OS9 (gene)

Osteosarcoma amplified 9, endoplasmic reticulum lectin
Identifiers
Symbols	OS9; ERLEC2; OS-9
External IDs	OMIM: 609677 MGI: 1924301 HomoloGene: 31409 GeneCards: OS9 Gene
Gene Ontology Molecular function • glycoprotein binding • protein binding • sugar binding Cellular component • Hrd1p ubiquitin ligase complex • endoplasmic reticulum • endoplasmic reticulum lumen Biological process • protein retention in ER lumen • protein ubiquitination • ER-associated protein catabolic process • response to endoplasmic reticulum stress • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10956	216440
Ensembl	ENSG00000135506	ENSMUSG00000040462
UniProt	Q13438	n/a
RefSeq (mRNA)	NM_001017956.2	NM_177614
RefSeq (protein)	NP_001017956.1	NP_808282
Location (UCSC)	Chr 12: 58.09 – 58.12 Mb	Chr 10: 126.53 – 126.56 Mb
PubMed search	[1]	[2]

Protein OS-9 is a protein that in humans is encoded by the OS9 gene.^{[1][2][3][4][5]}

This gene encodes a protein that is highly expressed in osteosarcomas. This protein binds to the hypoxia-inducible factor 1 (HIF-1), a key regulator of the hypoxic response and angiogenesis, and promotes the degradation of one of its subunits. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[5]

References

1. ^ Su YA, Hutter CM, Trent JM, Meltzer PS (Jul 1996). "Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas". Mol Carcinog 15 (4): 270–275. doi:10.1002/(SICI)1098-2744(199604)15:4<270::AID-MC4>3.0.CO;2-K. PMID 8634085. 
2. ^ Kimura Y, Nakazawa M, Tsuchiya N, Asakawa S, Shimizu N, Yamada M (Apr 1998). "Genomic organization of the OS-9 gene amplified in human sarcomas". J Biochem 122 (6): 1190–5. PMID 9498564. 
3. ^ Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K (Jun 2009). "Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans". J Biol Chem 284 (25): 17061–17068. doi:10.1074/jbc.M809725200. PMC 2719344. PMID 19346256. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2719344. 
4. ^ Christianson JC, Shaler TA, Tyler RE, Kopito RR (Mar 2008). "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD". Nat Cell Biol 10 (3): 272–282. doi:10.1038/ncb1689. PMC 2757077. PMID 18264092. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2757077. 
5. ^ ^{a b} "Entrez Gene: OS9 amplified in osteosarcoma". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10956. 

Further reading

• Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Baek JH, Mahon PC, Oh J et al. (2005). "OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha". Mol. Cell 17 (4): 503–512. doi:10.1016/j.molcel.2005.01.011. PMID 15721254. 
• Colland F, Jacq X, Trouplin V et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–1332. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442148. 
• Vigneron N, Ooms A, Morel S et al. (2003). "Identification of a new peptide recognized by autologous cytolytic T lymphocytes on a human melanoma". Cancer Immun. 2: 9. PMID 12747754. 
• 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Litovchick L, Friedmann E, Shaltiel S (2002). "A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta". J. Biol. Chem. 277 (37): 34413–34423. doi:10.1074/jbc.M203986200. PMID 12093806. 
• Friedmann E, Salzberg Y, Weinberger A et al. (2002). "YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins". J. Biol. Chem. 277 (38): 35274–35281. doi:10.1074/jbc.M201044200. PMID 12077121. 
• Nakayama T, Yaoi T, Kuwajima G et al. (1999). "Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma". FEBS Lett. 453 (1–2): 77–80. doi:10.1016/S0014-5793(99)00700-0. PMID 10403379. 
• Kimura Y, Nakazawa M, Yamada M (1998). "Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines". J. Biochem. 123 (5): 876–82. PMID 9562620. 
• Elkahloun AG, Krizman DB, Wang Z et al. (1997). "Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers". Genomics 42 (2): 295–301. doi:10.1006/geno.1997.4727. PMID 9192850.