Search Results
Overview
| Uniprot ID | Q9NPD8 |
|---|---|
| Protein Name | Ubiquitin-conjugating enzyme E2 T |
| Gene Name | UBE2T |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 180 | RVHNSTQKRKASQLV |
| 182 | HNSTQKRKASQLVGI |
| 191 | SQLVGIEKKFHPDV* |
| 192 | QLVGIEKKFHPDV** |
Function
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair. Acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784, PubMed:28437106). Also mediates monoubiquitination of FANCL and FANCI (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784). May contribute to ubiquitination and degradation of BRCA1 (PubMed:19887602). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:20061386)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0061631 | ubiquitin conjugating enzyme activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0004842 | ubiquitin-protein transferase activity |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0051865 | protein autoubiquitination |
| Biological Process | GO:0070979 | protein K11-linked ubiquitination |
| Biological Process | GO:0044314 | protein K27-linked ubiquitination |
| Biological Process | GO:0035519 | protein K29-linked ubiquitination |
| Biological Process | GO:0070936 | protein K48-linked ubiquitination |
| Biological Process | GO:0085020 | protein K6-linked ubiquitination |
| Biological Process | GO:0070534 | protein K63-linked ubiquitination |
| Biological Process | GO:0006513 | protein monoubiquitination |
| Biological Process | GO:0000209 | protein polyubiquitination |
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] 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.
[4] 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.
[5] 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.