Search Results
Overview
| Uniprot ID | Q9UQR1 |
|---|---|
| Protein Name | Zinc finger protein 148 |
| Gene Name | ZNF148 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 142 | REPVDLQKKKKRKQR |
| 143 | EPVDLQKKKKRKQRS |
| 153 | RKQRSPAKILTINED |
| 291 | KLNRCAIKGGLLTSE |
| 314 | PKDNSLPKKKRQKTE |
| 323 | KRQKTEKKSSGMDKE |
| 335 | DKESALDKSDLKKDK |
| 342 | KSDLKKDKNDYLPLY |
| 389 | SGEIHPPKLVLKKIN |
| 424 | YEESKVSKYAFELVD |
| 472 | DDAMQFLKKKRYLQA |
Function
Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0003700 | DNA-binding transcription factor activity |
| Molecular Function | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0043565 | sequence-specific DNA binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006968 | cellular defense response |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0021762 | substantia nigra development |
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] 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.