UBL4A cDNA ORF clone, Homo sapiens(human)

A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Hein MY, Hubner NC, Poser I, Cox J, Nagaraj N, Toyoda Y, Gak IA, Weisswange I, Mansfeld J, Buchholz F, Hyman AA, Mann M
Cell163(3)712-23(2015 Oct)

Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis.
Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R
The Journal of biological chemistry290(15)9387-98(2015 Apr)

Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain.
Mock JY, Chartron JW, Zaslaver M, Xu Y, Ye Y, Clemons WM Jr
Proceedings of the National Academy of Sciences of the United States of America112(1)106-11(2015 Jan)

Both TRC35 and Ubl4A have distinct C-terminal binding sites on Bag6 defining a minimal Bag6 complex.
Title: Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain.

Data show that molecular chaperone BAG6_ubiquitin-like domain (UBL) and ubiquitin-like 4A UBL4A_UBL compete for the same binding site on N-terminal dimerisation domain of SGTA protein (SGTA_NT).
Title: Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A.

The authors identify USP13 as a gp78-associated deubiquitinase that eliminates ubiquitin conjugates from Ubl4A to maintain the functionality of Bag6.
Title: USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation.

Data indicate that BCL2-associated athanogene 6 (BAG6) appears to be the central component for the process, as depletion of BAG6 leads to the loss of both UBL4A and GET4 proteins and resistance to cell killing by DNA-damaging agents.
Title: Nuclear BAG6-UBL4A-GET4 complex mediates DNA damage signaling and cell death.

Data indicate that the Bag6-Ubl4A-Trc35 complex is localized to the endoplasmic reticulum (ER) membrane to regulate ER-associated degradation (ERAD).
Title: A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation.