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Q14061 (COX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase copper chaperone
Gene names
Name:COX17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length63 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with COA1. Interacts with the chaperone CHCHD4; this is important for correct folding and the formation of disulfide bonds that stabilize the structure. Ref.7

Subcellular location

Mitochondrion intermembrane space By similarity.

Tissue specificity

Ubiquitous. Ref.2

Sequence similarities

Belongs to the COX17 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6363Cytochrome c oxidase copper chaperone
PRO_0000213538

Regions

Compositional bias2 – 2726Ala/Pro-rich

Sites

Metal binding231Copper
Metal binding241Copper

Amino acid modifications

Disulfide bond26 ↔ 55 Ref.8 Ref.9 Ref.10
Disulfide bond36 ↔ 45 Ref.8 Ref.9 Ref.10

Secondary structure

......... 63
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14061 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E97090F939E78276

FASTA636,915
        10         20         30         40         50         60 
MPGLVDSNPA PPESQEKKPL KPCCACPETK KARDACIIEK GEEHCGHLIE AHKECMRALG 


FKI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"A structural-dynamical characterization of human Cox17."
Banci L., Bertini I., Ciofi-Baffoni S., Janicka A., Martinelli M., Kozlowski H., Palumaa P.
J. Biol. Chem. 283:7912-7920(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN APO AND COPPER-BOUND FORMS, DISULFIDE BONDS.
[9]"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.
[10]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2993.1.
PIRT09533.
RefSeqNP_005685.1. NM_005694.1.
UniGeneHs.534383.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0YNMR-B1-63[»]
2LGQNMR-A1-63[»]
2RN9NMR-A1-63[»]
2RNBNMR-A1-63[»]
DisProtDP00543.
ProteinModelPortalQ14061.
SMRQ14061. Positions 1-63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115374. 14 interactions.
DIPDIP-46087N.
IntActQ14061. 12 interactions.
MINTMINT-1373812.
STRING9606.ENSP00000261070.

PTM databases

PhosphoSiteQ14061.

Polymorphism databases

DMDM2493873.

Proteomic databases

MaxQBQ14061.
PaxDbQ14061.
PRIDEQ14061.

Protocols and materials databases

DNASU10063.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261070; ENSP00000261070; ENSG00000138495.
ENST00000468918; ENSP00000417805; ENSG00000138495.
ENST00000497116; ENSP00000417923; ENSG00000138495.
GeneID10063.
KEGGhsa:10063.
UCSCuc003ecz.1. human.

Organism-specific databases

CTD10063.
GeneCardsGC03M119373.
HGNCHGNC:2264. COX17.
HPAHPA042226.
HPA048158.
MIM604813. gene.
neXtProtNX_Q14061.
PharmGKBPA26780.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136703.
HOGENOMHOG000195037.
HOVERGENHBG054258.
InParanoidQ14061.
KOK02260.
PhylomeDBQ14061.
TreeFamTF105074.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ14061.
CleanExHS_COX17.
GenevestigatorQ14061.

Family and domain databases

Gene3D1.10.810.10. 1 hit.
InterProIPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]
PANTHERPTHR16719. PTHR16719. 1 hit.
PfamPF05051. COX17. 1 hit.
[Graphical view]
ProDomPD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47072. SSF47072. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14061.
GeneWikiCOX17.
GenomeRNAi10063.
NextBio38033.
PROQ14061.
SOURCESearch...

Entry information

Entry nameCOX17_HUMAN
AccessionPrimary (citable) accession number: Q14061
Secondary accession number(s): B2R5D2, D3DN84, Q3MHD6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM