Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein S100-A9  

UniProtKB / Swiss-Prot ID :  S10A9_RAT

Gene Name (Synonyms) : 
S100a9, Mrp14  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  Secreted (By similarity). Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein (By similarity). Note=Associates with tubulin filaments in activated monocytes. Targeted to the cell surface upon calcium influx. Released from blood 

Protein Function :  Calcium-binding protein. Has antimicrobial activity towards bacteria and fungi. Important for resistance to invasion by pathogenic bacteria. Up-regulates transcription of genes that are under the control of NF-kappa-B. Plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). Promotes tubulin polymerization when unphosphorylated. Promotes phagocyte migration and infiltration of granulocytes at sites of wounding. Plays a role as pro- inflammatory mediator in acute and chronic inflammation and up- regulates the release of IL8 and cell-surface expression of ICAM1. Extracellular calprotectin binds to target cells and promotes apoptosis. Antimicrobial and proapoptotic activity is inhibited by zinc ions (By similarity). Stimulates proliferation of fibroblast cells as both a monomer and a homodimer. May act as a mitogen during chronic inflammation. 

Protein Sequence MAAKTGSQLERSISTIINVFHQYSRKYGHPDTLNKAEFKEMVNKDLPNFLKREKRNENLLRDIMEDLDTN...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAKTG
---CCCCCC
20.05UniProtKB
Link-
107Pros-methylhistidine.HDHSHGKGC
CCCCCCCCC
38.27UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Identification of posttranslational modifications and cDNA sequencingerrors in the rat S100 proteins MRP8 and 14 using electrosprayionization mass spectrometry.";
Raftery M.J., Geczy C.L.;
Anal. Biochem. 258:285-292(1998).
Cited for: PROTEIN SEQUENCE OF 2-57; 62-65 AND 72-113, MASS SPECTROMETRY,ACETYLATION AT ALA-2, AND METHYLATION AT HIS-107.
Methylation
ReferencePubMed
"Identification of posttranslational modifications and cDNA sequencingerrors in the rat S100 proteins MRP8 and 14 using electrosprayionization mass spectrometry.";
Raftery M.J., Geczy C.L.;
Anal. Biochem. 258:285-292(1998).
Cited for: PROTEIN SEQUENCE OF 2-57; 62-65 AND 72-113, MASS SPECTROMETRY,ACETYLATION AT ALA-2, AND METHYLATION AT HIS-107.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures