Aliases for PIAS1 Gene
External Ids for PIAS1 Gene
Previous HGNC Symbols for PIAS1 Gene
Previous GeneCards Identifiers for PIAS1 Gene
This gene encodes a member of the protein inhibitor of activated STAT (PIAS) family. PIAS proteins function as SUMO E3 ligases and play important roles in many cellular processes by mediating the sumoylation of target proteins. This protein plays a central role as a transcriptional coregulator of numerous cellular pathways includign the STAT1 and nuclear factor kappaB pathways. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]
GeneCards Summary for PIAS1 Gene
PIAS1 (Protein Inhibitor Of Activated STAT 1) is a Protein Coding gene. Diseases associated with PIAS1 include Testicular Germ Cell Cancer. Among its related pathways are Interferon gamma signaling and Integrated Breast Cancer Pathway. GO annotations related to this gene include nucleic acid binding and ligase activity. An important paralog of this gene is PIAS3.
UniProtKB/Swiss-Prot for PIAS1 Gene
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (atLys-65 and Lys-160) and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).