Search Results
Overview
| Uniprot ID | O60231 |
|---|---|
| Protein Name | Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 |
| Gene Name | DHX16 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1027 | ELEDPHAKKMPKKIG |
| 1028 | LEDPHAKKMPKKIGK |
| 131 | KRKHLRKKREEEEEE |
| 210 | KAYEEAQKRLKMAEE |
| 213 | EEAQKRLKMAEEDRK |
| 302 | TNRYHMPKETRGQPA |
| 340 | RLGAASLKFGARDAA |
| 73 | LWNKVPRKAVVEKPA |
| 78 | PRKAVVEKPARAAER |
| 93 | EARALLEKNRSYRLL |
Function
Required for pre-mRNA splicing as a component of the spliceosome (PubMed:20423332, PubMed:20841358, PubMed:25296192, PubMed:29360106). Contributes to pre-mRNA splicing after spliceosome formation and prior to the first transesterification reaction. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Also plays a role in innate antiviral response by acting as a pattern recognition receptor sensing splicing signals in viral RNA (PubMed:35263596). Mechanistically, TRIM6 promotes the interaction between unanchored 'Lys-48'-polyubiquitin chains and DHX16, leading to DHX16 interaction with RIGI and ssRNA to amplify RIGI-dependent innate antiviral immune responses (PubMed:35263596)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0004386 | helicase activity |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0038187 | pattern recognition receptor activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003724 | RNA helicase activity |
| Molecular Function | GO:0043130 | ubiquitin binding |
| Biological Process | GO:0140374 | antiviral innate immune response |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0008380 | RNA splicing |
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.