Search Results
Overview
| Uniprot ID | Q9UPT9 |
|---|---|
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 22 |
| Gene Name | USP22 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 137 | EEQRKAWKMQGVGEK |
| 159 | KRELELLKHNPKRRK |
| 166 | KHNPKRRKITSNCTI |
| 417 | KRFEHSAKLRRKITT |
Function
Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. As part of the transcription regulatory histone acetylation (HAT) complex SAGA, catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a transcriptional coactivator (PubMed:18206972, PubMed:18206973, PubMed:18469533). Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Facilitates cell-cycle progression by stabilizing CCNB1 and antagonizing its proteasome-mediated degradation in a cell cycle-specific manner (PubMed:27030811). Modulates cell cycle progression and apoptosis also by antagonizing TP53 transcriptional activation through deacetylase SIRT1 stabilization (PubMed:22542455). Plays multiple roles in immunity and inflammation. Participates in antiviral response by deubiquitinating the importin KPNA2, leading to IRF3 nuclear translocation and subsequent type I interferon production (PubMed:32130408). Acts as a central regulator of type III IFN signaling by negatively regulating STING1 activation and ubiquitination (PubMed:35933402). Inhibits NLRP3 inflammasome activation by promoting NLRP3 degradation through ATG5-dependent autophagy (By similarity). Deubiquitinates CD274 to induce its stabilization and thereby participates in maintenance of immune tolerance to self (PubMed:31399419). Controls necroptotic cell death by regulating RIPK3 phosphorylation and ubiquitination (PubMed:33369872). During bacterial infection, promotes pro-inflammatory response by targeting TRAF6 and removing its 'Lys-48'-linked polyubiquitination (By similarity)
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:0000124 | SAGA complex |
| Molecular Function | GO:0004843 | cysteine-type deubiquitinase activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0140950 | histone H2A deubiquitinase activity |
| Molecular Function | GO:0140936 | histone H2B deubiquitinase activity |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0009792 | embryo development ending in birth or egg hatching |
| Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0045931 | positive regulation of mitotic cell cycle |
| Biological Process | GO:0032481 | positive regulation of type I interferon production |
| Biological Process | GO:0016579 | protein deubiquitination |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0006282 | regulation of DNA repair |
| Biological Process | GO:0043484 | regulation of RNA splicing |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
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] 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.