HERC3: Difference between revisions
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'''Probable E3 ubiquitin-protein ligase HERC3''' is an [[enzyme]] that in humans is encoded by the ''HERC3'' [[gene]].<ref name="The HERC proteins: functional and evolutionary insights">{{cite journal | vauthors = Garcia-Gonzalo FR, Rosa JL | title = The HERC proteins: functional and evolutionary insights | journal = Cell Mol Life Sci | volume = 62 | issue = 16 | pages = 1826–1838 | date = Aug 2005 | doi = 10.1007/s00018-005-5119-y | pmid = 15968461}}</ref><ref name="Functional and pathological relevance of HERC family proteins: a decade later">{{cite journal | vauthors = Sánchez-Tena S, Cubillos-Rojas M, Schneider T, Rosa JL | title = Functional and pathological relevance of HERC family proteins: a decade later | journal = Cell Mol Life Sci | volume = 73 | issue = 10 | pages = | '''Probable E3 ubiquitin-protein ligase HERC3''' is an [[enzyme]] that in humans is encoded by the ''HERC3'' [[gene]].<ref name="The HERC proteins: functional and evolutionary insights">{{cite journal | vauthors = Garcia-Gonzalo FR, Rosa JL | title = The HERC proteins: functional and evolutionary insights | journal = Cell Mol Life Sci | volume = 62 | issue = 16 | pages = 1826–1838 | date = Aug 2005 | doi = 10.1007/s00018-005-5119-y | pmid = 15968461}}</ref><ref name="Functional and pathological relevance of HERC family proteins: a decade later">{{cite journal | vauthors = Sánchez-Tena S, Cubillos-Rojas M, Schneider T, Rosa JL | title = Functional and pathological relevance of HERC family proteins: a decade later | journal = Cell Mol Life Sci | volume = 73 | issue = 10 | pages = 18955–1968 | date = May 2016 | doi = 10.1007/s00018-016-2139-8 | pmid = 26801221}}</ref> 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 [[COPB1|β-COP]], [[ADP ribosylation factor|ARF]], and [[Rab (G-protein)|Rab5]]. Since HERC3 can itself be ubiquitinated and degraded by the proteasome, it likely has roles in both vesicular traffic and ubiquitin-dependent processes.<ref name="Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B">{{cite journal | vauthors = Hochrainer K, Kroismayr R, Baranyi U, Binder BR, Lipp J | title = Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B | journal = Cell Mol Life Sci | volume = 65 | issue = 13 | pages = 2105–2117 | date = Jul 2008 | doi = 10.1007/s00018-008-8148-5 | pmid = 18535780}}</ref><ref name="HERC3 binding to and regulation by ubiquitin">{{cite journal | vauthors = Cruz C, Ventura F, Bartrons R, Rosa JL | title = HERC3 binding to and regulation by ubiquitin | journal = FEBS Lett | volume = 488 | issue = 1–2 | pages = 74–80 | date = Jan 2001 | pmid = 11163799}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HERC3 | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8916| accessdate = }}</ref> | ||
==References== | ==References== | ||
| Line 35: | Line 35: | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{ cite journal |vauthors= Hochrainer K, Pejanovic N, Olaseun VA, Zhang S, Iadecola C, Anrather J | title= The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation | journal= Nucleic Acids Res | volume= 43 | issue= 20 | pages= 9889–9904 | date= 16 Nov 2015 | pmc= 4787756 | doi= 10.1093/nar/gkv1064 | | *{{ cite journal |vauthors= Hochrainer K, Pejanovic N, Olaseun VA, Zhang S, Iadecola C, Anrather J | title= The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation | journal= Nucleic Acids Res | volume= 43 | issue= 20 | pages= 9889–9904 | date= 16 Nov 2015 | pmc= 4787756 | doi= 10.1093/nar/gkv1064 | pmid= 26476452 }} | ||
