Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51044Zinc finger SP-RING-type profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51044
SIZ1, SIZ2, and PIAS (protein inhibitor of activated STAT) proteins form a conserved family defined by an unusual RING-related domain, the Siz/PIAS RING finger (SP-RING) [1]. While RING fingers coordinate two Zn2+ ions, with a cross-brace architecture, the SP-RING finger contains only one Zn2+ ion in site B, which is coordinated in a tetrahedral configuration (see <PDB:3I2D>). Three of the four amino acid side chains that coordinate the Zn2+ ion at site A in RING proteins are lacking in Siz/PIAS proteins [2]. Like classical RING fingers SP-RINGs function as an E3 enzyme but specific for sumoylation (see <PDOC00449> for more details on the ubiquitination pathway). The SP-RING zinc finger has the capacity to interact with Ubc9 (the SUMO specific E2 enzyme) and the substrate and thus can increase the rate of substrate sumoylation [3,4].
Some proteins known to contain an SP-RING zinc finger are listed below:
- Mammalian PIAS proteins (PIAS 1,3,x and y). They bind to STAT transcription factors and prevent STAT-activated transcription. The mouse PIAS3 protein has also been called Msx-interacting-zinc finger protein (Miz1) [5].
- Drosophila Su(var)2-10. It is required for proper chromosome structure and chromosome inheritance [6].
- Yeast SIZ1 and SIZ2. They are required for SUMO attachment to the cytoskeletal septin proteins.
- Pli1, the unique fission yeast member of the SP-RING family. It is involved in centromeric function.
The profile we developed covers the whole SP-RING-type zinc finger.
Note:The SP-RING-type zinc finger is also known as the MIZ-type zinc finger [5].
Last update:March 2021 / Profile revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Hochstrasser M. |
| Title | SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. | |
| Source | Cell 107:5-8(2001). | |
| PubMed ID | 11595179 |
| 2 | Authors | Yunus A.A. Lima C.D. |
| Title | Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. | |
| Source | Mol. Cell 35:669-682(2009). | |
| PubMed ID | 19748360 | |
| DOI | 10.1016/j.molcel.2009.07.013 |
| 3 | Authors | Johnson E.S. Gupta A.A. |
| Title | An E3-like factor that promotes SUMO conjugation to the yeast septins. | |
| Source | Cell 106:735-744(2001). | |
| PubMed ID | 11572779 |
| 4 | Authors | Seeler J.S. Dejean A. |
| Title | Nuclear and unclear functions of SUMO. | |
| Source | Nat. Rev. Mol. Cell Biol. 4:690-699(2003). | |
| PubMed ID | 14506472 | |
| DOI | 10.1038/nrm1200 |
| 5 | Authors | Wu L. Wu H. Ma L. Sangiorgi F. Wu N. Bell J.R. Lyons G.E. Maxson R. |
| Title | Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA. | |
| Source | Mech. Dev. 65:3-17(1997). | |
| PubMed ID | 9256341 |
| 6 | Authors | Hari K.L. Cook K.R. Karpen G.H. |
| Title | The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family. | |
| Source | Genes Dev. 15:1334-1348(2001). | |
| PubMed ID | 11390354 | |
| DOI | 10.1101/gad.877901 |
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.