Derlin-2

Der1-like domain family, member 2
Identifiers
Symbols	DERL2; F-LAN-1; F-LANa; FLANa
External IDs	OMIM: 610304 MGI: 2151483 HomoloGene: 9356 GeneCards: DERL2 Gene
Gene Ontology Molecular function • protein binding Cellular component • endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral to membrane • integral to endoplasmic reticulum membrane Biological process • response to unfolded protein • positive regulation of cell proliferation • positive regulation of cell growth • ER-associated protein catabolic process • endoplasmic reticulum unfolded protein response • retrograde protein transport, ER to cytosol Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51009	116891
Ensembl	ENSG00000072849	ENSMUSG00000018442
UniProt	Q9GZP9	Q3U957
RefSeq (mRNA)	NM_016041	NM_033562.3
RefSeq (protein)	NP_057125	NP_291040.1
Location (UCSC)	Chr 17: 5.37 – 5.39 Mb	Chr 11: 70.82 – 70.83 Mb
PubMed search	[1]	[2]

Derlin-2 is a protein that in humans is encoded by the DERL2 gene.^[1][2][3]

See also

• Derlin-1
• Derlin-3

References

1. ^ Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (Aug 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310876. 
2. ^ Ying H, Yu Y, Xu Y (Aug 2001). "Cloning and characterization of F-LANa, upregulated in human liver cancer". Biochem Biophys Res Commun 286 (2): 394–400. doi:10.1006/bbrc.2001.5390. PMID 11500051. 
3. ^ "Entrez Gene: DERL2 Der1-like domain family, member 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51009. 

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Lilley BN, Ploegh HL (2004). "A membrane protein required for dislocation of misfolded proteins from the ER.". Nature 429 (6994): 834–40. doi:10.1038/nature02592. PMID 15215855. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Lilley BN, Ploegh HL (2006). "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14296–301. doi:10.1073/pnas.0505014102. PMC 1242303. PMID 16186509. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1242303. 
• Oda Y, Okada T, Yoshida H, et al. (2006). "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation.". J. Cell Biol. 172 (3): 383–93. doi:10.1083/jcb.200507057. PMC 2063648. PMID 16449189. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2063648. 
• Rhee S, Grinnell F (2006). "P21-activated kinase 1: convergence point in PDGF- and LPA-stimulated collagen matrix contraction by human fibroblasts.". J. Cell Biol. 172 (3): 423–32. doi:10.1083/jcb.200505175. PMC 2063651. PMID 16449192. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2063651. 
• Maas C, Tagnaouti N, Loebrich S, et al. (2006). "Neuronal cotransport of glycine receptor and the scaffold protein gephyrin.". J. Cell Biol. 172 (3): 441–51. doi:10.1083/jcb.200506066. PMC 2063653. PMID 16449194. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2063653. 
• Lilley BN, Gilbert JM, Ploegh HL, Benjamin TL (2006). "Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection.". J. Virol. 80 (17): 8739–44. doi:10.1128/JVI.00791-06. PMC 1563856. PMID 16912321. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1563856.