Search Results
Overview
| Uniprot ID | Q01658 |
|---|---|
| Protein Name | Protein Dr1 |
| Gene Name | DR1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 128 | QQQELFAKARQQQAE |
| 95 | KEVLQECKTVALKRR |
Function
The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0140672 | ATAC complex |
| Cellular Component | GO:0072686 | mitotic spindle |
| Cellular Component | GO:0017054 | negative cofactor 2 complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0090575 | RNA polymerase II transcription regulator complex |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0016251 | RNA polymerase II general transcription initiation factor activity |
| Molecular Function | GO:0017025 | TBP-class protein binding |
| Biological Process | GO:0017055 | negative regulation of RNA polymerase II transcription preinitiation complex assembly |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0051302 | regulation of cell division |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0045995 | regulation of embryonic development |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0090043 | regulation of tubulin deacetylation |
| Biological Process | GO:0051123 | RNA polymerase II preinitiation complex assembly |
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] 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.
[4] 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.
[5] 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.
[6] 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.