Derlin-2

Derlin 2
Identifiers
Symbols	DERL2 ; CGI-101; DERtrin-2; 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 • early endosome • late endosome • endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral component of endoplasmic reticulum membrane Biological process • suckling behavior • positive regulation of cell proliferation • positive regulation of cell growth • ER-associated ubiquitin-dependent protein catabolic process • endoplasmic reticulum unfolded protein response • retrograde protein transport, ER to cytosol • negative regulation of 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	Q8BNI4
RefSeq (mRNA)	NM_001304777	NM_001291146
RefSeq (protein)	NP_001291706	NP_001278075
Location (UCSC)	Chr 17: 5.47 – 5.49 Mb	Chr 11: 71.01 – 71.02 Mb
PubMed search

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.
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".

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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.