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Q14061

- COX17_HUMAN

UniProt

Q14061 - COX17_HUMAN

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
  1. 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

    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: UniProtKB-SubCell

    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.
    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 – 243
    Helixi27 – 3913
    Helixi42 – 443
    Helixi49 – 6214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    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: October 1, 2014
    This is version 120 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