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IID50133
UniprotO08623
ProteinSequestosome-1
GeneSqstm1
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
439
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 3-100 Homo dimer :
 Evidence NMR 2ktr A Reference
       Region 2ktr A 3-100 order
 Evidence NMR 2ktr B Reference
       Region 2ktr B 3-100 order
Seq 3-100 Monomer :
 Evidence NMR 2kkc A Reference
       Region 2kkc A 3-100 order
Seq 331-346 Hetero dimer : IID50112Complex
 Evidence NMR 2k6q B Reference
       Region 2k6q B 331-346 order
       Region 2k6q B 331-332 high_rmsd
SeqProS possible 331-346 Probably the linker between zinc finger domain and UBAdomain is considered to be disordered.(PubMed=19049332). Hetero dimer : IID50112Complex
       Region 2k6q B 331-346 order
Seqphosphorylation
    145-145 Phosphotyrosine
    173-173 Phosphoserine
    360-360 Phosphoserine
    402-402 Phosphoserine; by ULK1 and TBK1
    406-406 Phosphoserine
    364-364 Phosphoserine
    365-365 Phosphoserine
    354-354 Phosphoserine
    24-24 Phosphoserine
    327-327 Phosphoserine
    331-331 Phosphoserine
    348-348 Phosphoserine
    281-281 Phosphoserine
    305-305 Phosphoserine
    269-269 Phosphoserine
    263-263 Phosphoserine
    266-266 Phosphothreonine
    175-175 Phosphoserine
    204-204 Phosphoserine
    246-246 Phosphoserine
Seqacetylation
    434-434 N6-acetyllysine; alternate
    419-419 N6-acetyllysine; alternate
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 170-184,207-229,235-382,434-439
Order 1-169,185-206,230-234,383-433
ProS 170-184,207-229,235-264,297-304,328-340
AlphaFold
Disorder 1-2,28-38,102-117,169-227,261-261,265-389,432-439
Order 3-27,39-101,118-168,228-260,262-264,390-431
Pfam Hmmer
PF00564 20-100 5.7e-15
PF00569 119-162 5.1e-11
SEG 29-43
Function
Function in SwissProt
Isoform 1
More potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.