HERC3
| HERC3 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | HERC3 | ||||||
| Alt. names | HECT domain and RCC1-like domain-containing protein 3, HECT-type E3 ubiquitin transferase HERC3, KIAA0032 | ||||||
Chr. 4 q22.1:88,592,422-88,709,302 | |||||||
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Probable E3 ubiquitin-protein ligase HERC3 is an
ubiquitin ligases and encodes a protein with a HECT domain and an RCC1-like domain (RLD). It binds ubiquitin and hPLIC-1/2 via its HECT domain. Alternatively spiced transcript variants encoding multiple isoforms have been observed, and mutations in this gene have been linked to colorectal and gastric carcinomas. The protein is localized in the cytosol and vesicular-like structures containing β-COP, ARF, and Rab5. Since HERC3 can itself be ubiquitinated and degraded by the proteasome, it likely has roles in both vesicular traffic and ubiquitin-dependent processes.[3][4][5]
References
Further reading
- Hochrainer K, Pejanovic N, Olaseun VA, Zhang S, Iadecola C, Anrather J (16 Nov 2015). "The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation". Nucleic Acids Res. 43 (20): 9889–9904. PMID 26476452.
- Cowley M, Wood AJ, Böhm S, Schulz R, Oakey RJ (Oct 2012). "Epigenetic control of alternative mRNA processing at the imprinted Herc3/Nap1l5 locus". Nucleic Acids Res. 40 (18): 8917–8926. PMID 22790983.
- Yoo NJ, Park SJ, Lee SH (Dec 2011). "Frameshift mutations of ubiquitination-related genes HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B in gastric and colorectal carcinomas with microsatellite instability". Pathology. 43 (7): 753–755. PMID 22124266.
- Scheffner M, Staub O (22 Nov 2007). "HECT E3s and human disease". BMC Biochem. 8 ((Suppl 1):S6): S6. PMID 18047743.
- Cruz C, Nadal M, Ventura F, Bartrons R, Estivill X, Rosa JL (1999). "The human HERC3 gene maps to chromosome 4q21 by fluorescence in situ hybridization". Cytogenet Cell Genet. 87 (3–4): 263–264. S2CID 42602080.
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