PROSITE documentation PDOC51872Zinc finger ZBR-type profile
The post-translational modification of proteins by the covalent attachment of ubiquitin (ubiquitylation) regulates various cellular processes of eukaryotes. The ubiquitylation reaction is catalyzed by a set of three enzymes: ubiquitin-activating enzyme, E1; ubiquitin-conjugating enzyme, E2; and ubiquitin ligase, E3. The anaphase-promoting complex or cyclosome (APC/C) is a multisubunit E3 ligase enzyme that regulates cell division by promoting timely ubiquitin-mediated proteolysis of key cell-cycle regulatory proteins. Emi1/Fbx5 (early mitotic inhibitor 1; gene symbol, FBX05) and Emi2/Erp1/Fbx43 (endogenous meiotic inhibitor 2 or Emi1-related protein 1; gene symbol, FBX043) constitute the Emi/Erp protein family of APC/C inhibitors against the APC/C function, which controls cell division progress. Emi1 and Emi2 share the F-box (see <PDOC50181>) and DB motifs, the zinc-binding region (ZBR) with the in-between-RING (IBR) topology and the C6HC-type zinc-binding motif, and the C-terminal region with a conserved 14-residue sequence ending in the RL residues, termed the RL tail [1,2,3].
The ZBR-type zinc finger is an autonomously folded domain with a central, twisted, four-stranded β-sheet and two zinc ions on opposite ends of the sheet (see <PDB:2M6N>). One zinc is chelated by the β1-β2 and β3-β4 loops and the other by the β2-β3 loop and a loop following β 4. The ZBR finger displays an In-Between-RING (IBR) domain topology [1,2,3].
The profile we developed covers the entire ZBR-type zinc finger.
Last update:August 2018 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Shoji S. Muto Y. Ikeda M. He F. Tsuda K. Ohsawa N. Akasaka R. Terada T. Wakiyama M. Shirouzu M. Yokoyama S. |
| Title | The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation. | |
| Source | FEBS Open Bio 4:689-703(2014). | |
| PubMed ID | 25161877 | |
| DOI | 10.1016/j.fob.2014.06.010 |
| 2 | Authors | Frye J.J. Brown N.G. Petzold G. Watson E.R. Grace C.R.R. Nourse A. Jarvis M.A. Kriwacki R.W. Peters J.-M. Stark H. Schulman B.A. |
| Title | Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. | |
| Source | Nat. Struct. Mol. Biol. 20:827-835(2013). | |
| PubMed ID | 23708605 | |
| DOI | 10.1038/nsmb.2593 |
| 3 | Authors | Chang L. Zhang Z. Yang J. McLaughlin S.H. Barford D. |
| Title | Atomic structure of the APC/C and its mechanism of protein ubiquitination. | |
| Source | Nature 522:450-454(2015). | |
| PubMed ID | 26083744 | |
| DOI | 10.1038/nature14471 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)