DERL1

From Wikipedia, the free encyclopedia

Der1-like domain family, member 1

Identifiers

DERL1; DER-1; DER1; FLJ13784; FLJ42092; MGC3067; PRO2577

External IDs

OMIM: 608813 MGI: 1915069 HomoloGene: 11483

Gene ontology
Molecular Function:	• receptor activity • protein binding • MHC class I protein binding
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane • integral to endoplasmic reticulum membrane
Biological Process:	• protein transport • intracellular transport of viral proteins in host cell • ER-associated protein catabolic process • unfolded protein response • retrograde protein transport, ER to cytosol

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_024295 (mRNA)
NP_077271 (protein)

NM_024207 (mRNA)
NP_077169 (protein)

Location

Chr 8: 124.09 - 124.12 Mb

Chr 15: 57.7 - 57.72 Mb

Pubmed search

[1]

[2]

Der1-like domain family, member 1, also known as DERL1, is a human gene.^[1]

[edit] References

^ Entrez Gene: DERL1 Der1-like domain family, member 1.

[edit] Further reading

Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174.
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. PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265-70. doi:10.1101/gr.1293003. PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
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.
Ye Y, Shibata Y, Yun C, et al. (2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.". Nature 429 (6994): 841-7. doi:10.1038/nature02656. PMID 15215856.
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. PMID 15489334.
Katiyar S, Joshi S, Lennarz WJ (2006). "The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum.". Mol. Biol. Cell 16 (10): 4584-94. doi:10.1091/mbc.E05-04-0345. PMID 16055502.
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. PMID 16186509.
Ye Y, Shibata Y, Kikkert M, et al. (2006). "Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132-8. doi:10.1073/pnas.0505006102. PMID 16186510.
Schulze A, Standera S, Buerger E, et al. (2006). "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway.". J. Mol. Biol. 354 (5): 1021-7. doi:10.1016/j.jmb.2005.10.020. PMID 16289116.
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. PMID 16449189.
Schubert V, Da Silva JS, Dotti CG (2006). "Localized recruitment and activation of RhoA underlies dendritic spine morphology in a glutamate receptor-dependent manner.". J. Cell Biol. 172 (3): 453-67. doi:10.1083/jcb.200506136. PMID 16449195.
Sun F, Zhang R, Gong X, et al. (2007). "Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants.". J. Biol. Chem. 281 (48): 36856-63. doi:10.1074/jbc.M607085200. PMID 16954204.
Crawshaw SG, Cross BC, Wilson CM, High S (2007). "The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress.". Mol. Membr. Biol. 24 (2): 113-20. doi:10.1080/09687860600988727. PMID 17453418.