Search Results
Overview
| Uniprot ID | P25490 |
|---|---|
| Protein Name | Transcriptional repressor protein YY1 |
| Gene Name | YY1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 183 | GGKKSGKKSYLSGGA |
| 203 | GGADPGNKKWEQKQV |
| 204 | GADPGNKKWEQKQVQ |
| 208 | GNKKWEQKQVQIKTL |
| 286 | FARMKPRKIKEDDAP |
| 301 | RTIACPHKGCTKMFR |
| 409 | SHILTHAKAKNNQ** |
Function
Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence (PubMed:1655281). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed (PubMed:11158321). Involved in DNA repair (PubMed:18026119, PubMed:28575647). In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation (PubMed:28575647). Recruits the PR-DUB complex to specific gene-regulatory regions (PubMed:20805357)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005677 | chromatin silencing complex |
| Cellular Component | GO:0001650 | fibrillar center |
| Cellular Component | GO:0031011 | Ino80 complex |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0031519 | PcG protein complex |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Molecular Function | GO:0000987 | cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0001228 | DNA-binding transcription activator activity, RNA polymerase II-specific |
| Molecular Function | GO:0000981 | DNA-binding transcription factor activity, RNA polymerase II-specific |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0001217 | DNA-binding transcription repressor activity |
| Molecular Function | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific |
| Molecular Function | GO:0000400 | four-way junction DNA binding |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:1990837 | sequence-specific double-stranded DNA binding |
| Molecular Function | GO:0046332 | SMAD binding |
| Molecular Function | GO:0000976 | transcription cis-regulatory region binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0030183 | B cell differentiation |
| Biological Process | GO:0071347 | cellular response to interleukin-1 |
| Biological Process | GO:0034644 | cellular response to UV |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0000724 | double-strand break repair via homologous recombination |
| Biological Process | GO:0071707 | immunoglobulin heavy chain V-D-J recombination |
| Biological Process | GO:0061052 | negative regulation of cell growth involved in cardiac muscle cell development |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0032688 | negative regulation of interferon-beta production |
| Biological Process | GO:1902894 | negative regulation of miRNA transcription |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:1904507 | positive regulation of telomere maintenance in response to DNA damage |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0033044 | regulation of chromosome organization |
| Biological Process | GO:0006275 | regulation of DNA replication |
| Biological Process | GO:0060382 | regulation of DNA strand elongation |
| Biological Process | GO:0045995 | regulation of embryonic development |
| Biological Process | GO:0034696 | response to prostaglandin F |
| Biological Process | GO:0010225 | response to UV-C |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0000723 | telomere maintenance |
Reference
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[2] 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.
[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.