Search Results
Overview
| Uniprot ID | Q9BZV1 |
|---|---|
| Protein Name | UBX domain-containing protein 6 |
| Gene Name | UBXN6 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 15 | FKADIKFKSAGPGQK |
| 166 | MKIYTFNKDQDRVKL |
| 3 | *****MKKFFQEFKA |
Function
May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes (PubMed:26475856). As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation (PubMed:21822278, PubMed:23335559). It may also play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (PubMed:19275885). Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (PubMed:27753622)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031901 | early endosome membrane |
| Cellular Component | GO:0005768 | endosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031902 | late endosome membrane |
| Cellular Component | GO:0005765 | lysosomal membrane |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0051117 | ATPase binding |
| Biological Process | GO:0032510 | endosome to lysosome transport via multivesicular body sorting pathway |
| Biological Process | GO:0036503 | ERAD pathway |
| Biological Process | GO:0016236 | macroautophagy |
| Biological Process | GO:0000423 | mitophagy |
| Biological Process | GO:0043335 | protein unfolding |
Reference
[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[2] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[3] 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.