Derlin-2

DERL2
Identifiers
Aliases	DERL2, F-LAN-1, F-LANa, FLANa, CGI-101, DERtrin-2, derlin 2, derlin-2
External IDs	OMIM: 610304; MGI: 2151483; HomoloGene: 9356; GeneCards: DERL2; OMA:DERL2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 5,471,254 bp End 5,486,811 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B4|11 43.21 cM Start 70,897,990 bp End 70,910,667 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right testis left testis body of pancreas Achilles tendon right lobe of liver parotid gland mucosa of transverse colon olfactory zone of nasal mucosa right adrenal gland granulocyte Top expressed in cumulus cell left lobe of liver seminal vesicula lacrimal gland decidua right lung lobe stroma of bone marrow islet of Langerhans right kidney yolk sac More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding serine-type endopeptidase activity Cellular component integral component of membrane integral component of endoplasmic reticulum membrane late endosome early endosome endoplasmic reticulum membrane endoplasmic reticulum membrane endoplasmic reticulum quality control compartment signal recognition particle receptor complex signal recognition particle Biological process endoplasmic reticulum unfolded protein response positive regulation of cell growth retrograde protein transport, ER to cytosol response to unfolded protein negative regulation of retrograde protein transport, ER to cytosol positive regulation of cell population proliferation ubiquitin-dependent ERAD pathway suckling behavior endoplasmic reticulum mannose trimming proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51009 116891 Ensembl ENSG00000072849 ENSMUSG00000018442 UniProt Q9GZP9 Q8BNI4 RefSeq (mRNA) NM_001304777 NM_001304779 NM_016041 NM_001291146 NM_001291147 NM_001291148 NM_033562 RefSeq (protein) NP_001291706 NP_001291708 NP_057125 NP_001278075 NP_001278076 NP_001278077 NP_291040 Location (UCSC) Chr 17: 5.47 – 5.49 Mb Chr 11: 70.9 – 70.91 Mb PubMed search
Wikidata
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Derlin-2 is a protein that in humans is encoded by the DERL2 gene.

See also

• Derlin-1
• Derlin-3

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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.429..834L. doi:10.1038/nature02592. PMID 15215855. S2CID 29483256.
• 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. Bibcode:2005PNAS..10214296L. 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.