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O08997

- ATOX1_MOUSE

UniProt

O08997 - ATOX1_MOUSE

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Protein

Copper transport protein ATOX1

Gene
Atox1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 By similarity.

Sites

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

GO - Molecular functioni

  1. copper chaperone activity Source: Ensembl

GO - Biological processi

  1. cellular copper ion homeostasis Source: MGI
  2. copper ion transport Source: MGI
  3. response to oxidative stress Source: Ensembl
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_189141. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1333855. Atox1.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6868Copper transport protein ATOX1PRO_0000212538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO08997.
PaxDbiO08997.
PRIDEiO08997.

PTM databases

PhosphoSiteiO08997.

Expressioni

Gene expression databases

BgeeiO08997.
CleanExiMM_ATOX1.
GenevestigatoriO08997.

Interactioni

Subunit structurei

Interacts with ATP7B By similarity.

Protein-protein interaction databases

IntActiO08997. 2 interactions.
MINTiMINT-1855862.
STRINGi10090.ENSMUSP00000104485.

Structurei

3D structure databases

ProteinModelPortaliO08997.
SMRiO08997. Positions 2-66.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6867HMAAdd
BLAST

Sequence similaritiesi

Belongs to the ATX1 family.
Contains 1 HMA domain.

Phylogenomic databases

eggNOGiNOG238748.
GeneTreeiENSGT00390000005805.
HOGENOMiHOG000038877.
HOVERGENiHBG050610.
InParanoidiQ5NCU2.
KOiK07213.
OrthoDBiEOG786H6B.
PhylomeDBiO08997.
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.

O08997-1 [UniParc]FASTAAdd to Basket

« Hide

MPKHEFSVDM TCEGCAEAVS RVLNKLGGVE FNIDLPNKKV CIDSEHSSDT   50
LLATLNKTGK AVSYLGPK 68
Length:68
Mass (Da):7,338
Last modified:July 1, 1997 - v1
Checksum:i85D11908CCDC6372
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004591 mRNA. Translation: AAB61465.1.
AK002432 mRNA. Translation: BAB22098.1.
AL596207 Genomic DNA. Translation: CAI35353.1.
BC027632 mRNA. Translation: AAH27632.1.
CCDSiCCDS36158.1.
RefSeqiNP_033850.1. NM_009720.2.
UniGeneiMm.217759.

Genome annotation databases

EnsembliENSMUST00000108857; ENSMUSP00000104485; ENSMUSG00000018585.
GeneIDi11927.
KEGGimmu:11927.
UCSCiuc007izj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF004591 mRNA. Translation: AAB61465.1 .
AK002432 mRNA. Translation: BAB22098.1 .
AL596207 Genomic DNA. Translation: CAI35353.1 .
BC027632 mRNA. Translation: AAH27632.1 .
CCDSi CCDS36158.1.
RefSeqi NP_033850.1. NM_009720.2.
UniGenei Mm.217759.

3D structure databases

ProteinModelPortali O08997.
SMRi O08997. Positions 2-66.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O08997. 2 interactions.
MINTi MINT-1855862.
STRINGi 10090.ENSMUSP00000104485.

PTM databases

PhosphoSitei O08997.

Proteomic databases

MaxQBi O08997.
PaxDbi O08997.
PRIDEi O08997.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000108857 ; ENSMUSP00000104485 ; ENSMUSG00000018585 .
GeneIDi 11927.
KEGGi mmu:11927.
UCSCi uc007izj.1. mouse.

Organism-specific databases

CTDi 475.
MGIi MGI:1333855. Atox1.

Phylogenomic databases

eggNOGi NOG238748.
GeneTreei ENSGT00390000005805.
HOGENOMi HOG000038877.
HOVERGENi HBG050610.
InParanoidi Q5NCU2.
KOi K07213.
OrthoDBi EOG786H6B.
PhylomeDBi O08997.
TreeFami TF352589.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 280009.
PROi O08997.
SOURCEi Search...

Gene expression databases

Bgeei O08997.
CleanExi MM_ATOX1.
Genevestigatori O08997.

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

« Hide 'large scale' publications
  1. "Structure, expression, and chromosomal localization of the mouse Atox1 gene."
    Hamza I., Klomp L.W.J., Gaedigk R., White R.A., Gitlin J.D.
    Genomics 63:294-297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiATOX1_MOUSE
AccessioniPrimary (citable) accession number: O08997
Secondary accession number(s): Q5NCU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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