Mouse Anti-YY1 Recombinant Antibody (4A5) (CBMAB-Y0050-LY)

YY1

YY1 is a ubiquitously distributed transcription factor belonging to the GLI-Kruppel class of zinc finger proteins. The protein is involved in repressing and activating a diverse number of promoters. YY1 may direct histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter, thus implicating histone modification in the function of YY1. 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. 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.

DELTA; NF-E1; UCRBP; GADEVS; INO80S; YIN-YANG-1

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).
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.

Biological Process anterior/posterior pattern specification Source:Ensembl
Biological Process B cell differentiation Source:Ensembl
Biological Process camera-type eye morphogenesis Source:Ensembl
Biological Process cellular response to DNA damage stimulus Source:UniProtKB1 Publication
Biological Process cellular response to interleukin-1 Source:Ensembl
Biological Process cellular response to UV Source:UniProtKB1 Publication
Biological Process chromatin remodeling Source:ComplexPortal1 Publication
Biological Process double-strand break repair via homologous recombination Source:UniProtKB1 Publication
Biological Process immunoglobulin heavy chain V-D-J recombination Source:Ensembl
Biological Process negative regulation of cell growth involved in cardiac muscle cell development Source:Ensembl
Biological Process negative regulation of gene expression Source:CACAO1 Publication
Biological Process negative regulation of interferon-beta production Source:UniProtKB1 Publication
Biological Process negative regulation of miRNA transcription Source:Ensembl
Biological Process negative regulation of transcription by RNA polymerase II Source:UniProtKB1 Publication
Biological Process positive regulation of DNA repair Source:ComplexPortal
Biological Process positive regulation of DNA-templated transcription Source:ComplexPortal1 Publication
Biological Process positive regulation of gene expression Source:Ensembl
Biological Process positive regulation of telomere maintenance in response to DNA damage Source:ComplexPortal
Biological Process positive regulation of transcription by RNA polymerase II Source:BHF-UCL1 Publication
Biological Process regulation of cell cycle Source:ComplexPortal1 Publication
Biological Process regulation of chromosome organization Source:ComplexPortal1 Publication
Biological Process regulation of DNA repair Source:ComplexPortal
Biological Process regulation of DNA replication Source:ComplexPortal1 Publication
Biological Process regulation of DNA strand elongation Source:ComplexPortal1 Publication
Biological Process regulation of embryonic development Source:ComplexPortal
Biological Process regulation of transcription by RNA polymerase II Source:GO_Central1 Publication
Biological Process response to prostaglandin F Source:Ensembl
Biological Process response to UV-C Source:UniProtKB1 Publication
Biological Process RNA localization Source:Ensembl
Biological Process spermatogenesis Source:UniProtKB-KW
Biological Process telomere maintenance Source:ComplexPortal

Nucleus matrix
Associated with the nuclear matrix.

Gabriele-de Vries syndrome (GADEVS):
An autosomal dominant neurodevelopmental disorder characterized by delayed psychomotor development and intellectual disability. Most patients have behavioral and feeding problems, movement abnormalities, mild distal skeletal anomalies, and dysmorphic facial features.

Phosphorylation at Ser-118 by CK2 prevents proteolytic cleavage by caspase-7 (CASP7) during apoptosis.
Proteolytically cleaved by caspase-7 (CASP7) in response to apoptosis (PubMed:22184066).
Phosphorylation at Ser-118 protects against proteolytic cleavage (PubMed:22184066).
Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with the effect of decreasing affinity of YY1 to its cognate DNA binding sites.
Ubiquitinated.