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Cation-transporting ATPase 13A2 (EC 3.6.3.-)

 AT132_HUMAN             Reviewed;        1180 AA.
Q9NQ11; O75700; Q5JXY1; Q5JXY2; Q6S9Z9;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
25-OCT-2017, entry version 162.
RecName: Full=Cation-transporting ATPase 13A2;
EC=3.6.3.-;
Name=ATP13A2 {ECO:0000312|HGNC:HGNC:30213};
Synonyms=PARK9 {ECO:0000303|PubMed:21542062};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Rhodes S., Huckle E.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Liu J.-P., Li H.;
"Homo sapiens putative ATPase (N-ATPase) mRNA.";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Brain, and Fetus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1180 (ISOFORM A).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 855-1180 (ISOFORM B).
Casciano I., Volpi E.V., De Ambrosis A., Marchi J.M., Romani M.;
"YAC analysis and genes identification at a site of viral integration
in the 1p36.1-36.2 chromosomal site.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=22186024; DOI=10.1093/hmg/ddr606;
Ramonet D., Podhajska A., Stafa K., Sonnay S., Trancikova A.,
Tsika E., Pletnikova O., Troncoso J.C., Glauser L., Moore D.J.;
"PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
and regulates cation homeostasis and neuronal integrity.";
Hum. Mol. Genet. 21:1725-1743(2012).
[10]
INVOLVEMENT IN KRS.
PubMed=16964263; DOI=10.1038/ng1884;
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.;
"Hereditary parkinsonism with dementia is caused by mutations in
ATP13A2, encoding a lysosomal type 5 P-type ATPase.";
Nat. Genet. 38:1184-1191(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
VARIANT KRS ARG-504, AND VARIANTS MET-12 AND ARG-533.
PubMed=17485642; DOI=10.1212/01.wnl.0000260963.08711.08;
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., Meco G., Martignoni E.,
Lopiano L., Jardim L.B., Oostra B.A., Barbosa E.R., Bonifati V.;
"ATP13A2 missense mutations in juvenile parkinsonism and young onset
Parkinson disease.";
Neurology 68:1557-1562(2007).
[13]
VARIANT KRS LEU-182.
PubMed=18413573; DOI=10.1212/01.wnl.0000310427.72236.68;
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.;
"PARK9-linked parkinsonism in eastern Asia: mutation detection in
ATP13A2 and clinical phenotype.";
Neurology 70:1491-1493(2008).
[14]
VARIANT THR-746.
PubMed=19015489; DOI=10.1212/01.wnl.0000335167.72412.68;
Lin C.H., Tan E.K., Chen M.L., Tan L.C., Lim H.Q., Chen G.S., Wu R.M.;
"Novel ATP13A2 variant associated with Parkinson disease in Taiwan and
Singapore.";
Neurology 71:1727-1732(2008).
[15]
VARIANTS SER-49; GLN-294; LEU-389; GLY-578; TRP-762; ILE-776 AND
PHE-946.
PubMed=19085912; DOI=10.1002/humu.20877;
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.;
"ATP13A2 variability in Parkinson disease.";
Hum. Mutat. 30:406-410(2009).
[16]
INVOLVEMENT IN KRS.
PubMed=20683840; DOI=10.1002/mds.22996;
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., Hagenah J., Klein C., Ramirez A.;
"Clinical spectrum of Kufor-Rakeb syndrome in the Chilean kindred with
ATP13A2 mutations.";
Mov. Disord. 25:1929-1937(2010).
[17]
VARIANT KRS ARG-1059, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
VARIANT KRS ARG-1059.
PubMed=21542062; DOI=10.1002/humu.21527;
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.;
"Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
(PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
parkinsonism.";
Hum. Mutat. 32:956-964(2011).
[18]
VARIANT KRS ARG-877.
PubMed=20853184; DOI=10.1007/s10048-010-0259-0;
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.;
"Novel ATP13A2 (PARK9) homozygous mutation in a family with marked
phenotype variability.";
Neurogenetics 12:33-39(2011).
[19]
VARIANT KRS ARG-854.
PubMed=22388936; DOI=10.1093/hmg/dds089;
Bras J., Verloes A., Schneider S.A., Mole S.E., Guerreiro R.J.;
"Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-
lipofuscinosis.";
Hum. Mol. Genet. 21:2646-2650(2012).
[20]
VARIANT KRS VAL-522, AND FUNCTION.
PubMed=22296644; DOI=10.1016/j.neurobiolaging.2011.12.035;
Gruenewald A., Arns B., Seibler P., Rakovic A., Muenchau A.,
Ramirez A., Sue C.M., Klein C.;
"ATP13A2 mutations impair mitochondrial function in fibroblasts from
patients with Kufor-Rakeb syndrome.";
Neurobiol. Aging 33:1843.E1-1843.E7(2012).
