005684 | U2-type spliceosomal complex |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:1990935 | splicing factor binding |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0006282 | regulation of DNA repair |
| Biological Process | GO:0043484 | regulation of RNA splicing |
| Biological Process | GO:0000387 | spliceosomal snRNP assembly |
| Biological Process | GO:0000388 | spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) |
| Biological Process | GO:1903241 | U2-type prespliceosome assembly |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.