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Protein

Probable cation-transporting ATPase 13A2

Gene

ATP13A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in intracellular cation homeostasis and the maintenance of neuronal integrity.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei513 – 51314-aspartylphosphate intermediateBy similarity
Metal bindingi878 – 8781MagnesiumBy similarity
Metal bindingi882 – 8821MagnesiumBy similarity

GO - Molecular functioni

  • ATPase activity Source: ParkinsonsUK-UCL
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cation transport Source: InterPro
  • cellular response to manganese ion Source: ParkinsonsUK-UCL
  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Protein family/group databases

TCDBi3.A.3.10.7. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cation-transporting ATPase 13A2 (EC:3.6.3.-)
Gene namesi
Name:ATP13A2
Synonyms:PARK9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30213. ATP13A2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3422HelicalSequence AnalysisAdd
BLAST
Topological domaini35 – 4511ExtracellularSequence AnalysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 230164CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei231 – 25323HelicalSequence AnalysisAdd
BLAST
Topological domaini254 – 2563ExtracellularSequence Analysis
Transmembranei257 – 27620HelicalSequence AnalysisAdd
BLAST
Topological domaini277 – 425149CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei426 – 44520HelicalSequence AnalysisAdd
BLAST
Topological domaini446 – 45914ExtracellularSequence AnalysisAdd
BLAST
Transmembranei460 – 48021HelicalSequence AnalysisAdd
BLAST
Topological domaini481 – 932452CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei933 – 95220HelicalSequence AnalysisAdd
BLAST
Topological domaini953 – 96311ExtracellularSequence AnalysisAdd
BLAST
Transmembranei964 – 98118HelicalSequence AnalysisAdd
BLAST
Topological domaini982 – 99716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei998 – 101821HelicalSequence AnalysisAdd
BLAST
Topological domaini1019 – 104628ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1047 – 106620HelicalSequence AnalysisAdd
BLAST
Topological domaini1067 – 107913CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1080 – 109718HelicalSequence AnalysisAdd
BLAST
Topological domaini1098 – 111316ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1114 – 113421HelicalSequence AnalysisAdd
BLAST
Topological domaini1135 – 118046CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Kufor-Rakeb syndrome (KRS)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:606693
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821F → L in KRS. 1 Publication
VAR_066019
Natural varianti504 – 5041G → R in KRS. 1 Publication
Corresponds to variant rs121918227 [ dbSNP | Ensembl ].
VAR_058455
Natural varianti877 – 8771G → R in KRS; found in two affected brothers also carrying C-481 in FBXO7. 1 Publication
VAR_066020
Natural varianti1059 – 10591L → R in KRS; the mutant protein is retained in the endoplasmic reticulum. 1 Publication
VAR_066021
Ceroid lipofuscinosis, neuronal, 12 (CLN12)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.

See also OMIM:606693
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti854 – 8541M → R in CLN12. 1 Publication
VAR_070194

Keywords - Diseasei

Disease mutation, Neurodegeneration, Neuronal ceroid lipofuscinosis, Parkinsonism

Organism-specific databases

MIMi606693. phenotype.
Orphaneti306674. Kufor-Rakeb syndrome.
314632. Parkinsonim due to ATP13A2 deficiency.
PharmGKBiPA134897221.

Polymorphism and mutation databases

BioMutaiATP13A2.
DMDMi14285364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11801180Probable cation-transporting ATPase 13A2PRO_0000046423Add
BLAST

Proteomic databases

MaxQBiQ9NQ11.
PaxDbiQ9NQ11.
PRIDEiQ9NQ11.

PTM databases

PhosphoSiteiQ9NQ11.

Expressioni

Tissue specificityi

Expressed in brain; protein levels are markedly increased in brain from subjects with Parkinson disease and subjects with dementia with Lewy bodies. Detected in pyramidal neurons located throughout the cingulate cortex (at protein level). In the substantia nigra, it is found in neuromelanin-positive dopaminergic neurons (at protein level).1 Publication

Gene expression databases

BgeeiQ9NQ11.
CleanExiHS_ATP13A2.
ExpressionAtlasiQ9NQ11. baseline and differential.
GenevestigatoriQ9NQ11.

