Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:O75925 PIAS1
| Class:Id | ReferenceGeneProduct:61690 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 6 2015;chain:2-651 added on Fri February 6 2015;initiator methionine:1 for 61690 removed on Fri Nov 03 2023;initiator methionine: for 61690 added on Fri Nov 03 2023;initiator methionine: for 61690 removed on Fri Aug 15 2025;initiator methionine:1 for 61690 added on Fri Aug 15 2025 |
| _displayName | UniProt:O75925 PIAS1 |
| _timestamp | 2026-02-20 22:25:26 |
| chain | initiator methionine:1 chain:2-651 |
| checksum | AA69338221124119 |
| comment | 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 (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:15280358, PubMed:21965678, PubMed:36050397). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2, PML and ZNF76 (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:15280358, PubMed:21965678, PubMed:36050397). 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 (PubMed:11583632, PubMed:11867732). In vitro, binds A/T-rich DNA (PubMed:15133049). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Mediates sumoylation of MRE11, stabilizing MRE11 on chromatin during end resection (PubMed:36050397). Sumoylates PML (at 'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation (By similarity). 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 (PubMed:21965678). Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (By similarity). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumoylation activity (By similarity). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (By similarity).FUNCTION (Microbial infection) Restricts Epstein-Barr virus (EBV) lytic replication by acting as an inhibitor for transcription factors involved in lytic gene expression (PubMed:29262325). The virus can use apoptotic caspases to antagonize PIAS1-mediated restriction and express its lytic genes (PubMed:29262325).PATHWAY Protein modification; protein sumoylation.SUBUNIT Interacts with NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). 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. Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with PML (By similarity). Interacts with MTA1. Interacts with SUMO1P1/SUMO5 (PubMed:27211601). Interacts with PRDM1/Blimp-1 (PubMed:28842558). Interacts (via N-terminus) with MSX1 (via C-terminus); the interaction is required for the localization of both proteins to the nuclear periphery and specific binding of MSX1 to the core enhancer region in target gene promoters (PubMed:16600910).SUBUNIT (Microbial infection) Interacts with ebolavirus VP35; this interaction mediates the sumoylation of IRF7 and contributes to the viral inhibition of IFN-type I production.INTERACTION Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (PubMed:11672422). Interaction with MSX1 is required for localization to the nuclear periphery (By similarity).ALTERNATIVE PRODUCTS Expressed in numerous tissues with highest level in testis.DOMAIN The LXXLL motif is a transcriptional coregulator signature.DOMAIN The SP-RING-type domain is required for promoting EKLF sumoylation.PTM Sumoylated.SIMILARITY Belongs to the PIAS family.CAUTION A paper showing that PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling has been retracted, because some of the data was found to be deliberately falsified. |
| description | recommendedName: E3 SUMO-protein ligase PIAS1 ecNumber evidence="19 29"2.3.2.- alternativeName: DEAD/H box-binding protein 1 alternativeName: fullName evidence="34"E3 SUMO-protein transferase PIAS1 alternativeName: Gu-binding protein shortName: GBP alternativeName: Protein inhibitor of activated STAT protein 1 alternativeName: RNA helicase II-binding protein |
| geneName | PIAS1 DDXBP1 |
| identifier | O75925 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing Cytoplasm Cytoskeleton DNA-binding Host-virus interaction Isopeptide bond Metal-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat Transcription Transcription regulation Transferase Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | PIAS1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9004893] ENSEMBL:ENSG00000033800 PIAS1 [Homo sapiens] |
| secondaryIdentifier | PIAS1_HUMAN B2RB67 B3KSY9 C5J4B4 Q147X4 Q99751 Q9UN02 |
| sequenceLength | 651 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:8972098] UniProt:O75925-1 PIAS1 [Homo sapiens] [ReferenceIsoform:8972099] UniProt:O75925-2 PIAS1 [Homo sapiens] [ReferenceIsoform:8972100] UniProt:O75925-3 PIAS1 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:877307] PIAS1 [nucleoplasm] [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:O75925 PIAS1 (61690)
