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IID50019
UniprotP04631
ProteinProtein S100-B
GeneS100b
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
92
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-92 Homo dimer :
 Evidence NMR 1xyd B Reference
       Region 1xyd B 1-92 order
 Evidence NMR 1xyd A Reference
       Region 1xyd A 1-92 order
 Evidence NMR 1sym B Reference
       Region 1sym B 1-92 order
       Region 1sym B 92-92 high_rmsd
 Evidence NMR 1sym A Reference
       Region 1sym A 1-92 order
       Region 1sym A 92-92 high_rmsd
 Evidence NMR 1qlk B Reference
       Region 1qlk B 1-92 order
 Evidence NMR 1qlk A Reference
       Region 1qlk A 1-92 order
 Evidence NMR 2k7o B Reference
       Region 2k7o B 2-92 order
       Region 2k7o B 90-92 high_rmsd
 Evidence NMR 2k7o A Reference
       Region 2k7o A 2-92 order
       Region 2k7o A 90-92 high_rmsd
 Evidence NMR 1b4c B Reference
       Region 1b4c B 1-92 order
 Evidence NMR 1b4c A Reference
       Region 1b4c A 1-92 order
Seq 1-92 Hetero tetramer : IID00015Complex
 Evidence NMR 1dt7 B Reference
       Region 1dt7 B 1-92 order
       Region 1dt7 B 22-23 high_rmsd
       Region 1dt7 B 49-50 high_rmsd
       Region 1dt7 B 91-92 high_rmsd
 Evidence NMR 1dt7 A Reference
       Region 1dt7 A 1-92 order
       Region 1dt7 A 22-24 high_rmsd
       Region 1dt7 A 49-51 high_rmsd
       Region 1dt7 A 91-92 high_rmsd
Seq 1-92 Hetero tetramer : IID00122Complex
 Evidence NMR 1mwn B Reference
       Region 1mwn B 1-1 disorder
       Region 1mwn B 2-92 order
       Region 1mwn B 23-23 high_rmsd
       Region 1mwn B 90-92 high_rmsd
 Evidence NMR 1mwn A Reference
       Region 1mwn A 1-1 disorder
       Region 1mwn A 2-92 order
       Region 1mwn A 23-23 high_rmsd
       Region 1mwn A 90-92 high_rmsd
Seqacetylation
    2-2 N-acetylserine
 
Prediction
NeProc
Order 1-92
AlphaFold
Disorder 91-92
Order 1-90
Pfam Hmmer
PF01023 4-47 6.7e-24
PF00036 53-81 8.7e-05
SEG 27-42
Function
Function in SwissProt
Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Biological Process
Diagram with PDB data
s100b/s100bCa2+-S100B, refined with RDCs
See also
Diagram with PDB data
TP53/S100BSOLUTION STRUCTURE OF THE C-TERMINAL NEGATIVE REGULATORY DOMAIN OF P53 IN A COMPLEX WITH CA2+-BOUND S100B(BB)