• The protein encoded by this gene is a protease that functions as a deubiquitinating enzyme. The encoded protein is thought to help regulate the spindle assembly checkpoint by preventing early anaphase onset. This protein specifically deubiquitinates CDC20, which stabilizes the anaphase promoting complex/cyclosome. [provided by RefSeq, Dec 2016]
  

USP44 (Ubiquitin Specific Peptidase 44) is a Protein Coding gene. Diseases associated with USP44 include T-Cell Acute Lymphoblastic Leukemia and Embryonal Carcinoma. Among its related pathways are Deubiquitination and Metabolism of proteins. Gene Ontology (GO) annotations related to this gene include cysteine-type endopeptidase activity and cysteine-type deubiquitinase activity. An important paralog of this gene is USP49.

Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C) (PubMed:17443180). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C (PubMed:17443180). Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint (PubMed:17443180). Promotes also the deubiquitination of histone H2A and H2B (PubMed:23615962, 27880911). Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin (PubMed:23615962). Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin (By similarity). Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability (PubMed:32644293). Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-linked polyubiquitin chains and stabilizing it (PubMed:31968013). ( UBP44_HUMAN,Q9H0E7 )