Organism-specific databases

HPAiCAB037111.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AAK1Q2M2I82EBI-6308763,EBI-1383433
BNIP3LO602382EBI-6308763,EBI-849893
GAKO149762EBI-6308763,EBI-714707
HDAC6Q9UBN72EBI-6308763,EBI-301697
HSPA8P111422EBI-6308763,EBI-351896
SYT11Q9BT882EBI-6308763,EBI-751770
YIF1AO950702EBI-6308763,EBI-2799703

Protein-protein interaction databases

BioGridi116973. 56 interactions.
IntActiQ9NQ11. 43 interactions.
MINTiMINT-4781194.
STRINGi9606.ENSP00000327214.

Structurei

3D structure databases

ProteinModelPortaliQ9NQ11.
SMRiQ9NQ11. Positions 254-1033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00530000063001.
HOGENOMiHOG000171813.
HOVERGENiHBG065757.
InParanoidiQ9NQ11.
KOiK13526.
OMAiWQLFTVQ.
OrthoDBiEOG7B5WV2.
PhylomeDBiQ9NQ11.
TreeFamiTF300331.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q9NQ11-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY
60 70 80 90 100
HVVVWMMAGI PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW
110 120 130 140 150
QLFTVQVQTE AIGEGSLEPS PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK
160 170 180 190 200
SEEAVSVGQK RVLRYYLFQG QRYIWIETQQ AFYQVSLLDH GRSCDDVHRS
210 220 230 240 250
RHGLSLQDQM VRKAIYGPNV ISIPVKSYPQ LLVDEALNPY YGFQAFSIAL
260 270 280 290 300
WLADHYYWYA LCIFLISSIS ICLSLYKTRK QSQTLRDMVK LSMRVCVCRP
310 320 330 340 350
GGEEEWVDSS ELVPGDCLVL PQEGGLMPCD AALVAGECMV NESSLTGESI
360 370 380 390 400
PVLKTALPEG LGPYCAETHR RHTLFCGTLI LQARAYVGPH VLAVVTRTGF
410 420 430 440 450
CTAKGGLVSS ILHPRPINFK FYKHSMKFVA ALSVLALLGT IYSIFILYRN
460 470 480 490 500
RVPLNEIVIR ALDLVTVVVP PALPAAMTVC TLYAQSRLRR QGIFCIHPLR
510 520 530 540 550
INLGGKLQLV CFDKTGTLTE DGLDVMGVVP LKGQAFLPLV PEPRRLPVGP
560 570 580 590 600
LLRALATCHA LSRLQDTPVG DPMDLKMVES TGWVLEEEPA ADSAFGTQVL
610 620 630 640 650
AVMRPPLWEP QLQAMEEPPV PVSVLHRFPF SSALQRMSVV VAWPGATQPE
660 670 680 690 700
AYVKGSPELV AGLCNPETVP TDFAQMLQSY TAAGYRVVAL ASKPLPTVPS
710 720 730 740 750
LEAAQQLTRD TVEGDLSLLG LLVMRNLLKP QTTPVIQALR RTRIRAVMVT
760 770 780 790 800
GDNLQTAVTV ARGCGMVAPQ EHLIIVHATH PERGQPASLE FLPMESPTAV
810 820 830 840 850
NGVKDPDQAA SYTVEPDPRS RHLALSGPTF GIIVKHFPKL LPKVLVQGTV
860 870 880 890 900
FARMAPEQKT ELVCELQKLQ YCVGMCGDGA NDCGALKAAD VGISLSQAEA
910 920 930 940 950
SVVSPFTSSM ASIECVPMVI REGRCSLDTS FSVFKYMALY SLTQFISVLI
960 970 980 990 1000
LYTINTNLGD LQFLAIDLVI TTTVAVLMSR TGPALVLGRV RPPGALLSVP
1010 1020 1030 1040 1050
VLSSLLLQMV LVTGVQLGGY FLTLAQPWFV PLNRTVAAPD NLPNYENTVV
1060 1070 1080 1090 1100
FSLSSFQYLI LAAAVSKGAP FRRPLYTNVP FLVALALLSS VLVGLVLVPG
1110 1120 1130 1140 1150
LLQGPLALRN ITDTGFKLLL LGLVTLNFVG AFMLESVLDQ CLPACLRRLR
1160 1170 1180
PKRASKKRFK QLERELAEQP WPPLPAGPLR
Length:1,180
Mass (Da):128,794
Last modified:June 1, 2001 - v2
Checksum:i98D13745D3B615BE
GO
Isoform B (identifier: Q9NQ11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     805-843: Missing.
     1079-1180: VPFLVALALL...WPPLPAGPLR → ERARPVPPRL...PQLPSVLLSV

Show »
Length:1,158
Mass (Da):125,977
Checksum:i1A7D35DF1CD34396
GO
Isoform 3 (identifier: Q9NQ11-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.

Show »
Length:1,175
Mass (Da):128,323
Checksum:i6418CB82F086E30C
GO

Sequence cautioni

The sequence CAA08912.1 differs from that shown. Reason: Frameshift at position 1054. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221Q → R in AAH30267 (PubMed:15489334).Curated
Sequence conflicti855 – 8584APEQ → IPRA in CAA08912 (Ref. 8) Curated
Sequence conflicti861 – 8611E → V in CAA08912 (Ref. 8) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121T → M.1 Publication
Corresponds to variant rs151117874 [ dbSNP | Ensembl ].
VAR_058451
Natural varianti49 – 491G → S.1 Publication
Corresponds to variant rs56379718 [ dbSNP | Ensembl ].
VAR_058452
Natural varianti182 – 1821F → L in KRS. 1 Publication
VAR_066019
Natural varianti294 – 2941R → Q.1 Publication
Corresponds to variant rs56367069 [ dbSNP | Ensembl ].
VAR_058453
Natural varianti389 – 3891P → L.1 Publication
Corresponds to variant rs56275621 [ dbSNP | Ensembl ].
VAR_058454
Natural varianti504 – 5041G → R in KRS. 1 Publication
Corresponds to variant rs121918227 [ dbSNP | Ensembl ].
VAR_058455
Natural varianti533 – 5331G → R in a patient with early onset Parkinson disease. 1 Publication
VAR_058456
Natural varianti578 – 5781V → G.1 Publication
Corresponds to variant rs56186751 [ dbSNP | Ensembl ].
VAR_058457
Natural varianti746 – 7461A → T.1 Publication
Corresponds to variant rs147277743 [ dbSNP | Ensembl ].
VAR_058458
Natural varianti762 – 7621R → W.1 Publication
Corresponds to variant rs55635527 [ dbSNP | Ensembl ].
VAR_058459
Natural varianti776 – 7761V → I.1 Publication
Corresponds to variant rs56170027 [ dbSNP | Ensembl ].
VAR_058460
Natural varianti854 – 8541M → R in CLN12. 1 Publication
VAR_070194
Natural varianti877 – 8771G → R in KRS; found in two affected brothers also carrying C-481 in FBXO7. 1 Publication
VAR_066020
Natural varianti946 – 9461I → F.1 Publication
Corresponds to variant rs55708915 [ dbSNP | Ensembl ].
VAR_058461
Natural varianti1059 – 10591L → R in KRS; the mutant protein is retained in the endoplasmic reticulum. 1 Publication
VAR_066021

