Search Results
Overview
| Uniprot ID | P35269 |
|---|---|
| Protein Name | General transcription factor IIF subunit 1 |
| Gene Name | GTF2F1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 169 | EEWERRNKVLNHFSI |
| 242 | KKKAPLAKGGRKKKK |
| 407 | TLRAAASKLEQGKRV |
| 421 | VSEMPAAKRLRLDTG |
| 435 | GPQSLSGKSTPQPPS |
| 444 | TPQPPSGKTTPNSGD |
| 83 | REEARRKKYGIVLKE |
Function
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0019211 | phosphatase activator activity |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0019903 | protein phosphatase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0016251 | RNA polymerase II general transcription initiation factor activity |
| Molecular Function | GO:0001091 | RNA polymerase II general transcription initiation factor binding |
| Molecular Function | GO:0001096 | TFIIF-class transcription factor complex binding |
| Biological Process | GO:0032091 | negative regulation of protein binding |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0032968 | positive regulation of transcription elongation by RNA polymerase II |
| Biological Process | GO:0009615 | response to virus |
| Biological Process | GO:0006366 | transcription by RNA polymerase II |
| Biological Process | GO:0006368 | transcription elongation by RNA polymerase II |
| Biological Process | GO:0006367 | transcription initiation at RNA polymerase II promoter |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0005669 | transcription factor TFIID complex |
| Cellular Component | GO:0005674 | transcription factor TFIIF complex |
| Molecular Function | GO:0003677 | DNA binding |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] 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.
[6] 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.
[7] 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.
[8] 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.
[9] 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.
[10] 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.