MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint bruey-2000-1 Hsp27 negatively regulates cell death by interacting with cytochrome c. in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Bruey JM., Ducasse C., Bonniaud P., Ravagnan L., Susin SA., Diaz-Latoud C., Gurbuxani S., Arrigo AP., Kroemer G., Solary E., Garrido C. Virus - Publications including interactions involving viral proteins Nat. Cell Biol. (1465-7392) 2000 cyc_pantr Cytochrome c CYCS CYC protein protein pantr Pan troglodytes (Chimpanzee) Chimpanzee MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain mint Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases hspb1_human Heat shock protein beta-1 HSPB1 HSP27 HSP28 Heat shock 27 kDa protein Stress-responsive protein 27 Estrogen-regulated 24 kDa protein 28 kDa heat shock protein protein protein human Homo sapiens Human MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK 1B4DC44A6F6606D5 hspb1-cycs 6000 cyc_pantr 6001 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 hspb1_human 6002 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 physical association physical association false false false Mutation studies showed that, besides amino acids 51-88, even cys137 is necessary for cytochrome c binding. mint