ATP13A2
entrez
23400
canonical
uniprot
Q9NQ11
canonical
ensembl
ENSG00000159363
resolver
ensp
ENSP00000327214
resolver
ensp
ENSP00000341115
resolver
ensp
ENSP00000413307
resolver
ensp
ENSP00000649226
resolver
ensp
ENSP00000649227
resolver
ensp
ENSP00000649228
resolver
ensp
ENSP00000649229
resolver
ensp
ENSP00000649231
resolver
ensp
ENSP00000691150
resolver
ensp
ENSP00000691152
resolver
genesymbol
ATP13A2
resolver
genesymbol_syn
PARK9
resolver
hgnc
HGNC:30213
resolver
uniprot
O75700
resolver
uniprot
Q5JXY1
resolver
uniprot
Q5JXY2
resolver
uniprot
Q6S9Z9
resolver
uniprot
Q8N4D4
resolver
uniprot
Q8NBS1
resolver
uniprot_entry
AT132_HUMAN
resolver
uniprot_entry
Q8N4D4_HUMAN
resolver
uniprot_entry
Q8NBS1_HUMAN
resolver
uniprot_sec
O75700
resolver
uniprot_sec
Q5JXY1
resolver
uniprot_sec
Q5JXY2
resolver
uniprot_sec
Q6S9Z9
resolver
activity_regulation
ACTIVITY REGULATION: Accumulates in an inactive autophosphorylated state (PubMed:26134396). The presence of spermine results in a dose-dependent reduction in autophosphorylation (PubMed:31996848). {ECO:0000269|PubMed:26134396, ECO:0000269|PubMed:31996848}.
uniprot
proteins
amino_acid_sequence
MSADSSPLVGSTPTGYGTLTIGTSIDPLSSSVSSVRLSGYCGSPWRVIGYHVVVWMMAGIPLLLFRWKPLWGVRLRLRPCNLAHAETLVIEIRDKEDSSWQLFTVQVQTEAIGEGSLEPSPQSQAEDGRSQAAVGAVPEGAWKDTAQLHKSEEAVSVGQKRVLRYYLFQGQRYIWIETQQAFYQVSLLDHGRSCDDVHRSRHGLSLQDQMVRKAIYGPNVISIPVKSYPQLLVDEALNPYYGFQAFSIALWLADHYYWYALCIFLISSISICLSLYKTRKQSQTLRDMVKLSMRVCVCRPGGEEEWVDSSELVPGDCLVLPQEGGLMPCDAALVAGECMVNESSLTGESIPVLKTALPEGLGPYCAETHRRHTLFCGTLILQARAYVGPHVLAVVTRTGFCTAKGGLVSSILHPRPINFKFYKHSMKFVAALSVLALLGTIYSIFILYRNRVPLNEIVIRALDLVTVVVPPALPAAMTVCTLYAQSRLRRQGIFCIHPLRINLGGKLQLVCFDKTGTLTEDGLDVMGVVPLKGQAFLPLVPEPRRLPVGPLLRALATCHALSRLQDTPVGDPMDLKMVESTGWVLEEEPAADSAFGTQVLAVMRPPLWEPQLQAMEEPPVPVSVLHRFPFSSALQRMSVVVAWPGATQPEAYVKGSPELVAGLCNPETVPTDFAQMLQSYTAAGYRVVALASKPLPTVPSLEAAQQLTRDTVEGDLSLLGLLVMRNLLKPQTTPVIQALRRTRIRAVMVTGDNLQTAVTVARGCGMVAPQEHLIIVHATHPERGQPASLEFLPMESPTAVNGVKDPDQAASYTVEPDPRSRHLALSGPTFGIIVKHFPKLLPKVLVQGTVFARMAPEQKTELVCELQKLQYCVGMCGDGANDCGALKAADVGISLSQAEASVVSPFTSSMASIECVPMVIREGRCSLDTSFSVFKYMALYSLTQFISVLILYTINTNLGDLQFLAIDLVITTTVAVLMSRTGPALVLGRVRPPGALLSVPVLSSLLLQMVLVTGVQLGGYFLTLAQPWFVPLNRTVAAPDNLPNYENTVVFSLSSFQYLILAAAVSKGAPFRRPLYTNVPFLVALALLSSVLVGLVLVPGLLQGPLALRNITDTGFKLLLLGLVTLNFVGAFMLESVLDQCLPACLRRLRPKRASKKRFKQLERELAEQPWPPLPAGPLR
uniprot
proteins
disease_involvement
DISEASE: Kufor-Rakeb syndrome (KRS) [MIM:606693]: A rare form of autosomal recessive juvenile or early-onset, levodopa-responsive parkinsonism. In addition to typical parkinsonian signs, clinical manifestations of Kufor-Rakeb syndrome include behavioral problems, facial tremor, pyramidal tract dysfunction, supranuclear gaze palsy, and dementia. {ECO:0000269|PubMed:16964263, ECO:0000269|PubMed:17485642, ECO:0000269|PubMed:18413573, ECO:0000269|PubMed:20683840, ECO:0000269|PubMed:20853184, ECO:0000269|PubMed:21542062, ECO:0000269|PubMed:22296644, ECO:0000269|PubMed:22388936, ECO:0000269|PubMed:22768177, ECO:0000269|PubMed:28137957, ECO:0000269|PubMed:29903538, ECO:0000269|PubMed:30538141, ECO:0000269|PubMed:31996848}. Note=The disease is caused by variants affecting the gene represented in this entry. KRS has also been referred to as neuronal ceroid lipofuscinosis 12 (CLN12), due to neuronal and glial lipofuscin deposits detected in the cortex, basal nuclei and cerebellum of some patients. {ECO:0000269|PubMed:22388936}.; DISEASE: Spastic paraplegia 78, autosomal recessive (SPG78) [MIM:617225]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:27217339, ECO:0000269|PubMed:28137957, ECO:0000269|PubMed:38252374}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
function
FUNCTION: ATPase which acts as a lysosomal polyamine exporter with high affinity for spermine (PubMed:31996848). Also stimulates cellular uptake of polyamines and protects against polyamine toxicity (PubMed:31996848). Plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity (PubMed:22186024). Contributes to cellular zinc homeostasis (PubMed:24603074). Confers cellular protection against Mn(2+) and Zn(2+) toxicity and mitochondrial stress (PubMed:26134396). Required for proper lysosomal and mitochondrial maintenance (PubMed:22296644, PubMed:28137957). Regulates the autophagy-lysosome pathway through the control of SYT11 expression at both transcriptional and post-translational levels (PubMed:27278822). Facilitates recruitment of deacetylase HDAC6 to lysosomes to deacetylate CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141). Promotes secretion of exosomes as well as secretion of SCNA via exosomes (PubMed:24603074, PubMed:25392495). Plays a role in lipid homeostasis (PubMed:31132336). {ECO:0000269|PubMed:22186024, ECO:0000269|PubMed:22296644, ECO:0000269|PubMed:24603074, ECO:0000269|PubMed:25392495, ECO:0000269|PubMed:26134396, ECO:0000269|PubMed:27278822, ECO:0000269|PubMed:28137957, ECO:0000269|PubMed:30538141, ECO:0000269|PubMed:31132336, ECO:0000269|PubMed:31996848}.
