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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Protein S100-B
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| http://www.biopax.org/relea... |
S100B_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
S-100 protein beta chain,
S-100 protein subunit beta,
S100 calcium-binding protein B
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| http://www.biopax.org/relea... |
FUNCTION: 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 (By similarity). SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. The S100B dimer binds two molecules of STK38. Interacts with AGER (By similarity). The S100B dimer interacts with two molecules of CAPZA1. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues. MISCELLANEOUS: In addition to metal-ion binding, this protein is involved with the regulation of protein phosphorylation in brain tissue. SIMILARITY: Belongs to the S-101 family. SIMILARITY: Contains 2 EF-hand domains. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/S100BID42195ch21q22.html"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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