(3) ZMIZ3 (15q23) E3 SUMO-proteiiniligaasi PIAS1, DDXBP1, GRP, GU/RH-II, Aktivoidun STAT1-proteiinin estäjä

(3) ZMIZ3, (PIAS1), (15q23) ) https://www.ncbi.nlm.nih.gov/gene/8554

 Päivitystä 5.1.2022.

PIAS1 on aktivoidun STAT1-proteiinin estäjä.   PIAS-geenifunktio on ihmiselle elintärkeä.

PIAS1 protein inhibitor of activated STAT 1 [ Homo sapiens (human) ]

PIAS1 Also known as

GBP; ZMIZ3; DDXBP1; GU/RH-II

Summary

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 including the STAT1 and nuclear factor kappaB pathways. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]

Expression

Ubiquitous expression in thyroid (RPKM 10.0), ovary (RPKM 9.9) and 25 other tissues See more

Orthologs

mouse all

Preferred Names

E3 SUMO-protein ligase PIAS1

Names

AR interacting protein

DEAD/H (Asp-Glu-Ala-Asp/His) box binding protein 1

DEAD/H box-binding protein 1

E3 SUMO-protein transferase PIAS1

RNA helicase II-binding protein

gu-binding protein

protein inhibitor of activated STAT protein 1

zinc finger, MIZ-type containing 3 Conserved Domains (3) summary

NP_001307616.1  E3 SUMO-protein ligase PIAS1 isoform 1

Conserved Domains (3) summary

smart00513
Location:13 → 47

SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation

pfam02891
Location:333 → 381

zf-MIZ; MIZ/SP-RING zinc finger

pfam14324
Location:137 → 273

PINIT; PINIT domain

Related articles in PubMed

1. B Cell Receptor Activation and Chemical Induction Trigger Caspase-Mediated Cleavage of PIAS1 to Facilitate Epstein-Barr Virus Reactivation. Zhang K, et al. Cell Rep, 2017 Dec 19. PMID 29262325, Free PMC Article
2. Identification of the SUMO E3 ligase PIAS1 as a potential survival biomarker in breast cancer. Chanda A, et al. PLoS One, 2017. PMID 28493978, Free PMC Article
3. Hepatitis B virus surface protein-induced hPIAS1 transcription requires TAL1, E47, MYOG, NFI, and MAPK signal pathways. Wang H, et al. Biol Chem, 2016 Nov 1. PMID 27276529
4. SUMO Ligase Protein Inhibitor of Activated STAT1 (PIAS1) Is a Constituent Promyelocytic Leukemia Nuclear Body Protein That Contributes to the Intrinsic Antiviral Immune Response to Herpes Simplex Virus 1. Brown JR, et al. J Virol, 2016 Jul 1. PMID 27099310, Free PMC Article
5. PIAS1 is a crucial factor for prostate cancer cell survival and a valid target in docetaxel resistant cells. Puhr M, et al. Oncotarget, 2014 Dec 15. PMID 25474038, Free PMC Article

See all (187) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

 

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. Rad18, independently of its ubiquitin ligase activity, promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci.
2. PIAS1 as a key regulator of Epstein-Barr Virus lytic replication. PIAS1 acts as an inhibitor for transcription factors involved in lytic gene expression.
3. these results indicate that PIAS1 is a positive regulator of MYC.
4. PIAS1 is a prognostic biomarker in breast cancer
5. PIAS1 is a determinant of poor survival and acts as a positive feedback regulator of AR signaling through enhanced AR stabilization in prostate cancer
6. PIAS1 overexpression exacerbated mutant Huntingtin-associated phenotypes and aberrant protein accumulation
7. HBs protein-induced hPIAS1 transcription requires TAL1, E47, MYOG, NFI, and MAPK signal pathways
8. identified the SUMO ligase PIAS1 as a constituent PML-NB antiviral protein. This finding distinguishes a SUMO ligase that may mediate signaling events important in promyelocytic leukemia nuclear body mediated intrinsic immunity.
9. PIAS1 enhances p300 recruitment to c-Myb-bound sites through interaction with both proteins. In addition, the E3 activity of PIAS1 enhances further its coactivation
10. Results show that apocrine breast cancer and prostate cancer cells share a core AR cistrome and target gene signature linked to cancer cell growth, and PIAS1 plays a similar coregulatory role for AR in both cancer cell types.

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