Search Results
Overview
| Uniprot ID | Q9Y4L1 |
|---|---|
| Protein Name | Hypoxia up-regulated protein 1 |
| Gene Name | HYOU1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 106 | YFQHLLGKQADNPHV |
| 398 | RVQEVLLKAVGKEEL |
| 433 | LSKAFKVKPFVVRDA |
| 463 | EPGIHSLKHNKRVLF |
| 62 | PMEIVLNKESRRKTP |
| 67 | LNKESRRKTPVIVTL |
| 685 | APAPEGEKKQKPARK |
| 722 | KLAQSVQKLQDLTLR |
| 75 | TPVIVTLKENERFFG |
| 797 | TTVMLKEKLAELRKL |
| 803 | EKLAELRKLCQGLFF |
| 883 | AKLPATEKPVLLSKD |
| 889 | EKPVLLSKDIEAKMM |
| 908 | EVQYLLNKAKFTKPR |
| 91 | SAASMAIKNPKATLR |
| 910 | QYLLNKAKFTKPRPR |
Function
Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. Promotes HSPA5/BiP-mediated ATP nucleotide exchange and thereby activates the unfolded protein response (UPR) pathway in the presence of endoplasmic reticulum stress (By similarity). May play a role as a molecular chaperone and participate in protein folding
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071682 | endocytic vesicle lumen |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0034663 | endoplasmic reticulum chaperone complex |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005790 | smooth endoplasmic reticulum |
| Molecular Function | GO:0000774 | adenyl-nucleotide exchange factor activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0071456 | cellular response to hypoxia |
| Biological Process | GO:0006888 | endoplasmic reticulum to Golgi vesicle-mediated transport |
| Biological Process | GO:1903382 | negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway |
| Biological Process | GO:1903298 | negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
| Biological Process | GO:0002931 | response to ischemia |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.