PROSITE documentation PDOC51044Zinc finger SP-RING-type profile
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.
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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 |
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