[21]
FUNCTION, CHARACTERIZATION OF VARIANTS KRS MET-12; LEU-182; ARG-504;
ARG-533; THR-746 AND ARG-877, SUBCELLULAR LOCATION, AND CATALYTIC
ACTIVITY.
PubMed=22768177; DOI=10.1371/journal.pone.0039942;
Podhajska A., Musso A., Trancikova A., Stafa K., Moser R., Sonnay S.,
Glauser L., Moore D.J.;
"Common pathogenic effects of missense mutations in the P-type ATPase
ATP13A2 (PARK9) associated with early-onset parkinsonism.";
PLoS ONE 7:E39942-E39942(2012).
[22]
INVOLVEMENT IN SPG78.
PubMed=27217339; DOI=10.1093/brain/aww111;
Kara E., Tucci A., Manzoni C., Lynch D.S., Elpidorou M.,
Bettencourt C., Chelban V., Manole A., Hamed S.A., Haridy N.A.,
Federoff M., Preza E., Hughes D., Pittman A., Jaunmuktane Z.,
Brandner S., Xiromerisiou G., Wiethoff S., Schottlaender L.,
Proukakis C., Morris H., Warner T., Bhatia K.P., Korlipara L.V.,
Singleton A.B., Hardy J., Wood N.W., Lewis P.A., Houlden H.;
"Genetic and phenotypic characterization of complex hereditary spastic
paraplegia.";
Brain 139:1904-1918(2016).
[23]
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, AND MUTAGENESIS OF ASP-513.
PubMed=28137957; DOI=10.1093/brain/aww307;
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.;
"Loss-of-function mutations in the ATP13A2/PARK9 gene cause
complicated hereditary spastic paraplegia (SPG78).";
Brain 140:287-305(2017).
-!- FUNCTION: ATPase that plays a role in intracellular cation
homeostasis and the maintenance of neuronal integrity
(PubMed:22186024). Required for a proper lysosomal and
mitochondrial maintenance (PubMed:22296644, PubMed:28137957).
{ECO:0000269|PubMed:22186024, ECO:0000269|PubMed:22296644,
ECO:0000269|PubMed:28137957}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:22768177}.
-!- INTERACTION:
Q2M2I8:AAK1; NbExp=2; IntAct=EBI-6308763, EBI-1383433;
O60238:BNIP3L; NbExp=2; IntAct=EBI-6308763, EBI-849893;
O14976:GAK; NbExp=2; IntAct=EBI-6308763, EBI-714707;
Q9UBN7:HDAC6; NbExp=2; IntAct=EBI-6308763, EBI-301697;
P11142:HSPA8; NbExp=2; IntAct=EBI-6308763, EBI-351896;
Q9BT88:SYT11; NbExp=2; IntAct=EBI-6308763, EBI-751770;
O95070:YIF1A; NbExp=2; IntAct=EBI-6308763, EBI-2799703;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Lysosome {ECO:0000269|PubMed:21542062,
ECO:0000269|PubMed:22186024, ECO:0000269|PubMed:28137957}.
Lysosome membrane {ECO:0000269|PubMed:22768177}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=Q9NQ11-1; Sequence=Displayed;
Name=B;
IsoId=Q9NQ11-2; Sequence=VSP_007310, VSP_007311, VSP_007312;
Name=3;
IsoId=Q9NQ11-3; Sequence=VSP_007310;
-!- 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).
{ECO:0000269|PubMed:22186024}.
-!- PTM: Autophosphorylated. {ECO:0000305|PubMed:28137957}.
-!- 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}. Note=The disease is caused by
mutations 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}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type V subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA08912.1; Type=Frameshift; Positions=1054; Evidence={ECO:0000305};
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EMBL; AL354615; CAB89728.1; -; mRNA.
EMBL; AY461712; AAR23423.1; -; mRNA.
EMBL; AK290210; BAF82899.1; -; mRNA.
EMBL; AL049569; CAI20366.1; -; Genomic_DNA.
EMBL; CH471134; EAW94825.1; -; Genomic_DNA.
EMBL; CH471134; EAW94827.1; -; Genomic_DNA.
EMBL; BC030267; AAH30267.1; -; mRNA.
EMBL; AL833966; CAD38813.2; -; mRNA.
EMBL; AJ009947; CAA08912.1; ALT_FRAME; mRNA.
CCDS; CCDS175.1; -. [Q9NQ11-1]
CCDS; CCDS44072.1; -. [Q9NQ11-2]
CCDS; CCDS44073.1; -. [Q9NQ11-3]
RefSeq; NP_001135445.1; NM_001141973.2. [Q9NQ11-3]
RefSeq; NP_001135446.1; NM_001141974.2. [Q9NQ11-2]
RefSeq; NP_071372.1; NM_022089.3. [Q9NQ11-1]
UniGene; Hs.128866; -.
ProteinModelPortal; Q9NQ11; -.
BioGrid; 116973; 82.
IntAct; Q9NQ11; 49.
MINT; MINT-4781194; -.
STRING; 9606.ENSP00000327214; -.
TCDB; 3.A.3.10.7; the p-type atpase (p-atpase) superfamily.
iPTMnet; Q9NQ11; -.
PhosphoSitePlus; Q9NQ11; -.
BioMuta; ATP13A2; -.
DMDM; 14285364; -.
MaxQB; Q9NQ11; -.
PaxDb; Q9NQ11; -.
PeptideAtlas; Q9NQ11; -.
PRIDE; Q9NQ11; -.
Ensembl; ENST00000326735; ENSP00000327214; ENSG00000159363. [Q9NQ11-1]
Ensembl; ENST00000341676; ENSP00000341115; ENSG00000159363. [Q9NQ11-2]
Ensembl; ENST00000452699; ENSP00000413307; ENSG00000159363. [Q9NQ11-3]
GeneID; 23400; -.
KEGG; hsa:23400; -.
UCSC; uc001baa.3; human. [Q9NQ11-1]
CTD; 23400; -.
DisGeNET; 23400; -.
EuPathDB; HostDB:ENSG00000159363.17; -.
GeneCards; ATP13A2; -.
GeneReviews; ATP13A2; -.
HGNC; HGNC:30213; ATP13A2.
HPA; CAB037038; -.
HPA; CAB037111; -.
HPA; HPA050910; -.
HPA; HPA054717; -.
MalaCards; ATP13A2; -.
MIM; 606693; phenotype.
MIM; 610513; gene.
MIM; 617225; phenotype.
neXtProt; NX_Q9NQ11; -.
OpenTargets; ENSG00000159363; -.
Orphanet; 306674; Kufor-Rakeb syndrome.
Orphanet; 314632; Parkinsonim due to ATP13A2 deficiency.
PharmGKB; PA134897221; -.
eggNOG; KOG0208; Eukaryota.
eggNOG; ENOG410XRCA; LUCA.
GeneTree; ENSGT00530000063001; -.
HOGENOM; HOG000171813; -.
HOVERGEN; HBG065757; -.
InParanoid; Q9NQ11; -.
KO; K13526; -.
OMA; PYCPETH; -.
OrthoDB; EOG091G01IL; -.
PhylomeDB; Q9NQ11; -.
TreeFam; TF300331; -.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP13A2; human.
GeneWiki; ATP13A2; -.
GenomeRNAi; 23400; -.
PRO; PR:Q9NQ11; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159363; -.
CleanEx; HS_ATP13A2; -.
ExpressionAtlas; Q9NQ11; baseline and differential.
Genevisible; Q9NQ11; HS.
GO; GO:0005776; C:autophagosome; IDA:ParkinsonsUK-UCL.
GO; GO:1905103; C:integral component of lysosomal membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0016021; C:integral component of membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005770; C:late endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005771; C:multivesicular body; IDA:ParkinsonsUK-UCL.
GO; GO:0032585; C:multivesicular body membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0030133; C:transport vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0031982; C:vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; NAS:ParkinsonsUK-UCL.
GO; GO:0005388; F:calcium-transporting ATPase activity; IBA:GO_Central.
GO; GO:0019829; F:cation-transporting ATPase activity; TAS:Reactome.
GO; GO:1903135; F:cupric ion binding; ISS:ParkinsonsUK-UCL.
GO; GO:0030145; F:manganese ion binding; ISS:ParkinsonsUK-UCL.
GO; GO:0070300; F:phosphatidic acid binding; IDA:ParkinsonsUK-UCL.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; ISS:ParkinsonsUK-UCL.
GO; GO:1905037; P:autophagosome organization; IDA:ParkinsonsUK-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:ParkinsonsUK-UCL.
GO; GO:0030003; P:cellular cation homeostasis; TAS:ParkinsonsUK-UCL.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:ParkinsonsUK-UCL.
GO; GO:0071287; P:cellular response to manganese ion; IMP:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0071294; P:cellular response to zinc ion; TAS:ParkinsonsUK-UCL.
GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:ParkinsonsUK-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; ISS:ParkinsonsUK-UCL.
GO; GO:1990938; P:peptidyl-aspartic acid autophosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:1905122; P:polyamine import; IDA:ParkinsonsUK-UCL.
GO; GO:1903543; P:positive regulation of exosomal secretion; IDA:ParkinsonsUK-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:ParkinsonsUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; TAS:ParkinsonsUK-UCL.
