Sequence information
Variant position: 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1180 The length of the canonical sequence.
Location on the sequence:
VLRYYLFQGQRYIWIETQQA
F YQVSLLDHGRSCDDVHRSRH
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VLRYYLFQGQRYIWIETQQAF YQVSLLDHGRSCDDVHRSRH
Mouse VLRYYVLQGQRYVWMETQQAF CQVSLLDHGRTCDDVHCSSS
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
1 – 1180
Polyamine-transporting ATPase 13A2
Topological domain
66 – 235
Cytoplasmic
Literature citations
ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion.
Wang R.; Tan J.; Chen T.; Han H.; Tian R.; Tan Y.; Wu Y.; Cui J.; Chen F.; Li J.; Lv L.; Guan X.; Shang S.; Lu J.; Zhang Z.;
J. Cell Biol. 218:267-284(2019)
Cited for: FUNCTION; INTERACTION WITH HDAC6; CHARACTERIZATION OF VARIANTS KRS LEU-182 AND ARG-504;
PARK9-linked parkinsonism in eastern Asia: mutation detection in ATP13A2 and clinical phenotype.
Ning Y.P.; Kanai K.; Tomiyama H.; Li Y.; Funayama M.; Yoshino H.; Sato S.; Asahina M.; Kuwabara S.; Takeda A.; Hattori T.; Mizuno Y.; Hattori N.;
Neurology 70:1491-1493(2008)
Cited for: VARIANT KRS LEU-182;
Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism.
Podhajska A.; Musso A.; Trancikova A.; Stafa K.; Moser R.; Sonnay S.; Glauser L.; Moore D.J.;
PLoS ONE 7:E39942-E39942(2012)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS KRS MET-12; LEU-182; ARG-504; ARG-533; THR-746 AND ARG-877; SUBCELLULAR LOCATION;
Loss-of-function mutations in the ATP13A2/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78).
Estrada-Cuzcano A.; Martin S.; Chamova T.; Synofzik M.; Timmann D.; Holemans T.; Andreeva A.; Reichbauer J.; De Rycke R.; Chang D.I.; van Veen S.; Samuel J.; Schoels L.; Poeppel T.; Mollerup Soerensen D.; Asselbergh B.; Klein C.; Zuchner S.; Jordanova A.; Vangheluwe P.; Tournev I.; Schuele R.;
Brain 140:287-305(2017)
Cited for: INVOLVEMENT IN SPG78; VARIANT SPG78 ILE-517; CHARACTERIZATION OF VARIANT KRS LEU-182; CHARACTERIZATION OF VARIANT SPG78 ILE-517; CHARACTERIZATION OF VARIANT ARG-533; SUBCELLULAR LOCATION; AUTOPHOSPHORYLATION; MUTAGENESIS OF ASP-513;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.