Species	Reference gene ID	Possible function	Papers / DOI
Arabidopsis	At5g14420	E3 ubiquitin-protein ligase that mediates the formation of 'Lys-63'-linked ubiquitin chains.	Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.; 2007; DOI: 10.1105/tpc.107.052035; PMID: 17586653; https://pubmed.ncbi.nlm.nih.gov/17586653/ | Arabidopsis RGLG2, functioning as a RING E3 ligase, interacts with AtERF53 and negatively regulates the plant drought stress response.; 2012; DOI: 10.1104/pp.111.189738; PMID: 22095047; https://pubmed.ncbi.nlm.nih.gov/22095047/
Arabidopsis	At3g01650	E3 ubiquitin-protein ligase that mediates the formation of 'Lys-63'-linked ubiquitin chains.	Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.; 2007; DOI: 10.1105/tpc.107.052035; PMID: 17586653; https://pubmed.ncbi.nlm.nih.gov/17586653/ | Arabidopsis RGLG2, functioning as a RING E3 ligase, interacts with AtERF53 and negatively regulates the plant drought stress response.; 2012; DOI: 10.1104/pp.111.189738; PMID: 22095047; https://pubmed.ncbi.nlm.nih.gov/22095047/
Arabidopsis	At1g67800	Together with RGLG1, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA.	No verified direct reference in this release
Arabidopsis	At5g63970	Possesses E3 ubiquitin-protein ligase in vitro.	Two novel RING-type ubiquitin ligases, RGLG3 and RGLG4, are essential for jasmonate-mediated responses in Arabidopsis.; 2012; DOI: 10.1104/pp.112.203422; PMID: 22898498; https://pubmed.ncbi.nlm.nih.gov/22898498/ | Hijacking of the jasmonate pathway by the mycotoxin fumonisin B1 (FB1) to initiate programmed cell death in Arabidopsis is modulated by RGLG3 and RGLG4.; 2015; DOI: 10.1093/jxb/erv068; PMID: 25788731; https://pubmed.ncbi.nlm.nih.gov/25788731/ | The Arabidopsis Iron-Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 Ligases RGLG3 and RGLG4.; 2016; DOI: 10.1093/pcp/pcw122; PMID: 27497447; https://pubmed.ncbi.nlm.nih.gov/27497447/
Arabidopsis	At1g79380	Possesses E3 ubiquitin-protein ligase in vitro.	Two novel RING-type ubiquitin ligases, RGLG3 and RGLG4, are essential for jasmonate-mediated responses in Arabidopsis.; 2012; DOI: 10.1104/pp.112.203422; PMID: 22898498; https://pubmed.ncbi.nlm.nih.gov/22898498/ | Hijacking of the jasmonate pathway by the mycotoxin fumonisin B1 (FB1) to initiate programmed cell death in Arabidopsis is modulated by RGLG3 and RGLG4.; 2015; DOI: 10.1093/jxb/erv068; PMID: 25788731; https://pubmed.ncbi.nlm.nih.gov/25788731/ | The Arabidopsis Iron-Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 Ligases RGLG3 and RGLG4.; 2016; DOI: 10.1093/pcp/pcw122; PMID: 27497447; https://pubmed.ncbi.nlm.nih.gov/27497447/