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UniProt functional annotation for O75925 | ||
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| UniProt code: O75925. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| 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 and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. 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. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:21965678}. |
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| 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). {ECO:0000250, ECO:0000269|PubMed:11583632, ECO:0000269|PubMed:11672422, ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:12356736, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:14701874, ECO:0000269|PubMed:15133049, ECO:0000269|PubMed:15208321, ECO:0000269|PubMed:16617055, ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17540171, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:9177271, ECO:0000269|PubMed:9724754}. |
| 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. {ECO:0000269|PubMed:19557165}. |
| Subcellular location: | |
Nucleus speckle {ECO:0000269|PubMed:12393906, ECO:0000269|PubMed:9177271}. Nucleus, PML body {ECO:0000250}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton. |
| Tissue specificity: | |
Expressed in numerous tissues with highest level in testis. {ECO:0000269|PubMed:11439351, ECO:0000269|PubMed:9177271}. |
| Domain: | |
The LXXLL motif is a transcriptional coregulator signature. |
| Domain: | |
The SP-RING-type domain is required for promoting EKLF sumoylation. {ECO:0000250}. |
| Ptm: | |
Sumoylated. {ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12393906}. |
| Similarity: | |
Belongs to the PIAS family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.