Search Results
Overview
| Uniprot ID | Q9BUQ8 |
|---|---|
| Protein Name | Probable ATP-dependent RNA helicase DDX23 |
| Gene Name | DDX23 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 196 | EEERKKRKQFQDLGR |
| 259 | ERYLGGIKKRRRTRH |
| 260 | RYLGGIKKRRRTRHL |
| 310 | FIAGIDLKQQKREQS |
| 698 | ACTLHGGKGQEQREF |
| 711 | EFALSNLKAGAKDIL |
| 811 | KPGTILTKKRREETI |
| 812 | PGTILTKKRREETIF |
Function
Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation (PubMed:18425142). Independently of its spliceosome formation function, required for the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0046540 | U4/U6 x U5 tri-snRNP complex |
| Cellular Component | GO:0005682 | U5 snRNP |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003724 | RNA helicase activity |
| Biological Process | GO:0000354 | cis assembly of pre-catalytic spliceosome |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0062176 | R-loop processing |
| Biological Process | GO:0008380 | RNA splicing |
| Biological Process | GO:0000375 | RNA splicing, via transesterification reactions |
| Biological Process | GO:0000387 | spliceosomal snRNP assembly |
| Biological Process | GO:0000244 | spliceosomal tri-snRNP complex assembly |
| Biological Process | GO:0000388 | spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) |
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] 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.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] 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.
[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[6] 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.