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IID00350
UniprotP55854
ProteinSmall ubiquitin-related modifier 3
GeneSUMO3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
103
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2-92 Hetero trimer : Q9QZS2
 Evidence NMR 2mp2 B Reference
       Region 2mp2 B 2-90 order
 Evidence NMR 2mp2 A Reference
       Region 2mp2 A 12-92 order
       Region 2mp2 A 12-12 high_rmsd
Seq 14-92 Monomer :
 Evidence NMR 1u4a A Reference
       Region 1u4a A 14-92 order
       Region 1u4a A 89-92 high_rmsd
Seq 14-103 Hetero dimer : Q9HC62
 Evidence X-RAY 2io1 F Reference
       Region 2io1 F 14-14 disorder
       Region 2io1 F 15-95 order
       Region 2io1 F 96-103 disorder
 Evidence X-RAY 2io1 D Reference
       Region 2io1 D 14-14 disorder
       Region 2io1 D 15-96 order
       Region 2io1 D 97-103 disorder
 Evidence X-RAY 2io1 B Reference
       Region 2io1 B 14-14 disorder
       Region 2io1 B 15-95 order
       Region 2io1 B 96-103 disorder
 
Prediction
NeProc
Disorder 1-14
Order 15-103
ProS 9-14
AlphaFold
Disorder 1-1,3-14,89-103
Order 2-2,15-88
Pfam Hmmer
PF00240 20-90 1.2e-12
Function
Function in SwissProt
Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).