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proteins. Page last changed on 19 Dec 2016.
Der1-like domain family, member 2
Derlin-2, Carcinoma-related, FLAN I, DERL-2, hF-LANa, F-LANa
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. DERL2 is involved in the degradation of misfolded glycoproteins in the ER (Oda et al., 2006 [PubMed 16449189]).[supplied by OMIM, Mar 2008] (from
Bradley et al., Los Angeles, United States. In Plos Pathog, 2014
Here we show that three central components of the host ER associated degradation (ERAD) machinery, Derlin-2 (Derl2), the E3 ubiquitin-protein ligase Hrd1, and the AAA ATPase p97, are required for intoxication by some CDTs.
Wlodarska et al., Leuven, Belgium. In Plos One, 2013
We report here results of an integrative genomic and transcriptomic (expression microarray and RNA-sequencing) study of six i(7)(q10)-positive HSTL cases, including HSTL-derived cell line (DERL-2), and three cases with ring 7 [r(7)], the recently identified rare variant aberration.
Lebbink et al., Utrecht, Netherlands. In Nat Commun, 2013
TMEM129 is an unconventional C4C4-type RING finger E3 ubiquitin ligase that resides within a complex containing various other ERAD components, including Derlin-1, Derlin-2, VIMP and p97, indicating that TMEM129 is an integral part of the ER-resident dislocation complex mediating US11-induced HLA class I degradation.
Gladyshev et al., Boston, United States. In J Biol Chem, 2012
In this complex, SelK showed higher affinity for Derlin-1, whereas SelS had higher affinity for Derlin-2, suggesting that these selenoproteins could determine the nature of the substrate translocated through the Derlin channel.
Ploegh et al., Boston, United States. In Proc Natl Acad Sci U S A, 2005
Derlin-2 forms a robust multiprotein complex with the p97 AAA ATPase as well as the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex, and participates in the degradation of proteins from the ER.