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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	63 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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	copper ion transport Traceable author statement. Source: ProtInc generation of precursor metabolites and energy Traceable author statement. Source: ProtInc
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper chaperone activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 63

62

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

Redox-active Ref.7

Disulfide bond

36 ↔ 45

Redox-active Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

63

Helix Strand Turn

Details...

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: 9050918] [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: 10982038] [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: 14702039] [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: 15489334] [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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"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: 18093982] [Abstract] Cited for: STRUCTURE BY NMR IN APO AND COPPER-BOUND FORMS, 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.

SMR

Q14061. Positions 1-63.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46087N.

IntAct

Q14061. 11 interactions.

MINT

MINT-1373812.

STRING

Q14061.

PTM databases

PhosphoSite

Q14061.

Polymorphism databases

DMDM

2493873.

Proteomic databases

PRIDE

Q14061.

Protocols and materials databases

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.

H-InvDB

HIX0030792.

HGNC

HGNC:2264. COX17.

MIM

604813. gene.

neXtProt

NX_Q14061.

PharmGKB

PA26780.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21420.

HOGENOM

HBG558801.

HOVERGEN

HBG054258.

InParanoid

Q14061.

OMA

GEENCGH.

OrthoDB

EOG4FBHVN.

PhylomeDB

Q14061.

Gene expression databases

ArrayExpress

Q14061.

CleanEx

HS_COX17.

Genevestigator

Q14061.

GermOnline

ENSG00000138495. Homo sapiens.

Family and domain databases

InterPro

IPR007745. Cyt_c_oxidase_Cu-chaperone.
IPR009069. MTCP1.
[Graphical view]

KO

K02260.

PANTHER

PTHR16719. COX17. 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

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:	January 25, 2012
This is version 94 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.