Cytochrome c structure
P99999
CYC_HUMAN
CYCS

Cytochrome c

Homo sapiensTaxon: 9606

3D-structureAcetylationApoptosisDirect protein sequencingDisease variantElectron transportHemeIronMetal-bindingMitochondrionPhosphoproteinProteomics identification+3
Longueur de Séquence

105

acides aminés

Poids Moléculaire

11.7 kDa

théorique

Structures Expérimentales

13

entrées PDB

Maladies Associées

1

enregistrées

Fonction

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 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

Maladies Associées

Thrombocytopenia 4

A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.

Séquence d'Acides Aminés

MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIW
GEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE

Format FASTA · 105 acides aminés · masse 11.7 kDa

Structures Expérimentales

13 entrées PDB
1J3S2N3Y2N9I2N9J3NWV3ZCF3ZOO5EXQ5O105TY36DUJ6ECJ6XNK

Modifications Post-Traductionnelles

  • Binds 1 heme c group covalently per subunit
  • Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration