HERC5

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

E3 ISG15–protein ligase HERC5 is an enzyme that in humans is encoded by the HERC5 gene.{{cite journal |vauthors=Mitsui K, Nakanishi M, Ohtsuka S, Norwood TH, Okabayashi K, Miyamoto C, Tanaka K, Yoshimura A, Ohtsubo M | title = A novel human gene encoding HECT domain and RCC1-like repeats interacts with cyclins and is potentially regulated by the tumor suppressor proteins | journal = Biochem Biophys Res Commun | volume = 266 | issue = 1 | pages = 115–22 |date=Jan 2000 | pmid = 10581175 | doi = 10.1006/bbrc.1999.1777 }}{{cite web | title = Entrez Gene: HERC5 hect domain and RLD 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51191}}

This gene is a member of the HERC family of ubiquitin ligases and encodes a protein with a HECT domain and five RCC1 repeats. Pro-inflammatory cytokines upregulate expression of this gene in endothelial cells. The protein localizes to the cytoplasm and perinuclear region and functions as an interferon-induced E3 protein ligase that mediates ISGylation of protein targets. The gene lies in a cluster of HERC family genes on chromosome 4. HERC5 has been shown to exhibit antiviral activity towards HIV-1, influenza A virus and human papillomavirus.{{cite journal |vauthors=Woods MW, Kelly JN, Hattlmann CJ, Tong JG, Xu LS, Coleman MD, Quest GR, Smiley JR, Barr SD | title = Human HERC5 restricts an early stage of HIV-1 assembly by a mechanism correlating with the ISGylation of Gag | journal = Retrovirology | volume = 8 | pages = 95 |date=Nov 2011 | pmid = 22093708 | pmc = 3228677| doi = 10.1186/1742-4690-8-95 | doi-access = free }}{{cite journal |vauthors=Tang Y, Zhong G, Zhu L, Liu X, Shan Y, Feng H, Bu Z, Chen H, Wang C | title = Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein | journal = J Immunol | volume = 184 | issue = 10 | pages = 5777–90 |date=May 2010 | pmid = 20385878 | doi = 10.4049/jimmunol.0903588 | doi-access = free }}{{cite journal |vauthors=Durfee LA, Lyon N, Seo K, Huibregtse JM | title = The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15 | journal = Mol Cell | volume = 38 | issue = 5 | pages = 722–32 |date=June 2010 | pmid = 20542004 | pmc = 2887317| doi = 10.1016/j.molcel.2010.05.002 }}