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Validated All-in-One™ qPCR Primer for PIAS1(NM_016166.2) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the mammalian PIAS [protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1)] family. This member contains a putative zinc-binding motif and a highly acidic region. It inhibits STAT1-mediated gene activation and the DNA binding activity, binds to Gu protein/RNA helicase II/DEAD box polypeptide 21, and interacts with androgen receptor (AR). It functions in testis as a nuclear receptor transcriptional coregulator and may have a role in AR initiation and maintenance of spermatogenesis. [provided by RefSeq].
Gene References into function
- novel function of PIAS1 in the induction of JNK-dependent apoptosis, independent of the previously known inhibitory activity of PIAS1 in STAT-mediated gene activation.
- protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses
- Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators.
- PIAS1 and PIASxalpha modulate the AR-dependent transactivation, which, at least in part, can be attributed to their SUMO-E3 activity toward AR.
- PIAS1 has a role in sumoylation of MDM2 in the cell nucleus
- found to strongly stimulate sumoylation of STAT1 at Lys703; results suggest a negative regulatory function for sumoylation.
- PIAS1 interacts with the N-terminal domain of human mineralocorticoid receptor and represses its ligand-dependent transcription.
- three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase
- GATA4 is a SUMO-1-targeted transcription factor and together with PIAS1 is a potent regulator of cardiac gene activity
- PIAS1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73.
- PIAS1 interacts with DNA cross-link repair SNM1A in nuclear focus formation.
- data support a physiological role of Ubc9 and PIAS1 as transcriptional coactivators in COUP-TFI-mediated CYP11B2 transcription
- Results suggest that recombinant human interleukin-12 upregulates STAT-1 expression and that increased expression may be dose dependent.
- PIAS1 modulates transcriptional activation of smooth muscle cells marker genes through cooperative interactions with both serum response factor and class I basic helix-loop-helix proteins proteins.
- Pias1 binds to and sumoylates metabotropic glutamate receptor 8
- In this study, we demonstrate that MEF2A undergoes sumoylation primarily at a single lysine residue (K395) both in vitro and in vivo. We also show that the nuclear E3 ligase, PIAS1, promotes sumoylation of MEF2A.
- PIAS1 is required for the appropriate localization and retention of Msx1 at the nuclear periphery in myoblast cells.
- TGF-beta rapidly suppresses IFN-gamma-driven STAT1 signaling by reducing DNA binding via promotion of STAT1--PIAS1 interactions and not inhibition of STAT1 activation.
- These results suggest that KyoT2 is a substrate of SUMO modification catalyzed by PIAS1, and that SUMOylation may modulate the transcriptional repression effect of KyoT2 on the Notch/RBP-J signaling pathway [Kyot2].
- PIASy cooperates with PIAS1 to down-regulate the specificity and magnitude of NF-kappa B/STAT1-mediated gene activation.
- the transcriptional repressor activity of ZNF133 is regulated by both the KRAB domain and the zinc finger motifs, and that the repressive effect by zinc finger motifs is mediated by PIAS1
- The data show that HCV NS3/4a is able to block the Jak-Stat signaling pathway at the stage of Stat-1 serine 727 phosphorylation.
- findings identify PRMT1 as a novel and crucial negative regulator of STAT1 activation that controls PIAS1-mediated repression by arginine methylation
