Otu deubiquitinase 5

OTUD5
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 3PFY, 3TMO, 3TMP
Identifiers
Aliases	OTUD5, DUBA, OTU deubiquitinase 5
External IDs	HomoloGene: 136483 GeneCards: OTUD5
Gene location (Human) Chr. X chromosome (human)[1] Band No data available Start 48,922,028 bp[1] End 48,958,386 bp[1]
Gene ontology Molecular function • thiol-dependent ubiquitinyl hydrolase activity • peptidase activity • cysteine-type peptidase activity • hydrolase activity • thiol-dependent ubiquitin-specific protease activity • Lys63-specific deubiquitinase activity • ubiquitinyl hydrolase activity • Lys48-specific deubiquitinase activity Cellular component • cytosol Biological process • negative regulation of type I interferon production • response to lipopolysaccharide • protein K63-linked deubiquitination • protein K48-linked deubiquitination • proteolysis • protein deubiquitination Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	55593	n/a
Ensembl	ENSG00000068308	n/a
UniProt	Q96G74	n/a
RefSeq (mRNA)	NM_001136157 NM_001136158 NM_001136159 NM_017602	n/a
RefSeq (protein)	NP_001129629 NP_001129630 NP_001129631 NP_060072	n/a
Location (UCSC)	Chr X: 48.92 – 48.96 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

OTU deubiquitinase 5 is a protein that in humans is encoded by the OTUD5 gene. ^[3]

Function

This gene encodes a member of the OTU (ovarian tumor) domain-containing cysteine protease superfamily. The OTU domain confers deubiquitinase activity and the encoded protein has been shown to suppress the type I interferon-dependent innate immune response by cleaving the polyubiquitin chain from an essential type I interferon adaptor protein. Cleavage results in disassociation of the adaptor protein from a downstream signaling complex and disruption of the type I interferon signaling cascade. Alternatively spliced transcript variants encoding different isoforms have been described.

References

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.