Derlin-2

Protein-coding gene in the species Homo sapiens

DERL2
Identifiers
AliasesDERL2, F-LAN-1, F-LANa, FLANa, CGI-101, DERtrin-2, derlin 2, derlin-2
External IDsOMIM: 610304; MGI: 2151483; HomoloGene: 9356; GeneCards: DERL2; OMA:DERL2 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for DERL2
Genomic location for DERL2
Band17p13.2Start5,471,254 bp[1]
End5,486,811 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for DERL2
Genomic location for DERL2
Band11 B4|11 43.21 cMStart70,897,990 bp[2]
End70,910,667 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 11: 70.9 – 70.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Derlin-2 is a protein that in humans is encoded by the DERL2 gene.[5][6][7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000072849 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018442 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ "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. 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.


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