S100A9
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- autophagy [IDA]
- cell-cell signaling [TAS]
- chemokine production [TAS]
- cytokine production [TAS]
- defense response to bacterium [TAS]
- defense response to fungus [TAS]
- inflammatory response [TAS]
- leukocyte migration involved in inflammatory response [IDA]
- neutrophil aggregation [IDA]
- neutrophil chemotaxis [IDA]
- positive regulation of NF-kappaB transcription factor activity [TAS]
- positive regulation of cell growth [TAS]
- positive regulation of inflammatory response [IDA]
- positive regulation of intrinsic apoptotic signaling pathway [IDA]
- regulation of cytoskeleton organization [TAS]
- sequestering of zinc ion [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
S100A9
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- autophagy [IDA]
- cell-cell signaling [TAS]
- chemokine production [TAS]
- cytokine production [TAS]
- defense response to bacterium [TAS]
- defense response to fungus [TAS]
- inflammatory response [TAS]
- leukocyte migration involved in inflammatory response [IDA]
- neutrophil aggregation [IDA]
- neutrophil chemotaxis [IDA]
- positive regulation of NF-kappaB transcription factor activity [TAS]
- positive regulation of cell growth [TAS]
- positive regulation of inflammatory response [IDA]
- positive regulation of intrinsic apoptotic signaling pathway [IDA]
- regulation of cytoskeleton organization [TAS]
- sequestering of zinc ion [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process.
Human MRP14 (hMRP14) is a Ca(2+)-binding protein from the S100 family of proteins. This protein is co-expressed with human MRP8 (hMRP8), a homologue protein in myeloid cells, and plays an indispensable role in Ca(2+)-dependent functions during inflammation. This role includes the activation of Mac-1, the beta(2) integrin which is involved in neutrophil adhesion to endothelial cells. The crystal structure of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| S100A9 S100A9 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - |
Curated By
- BioGRID