Search Results
Overview
| Uniprot ID | Q14739 |
|---|---|
| Protein Name | Delta(14)-sterol reductase LBR |
| Gene Name | LBR |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 147 | ERNDAPHKNTQEKFS |
| 152 | PHKNTQEKFSLSQES |
| 176 | RPRREEVKLKEIDSK |
| 186 | EIDSKEEKYVAKELA |
| 5 | ***MPSRKFADGEVV |
| 508 | FRGANSQKNAFRKNP |
| 524 | DPKLAHLKTIHTSTG |
| 594 | DEYHCKKKYGVAWEK |
Function
Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0005637 | nuclear inner membrane |
| Cellular Component | GO:0005652 | nuclear lamina |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0140463 | chromatin-protein adaptor activity |
| Molecular Function | GO:0070087 | chromo shadow domain binding |
| Molecular Function | GO:0050613 | Delta14-sterol reductase activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0005521 | lamin binding |
| Molecular Function | GO:0070402 | NADPH binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0006695 | cholesterol biosynthetic process |
| Biological Process | GO:0033489 | cholesterol biosynthetic process via desmosterol |
| Biological Process | GO:0030223 | neutrophil differentiation |
| Biological Process | GO:0060816 | random inactivation of X chromosome |
| Biological Process | GO:0036197 | zymosterol biosynthetic process |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] 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.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] 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.