title: Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation.
abstract: The E3 ubiquitin ligase activity and subcellular localisation of human TRIM69 (hTRIM69) gene were studied. It was found that hTRIM69 mediated ubiquitination in an E2 conjugating enzyme selective fashion in vitro and an intact RING finger domain was indispensible for the process. Further evidences showed that hTRIM69 could mediate ubiquitination in vivo, which could be enhanced by a proteasome inhibitor. hTRIM69 was found to localise in both the cytoplasm and the nucleus in a speckled aggregating pattern, which also required an intact RING finger domain. Collectively, hTRIM69 is a novel E3 ubiquitin ligase identified from human testis and may function to ubiquitinate its particular substrates during spermatogenesis.
authors.affiliation: State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, Tsinghua University, Beijing 100005, China.
authors.forename: Yongqing
authors.initials: Y
authors.lastname: Han
authors.forename: Rong
authors.initials: R
authors.lastname: Li
authors.forename: Jinlan
authors.initials: J
authors.lastname: Gao
authors.forename: Shiying
authors.initials: S
authors.lastname: Miao
authors.forename: Linfang
authors.initials: L
authors.lastname: Wang
mesh_terms: D002384:Catalysis; D057809:HEK293 Cells; D006367:HeLa Cells; D006801:Humans; D042541:Intracellular Space / Q000201:enzymology; D008297:Male; D054829:RING Finger Domains; D013091:Spermatogenesis; D013737:Testis / Q000201:enzymology*; D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D000070584:Tripartite Motif Proteins; C579345:TRIM69 protein, human; D044767:Ubiquitin-Protein Ligases