Recombinant Human Hypoxia up-regulated protein 1 (HYOU1), Truncated

Uniprot Id

Q9Y4L1

Target Species

Human

Target Name

HYOU1

Target Full Name

Hypoxia up-regulated protein 1

Target 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.

Target Subcellular Location

Endoplasmic reticulum lumen.

Target Protein Families

Heat shock protein 70 family

Target 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

Target Research Area

Cancer

Target Synonyms

150 kDa oxygen regulated protein; 150 kDa oxygen-regulated protein; 170 kDa glucose regulated protein; 170 kDa glucose-regulated protein; DKFZp686N08236; FLJ94899; FLJ97572; glucose regulated protein 170; Grp 170; GRP-170; Grp170; HSP 12A; HSP12A; Hyou1; HYOU1_HUMAN; Hypoxia up regulated 1; hypoxia up-regulated 1 precursor; Hypoxia up-regulated protein 1; Hypoxia upregulated 1; Orp 150; ORP-150; Orp150; oxygen regulated protein (150kD)

Target Background

The protein encoded by this gene belongs to the heat shock protein 70 family. This gene uses alternative transcription start sites. A cis-acting segment found in the 5' UTR is involved in stress-dependent induction, resulting in the accumulation of this protein in the endoplasmic reticulum (ER) under hypoxic conditions. 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. This gene also has an alternative translation initiation site, resulting in a protein that lacks the N-terminal signal peptide. This signal peptide-lacking protein, which is only 3 amino acids shorter than the mature protein in the ER, is thought to have a housekeeping function in the cytosol. In rat, this protein localizes to both the ER by a carboxy-terminal peptide sequence and to mitochondria by an amino-terminal targeting signal. Alternative splicing results in multiple transcript variants.