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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 B Reference
       Region 2ktr B 3-100 order
 Evidence NMR 2ktr A Reference
       Region 2ktr A 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
Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery (By similarity). Involved in midbody ring degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:11244088, PubMed:11500922). May play a role in titin/TTN downstream signaling in muscle cells (By similarity). May regulate signaling cascades through ubiquitination (By similarity). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels (By similarity). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (By similarity). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (By similarity).
Isoform 1
More potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.