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Protein

Cytochrome c oxidase copper chaperone

Gene

COX17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi23CopperCombined sources2 Publications1
Metal bindingi24CopperCombined sources2 Publications1

GO - Molecular functioni

  • copper chaperone activity Source: CAFA
  • copper ion binding Source: ProtInc
  • cuprous ion binding Source: CAFA

GO - Biological processi

  • brain development Source: Ensembl
  • copper ion transport Source: GO_Central
  • generation of precursor metabolites and energy Source: ProtInc
  • heart development Source: Ensembl
  • mitochondrial respiratory chain complex IV assembly Source: CAFA
  • positive regulation of cell proliferation Source: CAFA
  • positive regulation of cytochrome-c oxidase activity Source: CAFA

Keywordsi

Molecular functionChaperone
LigandCopper, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1268020. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase copper chaperone
Gene namesi
Name:COX17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000138495.6.
HGNCiHGNC:2264. COX17.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi10063.
OpenTargetsiENSG00000138495.
PharmGKBiPA26780.

Polymorphism and mutation databases

BioMutaiCOX17.
DMDMi2493873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002135382 – 63Cytochrome c oxidase copper chaperoneAdd BLAST62

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Disulfide bondi26 ↔ 55PROSITE-ProRule annotationCombined sources2 Publications
Disulfide bondi36 ↔ 45PROSITE-ProRule annotationCombined sources2 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ14061.
MaxQBiQ14061.
PaxDbiQ14061.
PeptideAtlasiQ14061.
PRIDEiQ14061.

PTM databases

iPTMnetiQ14061.
PhosphoSitePlusiQ14061.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000138495.
CleanExiHS_COX17.
ExpressionAtlasiQ14061. baseline and differential.
GenevisibleiQ14061. HS.

Organism-specific databases

HPAiHPA042226.
HPA048158.

Interactioni

Subunit structurei

Interacts with COA1. Interacts with the chaperone CHCHD4; this is important for correct folding and the formation of disulfide bonds that stabilize the structure.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KATNAL1Q9BW624EBI-711311,EBI-743591

Protein-protein interaction databases

BioGridi115374. 27 interactors.
DIPiDIP-46087N.
IntActiQ14061. 13 interactors.
MINTiMINT-1373812.
STRINGi9606.ENSP00000261070.

Structurei

Secondary structure

163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 24Combined sources3
Helixi27 – 39Combined sources13
Helixi42 – 44Combined sources3
Helixi49 – 62Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L0YNMR-B1-63[»]
2LGQNMR-A1-63[»]
2RN9NMR-A1-63[»]
2RNBNMR-A1-63[»]
DisProtiDP00543.
ProteinModelPortaliQ14061.
SMRiQ14061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 63CHCHPROSITE-ProRule annotationAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi26 – 36Cx9C motif 1PROSITE-ProRule annotationAdd BLAST11
Motifi45 – 55Cx9C motif 2PROSITE-ProRule annotationAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 27Ala/Pro-richAdd BLAST26

Sequence similaritiesi

Belongs to the COX17 family.Curated

Phylogenomic databases

eggNOGiKOG3496. Eukaryota.
ENOG410XVYQ. LUCA.
GeneTreeiENSGT00390000002329.
HOGENOMiHOG000195037.
HOVERGENiHBG054258.
InParanoidiQ14061.
KOiK02260.
PhylomeDBiQ14061.
TreeFamiTF105074.

Family and domain databases

InterProiView protein in InterPro
IPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
PANTHERiPTHR16719. PTHR16719. 1 hit.
PfamiView protein in Pfam
PF05051. COX17. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
SUPFAMiSSF47072. SSF47072. 1 hit.
PROSITEiView protein in PROSITE
PS51808. CHCH. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGLVDSNPA PPESQEKKPL KPCCACPETK KARDACIIEK GEEHCGHLIE
60
AHKECMRALG FKI
Length:63
Mass (Da):6,915
Last modified:January 23, 2007 - v2
Checksum:iE97090F939E78276
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77701 mRNA. Translation: AAA98114.1.
AF269244, AF269243 Genomic DNA. Translation: AAF82569.1.
AK312143 mRNA. Translation: BAG35079.1.
CH471052 Genomic DNA. Translation: EAW79545.1.
CH471052 Genomic DNA. Translation: EAW79547.1.
CH471052 Genomic DNA. Translation: EAW79548.1.
CH471052 Genomic DNA. Translation: EAW79550.1.
CH471052 Genomic DNA. Translation: EAW79551.1.
BC010933 mRNA. Translation: AAH10933.1.
BC105280 mRNA. Translation: AAI05281.1.
BC108317 mRNA. Translation: AAI08318.1.
CCDSiCCDS2993.1.
PIRiT09533.
RefSeqiNP_005685.1. NM_005694.1.
UniGeneiHs.534383.

Genome annotation databases

EnsembliENST00000261070; ENSP00000261070; ENSG00000138495.
ENST00000468918; ENSP00000417805; ENSG00000138495.
ENST00000497116; ENSP00000417923; ENSG00000138495.
GeneIDi10063.
KEGGihsa:10063.
UCSCiuc003ecz.2. human.

Similar proteinsi

Entry informationi

Entry nameiCOX17_HUMAN
AccessioniPrimary (citable) accession number: Q14061
Secondary accession number(s): B2R5D2, D3DN84, Q3MHD6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 145 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families