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Q9NQ11 (AT132_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cation-transporting ATPase 13A2

EC=3.6.3.-
Gene names
Name:ATP13A2
Synonyms:PARK9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1180 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in intracellular cation homeostasis and the maintenance of neuronal integrity. Ref.12

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Lysosome Ref.11 Ref.12.

Tissue specificity

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). Ref.12

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17

Ceroid lipofuscinosis, neuronal, 12 (CLN12) [MIM:606693]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily. [View classification]

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9NQ11-1)

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.
Isoform B (identifier: Q9NQ11-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     805-843: Missing.
     1079-1180: VPFLVALALL...WPPLPAGPLR → ERARPVPPRL...PQLPSVLLSV
Isoform 3 (identifier: Q9NQ11-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11801180Probable cation-transporting ATPase 13A2
PRO_0000046423

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3422Helical; Potential
Topological domain35 – 4511Extracellular Potential
Transmembrane46 – 6621Helical; Potential
Topological domain67 – 230164Cytoplasmic Potential
Transmembrane231 – 25323Helical; Potential
Topological domain254 – 2563Extracellular Potential
Transmembrane257 – 27620Helical; Potential
Topological domain277 – 425149Cytoplasmic Potential
Transmembrane426 – 44520Helical; Potential
Topological domain446 – 45914Extracellular Potential
Transmembrane460 – 48021Helical; Potential
Topological domain481 – 932452Cytoplasmic Potential
Transmembrane933 – 95220Helical; Potential
Topological domain953 – 96311Extracellular Potential
Transmembrane964 – 98118Helical; Potential
Topological domain982 – 99716Cytoplasmic Potential
Transmembrane998 – 101821Helical; Potential
Topological domain1019 – 104628Extracellular Potential
Transmembrane1047 – 106620Helical; Potential
Topological domain1067 – 107913Cytoplasmic Potential
Transmembrane1080 – 109718Helical; Potential
Topological domain1098 – 111316Extracellular Potential
Transmembrane1114 – 113421Helical; Potential
Topological domain1135 – 118046Cytoplasmic Potential

Sites

Active site51314-aspartylphosphate intermediate By similarity
Metal binding8781Magnesium By similarity
Metal binding8821Magnesium By similarity

Natural variations

Alternative sequence155 – 1595Missing in isoform B and isoform 3.
VSP_007310
Alternative sequence805 – 84339Missing in isoform B.
VSP_007311
Alternative sequence1079 – 1180102VPFLV…AGPLR → ERARPVPPRLPAPPPAQAGL QEALQAAGTRAGRAALAAAA RRPPEVVQAHGHPRHWNSLP LSHQLDPSPATPPPPPPTSL RLATVYTPPPRPPPPWGSVD YCPLPWTIPRRGGSPQLPSV LLSV in isoform B.
VSP_007312
Natural variant121T → M. Ref.13
Corresponds to variant rs151117874 [ dbSNP | Ensembl ].
VAR_058451
Natural variant491G → S. Ref.16
Corresponds to variant rs56379718 [ dbSNP | Ensembl ].
VAR_058452
Natural variant1821F → L in KRS. Ref.14
VAR_066019
Natural variant2941R → Q. Ref.16
Corresponds to variant rs56367069 [ dbSNP | Ensembl ].
VAR_058453
Natural variant3891P → L. Ref.16
Corresponds to variant rs56275621 [ dbSNP | Ensembl ].
VAR_058454
Natural variant5041G → R in KRS. Ref.13
Corresponds to variant rs121918227 [ dbSNP | Ensembl ].
VAR_058455
Natural variant5331G → R in a patient with early onset Parkinson disease. Ref.13
VAR_058456
Natural variant5781V → G. Ref.16
Corresponds to variant rs56186751 [ dbSNP | Ensembl ].
VAR_058457
Natural variant7461A → T. Ref.15
Corresponds to variant rs147277743 [ dbSNP | Ensembl ].
VAR_058458
Natural variant7621R → W. Ref.16
Corresponds to variant rs55635527 [ dbSNP | Ensembl ].
VAR_058459
Natural variant7761V → I. Ref.16
Corresponds to variant rs56170027 [ dbSNP | Ensembl ].
VAR_058460
Natural variant8541M → R in CLN12. Ref.18
VAR_070194
Natural variant8771G → R in KRS; found in two affected brothers also carrying C-481 in FBXO7. Ref.17
VAR_066020
Natural variant9461I → F. Ref.16
Corresponds to variant rs55708915 [ dbSNP | Ensembl ].
VAR_058461
Natural variant10591L → R in KRS; the mutant protein is retained in the endoplasmic reticulum. Ref.11
VAR_066021

Experimental info

Sequence conflict3221Q → R in AAH30267. Ref.6
Sequence conflict855 – 8584APEQ → IPRA in CAA08912. Ref.8
Sequence conflict8611E → V in CAA08912. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 98D13745D3B615BE

FASTA1,180128,794
        10         20         30         40         50         60 
MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY HVVVWMMAGI 

        70         80         90        100        110        120 
PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW QLFTVQVQTE AIGEGSLEPS 

       130        140        150        160        170        180 
PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK SEEAVSVGQK RVLRYYLFQG QRYIWIETQQ 

       190        200        210        220        230        240 
AFYQVSLLDH GRSCDDVHRS RHGLSLQDQM VRKAIYGPNV ISIPVKSYPQ LLVDEALNPY 

       250        260        270        280        290        300 
YGFQAFSIAL WLADHYYWYA LCIFLISSIS ICLSLYKTRK QSQTLRDMVK LSMRVCVCRP 

       310        320        330        340        350        360 
GGEEEWVDSS ELVPGDCLVL PQEGGLMPCD AALVAGECMV NESSLTGESI PVLKTALPEG 

       370        380        390        400        410        420 
LGPYCAETHR RHTLFCGTLI LQARAYVGPH VLAVVTRTGF CTAKGGLVSS ILHPRPINFK 

       430        440        450        460        470        480 
FYKHSMKFVA ALSVLALLGT IYSIFILYRN RVPLNEIVIR ALDLVTVVVP PALPAAMTVC 

       490        500        510        520        530        540 
TLYAQSRLRR QGIFCIHPLR INLGGKLQLV CFDKTGTLTE DGLDVMGVVP LKGQAFLPLV 

       550        560        570        580        590        600 
PEPRRLPVGP LLRALATCHA LSRLQDTPVG DPMDLKMVES TGWVLEEEPA ADSAFGTQVL 

       610        620        630        640        650        660 
AVMRPPLWEP QLQAMEEPPV PVSVLHRFPF SSALQRMSVV VAWPGATQPE AYVKGSPELV 

       670        680        690        700        710        720 
AGLCNPETVP TDFAQMLQSY TAAGYRVVAL ASKPLPTVPS LEAAQQLTRD TVEGDLSLLG 

       730        740        750        760        770        780 
LLVMRNLLKP QTTPVIQALR RTRIRAVMVT GDNLQTAVTV ARGCGMVAPQ EHLIIVHATH 

       790        800        810        820        830        840 
PERGQPASLE FLPMESPTAV NGVKDPDQAA SYTVEPDPRS RHLALSGPTF GIIVKHFPKL 

       850        860        870        880        890        900 
LPKVLVQGTV FARMAPEQKT ELVCELQKLQ YCVGMCGDGA NDCGALKAAD VGISLSQAEA 

       910        920        930        940        950        960 
SVVSPFTSSM ASIECVPMVI REGRCSLDTS FSVFKYMALY SLTQFISVLI LYTINTNLGD 

       970        980        990       1000       1010       1020 
LQFLAIDLVI TTTVAVLMSR TGPALVLGRV RPPGALLSVP VLSSLLLQMV LVTGVQLGGY 

      1030       1040       1050       1060       1070       1080 
FLTLAQPWFV PLNRTVAAPD NLPNYENTVV FSLSSFQYLI LAAAVSKGAP FRRPLYTNVP 

      1090       1100       1110       1120       1130       1140 
FLVALALLSS VLVGLVLVPG LLQGPLALRN ITDTGFKLLL LGLVTLNFVG AFMLESVLDQ 

      1150       1160       1170       1180 
CLPACLRRLR PKRASKKRFK QLERELAEQP WPPLPAGPLR 

« Hide

Isoform B [UniParc].

Checksum: 1A7D35DF1CD34396
Show »

FASTA1,158125,977
Isoform 3 [UniParc].

