PIAS2(PIASx) protein inhibitor of activated STAT 2 [ Homo sapiens (human) ]
(4) ZMIZ4 (18q21.1) ,
(PIAS2) https://www.ncbi.nlm.nih.gov/gene/9063
- PIAS2 , Also known as
- DIP; MIZ1; SIZ2; ARIP3; PIASX; ZMIZ4
- Summary
- This gene encodes a member of the protein inhibitor of activated STAT family, which function as SUMO E3 ligases and play important roles in many cellular processes by mediating the sumoylation of target proteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. Isoforms of the encoded protein enhance the sumoylation of specific target proteins including the p53 tumor suppressor protein, c-Jun, and the androgen receptor. A pseudogene of this gene is located on the short arm of chromosome 4. The symbol MIZ1 has also been associated with ZBTB17 which is a different gene located on chromosome 1. [provided by RefSeq, Aug 2017]
- Expression Broad expression in testis (RPKM 8.9), thyroid (RPKM 2.1) and 23 other tissues See more -Orthologs mouse all
- Preferred Names
- E3 SUMO-protein ligase PIAS2
- Names
- DAB2-interacting protein, (DIP)
- E3 SUMO-protein transferase PIAS2
- androgen receptor-interacting protein 3, (ARIP)
- msx-interacting zinc finger protein, (MIZ1)
- protein inhibitor of activated STAT X, (PIASX)
- zinc finger, MIZ-type containing 4, (ZMIZ4)
- NP_001310976.1 E3 SUMO-protein ligase PIAS2 isoform 5
- Conserved Domains (3) summary
-
smart00513
Location:2 → 36 - SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
-
pfam14324
Location:138 → 282 - PINIT; PINIT domain
-
cd16790
Location:334 → 381 - SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
Related articles in PubMed
-
Protein Inhibitor of Activated STAT2 Restricts HCV Replication by Modulating Viral Proteins Degradation. Guo J, et al. Viruses, 2017 Sep 30. PMID 28973998, Free PMC Article
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PIASxalpha differentially regulates the amplitudes of transcriptional responses following activation of the ERK and p38 MAPK pathways. Yang SH, et al. Mol Cell, 2006 May 19. PMID 16713578
- Molecular cloning and characterization of a novel splicing variant of PIASx. Zheng Y, et al. Acta Pharmacol Sin, 2004 Aug. PMID 15301740
- Compositional Control of Phase-Separated Cellular Bodies. Banani SF, et al. Cell, 2016 Jul 28. PMID 27374333, Free PMC Article
- Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. Song J, et al. J Biol Chem, 2005 Dec 2. PMID 16204249
GeneRIFs: Gene References Into Functions
- results indicated that PIAS2-mediated SUMOylation constrained HCV replication
- the expression of SENP8, SAE1, PIAS1, PIAS2 and ZMIZ1 is deregulated in the majority of PTC tissues, likely contributing to the PTC phenotype.
- UXT is a binding protein of PIAS2, and interaction between PIAS2 and UXT may be important for the transcriptional activation of AR.
- PIASxalpha is a novel SUMO E3 ligase for PTEN, and it positively regulates PTEN protein level in tumor suppression.
- These findings suggest that SUMO-1 modification of MDA5 possibly via PIAS2beta may play a role in the MDA5-mediated interferon response to viral infections.
- the repressive properties of PIASxalpha/ARIP3 require its physical interaction with FLI-1, identifying PIASxalpha as a novel corepressor of FLI-1
- PIASx may function as a co-repressor of Stat4
- Required for upregulation of a large group of genes in response to DNA damage, a function that is regulated by c-Myc, but not by 14-3-3eta and represses the expression of many genes
- PIASxalpha acts as a key signal integrator that permits different responses from the same transcription factor, depending on the signaling pathway that is activated.
- findings show that Epstein-Barr virus Rta interacts and colocalizes with PIASxalpha and PIASxbeta in the nucleus; these interactions seem to enhance Rta sumoylation
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