PET191 protein (Saccharomyces cerevisiae) - STRING interaction network
"PET191" - Protein required for assembly of cytochrome c oxidase in Saccharomyces cerevisiae
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Gene Fusion
PET191Protein required for assembly of cytochrome c oxidase; exists as an oligomer that is integral to the mitochondrial inner membrane and faces the intermembrane space; contains a twin Cx9C motif; Involved in the assembly of cytochrome c oxidase (108 aa)    
Predicted Functional Partners:
Protein required for cytochrome c oxidase assembly, located in the cytosol and mitochondrial intermembrane space; putative copper metallochaperone that delivers copper to cytochrome c oxidase; contains twin cysteine-x9-cysteine motifs; Required for the assembly of mitochondrial cytochrome c oxidase (98 aa)
Protein required for delivery of copper to Cox1p; mitochondrial inner membrane protein; association with mitochondrial ribosomes suggests that copper delivery may occur during translation of Cox1p; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I (300 aa)
Protein of the mitochondrial intermembrane space with a role in respiratory chain complex assembly or maintenance; contains twin Cx9C motifs that can form coiled coil-helix-coiled-coil helix fold; Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. May be involved in copper trafficking and distribution to mitochondrial COX and SOD1 (109 aa)
Mitochondrial intermembrane space protein that functions in mitochondrial copper homeostasis, essential for functional cytochrome oxidase expression; homologous to Cox17p; contains twin cysteine-x9-cysteine motifs; Required for the assembly of cytochrome c oxidase (151 aa)
Copper-binding protein of the mitochondrial inner membrane, required for cytochrome c oxidase activity and respiration; may function to deliver copper to cytochrome c oxidase; has similarity to thioredoxins; Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX (295 aa)
Heme A-farnesyltransferase, catalyzes the first step in the conversion of protoheme to the heme A prosthetic group required for cytochrome c oxidase activity; human ortholog is associated with mitochondrial disorders; Converts protoheme IX and farnesyl diphosphate to heme O (462 aa)
Copper metallochaperone that transfers copper to Sco1p and Cox11p for eventual delivery to cytochrome c oxidase; contains twin cysteine-x9-cysteine motifs; Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX (69 aa)
Mitochondrial inner membrane insertase, mediates the insertion of both mitochondrial- and nuclear-encoded proteins from the matrix into the inner membrane, interacts with mitochondrial ribosomes; conserved from bacteria to animals; Mitochondrial inner membrane insertase that mediates the insertion of both mitochondrion-encoded precursors and nuclear- encoded proteins from the matrix into the inner membrane. Links mitoribosomes with the inner membrane (PubMed-22904327). Forms pores capable of accommodating translocating protein segments (PubMed-22829595). Essential for the activity and [...] (402 aa)
Subunit VIb of cytochrome c oxidase, which is the terminal member of the mitochondrial inner membrane electron transport chain; required for assembly of cytochrome c oxidase but not required for activity after assembly; phosphorylated; This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. This protein may be one of the heme-binding subunits of the oxidase (83 aa)
Protein required for the hydroxylation of heme O to form heme A, which is an essential prosthetic group for cytochrome c oxidase; Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin and ferredoxin reductase (486 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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