[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Astrocytoma;
DOI=10.1006/bbrc.1996.5890; PubMed=9020069 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda J.,
Kaneda S.,
Kuwabara K.,
Ogawa S.,
Kobayashi T.,
Matsumoto M.,
Yura T.,
Yanagi H.;
"Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150.";
Biochem. Biophys. Res. Commun. 230:94-99(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
DOI=10.1007/s10930-006-9038-z; PubMed=17131193 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi S.;
"Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.";
Protein J. 25:517-528(2006).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
Suzuki Y.,
Sugano S.,
Totoki Y.,
Toyoda A.,
Takeda T.,
Sakaki Y.,
Tanaka A.,
Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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[4]
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PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, AND MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G.,
Chen W.-Q.,
Sun Y.;
Submitted (DEC-2008) to UniProtKB.
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[5]
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FUNCTION.
DOI=10.1074/jbc.274.10.6397; PubMed=10037731 [NCBI, ExPASy, EBI, Israel, Japan]
Ozawa K.,
Kuwabara K.,
Tamatani M.,
Takatsuji K.,
Tsukamoto Y.,
Kaneda S.,
Yanagi H.,
Stern D.M.,
Eguchi Y.,
Tsujimoto Y.,
Ogawa S.,
Tohyama M.;
"150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death.";
J. Biol. Chem. 274:6397-6404(1999).
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[6]
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COMPONENT OF A CHAPERONE COMPLEX.
DOI=10.1091/mbc.E02-05-0311; PubMed=12475965 [NCBI, ExPASy, EBI, Israel, Japan]
Meunier L.,
Usherwood Y.-K.,
Chung K.T.,
Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
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[7]
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GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H.,
Li X.-J.,
Martin D.B.,
Aebersold R.;
"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
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[8]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND ASN-931, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T.,
Qian W.-J.,
Gritsenko M.A.,
Camp D.G. II,
Monroe M.E.,
Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
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[9]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan]
Lewandrowski U.,
Moebius J.,
Walter U.,
Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
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[10]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[11]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R.,
Jiang X.,
Sun D.,
Han G.,
Wang F.,
Ye M.,
Wang L.,
Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
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- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.
- SUBUNIT: Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.
- INTERACTION:
Q93063:EXT2; NbExp=1; IntAct=EBI-1054186, EBI-1047761;
Q14164:IKBKE; NbExp=1; IntAct=EBI-1054186, EBI-307369;
- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
- TISSUE SPECIFICITY: Highly expressed in tissues that contain well-developed endoplasmic reticulum and synthesize large amounts of secretory proteins. Highly expressed in liver and pancreas and lower expression in brain and kidney. Also expressed in macrophages within aortic atherosclerotic plaques, and in breast cancers.
- INDUCTION: By hypoxia and also by 2-deoxyglucose or tunicamycin.
- SIMILARITY: Belongs to the heat shock protein 70 family.
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