HYOU1

Hypoxia up-regulated 1
Identifiers
Symbols	HYOU1 ; DKFZp686N08236; ORP150
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4658
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Hypoxia up-regulated 1, also known as HYOU1, is a human gene.

The protein encoded by this gene belongs to the heat shock protein 70 family. This gene has three mRNAs from the use of alternative transcription sites. A cis-acting segment is found at the 5' end of exon 1A which is involved in the stress-dependent induction. The transcript that begins with exon 1B is preferentially induced by hypoxia, resulting in the accumulation of this protein in the endoplasmic reticulum (ER). The protein encoded by this gene is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness. There is also an alternative translation site of this gene which lacks the signal peptide. This signal peptide-lacking protein, is only 3 amino acids shorter than the mature protein in the ER, and it is thought to have a housekeeping function in the cytosol.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
• Tsukamoto Y, Kuwabara K, Hirota S; et al. (1996). "150-kD oxygen-regulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein". J. Clin. Invest. 98 (8): 1930–41. PMID 8878445.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kuznetsov G, Chen LB, Nigam SK (1997). "Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum". J. Biol. Chem. 272 (5): 3057–63. PMID 9006956.CS1 maint: Multiple names: authors list (link)
• Ikeda J, Kaneda S, Kuwabara K; et al. (1997). "Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150". Biochem. Biophys. Res. Commun. 230 (1): 94–9. doi:10.1006/bbrc.1996.5890. PMID 9020069.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tsukamoto Y, Kuwabara K, Hirota S; et al. (1998). "Expression of the 150-kd oxygen-regulated protein in human breast cancer". Lab. Invest. 78 (6): 699–706. PMID 9645760.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ozawa K, Kuwabara K, Tamatani M; et al. (1999). "150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death". J. Biol. Chem. 274 (10): 6397–404. PMID 10037731.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bando Y, Ogawa S, Yamauchi A; et al. (2000). "150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells". Am. J. Physiol., Cell Physiol. 278 (6): C1172–82. PMID 10837345.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kaneda S, Yura T, Yanagi H (2000). "Production of three distinct mRNAs of 150 kDa oxygen-regulated protein (ORP150) by alternative promoters: preferential induction of one species under stress conditions". J. Biochem. 128 (3): 529–38. PMID 10965054.CS1 maint: Multiple names: authors list (link)
• Tamatani M, Matsuyama T, Yamaguchi A; et al. (2001). "ORP150 protects against hypoxia/ischemia-induced neuronal death". Nat. Med. 7 (3): 317–23. doi:10.1038/85463. PMID 11231630.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519.CS1 maint: Multiple names: authors list (link)
• Bando Y, Tsukamoto Y, Katayama T; et al. (2005). "ORP150/HSP12A protects renal tubular epithelium from ischemia-induced cell death". FASEB J. 18 (12): 1401–3. doi:10.1096/fj.03-1161fje. PMID 15240565.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.CS1 maint: Multiple names: authors list (link)
• Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach". Mol. Cell Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699.CS1 maint: Multiple names: authors list (link)
• Liu T, Qian WJ, Gritsenko MA; et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMID 16335952.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cechowska-Pasko M, Bankowski E, Chene P (2006). "The effect of hypoxia on the expression of 150 kDa oxygen-regulated protein (ORP 150) in HeLa cells". Cell. Physiol. Biochem. 17 (1–2): 89–96. doi:10.1159/000091467. PMID 16543725.CS1 maint: Multiple names: authors list (link)
• Takeuchi S (2007). "Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone". Protein J. 25 (7–8): 517–28. doi:10.1007/s10930-006-9038-z. PMID 17131193.
• Kitao Y, Matsuyama T, Takano K; et al. (2007). "Does ORP150/HSP12A protect dopaminergic neurons against MPTP/MPP(+)-induced neurotoxicity?". Antioxid. Redox Signal. 9 (5): 589–95. doi:10.1089/ars.2006.1518. PMID 17330988.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)