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O00244

- ATOX1_HUMAN

UniProt

O00244 - ATOX1_HUMAN

Protein

Copper transport protein ATOX1

Gene

ATOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. metallochaperone activity Source: UniProtKB

    GO - Biological processi

    1. cellular copper ion homeostasis Source: ProtInc
    2. copper ion transport Source: UniProtKB
    3. response to oxidative stress Source: ProtInc

    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

    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

    ArrayExpressiO00244.
    BgeeiO00244.
    CleanExiHS_ATOX1.
    GenevestigatoriO00244.

    Organism-specific databases

    HPAiHPA055036.

    Interactioni

    Subunit structurei

    Interacts with ATP7B.1 Publication

    Protein-protein interaction databases

    BioGridi106965. 3 interactions.
    MINTiMINT-105921.
    STRINGi9606.ENSP00000316854.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS47317.1.
    RefSeqi NP_004036.1. NM_004045.3.
    UniGenei Hs.125213.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FE0 X-ray 1.75 A/B 1-68 [» ]
    1FE4 X-ray 1.75 A/B 1-68 [» ]
    1FEE X-ray 1.80 A/B 1-68 [» ]
    1TL4 NMR - A 1-68 [» ]
    1TL5 NMR - A 1-68 [» ]
    2K1R NMR - B 1-68 [» ]
    2LQ9 NMR - A 1-68 [» ]
    3CJK X-ray 1.80 A 2-68 [» ]
    3IWL X-ray 1.60 A 1-68 [» ]
    3IWX X-ray 2.14 A/B 1-68 [» ]
    ProteinModelPortali O00244.
    SMRi O00244. Positions 2-67.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106965. 3 interactions.
    MINTi MINT-105921.
    STRINGi 9606.ENSP00000316854.

    PTM databases

    PhosphoSitei O00244.

    Proteomic databases

    MaxQBi O00244.
    PaxDbi O00244.
    PeptideAtlasi O00244.
    PRIDEi O00244.

    Protocols and materials databases

    DNASUi 475.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313115 ; ENSP00000316854 ; ENSG00000177556 .
    ENST00000522710 ; ENSP00000429814 ; ENSG00000177556 .
    ENST00000524142 ; ENSP00000430598 ; ENSG00000177556 .
    GeneIDi 475.
    KEGGi hsa:475.
    UCSCi uc003luk.3. human.

    Organism-specific databases

    CTDi 475.
    GeneCardsi GC05M151122.
    HGNCi HGNC:798. ATOX1.
    HPAi HPA055036.
    MIMi 602270. gene.
    neXtProti NX_O00244.
    PharmGKBi PA25096.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238748.
    HOGENOMi HOG000038877.
    HOVERGENi HBG050610.
    InParanoidi O00244.
    KOi K07213.
    PhylomeDBi O00244.
    TreeFami TF352589.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi ATOX1. human.
    EvolutionaryTracei O00244.
    GeneWikii ATOX1.
    GenomeRNAii 475.
    NextBioi 1967.
    PROi O00244.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00244.
    Bgeei O00244.
    CleanExi HS_ATOX1.
    Genevestigatori O00244.

    Family and domain databases

    InterProi IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    [Graphical view ]
    Pfami PF00403. HMA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55008. SSF55008. 1 hit.
    PROSITEi PS01047. HMA_1. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 127 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