ATPase 13A2

Alternative Names

  • ATP13A2

Associated Diseases

Kufor-Rakeb Syndrome
Back to search Result
OMIM Number

610513

NCBI Gene ID

23400

Uniprot ID

Q9NQ11

Length

26,015 bases

No. of Exons

29

No. of isoforms

3

Protein Name

Polyamine-transporting ATPase 13A2

Molecular Mass

128794 Da

Amino Acid Count

1180

Genomic Location

chr1:16,985,957-17,011,971

Gene Map Locus
1p36.13

Description

This gene encodes a member of the P5 subfamily of ATPases which transports inorganic cations as well as other substrates. Mutations in this gene are associated with Kufor-Rakeb syndrome (KRS), also referred to as Parkinson disease 9. Multiple transcript variants encoding different isoforms have been found for this gene. [From RefSeq]

Epidemiology in the Arab World

View Map
Variant NameCountryGenomic LocationClinical SignificanceCondition(s)HGVS ExpressionsdbSNPClinvar
NM_022089.3:c.1550C>T LebanonNC_000001.11:g.16993828G>APathogenicKufor-Rakeb SyndromeNG_009054.1:g.23101C>T; NM_022089.3:c.1550C>T ; NP_071372.1:p.Thr517Ile1057519291374888

Other Reports

Jordan

Hampshire et al. (2001) used autozygosity mapping on a family previously investigated by Najim Al-Din et al. (1994) as having Kufor-Rakeb syndrome. Samples were taken from the parents, four of the affected children, and one unaffected female whose age exceeds the age of onset. The fifth affected child was a female without distinguishing symptoms compared to her affected brothers. Hampshire et al. (2001) mapped the syndrome to a 9cM region in 1p36 with the markers GATA29A05 and D1S552 and further multipoint linkage analysis revealed D1S1592, D1S2826, D1S2644, and D1S199 markers with the highest lod score of 3.6. Ramirez et al. (2006) sheds more light on the pathogenesis of KRS and the transmembrane ATP13A2 function with a mutation analysis on the same Jordanian family and a control group of 480 German chromosomes. A homozygous 22bp duplication (1632_1653dup22, 552LfsX788) was identified in exon 16 in all affected members leading to a frameshift and stop codon after 236 extraneous amino acids. A possible consequence of this mutation is the removal of transmembrane domains leading to a loss of function and proteasomal degradation since the protein is retained in the endoplasmic reticulum. Ramirez et al. (2006) suggested that the neurodegradation in KRS may be explained by the overload and toxic aggregation of mutant ATP13A2 exacerbating the proteasomal normal function.

© CAGS 2021. All rights reserved.