HYOU1

HYOU1
Identifiers
Aliases	HYOU1, GRP-170, Grp170, HSP12A, ORP-150, ORP150, hypoxia up-regulated 1, IMD59
External IDs	OMIM: 601746; MGI: 108030; HomoloGene: 4658; GeneCards: HYOU1; OMA:HYOU1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q23.3 Start 119,044,188 bp End 119,057,227 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 A5.2 Start 44,290,787 bp End 44,303,666 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in islet of Langerhans body of pancreas anterior pituitary right testis left testis right lobe of thyroid gland stromal cell of endometrium left lobe of thyroid gland appendix right lobe of liver Top expressed in spermatocyte otic placode saccule spermatid supraoptic nucleus otic vesicle gastrula pyloric antrum tail of embryo ciliary body More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding chaperone binding ATP binding protein binding Cellular component endocytic vesicle lumen endoplasmic reticulum lumen membrane focal adhesion smooth endoplasmic reticulum endoplasmic reticulum chaperone complex extracellular region endoplasmic reticulum extracellular exosome Biological process negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway negative regulation of apoptotic process receptor-mediated endocytosis response to endoplasmic reticulum stress endoplasmic reticulum to Golgi vesicle-mediated transport IRE1-mediated unfolded protein response response to ischemia cellular response to hypoxia negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10525 12282 Ensembl ENSG00000280682 ENSG00000149428 ENSMUSG00000032115 UniProt Q9Y4L1 Q9BST8 Q9JKR6 RefSeq (mRNA) NM_001130991 NM_006389 NM_021395 RefSeq (protein) NP_001124463 NP_006380 NP_067370 Location (UCSC) Chr 11: 119.04 – 119.06 Mb Chr 9: 44.29 – 44.3 Mb PubMed search
Wikidata
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Hypoxia up-regulated protein 1 is a protein that in humans is encoded by the HYOU1 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1172/JCI118994. PMC 507633. PMID 8878445.
• 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. doi:10.1074/jbc.272.5.3057. PMID 9006956.
• 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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.
• 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. doi:10.1152/ajpcell.2000.278.6.C1172. PMID 10837345. S2CID 1841205.
• 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. doi:10.1093/oxfordjournals.jbchem.a022783. PMID 10965054.
• 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. S2CID 10152200.
• 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.
• 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. S2CID 581283.
• 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. S2CID 30637967.
• 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.
• 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.
• 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. PMC 1850943. PMID 16335952.
• 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.
• 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. S2CID 41452314.
• 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.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.