Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Copper
Metal bindingi24 – 241Copper

GO - Molecular functioni

  • copper chaperone activity Source: InterPro
  • copper ion binding Source: ProtInc

GO - Biological processi

  • brain development Source: Ensembl
  • copper ion transport Source: ProtInc
  • generation of precursor metabolites and energy Source: ProtInc
  • heart development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118595. 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
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2264. COX17.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • mitochondrial intermembrane space Source: UniProtKB-SubCell
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26780.

Polymorphism and mutation databases

BioMutaiCOX17.
DMDMi2493873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6363Cytochrome c oxidase copper chaperonePRO_0000213538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 55
Disulfide bondi36 ↔ 45

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ14061.
PaxDbiQ14061.
PRIDEiQ14061.

PTM databases

PhosphoSiteiQ14061.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ14061.
CleanExiHS_COX17.
ExpressionAtlasiQ14061. baseline.
GenevestigatoriQ14061.

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. 14 interactions.
DIPiDIP-46087N.
IntActiQ14061. 12 interactions.
MINTiMINT-1373812.
STRINGi9606.ENSP00000261070.

Structurei

Secondary structure

1
63
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Helixi27 – 3913Combined sources
Helixi42 – 443Combined sources
Helixi49 – 6214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0YNMR-B1-63[»]
2LGQNMR-A1-63[»]
2RN9NMR-A1-63[»]
2RNBNMR-A1-63[»]
DisProtiDP00543.
ProteinModelPortaliQ14061.
SMRiQ14061. Positions 1-63.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14061.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 2726Ala/Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the COX17 family.Curated

Phylogenomic databases

eggNOGiNOG136703.
GeneTreeiENSGT00390000002329.
HOGENOMiHOG000195037.
HOVERGENiHBG054258.
InParanoidiQ14061.
KOiK02260.
PhylomeDBiQ14061.
TreeFamiTF105074.

Family and domain databases

Gene3Di1.10.810.10. 1 hit.
InterProiIPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]
PANTHERiPTHR16719. PTHR16719. 1 hit.
PfamiPF05051. COX17. 1 hit.
[Graphical view]
ProDomiPD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47072. SSF47072. 1 hit.

Sequencei

Sequence statusi: Complete.

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.1. human.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0YNMR-B1-63[»]
2LGQNMR-A1-63[»]
2RN9NMR-A1-63[»]
2RNBNMR-A1-63[»]
DisProtiDP00543.
ProteinModelPortaliQ14061.
SMRiQ14061. Positions 1-63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115374. 14 interactions.
DIPiDIP-46087N.
IntActiQ14061. 12 interactions.
MINTiMINT-1373812.
STRINGi9606.ENSP00000261070.

PTM databases

PhosphoSiteiQ14061.

Polymorphism and mutation databases

BioMutaiCOX17.
DMDMi2493873.

Proteomic databases

MaxQBiQ14061.
PaxDbiQ14061.
PRIDEiQ14061.

Protocols and materials databases

DNASUi10063.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261070; ENSP00000261070; ENSG00000138495.
ENST00000468918; ENSP00000417805; ENSG00000138495.
ENST00000497116; ENSP00000417923; ENSG00000138495.
GeneIDi10063.
KEGGihsa:10063.
UCSCiuc003ecz.1. human.

Organism-specific databases

CTDi10063.
GeneCardsiGC03M119373.
HGNCiHGNC:2264. COX17.
HPAiHPA042226.
HPA048158.
MIMi604813. gene.
neXtProtiNX_Q14061.
PharmGKBiPA26780.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG136703.
GeneTreeiENSGT00390000002329.
HOGENOMiHOG000195037.
HOVERGENiHBG054258.
InParanoidiQ14061.
KOiK02260.
PhylomeDBiQ14061.
TreeFamiTF105074.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiQ14061.
GeneWikiiCOX17.
GenomeRNAii10063.
NextBioi38033.
PROiQ14061.
SOURCEiSearch...

Gene expression databases

BgeeiQ14061.
CleanExiHS_COX17.
ExpressionAtlasiQ14061. baseline.
GenevestigatoriQ14061.

Family and domain databases

Gene3Di1.10.810.10. 1 hit.
InterProiIPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]
PANTHERiPTHR16719. PTHR16719. 1 hit.
PfamiPF05051. COX17. 1 hit.
[Graphical view]
ProDomiPD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47072. SSF47072. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment."
    Amaravadi R., Glerum D.M., Tzagoloff A.
    Hum. Genet. 99:329-333(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization and localization of human COX17, a gene involved in mitochondrial copper transport."
    Punter F.A., Adams D.L., Glerum D.M.
    Hum. Genet. 107:69-74(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase."
    Szklarczyk R., Wanschers B.F., Cuypers T.D., Esseling J.J., Riemersma M., van den Brand M.A., Gloerich J., Lasonder E., van den Heuvel L.P., Nijtmans L.G., Huynen M.A.
    Genome Biol. 13:RESEARCH0012.1-RESEARCH0012.14(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COA1.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: STRUCTURE BY NMR IN APO AND COPPER-BOUND FORMS, DISULFIDE BONDS.
  10. "Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import."
    Banci L., Bertini I., Cefaro C., Cenacchi L., Ciofi-Baffoni S., Felli I.C., Gallo A., Gonnelli L., Luchinat E., Sideris D., Tokatlidis K.
    Proc. Natl. Acad. Sci. U.S.A. 107:20190-20195(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH CHCHD4, DISULFIDE BONDS.
  11. "Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective."
    Banci L., Bertini I., Cefaro C., Ciofi-Baffoni S., Gallo A.
    J. Biol. Chem. 286:34382-34390(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, COPPER-BINDING, DISULFIDE BONDS.

Entry informationi

Entry nameiCOX17_HUMAN
AccessioniPrimary (citable) accession number: Q14061
Secondary accession number(s): B2R5D2, D3DN84, Q3MHD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 126 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.