uniprot
proteins
mass_dalton
128794
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="G->A: No effect on lipid binding."; /evidence="ECO:0000269|PubMed:26134396"; MUTAGEN 66..68; /note="RWK->AWA: Reduces lipid binding."; /evidence="ECO:0000269|PubMed:26134396"; MUTAGEN 74..78; /note="RLRLR->ALALA: Reduces lipid binding."; /evidence="ECO:0000269|PubMed:26134396"; MUTAGEN 160..164; /note="KRVLR->AAVLA: Reduces lipid binding."; /evidence="ECO:0000269|PubMed:26134396"; MUTAGEN 348; /note="E->A: Autophosphorylated but displays limited spermine-induced ATPase activity and lacks spermine-induced dephosphorylation."; /evidence="ECO:0000269|PubMed:31996848"; MUTAGEN 472; /note="A->V: Reduced spermine-induced ATPase activity and lack of spermine-induced dephosphorylation."; /evidence="ECO:0000269|PubMed:31996848"; MUTAGEN 513; /note="D->N: Loss of ATPase function, autophosphorylation and protection against mitochondrial stress."; /evidence="ECO:0000269|PubMed:26134396, ECO:0000269|PubMed:28137957, ECO:0000269|PubMed:31996848"; MUTAGEN 967; /note="D->N: Reduced spermine-induced ATPase activity."; /evidence="ECO:0000269|PubMed:31996848"; MUTAGEN 1033; /note="N->A: Abolishes glycosylation."; /evidence="ECO:0000269|PubMed:26134396"; MUTAGEN 1067; /note="K->A: Reduced spermine-induced ATPase activity."; /evidence="ECO:0000269|PubMed:31996848
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated (PubMed:26134396, PubMed:28137957). Accumulates in an inactive autophosphorylated state and autophosphorylation is stimulated by phosphatidic acid and phosphatidylinositol 3,5-bisphosphate but not by Mn(2+) or Zn(2+) (PubMed:26134396). The presence of spermine results in a dose-dependent reduction in autophosphorylation (PubMed:31996848). {ECO:0000269|PubMed:26134396, ECO:0000269|PubMed:31996848, ECO:0000305|PubMed:28137957}.
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type V subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964263
uniprot
proteins
pubmed
17485642
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18413573
uniprot
proteins
pubmed
19015489
uniprot
proteins
pubmed
19085912
uniprot
proteins
pubmed
20683840
uniprot
proteins
pubmed
20853184
uniprot
proteins
pubmed
21542062
uniprot
proteins
pubmed
22186024
uniprot
proteins
pubmed
22296644
uniprot
proteins
pubmed
22388936
uniprot
proteins
pubmed
22768177
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24603074
uniprot
proteins
pubmed
25392495
uniprot
proteins
pubmed
26134396
uniprot
proteins
pubmed
27217339
uniprot
proteins
pubmed
27278822
uniprot
proteins
pubmed
28137957
uniprot
proteins
pubmed
29903538
uniprot
proteins
pubmed
30538141
uniprot
proteins
pubmed
31132336
uniprot
proteins
pubmed
31996848
uniprot
proteins
pubmed
38252374
uniprot
proteins
sequence_length
1180
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21542062, ECO:0000269|PubMed:22186024, ECO:0000269|PubMed:22768177, ECO:0000269|PubMed:24603074, ECO:0000269|PubMed:26134396, ECO:0000269|PubMed:28137957}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:24603074, ECO:0000269|PubMed:25392495, ECO:0000269|PubMed:26134396}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:24603074, ECO:0000269|PubMed:25392495}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:24603074}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 236..253; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 257..276; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 428..448; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 464..484; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 931..951; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 958..978; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 995..1015; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1049..1069; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1081..1101; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1118..1138; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins