Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Copper transport protein ATOX1

Gene

ATOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Copper
Metal bindingi15 – 151Copper

GO - Molecular functioni

  1. copper chaperone activity Source: UniProtKB
  2. copper-dependent protein binding Source: UniProtKB
  3. copper ion binding Source: UniProtKB
  4. copper ion transmembrane transporter activity Source: Ensembl
  5. metallochaperone activity Source: UniProtKB

GO - Biological processi

  1. cellular copper ion homeostasis Source: ProtInc
  2. copper ion transport Source: UniProtKB
  3. intracellular copper ion transport Source: Ensembl
  4. response to oxidative stress Source: ProtInc
  5. response to reactive oxygen species Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper transport protein ATOX1
Alternative name(s):
Metal transport protein ATX1
Gene namesi
Name:ATOX1
Synonyms:HAH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:798. ATOX1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6868Copper transport protein ATOX1PRO_0000212537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00244.
PaxDbiO00244.
PeptideAtlasiO00244.
PRIDEiO00244.

PTM databases

PhosphoSiteiO00244.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO00244.
CleanExiHS_ATOX1.
ExpressionAtlasiO00244. baseline and differential.
GenevestigatoriO00244.

Organism-specific databases

HPAiHPA055036.

Interactioni

Subunit structurei

Interacts with ATP7B.1 Publication

Protein-protein interaction databases

BioGridi106965. 6 interactions.
MINTiMINT-105921.
STRINGi9606.ENSP00000316854.

Structurei

Secondary structure

1
68
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi13 – 2614Combined sources
Beta strandi28 – 347Combined sources
Turni35 – 384Combined sources
Beta strandi39 – 468Combined sources
Helixi48 – 569Combined sources
Turni57 – 593Combined sources
Beta strandi62 – 665Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FE0X-ray1.75A/B1-68[»]
1FE4X-ray1.75A/B1-68[»]
1FEEX-ray1.80A/B1-68[»]
1TL4NMR-A1-68[»]
1TL5NMR-A1-68[»]
2K1RNMR-B1-68[»]
2LQ9NMR-A1-68[»]
3CJKX-ray1.80A2-68[»]
3IWLX-ray1.60A1-68[»]
3IWXX-ray2.14A/B1-68[»]
ProteinModelPortaliO00244.
SMRiO00244. Positions 2-67.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00244.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6867HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATX1 family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG238748.
GeneTreeiENSGT00390000005805.
HOGENOMiHOG000038877.
HOVERGENiHBG050610.
InParanoidiO00244.
KOiK07213.
PhylomeDBiO00244.
TreeFamiTF352589.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT
60
LLATLKKTGK TVSYLGLE
Length:68
Mass (Da):7,402
Last modified:July 1, 1997 - v1
Checksum:i0B364B1BD1279314
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70660 mRNA. Translation: AAC51227.1.
AY165037 Genomic DNA. Translation: AAN84554.1.
BT009786 mRNA. Translation: AAP88788.1.
AK293063 mRNA. Translation: BAF85752.1.
AY986502 Genomic DNA. Translation: AAX81411.1.
CH471062 Genomic DNA. Translation: EAW61663.1.
CH471062 Genomic DNA. Translation: EAW61664.1.
BC112248 mRNA. Translation: AAI12249.1.
BC112250 mRNA. Translation: AAI12251.1.
CCDSiCCDS47317.1.
RefSeqiNP_004036.1. NM_004045.3.
UniGeneiHs.125213.

Genome annotation databases

EnsembliENST00000313115; ENSP00000316854; ENSG00000177556.
ENST00000522710; ENSP00000429814; ENSG00000177556.
ENST00000524142; ENSP00000430598; ENSG00000177556.
GeneIDi475.
KEGGihsa:475.
UCSCiuc003luk.3. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70660 mRNA. Translation: AAC51227.1.
AY165037 Genomic DNA. Translation: AAN84554.1.
BT009786 mRNA. Translation: AAP88788.1.
AK293063 mRNA. Translation: BAF85752.1.
AY986502 Genomic DNA. Translation: AAX81411.1.
CH471062 Genomic DNA. Translation: EAW61663.1.
CH471062 Genomic DNA. Translation: EAW61664.1.
BC112248 mRNA. Translation: AAI12249.1.
BC112250 mRNA. Translation: AAI12251.1.
CCDSiCCDS47317.1.
RefSeqiNP_004036.1. NM_004045.3.
UniGeneiHs.125213.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FE0X-ray1.75A/B1-68[»]
1FE4X-ray1.75A/B1-68[»]
1FEEX-ray1.80A/B1-68[»]
1TL4NMR-A1-68[»]
1TL5NMR-A1-68[»]
2K1RNMR-B1-68[»]
2LQ9NMR-A1-68[»]
3CJKX-ray1.80A2-68[»]
3IWLX-ray1.60A1-68[»]
3IWXX-ray2.14A/B1-68[»]
ProteinModelPortaliO00244.
SMRiO00244. Positions 2-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106965. 6 interactions.
MINTiMINT-105921.
STRINGi9606.ENSP00000316854.

PTM databases

PhosphoSiteiO00244.

Proteomic databases

MaxQBiO00244.
PaxDbiO00244.
PeptideAtlasiO00244.
PRIDEiO00244.

Protocols and materials databases

DNASUi475.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313115; ENSP00000316854; ENSG00000177556.
ENST00000522710; ENSP00000429814; ENSG00000177556.
ENST00000524142; ENSP00000430598; ENSG00000177556.
GeneIDi475.
KEGGihsa:475.
UCSCiuc003luk.3. human.

Organism-specific databases

CTDi475.
GeneCardsiGC05M151122.
HGNCiHGNC:798. ATOX1.
HPAiHPA055036.
MIMi602270. gene.
neXtProtiNX_O00244.
PharmGKBiPA25096.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238748.
GeneTreeiENSGT00390000005805.
HOGENOMiHOG000038877.
HOVERGENiHBG050610.
InParanoidiO00244.
KOiK07213.
PhylomeDBiO00244.
TreeFamiTF352589.

Enzyme and pathway databases

ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiATOX1. human.
EvolutionaryTraceiO00244.
GeneWikiiATOX1.
GenomeRNAii475.
NextBioi1967.
PROiO00244.
SOURCEiSearch...

Gene expression databases

BgeeiO00244.
CleanExiHS_ATOX1.
ExpressionAtlasiO00244. baseline and differential.
GenevestigatoriO00244.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis."
    Klomp L.W.J., Lin S.-J., Yuan D.S., Klausner R.D., Culotta V.C., Gitlin J.D.
    J. Biol. Chem. 272:9221-9226(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Genomic organization of ATOX1, a human copper chaperone."
    Liu P.-C., Koeller D.M., Kaler S.G.
    BMC Genet. 4:4-4(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Uterus.
  5. NIEHS SNPs program
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins."
    Wernimont A.K., Huffman D.L., Lamb A.L., O'Halloran T.V., Rosenzweig A.C.
    Nat. Struct. Biol. 7:766-771(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), COPPER-BINDING SITES, INTERACTION WITH ATP7B.

Entry informationi

Entry nameiATOX1_HUMAN
AccessioniPrimary (citable) accession number: O00244
Secondary accession number(s): A8KAJ8
, D3DQI2, Q2M1R6, Q56AP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 131 of the entry and version 1 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 5
    Human chromosome 5: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.