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IID00038
UniprotP31946
Protein14-3-3 protein beta/alpha
GeneYWHAB
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
246
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-246 Homo dimer :
 Evidence X-RAY 4dnk B Reference
       Region 4dnk B 1-234 order
       Region 4dnk B 235-246 disorder
 Evidence X-RAY 4dnk A Reference
       Region 4dnk A 1-1 disorder
       Region 4dnk A 2-233 order
       Region 4dnk A 234-246 disorder
 Evidence X-RAY 2bq0 B Reference
       Region 2bq0 B 2-2 disorder
       Region 2bq0 B 3-233 order
       Region 2bq0 B 234-239 disorder
 Evidence X-RAY 2bq0 A Reference
       Region 2bq0 A 2-2 disorder
       Region 2bq0 A 3-232 order
       Region 2bq0 A 233-239 disorder
Seq 1-246 Hetero tetramer : IID00013Complex
 Evidence X-RAY 5n10 B Reference
       Region 5n10 B 1-233 order
       Region 5n10 B 234-246 disorder
 Evidence X-RAY 5n10 A Reference
       Region 5n10 A 1-2 disorder
       Region 5n10 A 3-233 order
       Region 5n10 A 234-246 disorder
Seq 2-239 Hetero tetramer : Q51451
 Evidence X-RAY 2c23 A Reference
       Region 2c23 A 2-2 disorder
       Region 2c23 A 3-70 order
       Region 2c23 A 71-75 disorder
       Region 2c23 A 76-232 order
       Region 2c23 A 233-239 disorder
Seqphosphorylation
    2-2 Phosphothreonine
    60-60 Phosphoserine
    186-186 Phosphoserine
    232-232 Phosphoserine
Seqacetylation
    1-1 N-acetylmethionine
    1-1 N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate
    2-2 N-acetylthreonine; in 14-3-3 protein beta/alpha
    5-5 N6-acetyllysine
    51-51 N6-acetyllysine; alternate
    70-70 N6-acetyllysine
    117-117 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-4,235-246
Order 5-234
ProS 235-246
AlphaFold
Disorder 1-1,236-246
Order 2-235
Pfam Hmmer
PF00244 5-238 1.9e-149
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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13.
Biological Process
See also
Diagram with PDB data
ESR1/SFN14-3-3 protein interaction with Estrogen Receptor Alpha provides a novel drug target interface
CFTR/YWHAZCrystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768