U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

COX2 cytochrome c oxidase subunit 2 [ Saccharomyces cerevisiae S288C ]

Gene ID: 854622, updated on 6-Jul-2026
Official Symbol
COX2
Official Full Name
cytochrome c oxidase subunit 2
Primary source
SGD:S000007281
Locus tag
Q0250
See related
AllianceGenome:SGD:S000007281; FungiDB:Q0250; VEuPathDB:Q0250
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Saccharomyces cerevisiae S288C (strain: S288C, substrain: FY1679)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
OXI1; OXII
Summary
Contributes to cytochrome-c oxidase activity. Involved in mitochondrial electron transport, cytochrome c to oxygen. Located in mitochondrion. Part of respiratory chain complex IV. Orthologous to human MT-CO2 (mitochondrially encoded cytochrome c oxidase II). [provided by Alliance of Genome Resources, Jul 2025]
Try the new Gene page
Try the new Transcripts and proteins table
See COX2 in Genome Data Viewer
Sequence:
Chromosome: MT; NC_001224.1 (73758..74513)

Chromosome MT - NC_001224.1Genomic Context describing neighboring genes Neighboring gene tRNA-Asn Neighboring gene tRNA-Met Neighboring gene maturase-like protein Neighboring gene tRNA-Phe Neighboring gene tRNA-Thr

Genomic Sequence:
NC_001224.1

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Deletion of the leader peptide of the mitochondrially encoded precursor of Saccharomyces cerevisiae cytochrome c oxidase subunit II. Torello AT, et al. Genetics, 1997 Apr. PMID 9093845, Free PMC Article
  2. A novel type of + 1 frameshift suppressor: a base substitution in the anticodon stem of a yeast mitochondrial serine-tRNA causes frameshift suppression. Hüttenhofer A, et al. EMBO J, 1990 Feb. PMID 1689242, Free PMC Article
  3. Escape of DNA from mitochondria to the nucleus in Saccharomyces cerevisiae. Thorsness PE, et al. Nature, 1990 Jul 26. PMID 2165219
  4. Engineering yeast endosymbionts as a step toward the evolution of mitochondria. Mehta AP, et al. Proc Natl Acad Sci U S A, 2018 Nov 13. PMID 30373839, Free PMC Article
  5. Plasmids can stably transform yeast mitochondria lacking endogenous mtDNA. Fox TD, et al. Proc Natl Acad Sci U S A, 1988 Oct. PMID 2459701, Free PMC Article

See all (185) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The cytosol-synthesized subunit II (Cox2) precursor with the point mutation W56R is correctly processed in yeast mitochondria to rescue cytochrome oxidase.
    Title: The cytosol-synthesized subunit II (Cox2) precursor with the point mutation W56R is correctly processed in yeast mitochondria to rescue cytochrome oxidase.
  2. A single mutation in the first Cox2 transmembrane domain was identified that results in the cellular expression of a Cox2 variant with a molecular mass indicative of mitochondrial targeting sequences cleavage.
    Title: A single mutation in the first transmembrane domain of yeast COX2 enables its allotopic expression.
  3. yeast prion causes newly synthesized prohibitins to aggregate in the cytosol, and therefore reduces their levels in mitochondria, which in turn reduces the stability of Cox2 and possibly of other proteins, not investigated here in detail.
    Title: Yeast prion [PSI+] lowers the levels of mitochondrial prohibitins.
  4. Yme1 probably chaperones the folding and/or assembly of Oxa1-exported Cox2 in the absence of Mrg1 or Mgr3, since respiratory growth and cytochrome c oxidase assembly in a cox18 mgr3 double-mutant strain overexpressing OXA1 is YME1 dependent
    Title: Translocation and assembly of mitochondrially coded Saccharomyces cerevisiae cytochrome c oxidase subunit Cox2 by Oxa1 and Yme1 in the absence of Cox18.
  5. These studies implicate different surfaces on Sco1 for interaction or function with Cox17 and Cox2.
    Title: Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis.
  6. Immunoblot analysis of yeast wild-type and Cox2p mutants revealed five cytochrome oxidase complexes or subcomplexes: a, b, c, d and f.
    Title: Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast.
  7. Data show that Rsm28p is a dispensable small-subunit mitochondrial ribosomal protein with a positive role in translation of several mitochondrial mRNAs, including COX2.
    Title: Alteration of a novel dispensable mitochondrial ribosomal small-subunit protein, Rsm28p, allows translation of defective COX2 mRNAs.
  8. The C-tail domain is recognized posttranslationally by a specialized translocation apparatus after the N-tail has been translocated by Oxa1.
    Title: Translocation of mitochondrially synthesized Cox2 domains from the matrix to the intermembrane space.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables cytochrome-c oxidase activity EXP
Inferred from Experiment
more info
 PubMed 
contributes_to cytochrome-c oxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
contributes_to cytochrome-c oxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables cytochrome-c oxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in ATP synthesis coupled electron transport IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in aerobic respiration IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in electron transport chain IEA
Inferred from Electronic Annotation
more info
  
involved_in mitochondrial electron transport, cytochrome c to oxygen IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in mitochondrial electron transport, cytochrome c to oxygen IEA
Inferred from Electronic Annotation
more info
  
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in mitochondrial inner membrane EXP
Inferred from Experiment
more info
 PubMed 
located_in mitochondrial inner membrane IEA
Inferred from Electronic Annotation
more info
  
located_in mitochondrial inner membrane TAS
Traceable Author Statement
more info
  
is_active_in mitochondrial membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in mitochondrion HDA PubMed 
part_of respiratory chain complex IV IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of respiratory chain complex IV IDA
Inferred from Direct Assay
more info
 PubMed 
part_of respiratory chain complex IV IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
cytochrome c oxidase subunit 2
NP_009326.1
  • Subunit II of cytochrome c oxidase (Complex IV); Complex IV is the terminal member of the mitochondrial inner membrane electron transport chain; one of three mitochondrially-encoded subunits

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001224.1 Reference assembly

    Range
    73758..74513
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_009326.1 cytochrome c oxidase subunit 2

    See identical proteins and their annotated locations for NP_009326.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    A0A0A7NYF9, P00410
    UniProtKB/TrEMBL
    I6QCX2
    Conserved Domains (1) summary
    MTH00154
    Location:24 → 249
    COX2; cytochrome c oxidase subunit II; Provisional
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00410.1

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases
Research Materials
Tools