Search Results
Overview
| Uniprot ID | Q75N03 |
|---|---|
| Protein Name | E3 ubiquitin-protein ligase Hakai |
| Gene Name | CBLL1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 288 | TFRISTRKHSNLITV |
| 29 | VRRRIPIKLISKQAN |
| 33 | IPIKLISKQANKAKP |
| 74 | EEERYDCKGGELFAN |
Function
E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 (By similarity). Targets CDH1 for endocytosis and degradation (By similarity). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Its function in the WMM complex is unknown (PubMed:29507755)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0036396 | RNA N6-methyladenosine methyltransferase complex |
| Cellular Component | GO:0000151 | ubiquitin ligase complex |
| Molecular Function | GO:0042802 | identical protein 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:0098609 | cell-cell adhesion |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0007162 | negative regulation of cell adhesion |
| Biological Process | GO:0030335 | positive regulation of cell migration |
| Biological Process | GO:0045807 | positive regulation of endocytosis |
| Biological Process | GO:0016567 | protein ubiquitination |
| Biological Process | GO:0030155 | regulation of cell adhesion |
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] 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.
[4] 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.
[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.