Search Results
Overview
| Uniprot ID | P06400 |
|---|---|
| Protein Name | Retinoblastoma-associated protein |
| Gene Name | RB1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 265 | NRSARIAKQLENDTR |
| 791 | HIPRSPYKFPSSPLR |
| 824 | EGLPTPTKMTPRSRI |
| 847 | GTSEKFQKINQMVCN |
| 873 | SNPPKPLKKLRFDIE |
| 874 | NPPKPLKKLRFDIEG |
| 900 | GESKFQQKLAEMTST |
Function
Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Biological Process | GO:0048667 | cell morphogenesis involved in neuron differentiation |
| Biological Process | GO:0032869 | cellular response to insulin stimulus |
| Biological Process | GO:0002062 | chondrocyte differentiation |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0051276 | chromosome organization |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0034088 | maintenance of mitotic sister chromatid cohesion |
| Biological Process | GO:0045445 | myoblast differentiation |
| Biological Process | GO:2001234 | negative regulation of apoptotic signaling pathway |
| Biological Process | GO:0045786 | negative regulation of cell cycle |
| Biological Process | GO:0030308 | negative regulation of cell growth |
| Biological Process | GO:0120163 | negative regulation of cold-induced thermogenesis |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:2000134 | negative regulation of G1/S transition of mitotic cell cycle |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:1903944 | negative regulation of hepatocyte apoptotic process |
| Biological Process | GO:0050728 | negative regulation of inflammatory response |
| Biological Process | GO:1904761 | negative regulation of myofibroblast differentiation |
| Biological Process | GO:0006469 | negative regulation of protein kinase activity |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0031175 | neuron projection development |
| Biological Process | GO:1904028 | positive regulation of collagen fibril organization |
| Biological Process | GO:1903055 | positive regulation of extracellular matrix organization |
| Biological Process | GO:0045842 | positive regulation of mitotic metaphase/anaphase transition |
| Biological Process | GO:2000679 | positive regulation of transcription regulatory region DNA binding |
| Biological Process | GO:0071459 | protein localization to chromosome, centromeric region |
| Biological Process | GO:0007265 | Ras protein signal transduction |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0043550 | regulation of lipid kinase activity |
| Biological Process | GO:0007346 | regulation of mitotic cell cycle |
| Biological Process | GO:0031134 | sister chromatid biorientation |
| Biological Process | GO:0007283 | spermatogenesis |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016605 | PML body |
| Cellular Component | GO:0035189 | Rb-E2F complex |
| Cellular Component | GO:0005819 | spindle |
| Cellular Component | GO:0016514 | SWI/SNF complex |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0061676 | importin-alpha family protein binding |
| Molecular Function | GO:0019900 | kinase binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0051219 | phosphoprotein binding |
| Molecular Function | GO:0000977 | RNA polymerase II transcription regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0003180 | aortic valve morphogenesis |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0030154 | cell differentiation |
Reference
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[2] 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.
[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] 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.
[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.