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YEAST:COX4

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) COX4
Protein Name(s) Cytochrome c oxidase subunit 4, mitochondrial

Cytochrome c oxidase polypeptide IV

External Links
UniProt P04037
EMBL X01418
X91489
Z72709
EF123139
Y00152
BK006941
PIR A22786
RefSeq NP_011328.1
PDB 1HR8
2ODX
PDBsum 1HR8
2ODX
ProteinModelPortal P04037
SMR P04037
BioGrid 33068
DIP DIP-2763N
IntAct P04037
MINT MINT-521387
TCDB 3.D.4.8.1
MaxQB P04037
PaxDb P04037
PeptideAtlas P04037
EnsemblFungi [example_ID YGL187C]
GeneID 852688
KEGG sce:YGL187C
CYGD YGL187c
SGD S000003155
eggNOG NOG326977
HOGENOM HOG000184129
InParanoid P04037
KO K02265
OMA ARCWECG
OrthoDB EOG7BS4NR
BioCyc MetaCyc:YGL187C-MONOMER
YEAST:YGL187C-MONOMER
Reactome REACT_189012
UniPathway UPA00705
EvolutionaryTrace P04037
NextBio 972014
PRO PR:P04037
Proteomes UP000002311
Genevestigator P04037
GO GO:0005743
GO:0005758
GO:0005751
GO:0005739
GO:0004129
GO:0008270
GO:0009060
GO:1902600
GO:0006123
Gene3D 2.60.11.10
InterPro IPR002124
IPR020893
PANTHER PTHR10122
Pfam PF01215
ProDom PD007270
PROSITE PS00848
PS51359

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0033617

mitochondrial respiratory chain complex IV assembly

PMID:22342701[1]

ECO:0000315

P

Figure 2 (B). The lack of band in lane 14 and 16 compared to the WT bands at the specific high molecular weight of 230 and 440 kDa indicates the lack of complex IV in mutant cox4.

complete
CACAO 4883

part_of

GO:0005739

mitochondrion

PMID:16823961[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24769239[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0033617

mitochondrial respiratory chain complex IV assembly

PMID:22342701[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24478450[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009060

aerobic respiration

PMID:163235[5]

ECO:0000353

physical interaction evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:17215247[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006123

mitochondrial electron transport, cytochrome c to oxygen

PMID:1331058[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005751

mitochondrial respiratory chain complex IV

PMID:1331058[7]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0004129

cytochrome-c oxidase activity

PMID:1331058[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

contributes_to

GO:0004129

cytochrome-c oxidase activity

PMID:7851399[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042776

mitochondrial ATP synthesis coupled proton transport

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000012880
WB:WBGene00000371

P

Seeded From UniProt

complete

involved_in

GO:0006123

mitochondrial electron transport, cytochrome c to oxygen

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000012880
SGD:S000003155

P

Seeded From UniProt

complete

contributes_to

GO:0004129

cytochrome-c oxidase activity

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000012880
SGD:S000003155

F

Seeded From UniProt

complete

enables

GO:0004129

cytochrome-c oxidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002124
InterPro:IPR036972

F

Seeded From UniProt

complete

part_of

GO:0005740

mitochondrial envelope

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002124
InterPro:IPR036972

C

Seeded From UniProt

complete

enables

GO:0004129

cytochrome-c oxidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.9.3.1

F

Seeded From UniProt

complete

part_of

GO:0005758

mitochondrial intermembrane space

Reactome:R-SCE-1268015

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

Reactome:R-SCE-1268019
Reactome:R-SCE-1268015
Reactome:R-SCE-1252249

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0999
UniProtKB-SubCell:SL-0168

C

Seeded From UniProt

complete

involved_in

GO:0006119

oxidative phosphorylation

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00705

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Vukotic, M et al. (2012) Rcf1 mediates cytochrome oxidase assembly and respirasome formation, revealing heterogeneity of the enzyme complex. Cell Metab. 15 336-47 PubMed GONUTS page
  2. Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  3. Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  4. Su, CH et al. (2014) The Cox3p assembly module of yeast cytochrome oxidase. Mol. Biol. Cell 25 965-76 PubMed GONUTS page
  5. Eytan, GD & Schatz, G (1975) Cytochrome c oxidase from bakers' yeast. V. Arrangement of the subunits in the isolated and membrane-bound enzyme. J. Biol. Chem. 250 767-74 PubMed GONUTS page
  6. Coyne, HJ 3rd et al. (2007) The characterization and role of zinc binding in yeast Cox4. J. Biol. Chem. 282 8926-34 PubMed GONUTS page
  7. 7.0 7.1 7.2 Taanman, JW & Capaldi, RA (1992) Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme. J. Biol. Chem. 267 22481-5 PubMed GONUTS page
  8. Geier, BM et al. (1995) Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method. Eur. J. Biochem. 227 296-302 PubMed GONUTS page
  9. 9.0 9.1 9.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page