Search Results
Overview
| Uniprot ID | Q9HCN4 |
|---|---|
| Protein Name | GPN-loop GTPase 1 |
| Gene Name | GPN1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 297 | EQLERLRKDMGSVAL |
Function
Small GTPase involved in the correct assembly of RNA polymerase II (RNAPII) complex, ensuring proper nuclear import of RNAPII (PubMed:11058119, PubMed:20855544, PubMed:21768307, PubMed:28153773). In vitro, exhibits a chaperone-like activity and a chaperone substrate protein can stimulate its GTPase activity. It is proposed to bind exposed hydrophobic peptide regions of newly synthesized RNAP II subunit, triggering the opening of a hydrophobic pocket in its GDP-bound state. This interaction likely traps exposed hydrophobic regions, preventing misassembly and providing a time window for association with the cognate RNAP II subunit. Peptide binding promotes GDP release, and increasing GTP affinity to facilitate GTP rebinding. Subsequent GTP hydrolysis would then lead to the release of the bound RNAP II subunit to enable association with cognate subunits and RNAP II assembly (By similarity). Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation (PubMed:17643375). May be involved in nuclear localization of XPA (PubMed:11058119)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0000993 | RNA polymerase II complex binding |
| Biological Process | GO:0006606 | protein import into nucleus |
Reference
[1] 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.
[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.