Search Results
Overview
| Uniprot ID | Q9UKN8 |
|---|---|
| Protein Name | General transcription factor 3C polypeptide 4 |
| Gene Name | GTF3C4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 119 | PLNSCLLKVGSKTEV |
| 137 | KEKFAASKDPTVSQT |
| 156 | RVFNPEGKALPPMRG |
| 351 | PVNLKAVKGYFTLRQ |
| 633 | TSSKQVVKQGLQERS |
| 736 | VLIGHISKKMNKQTF |
| 737 | LIGHISKKMNKQTFP |
| 740 | HISKKMNKQTFPEHC |
Function
Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin (PubMed:10523658). Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3 (PubMed:10523658). May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F (PubMed:10523658). May be localized close to the A box (PubMed:10523658)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000127 | transcription factor TFIIIC complex |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0036408 | histone H3K14 acetyltransferase activity |
| Molecular Function | GO:0000995 | RNA polymerase III general transcription initiation factor activity |
| Biological Process | GO:0042791 | 5S class rRNA transcription by RNA polymerase III |
| Biological Process | GO:0006383 | transcription by RNA polymerase III |
| Biological Process | GO:0006384 | transcription initiation at RNA polymerase III promoter |
| Biological Process | GO:0042797 | tRNA transcription by RNA polymerase III |
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] 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.
[7] 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.