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei155 – 1595Missing in isoform B and isoform 3. 4 PublicationsVSP_007310
Alternative sequencei805 – 84339Missing in isoform B. 2 PublicationsVSP_007311Add
BLAST
Alternative sequencei1079 – 1180102VPFLV…AGPLR → ERARPVPPRLPAPPPAQAGL QEALQAAGTRAGRAALAAAA RRPPEVVQAHGHPRHWNSLP LSHQLDPSPATPPPPPPTSL RLATVYTPPPRPPPPWGSVD YCPLPWTIPRRGGSPQLPSV LLSV in isoform B. 2 PublicationsVSP_007312Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354615 mRNA. Translation: CAB89728.1.
AY461712 mRNA. Translation: AAR23423.1.
AK290210 mRNA. Translation: BAF82899.1.
AL049569 Genomic DNA. Translation: CAI20366.1.
CH471134 Genomic DNA. Translation: EAW94825.1.
CH471134 Genomic DNA. Translation: EAW94827.1.
BC030267 mRNA. Translation: AAH30267.1.
AL833966 mRNA. Translation: CAD38813.2.
AJ009947 mRNA. Translation: CAA08912.1. Frameshift.
CCDSiCCDS175.1. [Q9NQ11-1]
CCDS44072.1. [Q9NQ11-2]
CCDS44073.1. [Q9NQ11-3]
RefSeqiNP_001135445.1. NM_001141973.2. [Q9NQ11-3]
NP_001135446.1. NM_001141974.2. [Q9NQ11-2]
NP_071372.1. NM_022089.3. [Q9NQ11-1]
UniGeneiHs.128866.

Genome annotation databases

EnsembliENST00000326735; ENSP00000327214; ENSG00000159363. [Q9NQ11-1]
ENST00000341676; ENSP00000341115; ENSG00000159363. [Q9NQ11-2]
ENST00000452699; ENSP00000413307; ENSG00000159363. [Q9NQ11-3]
GeneIDi23400.
KEGGihsa:23400.
UCSCiuc001baa.2. human. [Q9NQ11-1]
uc001bab.2. human. [Q9NQ11-3]
uc001bac.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354615 mRNA. Translation: CAB89728.1.
AY461712 mRNA. Translation: AAR23423.1.
AK290210 mRNA. Translation: BAF82899.1.
AL049569 Genomic DNA. Translation: CAI20366.1.
CH471134 Genomic DNA. Translation: EAW94825.1.
CH471134 Genomic DNA. Translation: EAW94827.1.
BC030267 mRNA. Translation: AAH30267.1.
AL833966 mRNA. Translation: CAD38813.2.
AJ009947 mRNA. Translation: CAA08912.1. Frameshift.
CCDSiCCDS175.1. [Q9NQ11-1]
CCDS44072.1. [Q9NQ11-2]
CCDS44073.1. [Q9NQ11-3]
RefSeqiNP_001135445.1. NM_001141973.2. [Q9NQ11-3]
NP_001135446.1. NM_001141974.2. [Q9NQ11-2]
NP_071372.1. NM_022089.3. [Q9NQ11-1]
UniGeneiHs.128866.

3D structure databases

ProteinModelPortaliQ9NQ11.
SMRiQ9NQ11. Positions 254-1033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116973. 56 interactions.
IntActiQ9NQ11. 43 interactions.
MINTiMINT-4781194.
STRINGi9606.ENSP00000327214.

Protein family/group databases

TCDBi3.A.3.10.7. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteiQ9NQ11.

Polymorphism and mutation databases

BioMutaiATP13A2.
DMDMi14285364.

Proteomic databases

MaxQBiQ9NQ11.
PaxDbiQ9NQ11.
PRIDEiQ9NQ11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326735; ENSP00000327214; ENSG00000159363. [Q9NQ11-1]
ENST00000341676; ENSP00000341115; ENSG00000159363. [Q9NQ11-2]
ENST00000452699; ENSP00000413307; ENSG00000159363. [Q9NQ11-3]
GeneIDi23400.
KEGGihsa:23400.
UCSCiuc001baa.2. human. [Q9NQ11-1]
uc001bab.2. human. [Q9NQ11-3]
uc001bac.2. human.

