E3 SUMO-protein ligase PIAS4 (Protein name
), PIAS4_HUMAN from NCBI database.
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General Annotation
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Gene name:
PIAS4(PIASG);
Protein name:
E3 SUMO-protein ligase PIAS4;
Alternative:
Protein inhibitor of activated STAT protein 4;PIASy;Protein inhibitor of activated STAT protein gamma(PIAS-gamma);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1 (IFNG-induced). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Interacts with TICAM1. 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 coregulation in various cellular pathways, including the STAT pathway, the p53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Promotes PARK7 sumoylation. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations.
Subcellular Location:
Nucleus
PML body
Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-510;INTERACTION WITH TP53
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Cited for: INTERACTION WITH STAT1;SUBCELLULAR LOCATION;MUTAGENESIS OF 23-LEU-LEU-24
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Cited for: INTERACTION WITH AR;TISSUE SPECIFICITY;MUTAGENESIS OF 23-LEU-LEU-24
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Cited for: FUNCTION IN SUMOYLATION OF TCF4;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-35 AND LYS-128
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Cited for: SUMOYLATION AT LYS-35 AND LYS-128;FUNCTION IN SUMOYLATION OF TCF4;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-35 AND LYS-128
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]