Q14061 (COX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase copper chaperone

Gene names

Name:

COX17

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	63 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	Copper Metal-binding
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from electronic annotation. Source: Compara copper ion transport Traceable author statement Ref.1. Source: ProtInc generation of precursor metabolites and energy Traceable author statement Ref.1. Source: ProtInc heart development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper chaperone activity Inferred from electronic annotation. Source: InterPro copper ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 63

63

Cytochrome c oxidase copper chaperone

PRO_0000213538

Regions

Compositional bias

2 – 27

26

Ala/Pro-rich

Sites

Metal binding

23

1

Copper

Metal binding

24

1

Copper

Amino acid modifications

Disulfide bond

26 ↔ 55

Ref.8 Ref.9 Ref.10

Disulfide bond

36 ↔ 45

Ref.8 Ref.9 Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

63

Helix Strand Turn

Details...

Beta strand

22 – 24

3

Helix

27 – 39

13

Helix

42 – 44

3

Helix

46 – 57

12

Turn

58 – 60

3

Sequences

	Sequence		Length	Mass (Da)
	Q14061 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E97090F939E78276	FASTA	63	6,915
	10 20 30 40 50 60 MPGLVDSNPA PPESQEKKPL KPCCACPETK KARDACIIEK GEEHCGHLIE AHKECMRALG FKI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00218144.

PIR

T09533.

RefSeq

NP_005685.1. NM_005694.1.

UniGene

Hs.534383.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q14061.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46087N.

IntAct

Q14061. 12 interactions.

MINT

MINT-1373812.

STRING

9606.ENSP00000261070.

PTM databases

PhosphoSite

Q14061.

Polymorphism databases

DMDM

2493873.

Proteomic databases

PaxDb

Q14061.

PRIDE

Q14061.

Protocols and materials databases

DNASU

10063.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261070; ENSP00000261070; ENSG00000138495.
ENST00000468918; ENSP00000417805; ENSG00000138495.
ENST00000497116; ENSP00000417923; ENSG00000138495.

GeneID

10063.

KEGG

hsa:10063.

UCSC

uc003ecz.1. human.

Organism-specific databases

CTD

10063.

GeneCards

GC03M119373.

HGNC

HGNC:2264. COX17.

HPA

HPA042226.
HPA048158.

MIM

604813. gene.

neXtProt

NX_Q14061.

PharmGKB

PA26780.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG136703.

HOGENOM

HOG000195037.

HOVERGEN

HBG054258.

InParanoid

Q14061.

KO

K02260.

OrthoDB

EOG4FBHVN.

PhylomeDB

Q14061.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

Q14061.

Bgee

Q14061.

CleanEx

HS_COX17.

Genevestigator

Q14061.

GermOnline

ENSG00000138495. Homo sapiens.

Family and domain databases

Gene3D

1.10.810.10. 1 hit.

InterPro

IPR009069. Cys_alpha_HP_mot_SF.
IPR007745. Cyt_c_oxidase_Cu-chaperone.
[Graphical view]

PANTHER

PTHR16719. PTHR16719. 1 hit.

Pfam

PF05051. COX17. 1 hit.
[Graphical view]

ProDom

PD014904. Cyt_c_oxidase_Cu-chaperone. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF47072. MTCP1. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q14061.

GenomeRNAi

10063.

NextBio

38033.

SOURCE

Search...

Entry information

Entry name

COX17_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.