Search Results
Overview
| Uniprot ID | O75182 |
|---|---|
| Protein Name | Paired amphipathic helix protein Sin3b |
| Gene Name | SIN3B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1059 | CDVDCRFKLSTHKMV |
| 292 | KMKLRGTKDLSIAAV |
| 319 | DKVRRVLKSQEVYEN |
| 395 | EIDYASCKRIGSSYR |
| 406 | SSYRALPKTYQQPKC |
| 412 | PKTYQQPKCSGRTAI |
| 622 | DTKALRSKSLLNEIE |
Function
Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030849 | autosome |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0070822 | Sin3-type complex |
| Cellular Component | GO:0000805 | X chromosome |
| Cellular Component | GO:0001741 | XY body |
| Cellular Component | GO:0000806 | Y chromosome |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0030336 | negative regulation of cell migration |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0060633 | negative regulation of transcription initiation by RNA polymerase II |
Reference
[1] 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.
[2] 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.
[3] 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.