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IID00512
UniprotP62258
Protein14-3-3 protein epsilon
GeneYWHAE
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
255
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-233 Hetero tetramer :
 Evidence X-RAY 2br9 A Reference
       Region 2br9 A 1-2 disorder
       Region 2br9 A 3-232 order
       Region 2br9 A 233-233 disorder
Seq 1-234 Hetero tetramer : IID00458Complex
 Evidence X-RAY 3ubw A Reference
       Region 3ubw A 1-2 disorder
       Region 3ubw A 3-232 order
       Region 3ubw A 233-234 disorder
 Evidence X-RAY 3ual A Reference
       Region 3ual A 1-2 disorder
       Region 3ual A 3-232 order
Seq 3-232 Monomer :
 Evidence X-RAY 6eih A Reference
       Region 6eih A 3-232 order
Seqphosphorylation
    65-65 Phosphoserine
    131-131 Phosphotyrosine
    137-137 Phosphothreonine
    210-210 Phosphoserine
    232-232 Phosphothreonine
Seqacetylation
    123-123 N6-acetyllysine
    1-1 N-acetylmethionine
    50-50 N6-acetyllysine; alternate
    69-69 N6-acetyllysine
    118-118 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-1,221-226,236-255
Order 2-220,227-235
ProS 221-226
AlphaFold
Disorder 1-1,237-247,251-255
Order 2-236,248-250
Pfam Hmmer
PF00244 4-239 1.7e-155
Function
Function in SwissProt
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326).
Biological Process
See also
Diagram with PDB data
FOXO3/YWHAECrystal Structure of 14-3-3 epsilon with FOXO3a peptide
MLF1/YWHAECrystal structure of 14-3-3 epsilon with Mlf1 peptide