Search Results
Overview
| Uniprot ID | P61086 |
|---|---|
| Protein Name | Ubiquitin-conjugating enzyme E2 K |
| Gene Name | UBE2K |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 18 | REFKEVLKSEETSKN |
Function
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Molecular Function | GO:0061631 | ubiquitin conjugating enzyme activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0004842 | ubiquitin-protein transferase activity |
| Molecular Function | GO:0034450 | ubiquitin-ubiquitin ligase activity |
| Biological Process | GO:0035458 | cellular response to interferon-beta |
| Biological Process | GO:0010994 | free ubiquitin chain polymerization |
| Biological Process | GO:0010800 | positive regulation of peptidyl-threonine phosphorylation |
| Biological Process | GO:1903265 | positive regulation of tumor necrosis factor-mediated signaling pathway |
| Biological Process | GO:0060340 | positive regulation of type I interferon-mediated signaling pathway |
| Biological Process | GO:0070936 | protein K48-linked ubiquitination |
| Biological Process | GO:0000209 | protein polyubiquitination |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0032433 | filopodium tip |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
Reference
[1] 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.
[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] 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.
[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.