USP16
Description
The USP16 (ubiquitin specific peptidase 16) is a protein-coding gene located on chromosome 21.
USP16 is a human gene that encodes a deubiquitinating enzyme. This enzyme is phosphorylated at the start of mitosis and dephosphorylated at the metaphase/anaphase transition. It can remove ubiquitin from histone H2A in vitro, and a mutant form of the protein was found to block cell division. Different isoforms of USP16 are produced through alternative splicing.
USP16 specifically removes ubiquitin from lysine 120 of histone H2A (H2AK119Ub), a modification that typically represses gene expression. This deubiquitination acts as a coactivator, promoting gene transcription. Deubiquitination of H2A is necessary for subsequent phosphorylation of serine 11 on histone H3 (H3S10ph), a step crucial for chromosome segregation during mitosis. In resting B and T lymphocytes, USP16 activity is increased by phosphorylation mediated by AURKB, contributing to the maintenance of transcription in these cells. USP16 regulates Hox gene expression by deubiquitinating H2A. It preferentially acts on nucleosomal substrates and does not remove ubiquitin from histone H2B. Additionally, USP16 deubiquitinates non-histone proteins, such as ribosomal protein RPS27A. This deubiquitination of monoubiquitinated RPS27A facilitates the maturation of the 40S ribosomal subunit.
USP16 is also known as UBP-M, UBPM.
Associated Diseases
- linear and whorled nevoid hypermelanosis
- thrombocytopenia 4
- eosinophil peroxidase deficiency
- macrothrombocytopenia, isolated, 2, autosomal dominant
- thrombocytopenia 2
- neutropenia, severe congenital, 1, autosomal dominant
- DIAPH1-related sensorineural hearing loss-thrombocytopenia syndrome
- platelet-type bleeding disorder 15
- autosomal dominant macrothrombocytopenia
- thrombocytopenia 7
- ichthyosis prematurity syndrome
