Q14061 · COX17_HUMAN
- ProteinCytochrome c oxidase copper chaperone
- GeneCOX17
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial intermembrane space | |
Molecular Function | copper chaperone activity | |
Molecular Function | copper ion binding | |
Molecular Function | cuprous ion binding | |
Molecular Function | enzyme activator activity | |
Biological Process | copper ion transport | |
Biological Process | generation of precursor metabolites and energy | |
Biological Process | mitochondrial cytochrome c oxidase assembly | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of cytochrome-c oxidase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c oxidase copper chaperone
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14061
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 88 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue (large scale data), modified residue, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000213538 | 2-63 | UniProt | Cytochrome c oxidase copper chaperone | |||
Sequence: PGLVDSNPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 14 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 18 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Disulfide bond | 26↔55 | UniProt | |||||
Sequence: CPETKKARDACIIEKGEEHCGHLIEAHKEC | |||||||
Modified residue | 30 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Disulfide bond | 36↔45 | UniProt | |||||
Sequence: CIIEKGEEHC |
Post-translational modification
Acetylation by KAT8 promotes assembly of the mitochondrial respiratory chain complex IV (CIV).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with COA1. Interacts with the chaperone CHCHD4; this is important for correct folding and the formation of disulfide bonds that stabilize the structure.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14061 | CHCHD4 Q8N4Q1-1 | 2 | EBI-711311, EBI-15755238 | |
BINARY | Q14061 | KATNAL1 Q9BW62 | 4 | EBI-711311, EBI-743591 | |
BINARY | Q14061 | KRTAP10-8 P60410 | 3 | EBI-711311, EBI-10171774 | |
BINARY | Q14061 | SCO1 O75880 | 3 | EBI-711311, EBI-6656171 | |
BINARY | Q14061 | SPRED1 Q7Z699 | 3 | EBI-711311, EBI-5235340 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MPGLVDSNPAPPESQEKKPL | ||||||
Domain | 23-63 | CHCH | ||||
Sequence: CCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI | ||||||
Motif | 26-36 | Cx9C motif 1 | ||||
Sequence: CPETKKARDAC | ||||||
Motif | 45-55 | Cx9C motif 2 | ||||
Sequence: CGHLIEAHKEC |
Sequence similarities
Belongs to the COX17 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length63
- Mass (Da)6,915
- Last updated2007-01-23 v2
- ChecksumE97090F939E78276
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L77701 EMBL· GenBank· DDBJ | AAA98114.1 EMBL· GenBank· DDBJ | mRNA | ||
AF269244 EMBL· GenBank· DDBJ | AAF82569.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF269243 EMBL· GenBank· DDBJ | AAF82569.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK312143 EMBL· GenBank· DDBJ | BAG35079.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79545.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79547.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79550.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW79551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010933 EMBL· GenBank· DDBJ | AAH10933.1 EMBL· GenBank· DDBJ | mRNA | ||
BC105280 EMBL· GenBank· DDBJ | AAI05281.1 EMBL· GenBank· DDBJ | mRNA | ||
BC108317 EMBL· GenBank· DDBJ | AAI08318.1 EMBL· GenBank· DDBJ | mRNA |