ATPase ASNA1

ATPase ASNA1 also known as arsenical pump-driving ATPase and arsenite-stimulated ATPase is an enzyme that in humans is encoded by the ASNA1 gene.[5][6]

ASNA1
Identifiers
AliasesASNA1, ARSA-I, ARSA1, ASNA-I, GET3, TRC40, hASNA-I, arsA arsenite transporter, ATP-binding, homolog 1 (bacterial)
External IDsOMIM: 601913 MGI: 1928379 HomoloGene: 31513 GeneCards: ASNA1
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19p13.13Start12,737,139 bp[1]
End12,748,323 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

439

56495

Ensembl

ENSG00000198356

ENSMUSG00000052456

UniProt

O43681

O54984

RefSeq (mRNA)

NM_004317

NM_019652
NM_001357202
NM_001357203

RefSeq (protein)

NP_004308
NP_001358417
NP_001358418

NP_062626
NP_001344131
NP_001344132

Location (UCSC)Chr 19: 12.74 – 12.75 MbChr 8: 85.02 – 85.03 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

ASNA1 is the human homolog of the bacterial arsA gene. In E. coli, arsA ATPase is the catalytic component of a multisubunit oxyanion pump that is responsible for resistance to arsenicals and antimonials.[6]

Interactions

ASNA1 is found to interact with FAM71D according to STRING [7]

References
  1. GRCh38: Ensembl release 89: ENSG00000198356 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000052456 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Kurdi-Haidar B, Aebi S, Heath D, Enns RE, Naredi P, Hom DK, Howell SB (Feb 1997). "Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter". Genomics. 36 (3): 486–91. doi:10.1006/geno.1996.0494. PMID 8884272.
  6. "Entrez Gene: ASNA1 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial)".
  7. "STRING 10".

Further reading
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Kurdi-Haidar B, Heath D, Aebi S, Howell SB (1998). "Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)". J. Biol. Chem. 273 (35): 22173–6. doi:10.1074/jbc.273.35.22173. PMID 9712828.
  • Kurdi-Haidar B, Hom DK, Flittner DE, et al. (1998). "Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated human ATPase (hASNA-I)". J. Cell. Biochem. 71 (1): 1–10. doi:10.1002/(SICI)1097-4644(19981001)71:1<1::AID-JCB1>3.0.CO;2-#. PMID 9736449.
  • Kurdi-Haidar B, Heath D, Lennon G, Howell SB (2000). "Chromosomal localization and genomic structure of the human arsenite-stimulated ATPase (hASNA-I)". Somat. Cell Mol. Genet. 24 (5): 307–11. doi:10.1023/B:SCAM.0000007134.16744.8b. PMID 10696239.
  • Kao G, Nordenson C, Still M, et al. (2007). "ASNA-1 positively regulates insulin secretion in C. elegans and mammalian cells". Cell. 128 (3): 577–87. doi:10.1016/j.cell.2006.12.031. PMID 17289575.
  • Stefanovic S, Hegde RS (2007). "Identification of a targeting factor for posttranslational membrane protein insertion into the ER". Cell. 128 (6): 1147–59. doi:10.1016/j.cell.2007.01.036. PMID 17382883.


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