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IID00136
UniprotO75928
ProteinE3 SUMO-protein ligase PIAS2
GenePIAS2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
621
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 147-488 Monomer :
 Evidence X-RAY 4fo9 A Reference
       Region 4fo9 A 147-216 order
       Region 4fo9 A 217-218 disorder
       Region 4fo9 A 219-242 order
       Region 4fo9 A 243-250 disorder
       Region 4fo9 A 251-311 order
       Region 4fo9 A 312-312 disorder
       Region 4fo9 A 313-328 order
       Region 4fo9 A 329-337 disorder
       Region 4fo9 A 338-420 order
       Region 4fo9 A 421-421 disorder
       Region 4fo9 A 422-426 order
       Region 4fo9 A 427-488 disorder
Seq 466-488 Hetero dimer : IID00378Complex
 Evidence NMR 2asq B Reference
       Region 2asq B 466-479 order
       Region 2asq B 480-488 disorder
SeqProS verified 466-479 Hetero dimer : IID00378Complex
       Region 2asq B 466-479 order
       Region 4fo9 A 427-488 disorder
Seqphosphorylation
    476-476 Phosphoserine
    477-477 Phosphoserine
    499-499 Phosphoserine
    478-478 Phosphoserine
 
Prediction
NeProc
Disorder 73-147,168-174,430-621
Order 1-67,148-167,175-429
ProS 142-147,168-174,468-475,531-535,549-556,612-621
AlphaFold
Disorder 1-2,67-144,245-254,429-468,471-621
Order 3-66,145-244,255-428,469-470
Pfam Hmmer
PF02037 11-45 1.1e-07
PF02891 342-394 2.2e-37
SEG 102-123 ,135-144 ,475-483 ,509-522 ,571-610
Function
Function in SwissProt
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 coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'.