Search Results

Overview

Uniprot IDQ9Y3B4
Protein NameSplicing factor 3B subunit 6
Gene NameSF3B6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 NANRAFQKMDTKKKE
7 *MAMQAAKRANIRLP

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: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, SF3B6 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). Within the 17S U2 SnRNP complex, SF3B6 directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing (PubMed:16432215). SF3B6 stabilizes the intron branch site-U2 snRNA duplex, thereby promoting-binding of introns with poor sequence complementarity (PubMed:34822310). 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

10 MAMQAAKRAN 20 IRLPPEVNRI 30 LYIRNLPYKI 40 TAEEMYDIFG 50 KYGPIRQIRV 60 GNTPETRGTA 70 YVVYEDIFDA 80 KNACDHLSGF 90 NVCNRYLVVL 100 YYNANRAFQK 110 MDTKKKEEQL 120 KLLKEKYGIN TDPPK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005689 U12-type spliceosomal complex
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000398 mRNA splicing, via spliceosome
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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[2] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.