Primary Information |
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| BoMiProt ID | Bomi5384 |
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| Protein Name | E3 ubiquitin-protein ligase TM129/RING-type E3 ubiquitin transferase TM129 |
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| Organism | Bos taurus |
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| Uniprot ID | Q08DK0 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001070332.1 |
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| Aminoacid Length | 362 |
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| Molecular Weight | 40454 |
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| FASTA Sequence |
Download |
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| Gene Name | TMEM129 |
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| Gene ID | 518991 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. |
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| Biochemical Properties | The E3s are a large, diverse group of proteins, characterized by one of several defining motifs. These include a HECT (homologous to E6-associated protein C-terminus), RING (really interesting new gene) or U-box (a modified RING motif without the full complement of Zn2+-binding ligands) domain. |
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| PTMs | Phosphorylation at Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 3TMHs; (7-29), (57-79), (92-114) |
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| Significance of PTMs | PINK1 phosphorylated ubiquitin at serine 65, homologous to the site phosphorylated by PINK1 in Parkin's ubiquitin-like domain. |
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| Additional Comments | In the ubiquitin-proteasome pathway, few quality control E3 ubiquitin ligases actively participate against misfolded protein aggregation generated via stress conditions. |
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| Bibliography | 1.Ardley HC, Robinson PA. E3 ubiquitin ligases. Essays Biochem. 2005;41:15-30. doi: 10.1042/EB0410015. PMID: 16250895. 2.Berndsen CE, Wolberger C. New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780. PMID: 24699078. |
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