Search Results
Overview
| Uniprot ID | P53999 |
|---|---|
| Protein Name | Activated RNA polymerase II transcriptional coactivator p15 |
| Gene Name | SUB1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | GEMKPGRKGISLNPE |
| 23 | DSDSEVDKKLKRKKQ |
| 29 | DKKLKRKKQVAPEKP |
| 35 | KKQVAPEKPVKKQKT |
| 38 | VAPEKPVKKQKTGET |
| 39 | APEKPVKKQKTGETS |
| 41 | EKPVKKQKTGETSRA |
| 53 | SRALSSSKQSSSSRD |
| 68 | DNMFQIGKMRYVSVR |
| 80 | SVRDFKGKVLIDIRE |
Function
General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0003697 | single-stranded DNA binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Biological Process | GO:0051053 | negative regulation of DNA metabolic process |
| Biological Process | GO:0060261 | positive regulation of transcription initiation by RNA polymerase II |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0001111 | RNA polymerase II promoter clearance |
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] 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] 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.
[7] 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.
[8] 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.
[9] 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.