*{{ cite journal |vauthors= Cowley M, Wood AJ, Böhm S, Schulz R, Oakey RJ | title= Epigenetic control of alternative mRNA processing at the imprinted Herc3/Nap1l5 locus | journal= Nucleic Acids Res | volume= 40 | issue= 18 | pages= 8917–8926 | date= Oct 2012 | pmc= 3467052 | doi= 10.1093/nar/gks654 | | *{{ cite journal |vauthors= Cowley M, Wood AJ, Böhm S, Schulz R, Oakey RJ | title= Epigenetic control of alternative mRNA processing at the imprinted Herc3/Nap1l5 locus | journal= Nucleic Acids Res | volume= 40 | issue= 18 | pages= 8917–8926 | date= Oct 2012 | pmc= 3467052 | doi= 10.1093/nar/gks654 | pmid= 22790983 }} | ||
*{{ cite journal |vauthors= Yoo NJ, Park SJ, Lee SH | title= Frameshift mutations of ubiquitination-related genes HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B in gastric and colorectal carcinomas with microsatellite instability | journal= Pathology | volume= 43 | issue= 7 | pages= 753–755 | date= Dec 2011 | pmid= 22124266 | doi= 10.1097/PAT.0b013e32834c7e78 | url= http://www.sciencedirect.com/science/article/pii/S003130251632952X?via%3Dihub }} | *{{ cite journal |vauthors= Yoo NJ, Park SJ, Lee SH | title= Frameshift mutations of ubiquitination-related genes HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B in gastric and colorectal carcinomas with microsatellite instability | journal= Pathology | volume= 43 | issue= 7 | pages= 753–755 | date= Dec 2011 | pmid= 22124266 | doi= 10.1097/PAT.0b013e32834c7e78 | url= http://www.sciencedirect.com/science/article/pii/S003130251632952X?via%3Dihub }} | ||
*{{ cite journal |vauthors= Scheffner M, Staub O | title= HECT E3s and human disease | journal= BMC Biochem | volume= 8 | issue= (Suppl 1):S6 | pages= | date= 22 Nov 2007 | doi= 10.1186/1471-2091-8-S1-S6 | pmc= 2106370 | pmid= 18047743 }} | *{{ cite journal |vauthors= Scheffner M, Staub O | title= HECT E3s and human disease | journal= BMC Biochem | volume= 8 | issue= (Suppl 1):S6 | pages= S6| date= 22 Nov 2007 | doi= 10.1186/1471-2091-8-S1-S6 | pmc= 2106370 | pmid= 18047743 }} | ||
*{{ cite journal |vauthors= Cruz C, Nadal M, Ventura F, Bartrons R, Estivill X, Rosa JL | title= The human HERC3 gene maps to chromosome 4q21 by fluorescence in situ hybridization | journal= Cytogenet Cell Genet | volume= 87 | issue= | *{{ cite journal |vauthors= Cruz C, Nadal M, Ventura F, Bartrons R, Estivill X, Rosa JL | title= The human HERC3 gene maps to chromosome 4q21 by fluorescence in situ hybridization | journal= Cytogenet Cell Genet | volume= 87 | issue= 3–4 | pages= 263–264 | date= 1999 | pmid= 10702688 | doi= 10.1159/000015442 }} | ||
{{refend}} | {{refend}} | ||
Latest revision as of 12:10, 10 January 2019
| HERC3 | |
|---|---|
| Identifiers | |
| Symbol | ? |
| Alt. names | HECT domain and RCC1-like domain-containing protein 3, HECT-type E3 ubiquitin transferase HERC3, KIAA0032 |
| Entrez | 8916 |
| HUGO | 4876 |
| OMIM | 605200 |
| PDB | Q15034 |
| RefSeq | NM_001271602, NM_001318505&rn=1 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
- ↑ 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. PMID 15968461.
- ↑ 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. PMID 26801221.
- ↑ 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. PMID 18535780.
- ↑ Cruz C, Ventura F, Bartrons R, Rosa JL (Jan 2001). "HERC3 binding to and regulation by ubiquitin". FEBS Lett. 488 (1–2): 74–80. PMID 11163799.
- ↑ "Entrez Gene: HERC3".
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. 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.
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