Organism-specific databases

CTDi23400.
GeneCardsiGC01M017312.
GeneReviewsiATP13A2.
HGNCiHGNC:30213. ATP13A2.
HPAiCAB037111.
MIMi606693. phenotype.
610513. gene.
neXtProtiNX_Q9NQ11.
Orphaneti306674. Kufor-Rakeb syndrome.
314632. Parkinsonim due to ATP13A2 deficiency.
PharmGKBiPA134897221.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00530000063001.
HOGENOMiHOG000171813.
HOVERGENiHBG065757.
InParanoidiQ9NQ11.
KOiK13526.
OMAiWQLFTVQ.
OrthoDBiEOG7B5WV2.
PhylomeDBiQ9NQ11.
TreeFamiTF300331.

Miscellaneous databases

ChiTaRSiATP13A2. human.
GeneWikiiATP13A2.
GenomeRNAii23400.
NextBioi45553.
PROiQ9NQ11.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQ11.
CleanExiHS_ATP13A2.
ExpressionAtlasiQ9NQ11. baseline and differential.
GenevestigatoriQ9NQ11.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Rhodes S., Huckle E.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
  2. "Homo sapiens putative ATPase (N-ATPase) mRNA."
    Liu J.-P., Li H.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Thalamus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM B).
    Tissue: Brain and Fetus.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1180 (ISOFORM A).
    Tissue: Amygdala.
  8. "YAC analysis and genes identification at a site of viral integration in the 1p36.1-36.2 chromosomal site."
    Casciano I., Volpi E.V., De Ambrosis A., Marchi J.M., Romani M.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 855-1180 (ISOFORM B).
  9. "Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase."
    Ramirez A., Heimbach A., Gruendemann J., Stiller B., Hampshire D., Cid L.P., Goebel I., Mubaidin A.F., Wriekat A.-L., Roeper J., Al-Din A., Hillmer A.M., Karsak M., Liss B., Woods C.G., Behrens M.I., Kubisch C.
    Nat. Genet. 38:1184-1191(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN KRS.
  10. Cited for: INVOLVEMENT IN KRS.
  11. "Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism."
    Park J.S., Mehta P., Cooper A.A., Veivers D., Heimbach A., Stiller B., Kubisch C., Fung V.S., Krainc D., Mackay-Sim A., Sue C.M.
    Hum. Mutat. 32:956-964(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, VARIANT KRS ARG-1059, CHARACTERIZATION OF VARIANT KRS ARG-1059.
  12. "PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity."
    Ramonet D., Podhajska A., Stafa K., Sonnay S., Trancikova A., Tsika E., Pletnikova O., Troncoso J.C., Glauser L., Moore D.J.
    Hum. Mol. Genet. 21:1725-1743(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  13. Cited for: VARIANT KRS ARG-504, VARIANTS MET-12 AND ARG-533.
  14. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT KRS LEU-182.
  15. "Novel ATP13A2 variant associated with Parkinson disease in Taiwan and Singapore."
    Lin C.H., Tan E.K., Chen M.L., Tan L.C., Lim H.Q., Chen G.S., Wu R.M.
    Neurology 71:1727-1732(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THR-746.
  16. Cited for: VARIANTS SER-49; GLN-294; LEU-389; GLY-578; TRP-762; ILE-776 AND PHE-946.
  17. Cited for: VARIANT KRS ARG-877.
  18. "Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis."
    Bras J., Verloes A., Schneider S.A., Mole S.E., Guerreiro R.J.
    Hum. Mol. Genet. 21:2646-2650(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CLN12 ARG-854.

Entry informationi

Entry nameiAT132_HUMAN
AccessioniPrimary (citable) accession number: Q9NQ11
Secondary accession number(s): O75700
, Q5JXY1, Q5JXY2, Q6S9Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.