Search by BoMiProt ID - Bomi5384


Primary Information

BoMiProt ID Bomi5384
Protein Name E3 ubiquitin-protein ligase TM129/RING-type E3 ubiquitin transferase TM129
Organism Bos taurus
Uniprot IdQ08DK0
Milk FractionWhey
Ref Sequence Id NP_001070332.1
Aminoacid Length 362
Molecular Weight 40454
Fasta Sequence https://www.uniprot.org/uniprot/Q08DK0.fasta
Gene Name TMEM129
Gene Id 518991
Protein Existence Status reviewed

Secondary Information

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. 
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.
PTMs Phosphorylation at Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 3TMHs; (7-29), (57-79), (92-114)
Significance of PTMs  PINK1 phosphorylated ubiquitin at serine 65, homologous to the site phosphorylated by PINK1 in Parkin's ubiquitin-like domain.
Additional Comments In the ubiquitin-proteasome pathway, few quality control E3 ubiquitin ligases actively participate against misfolded protein aggregation generated via stress conditions.
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.