HERC5

Probable E3 ubiquitin-protein ligase HERC5 is an enzyme that in humans is encoded by the HERC5 gene.[3][4]

HERC5
Identifiers
AliasesHERC5, CEB1, CEBP1, HECT and RLD domain containing E3 ubiquitin protein ligase 5
External IDsOMIM: 608242 HomoloGene: 81848 GeneCards: HERC5
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4q22.1Start88,457,119 bp[1]
End88,506,163 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

51191

n/a

Ensembl

ENSG00000138646

n/a

UniProt

Q9UII4

n/a

RefSeq (mRNA)

NM_016323

n/a

RefSeq (protein)

NP_057407

n/a

Location (UCSC)Chr 4: 88.46 – 88.51 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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.[4] HERC5 has been shown to exhibit antiviral activity towards HIV-1, influenza A virus and human papillomavirus.[5][6][7]

Interactions

HERC5 has been shown to interact with NME2[8] and Cyclin E1.[3]

References

  1. GRCh38: Ensembl release 89: ENSG00000138646 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. Mitsui K, Nakanishi M, Ohtsuka S, Norwood TH, Okabayashi K, Miyamoto C, Tanaka K, Yoshimura A, Ohtsubo M (Jan 2000). "A novel human gene encoding HECT domain and RCC1-like repeats interacts with cyclins and is potentially regulated by the tumor suppressor proteins". Biochem Biophys Res Commun. 266 (1): 115–22. doi:10.1006/bbrc.1999.1777. PMID 10581175.
  4. "Entrez Gene: HERC5 hect domain and RLD 5".
  5. Woods MW, Kelly JN, Hattlmann CJ, Tong JG, Xu LS, Coleman MD, Quest GR, Smiley JR, Barr SD (Nov 2011). "Human HERC5 restricts an early stage of HIV-1 assembly by a mechanism correlating with the ISGylation of Gag". Retrovirology. 8: 95. doi:10.1186/1742-4690-8-95. PMC 3228677. PMID 22093708.
  6. Tang Y, Zhong G, Zhu L, Liu X, Shan Y, Feng H, Bu Z, Chen H, Wang C (May 2010). "Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein". J Immunol. 184 (10): 5777–90. doi:10.4049/jimmunol.0903588. PMID 20385878.
  7. Durfee LA, Lyon N, Seo K, Huibregtse JM (June 2010). "The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15". Mol Cell. 38 (5): 722–32. doi:10.1016/j.molcel.2010.05.002. PMC 2887317. PMID 20542004.
  8. Hochrainer, K; Kroismayr R; Baranyi U; Binder B R; Lipp J (Jul 2008). "Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B". Cell. Mol. Life Sci. Switzerland. 65 (13): 2105–17. doi:10.1007/s00018-008-8148-5. ISSN 1420-682X. PMID 18535780.


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