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IID00397
UniprotQ9UBE0
ProteinSUMO-activating enzyme subunit 1
GeneSAE1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
346
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-346 Hetero trimer : IID00104Complex
 Evidence X-RAY 1y8r A Reference
       Region 1y8r A 1-8 disorder
       Region 1y8r A 9-179 order
       Region 1y8r A 180-202 disorder
       Region 1y8r A 203-345 order
       Region 1y8r A 346-346 disorder
 Evidence X-RAY 1y8r D Reference
       Region 1y8r D 1-8 disorder
       Region 1y8r D 9-177 order
       Region 1y8r D 178-203 disorder
       Region 1y8r D 204-345 order
       Region 1y8r D 346-346 disorder
Seq 1-346 Hetero dimer : IID00104Complex
 Evidence X-RAY 1y8q A Reference
       Region 1y8q A 1-9 disorder
       Region 1y8q A 10-179 order
       Region 1y8q A 180-202 disorder
       Region 1y8q A 203-345 order
       Region 1y8q A 346-346 disorder
 Evidence X-RAY 1y8q C Reference
       Region 1y8q C 1-8 disorder
       Region 1y8q C 9-177 order
       Region 1y8q C 178-203 disorder
       Region 1y8q C 204-345 order
       Region 1y8q C 346-346 disorder
Seq 1-346 Hetero trimer : IID00104Complex,IID00378Complex
 Evidence X-RAY 3kyc A Reference
       Region 3kyc A 1-8 disorder
       Region 3kyc A 9-180 order
       Region 3kyc A 181-204 disorder
       Region 3kyc A 205-345 order
       Region 3kyc A 346-346 disorder
 Evidence X-RAY 3kyd A Reference
       Region 3kyd A 1-24 disorder
       Region 3kyd A 25-183 order
       Region 3kyd A 184-203 disorder
       Region 3kyd A 204-345 order
       Region 3kyd A 346-346 disorder
Seqphosphorylation
    12-12 Phosphoserine
Seqacetylation
    198-198 N6-acetyllysine
    2-2 N-acetylvaline; in SUMO-activating enzyme subunit 1
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-14,186-196
Order 15-185,197-346
ProS 9-14,186-196
AlphaFold
Disorder 1-9,181-202,346-346
Order 10-180,203-345
Pfam Hmmer
PF00899 35-166 3.4e-12
SEG 3-17
Function
Function in SwissProt
The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.