| Primary Identifier | IPR033382 | Type | Family |
| Short Name | USP24 |
| description | Ubiquitin-specific peptidase 24 (USP24, MEROPS identifier C19.047) is a de-ubiquitinating enzyme that is associated with late-onset Parkinson's Disease []. The enzyme is known to remove ubiquitin from damage-specific DNA-binding protein 2 (DDB2), increasing its stability. DDB2 is involved in DNA damage recognition in the nucleotide excision repair pathway, and is a component of an E3 ligase that targets XPC, histones and DDB2 itself []. USP24 also de-ubiquitinates p53, and cells are resistant to apoptosis following UV irradiation if USP24 is depleted because p53 is stabilized []. Single-nucleotide polymorphisms of the USP24 gene have been identified in lung cancer malignancy and could be diagnostic markers for the disease []. The USP24 gene is up-regulated when the USP9X gene is down-regulated by shRNA, leading to increased survival of B-cell myeloma cells []. USP24 positively regulates ferritinophagy, a process in which ferritin is degraded in lysosomes and releases free iron []. |
