Search Results
Overview
| Uniprot ID | Q7Z6E9 |
|---|---|
| Protein Name | E3 ubiquitin-protein ligase RBBP6 |
| Gene Name | RBBP6 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1039 | ENIVKPAKGPQEKVD |
| 1122 | SKDVKSEKLTTKEEK |
| 1169 | SSSMKISKLEVTEIV |
| 1183 | VKPSPKRKMEPDTEK |
| 1207 | ISLSAPAKKIKLNRE |
| 1208 | SLSAPAKKIKLNRET |
| 1218 | LNRETGKKIGSTENI |
| 1350 | GKPASVIKNVSTKPS |
| 1361 | TKPSNIVKYPEKESE |
| 1378 | EKIQKFTKDVSHEII |
| 1390 | EIIQHEVKSSKNSAS |
| 1441 | LNEQGNFKSLSQSSK |
| 1465 | STRASSNKDFTPNRD |
| 1552 | HKATYDTKRPNEETK |
| 190 | ESGPRIKKSTGIPRS |
| 203 | RSFMMEVKDPNMKGA |
| 232 | AEAYAIGKKEKPPFL |
| 233 | EAYAIGKKEKPPFLP |
| 334 | GYTKRLRKQLPPPPP |
| 435 | PFRDSDNKILPAAAL |
| 657 | EEEKKKSKLDEFTND |
| 81 | RIPIGGVKSTSKTYV |
| 85 | GGVKSTSKTYVISRT |
| 901 | IGSNYPEKLSARDGH |
| 941 | KKHRKRRKGEESEGF |
Function
E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0061630 | ubiquitin protein ligase activity |
| Molecular Function | GO:0004842 | ubiquitin-protein transferase activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0016567 | protein ubiquitination |
| Biological Process | GO:0006275 | regulation of DNA replication |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[5] 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.
[6] 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.