Search Results
Overview
| Uniprot ID | O95785 |
|---|---|
| Protein Name | Protein Wiz |
| Gene Name | WIZ |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1108 | NPPGPSPKALAKMMG |
| 1112 | PSPKALAKMMGGAGP |
| 1138 | LHISPLAKKLPPPPG |
| 1139 | HISPLAKKLPPPPGS |
| 1175 | AAPSLPKKLKPEQIR |
| 1322 | PLAGRPGKPGAGPAQ |
| 1356 | YLGSVAAKRPLQEDR |
| 1382 | IQTELPFKAKTLHEK |
| 1384 | TELPFKAKTLHEKTS |
| 1448 | WIKHRPQKVGAYRSY |
| 1464 | QGGRPFTKKFRSAGH |
| 1477 | GHGRDSDKRPSLGLA |
| 1534 | HQRQNINKFERRQAR |
| 933 | GLPPGLAKKSSSLKE |
| 934 | LPPGLAKKSSSLKEV |
| 955 | PGLLSLAKPLDAPAV |
| 964 | LDAPAVNKAIKSPPG |
| 967 | PAVNKAIKSPPGFSA |
| 988 | PSSPLLKKTPLALAG |
Function
May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0000981 | DNA-binding transcription factor activity, RNA polymerase II-specific |
| Molecular Function | GO:1990226 | histone methyltransferase binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0001222 | transcription corepressor binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0010571 | positive regulation of nuclear cell cycle DNA replication |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
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] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.
[8] 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.