Search Results
Overview
| Uniprot ID | O95391 |
|---|---|
| Protein Name | Pre-mRNA-splicing factor SLU7 |
| Gene Name | SLU7 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 114 | KENSIITKYRKGACE |
| 117 | SIITKYRKGACENCG |
| 199 | KRTLKAQKLQEELAS |
| 355 | TKLELLYKSFKVKKE |
| 527 | KKHEKLKKALNAEEA |
Function
Required for pre-mRNA splicing as component of the spliceosome (PubMed:10197984, PubMed:28502770, PubMed:30705154). Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0030532 | small nuclear ribonucleoprotein complex |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Molecular Function | GO:0030628 | pre-mRNA 3'-splice site binding |
| Molecular Function | GO:0000386 | second spliceosomal transesterification activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0000380 | alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0034605 | cellular response to heat |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:0000389 | mRNA 3'-splice site recognition |
| Biological Process | GO:0045292 | mRNA cis splicing, via spliceosome |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0000375 | RNA splicing, via transesterification reactions |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[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.
[3] 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.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.