HERC3
| HERC3 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | HERC3 | ||||||
| Alt. names | HECT domain and RCC1-like domain-containing protein 3, HECT-type E3 ubiquitin transferase HERC3, KIAA0032 | ||||||
| NCBI gene | 8916 | ||||||
| HGNC | 4876 | ||||||
| OMIM | 605200 | ||||||
| PDB | Q15034 | ||||||
| RefSeq | NM_001271602, NM_001318505 NM_014606, NM_001271602, NM_001318505 | ||||||
| UniProt | Q15034 | ||||||
| Other data | |||||||
| EC number | 2.3.2.26 | ||||||
| Locus | Chr. 4 q22.1:88,592,422-88,709,302 | ||||||
| |||||||
Probable E3 ubiquitin-protein ligase HERC3 is an enzyme that in humans is encoded by the HERC3 gene.[1][2] The gene is a member of the HERC family of 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
[edit]- ^ Garcia-Gonzalo FR, Rosa JL (Aug 2005). "The HERC proteins: functional and evolutionary insights". Cell Mol Life Sci. 62 (16): 1826–1838. doi:10.1007/s00018-005-5119-y. PMC 11139159. PMID 15968461. S2CID 23391275.
- ^ Sánchez-Tena S, Cubillos-Rojas M, Schneider T, Rosa JL (May 2016). "Functional and pathological relevance of HERC family proteins: a decade later". Cell Mol Life Sci. 73 (10): 18955–1968. doi:10.1007/s00018-016-2139-8. PMC 11108380. PMID 26801221. S2CID 7457614.
- ^ Hochrainer K, Kroismayr R, Baranyi U, Binder BR, Lipp J (Jul 2008). "Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B". Cell Mol Life Sci. 65 (13): 2105–2117. doi:10.1007/s00018-008-8148-5. PMC 11131906. PMID 18535780. S2CID 6897759.
- ^ Cruz C, Ventura F, Bartrons R, Rosa JL (Jan 2001). "HERC3 binding to and regulation by ubiquitin". FEBS Lett. 488 (1–2): 74–80. doi:10.1016/S0014-5793(00)02371-1. PMID 11163799. S2CID 20091003.
- ^ "Entrez Gene: HERC3".
Further reading
[edit]- 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. doi:10.1093/nar/gkv1064. PMC 4787756. 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. doi:10.1093/nar/gks654. PMC 3467052. 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. doi:10.1097/PAT.0b013e32834c7e78. PMID 22124266.
- Scheffner M, Staub O (22 Nov 2007). "HECT E3s and human disease". BMC Biochem. 8 ((Suppl 1):S6): S6. doi:10.1186/1471-2091-8-S1-S6. PMC 2106370. 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. doi:10.1159/000015442. PMID 10702688. S2CID 42602080.
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