Derlin-2

From Wikipedia, the free encyclopedia

Derlin 2

Identifiers

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	• early endosome • late endosome • endoplasmic reticulum • integral to endoplasmic reticulum membrane
Biological process	• 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

ENSG00000072849

ENSMUSG00000018442

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
5.37 – 5.39 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

References

↑ 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.
↑ 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.
↑ "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.

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