E3 SUMO-protein ligase PIAS2 (Protein name
), PIAS2_HUMAN from NCBI database.
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General Annotation
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Gene name:
PIAS2(PIASX);
Protein name:
E3 SUMO-protein ligase PIAS2;
Alternative:
DAB2-interacting protein(DIP);Androgen receptor-interacting protein 3(ARIP3);PIAS-NY protein;Msx-interacting zinc finger protein(Miz1);Protein inhibitor of activated STAT2;Protein inhibitor of activated STAT x;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7, TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and with NCOA2 (By similarity). Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with PLAG1. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G(1) phase.
Function:
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 coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha.
Subcellular Location:
Nucleus speckle
Nucleus
PML body
Colocalizes at least partially with promyelocytic leukemia nuclear bodies.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PIAS2-ALPHA AND PIAS2-BETA)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3);TISSUE SPECIFICITY;DEVELOPMENTAL STAGE
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PIAS2-ALPHA)
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Cited for: SUMOYLATION OF MDM2;SUBCELLULAR LOCATION;MUTAGENESIS OF CYS-362
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Cited for: INTERACTION WITH JUN; TP53 AND UBE2I;SUMOYLATION;MUTAGENESIS OF CYS-362
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-477 AND SER-478;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH PML
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Cited for: STRUCTURE BY NMR OF 466-488 IN COMPLEX WITH SUMO1;MUTAGENESIS OF VAL-467; VAL-469; ILE-470; LEU-472 AND THR-473