Search Results
Overview
| Uniprot ID | Q9UPT8 |
|---|---|
| Protein Name | Zinc finger CCCH domain-containing protein 4 |
| Gene Name | ZC3H4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1051 | ELLSRILKTVNATGS |
| 1159 | RTPNAGGKATEPAAD |
| 1184 | NGKSSASKAKEPPFV |
| 1186 | KSSASKAKEPPFVRK |
| 1193 | KEPPFVRKSALEQPE |
| 1224 | SYNRPRPKAAAAPAA |
| 184 | LPKKAYSKMDSKSYG |
| 776 | LYLRIQQKQQEEEER |
| 851 | LGDPRLQKGHPTGSR |
Function
RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006353 | DNA-templated transcription termination |
| Biological Process | GO:0110064 | lncRNA catabolic process |
| Biological Process | GO:0032785 | negative regulation of DNA-templated transcription, elongation |
| Biological Process | GO:0140744 | negative regulation of lncRNA transcription |
| Biological Process | GO:0071027 | nuclear RNA surveillance |
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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[5] 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.
[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.