Primary Information |
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BoMiProt ID | Bomi5371 |
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Protein Name | E3 ubiquitin-protein ligase RNF126/RING finger protein 126 |
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Organism | Bos taurus |
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Uniprot ID | Q0II22 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001068782.1 |
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Aminoacid Length | 313 |
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Molecular Weight | 33954 |
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FASTA Sequence |
Download |
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Gene Name | RNF126 |
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Gene ID | 507447 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | ubiquitination oF target proteins. mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. |
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Biochemical Properties | RING finger domain at the C-terminus, a Zn finger domain at the N-terminus, and an AKT phosphorylation site in the middle.Zn finger domain can directly bind to ubiquitin, and the RING finger domain is essential for its E3 ligase activity, which binds both the E2 and the substrate before transferring an ubiquitin molecule from E2 to the substrate.has two unique regions, a serine-rich domain and an SH3-binding domain. |
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PTMs | Ubiquitinated. May undergo autoubiquitination.Acetylation ,phosphorylation, |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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Predicted Disorder Regions | 1-4, 37-78, 91-144, 201-222, 281-285, 292-313 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | phosphorylated by aKT.AKT phosphorylation site within a potential 14-3-3 binding domain. |
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Bibliography | Zhang R, Liu W, Sun J, Kong Y, Chen C. Roles of RNF126 and BCA2 E3 ubiquitin ligases in DNA damage repair signaling and targeted cancer therapy. Pharmacol Res. 2020 May;155:104748. doi: 10.1016/j.phrs.2020.104748. Epub 2020 Mar 6. PMID: 32147403. |