InterPro : IPR017335

Name  E3 ubiquitin ligase, RNF8 Short Name  E3_Ub_ligase_RNF8
Type  Family Description  Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, ), a ubiquitin-conjugating enzyme (E2, ), and a ubiquitin ligase (E3, , ), which work sequentially in a cascade. There are many different E3 ligases, which are responsible for the type of ubiquitin chain formed, the specificity of the target protein, and the regulation of the ubiquitinylation process []. Ubiquitinylation is an important regulatory tool that controls the concentration of key signalling proteins, such as those involved in cell cycle control, as well as removing misfolded, damaged or mutant proteins that could be harmful to the cell. Several ubiquitin-like molecules have been discovered, such as Ufm1 (), SUMO1 (), NEDD8, Rad23 (), Elongin B and Parkin (), the latter being involved in Parkinson's disease [].This entry represents E3 ubiquitin-protein ligase, which may be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. This enzyme promotes the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer [, ]. Substrates that are poly-ubiquitinated at 'Lys-63' are usually not targeted for degradation. E3 ubiquitin-protein ligase acts following DNA double-strand break (DSB) formation, and is recruited to the sites of damage by ATM-phosphorylated MDC1, where it promotes the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF) [, ]. It may play a role in the regulation of RXRA-mediated transcriptional activity, but is not involved in RXRA ubiquitination by UBE2E2.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

5 Contains

Id Name Short Name Type
IPR001841 Zinc finger, RING-type Znf_RING Domain
IPR018957 Zinc finger, C3HC4 RING-type Znf_C3HC4_RING-type Domain
IPR000253 Forkhead-associated (FHA) domain FHA_dom Domain
IPR013083 Zinc finger, RING/FYVE/PHD-type Znf_RING/FYVE/PHD Domain
IPR017907 Zinc finger, RING-type, conserved site Znf_RING_CS Conserved_site

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Hatakeyama S U-box proteins as a new family of ubiquitin ligases. 2003 Biochem Biophys Res Commun 302 635-45
Ross CA The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. 2004 Trends Cell Biol 14 703-11
Belgareh-Touzé N Versatile role of the yeast ubiquitin ligase Rsp5p in intracellular trafficking. 2008 Biochem Soc Trans 36 791-6
Loring GL Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and Ubc13/Mms2-dependent ubiquitination. 2008 Cell Cycle 7 96-105
Ouyang Y Loss of Ubr2, an E3 ubiquitin ligase, leads to chromosome fragility and impaired homologous recombinational repair. 2006 Mutat Res 596 64-75
Morris JR BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. 2004 Hum Mol Genet 13 807-17

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)