Checksum: 6418CB82F086E30C
Show »

FASTA1,175128,323

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Clinical spectrum of Kufor-Rakeb syndrome in the Chilean kindred with ATP13A2 mutations."
Behrens M.I., Bruggemann N., Chana P., Venegas P., Kagi M., Parrao T., Orellana P., Garrido C., Rojas C.V., Hauke J., Hahnen E., Gonzalez R., Seleme N., Fernandez V., Schmidt A., Binkofski F., Kompf D., Kubisch C. expand/collapse author list , Hagenah J., Klein C., Ramirez A.
Mov. Disord. 25:1929-1937(2010) [PubMed] [Europe PMC] [Abstract]
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]"ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease."
Di Fonzo A., Chien H.F., Socal M., Giraudo S., Tassorelli C., Iliceto G., Fabbrini G., Marconi R., Fincati E., Abbruzzese G., Marini P., Squitieri F., Horstink M.W., Montagna P., Libera A.D., Stocchi F., Goldwurm S., Ferreira J.J. expand/collapse author list , Meco G., Martignoni E., Lopiano L., Jardim L.B., Oostra B.A., Barbosa E.R., Bonifati V.
Neurology 68:1557-1562(2007) [PubMed] [Europe PMC] [Abstract]
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]"ATP13A2 variability in Parkinson disease."
Vilarino-Guell C., Soto A.I., Lincoln S.J., Ben Yahmed S., Kefi M., Heckman M.G., Hulihan M.M., Chai H., Diehl N.N., Amouri R., Rajput A., Mash D.C., Dickson D.W., Middleton L.T., Gibson R.A., Hentati F., Farrer M.J.
Hum. Mutat. 30:406-410(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-49; GLN-294; LEU-389; GLY-578; TRP-762; ILE-776 AND PHE-946.
[17]"Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability."
Santoro L., Breedveld G.J., Manganelli F., Iodice R., Pisciotta C., Nolano M., Punzo F., Quarantelli M., Pappata S., Di Fonzo A., Oostra B.A., Bonifati V.
Neurogenetics 12:33-39(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS175.1. [Q9NQ11-1]
CCDS44072.1. [Q9NQ11-2]
CCDS44073.1. [Q9NQ11-3]
RefSeqNP_001135445.1. NM_001141973.1. [Q9NQ11-3]
NP_001135446.1. NM_001141974.1. [Q9NQ11-2]
NP_071372.1. NM_022089.2. [Q9NQ11-1]
UniGeneHs.128866.

3D structure databases

ProteinModelPortalQ9NQ11.
SMRQ9NQ11. Positions 254-1033.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116973. 49 interactions.
IntActQ9NQ11. 43 interactions.
MINTMINT-4781194.
STRING9606.ENSP00000327214.

Protein family/group databases

TCDB3.A.3.10.7. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteQ9NQ11.

Polymorphism databases

DMDM14285364.

Proteomic databases

MaxQBQ9NQ11.
PaxDbQ9NQ11.
PRIDEQ9NQ11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326735; ENSP00000327214; ENSG00000159363. [Q9NQ11-1]
ENST00000341676; ENSP00000341115; ENSG00000159363. [Q9NQ11-2]
ENST00000452699; ENSP00000413307; ENSG00000159363. [Q9NQ11-3]
GeneID23400.
KEGGhsa:23400.
UCSCuc001baa.2. human. [Q9NQ11-1]
uc001bab.2. human. [Q9NQ11-3]

Organism-specific databases

CTD23400.
GeneCardsGC01M017312.
GeneReviewsATP13A2.
HGNCHGNC:30213. ATP13A2.
HPACAB037111.
MIM606693. phenotype.
610513. gene.
neXtProtNX_Q9NQ11.
Orphanet306674. Kufor-Rakeb syndrome.
314632. Parkinsonim due to ATP13A2 deficiency.
PharmGKBPA134897221.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000171813.
HOVERGENHBG065757.
InParanoidQ9NQ11.
KOK13526.
OMAWQLFTVQ.
OrthoDBEOG7B5WV2.
PhylomeDBQ9NQ11.
TreeFamTF300331.

Gene expression databases

ArrayExpressQ9NQ11.
BgeeQ9NQ11.
CleanExHS_ATP13A2.
GenevestigatorQ9NQ11.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR004014. ATPase_P-typ_cation-transptr_N.
IPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP13A2. human.
GeneWikiATP13A2.
GenomeRNAi23400.
NextBio45553.
PROQ9NQ11.
SOURCESearch...

Entry information

Entry nameAT132_HUMAN
AccessionPrimary (citable) accession number: Q9NQ11
Secondary accession number(s): O75700 expand/collapse secondary AC list , Q5JXY1, Q5JXY2, Q6S9Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM