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Q14061

- COX17_HUMAN

UniProt

Q14061 - COX17_HUMAN

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Protein

Cytochrome c oxidase copper chaperone

Gene

COX17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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

  1. copper chaperone activity Source: InterPro
  2. copper ion binding Source: ProtInc

GO - Biological processi

  1. brain development Source: Ensembl
  2. copper ion transport Source: ProtInc
  3. generation of precursor metabolites and energy Source: ProtInc
  4. 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: Chromosome 3

Organism-specific databases

HGNCiHGNC:2264. COX17.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. mitochondrial intermembrane space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26780.

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

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.

Polymorphism databases

DMDMi2493873.

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 .
CCDSi CCDS2993.1.
PIRi T09533.
RefSeqi NP_005685.1. NM_005694.1.
UniGenei Hs.534383.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L0Y NMR - B 1-63 [» ]
2LGQ NMR - A 1-63 [» ]
2RN9 NMR - A 1-63 [» ]
2RNB NMR - A 1-63 [» ]
DisProti DP00543.
ProteinModelPortali Q14061.
SMRi Q14061. Positions 1-63.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115374. 14 interactions.
DIPi DIP-46087N.
IntActi Q14061. 12 interactions.
MINTi MINT-1373812.
STRINGi 9606.ENSP00000261070.

PTM databases

PhosphoSitei Q14061.

Polymorphism databases

DMDMi 2493873.

Proteomic databases

MaxQBi Q14061.
PaxDbi Q14061.
PRIDEi Q14061.

Protocols and materials databases

DNASUi 10063.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261070 ; ENSP00000261070 ; ENSG00000138495 .
ENST00000468918 ; ENSP00000417805 ; ENSG00000138495 .
ENST00000497116 ; ENSP00000417923 ; ENSG00000138495 .
GeneIDi 10063.
KEGGi hsa:10063.
UCSCi uc003ecz.1. human.

Organism-specific databases

CTDi 10063.
GeneCardsi GC03M119373.
HGNCi HGNC:2264. COX17.
HPAi HPA042226.
HPA048158.
MIMi 604813. gene.
neXtProti NX_Q14061.
PharmGKBi PA26780.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG136703.
GeneTreei ENSGT00390000002329.
HOGENOMi HOG000195037.
HOVERGENi HBG054258.
InParanoidi Q14061.
KOi K02260.
PhylomeDBi Q14061.
TreeFami TF105074.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTracei Q14061.
GeneWikii COX17.
GenomeRNAii 10063.
NextBioi 38033.
PROi Q14061.
SOURCEi Search...

Gene expression databases

Bgeei Q14061.
CleanExi HS_COX17.
ExpressionAtlasi Q14061. baseline.
Genevestigatori Q14061.

Family and domain databases

Gene3Di 1.10.810.10. 1 hit.
InterProi IPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view ]
PANTHERi PTHR16719. PTHR16719. 1 hit.
Pfami PF05051. COX17. 1 hit.
[Graphical view ]
ProDomi PD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF47072. SSF47072. 1 hit.
ProtoNeti Search...

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. 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.

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: November 26, 2014
This is version 122 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