GO; GO:0016243; P:regulation of autophagosome size; IDA:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:1904714; P:regulation of chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0052548; P:regulation of endopeptidase activity; IMP:ParkinsonsUK-UCL.
GO; GO:1905123; P:regulation of glucosylceramidase activity; IEA:Ensembl.
GO; GO:0033157; P:regulation of intracellular protein transport; NAS:ParkinsonsUK-UCL.
GO; GO:1905165; P:regulation of lysosomal protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0016241; P:regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0010821; P:regulation of mitochondrion organization; IDA:ParkinsonsUK-UCL.
GO; GO:0055069; P:zinc ion homeostasis; IMP:ParkinsonsUK-UCL.
Gene3D; 3.40.1110.10; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006544; P-type_TPase_V.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF12409; P5-ATPase; 1.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR01657; P-ATPase-V; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Disease mutation; Hereditary spastic paraplegia; Hydrolase; Lysosome;
Magnesium; Membrane; Metal-binding; Neurodegeneration;
Neuronal ceroid lipofuscinosis; Nucleotide-binding; Parkinsonism;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1180 Cation-transporting ATPase 13A2.
/FTId=PRO_0000046423.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 34 Helical. {ECO:0000255}.
TOPO_DOM 35 45 Extracellular. {ECO:0000255}.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TOPO_DOM 67 230 Cytoplasmic. {ECO:0000255}.
TRANSMEM 231 253 Helical. {ECO:0000255}.
TOPO_DOM 254 256 Extracellular. {ECO:0000255}.
TRANSMEM 257 276 Helical. {ECO:0000255}.
TOPO_DOM 277 425 Cytoplasmic. {ECO:0000255}.
TRANSMEM 426 445 Helical. {ECO:0000255}.
TOPO_DOM 446 459 Extracellular. {ECO:0000255}.
TRANSMEM 460 480 Helical. {ECO:0000255}.
TOPO_DOM 481 932 Cytoplasmic. {ECO:0000255}.
TRANSMEM 933 952 Helical. {ECO:0000255}.
TOPO_DOM 953 963 Extracellular. {ECO:0000255}.
TRANSMEM 964 981 Helical. {ECO:0000255}.
TOPO_DOM 982 997 Cytoplasmic. {ECO:0000255}.
TRANSMEM 998 1018 Helical. {ECO:0000255}.
TOPO_DOM 1019 1046 Extracellular. {ECO:0000255}.
TRANSMEM 1047 1066 Helical. {ECO:0000255}.
TOPO_DOM 1067 1079 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1080 1097 Helical. {ECO:0000255}.
TOPO_DOM 1098 1113 Extracellular. {ECO:0000255}.
TRANSMEM 1114 1134 Helical. {ECO:0000255}.
TOPO_DOM 1135 1180 Cytoplasmic. {ECO:0000255}.
ACT_SITE 513 513 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 878 878 Magnesium. {ECO:0000250}.
METAL 882 882 Magnesium. {ECO:0000250}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 155 159 Missing (in isoform B and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2, ECO:0000303|Ref.8}.
/FTId=VSP_007310.
VAR_SEQ 805 843 Missing (in isoform B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.8}.
/FTId=VSP_007311.
VAR_SEQ 1079 1180 VPFLVALALLSSVLVGLVLVPGLLQGPLALRNITDTGFKLL
LLGLVTLNFVGAFMLESVLDQCLPACLRRLRPKRASKKRFK
QLERELAEQPWPPLPAGPLR -> ERARPVPPRLPAPPPAQ
AGLQEALQAAGTRAGRAALAAAARRPPEVVQAHGHPRHWNS
LPLSHQLDPSPATPPPPPPTSLRLATVYTPPPRPPPPWGSV
DYCPLPWTIPRRGGSPQLPSVLLSV (in isoform B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.8}.
/FTId=VSP_007312.
VARIANT 12 12 T -> M (in KRS; no effect on stability;
no effect on location; decreased ATPase
activity; dbSNP:rs151117874).
{ECO:0000269|PubMed:17485642,
ECO:0000269|PubMed:22768177}.
/FTId=VAR_058451.
VARIANT 49 49 G -> S (in dbSNP:rs56379718).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058452.
VARIANT 182 182 F -> L (in KRS; decreased protein
stability; loss of autophosphorylation;
increased degradation by proteasome;
novel location to endoplasmic reticulum;
loss of lysosomal membrane location).
{ECO:0000269|PubMed:18413573,
ECO:0000269|PubMed:22768177,
ECO:0000269|PubMed:28137957}.
/FTId=VAR_066019.
VARIANT 294 294 R -> Q (in dbSNP:rs56367069).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058453.
VARIANT 389 389 P -> L (in dbSNP:rs56275621).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058454.
VARIANT 504 504 G -> R (in KRS; decreased protein
stability; increased degradation by
proteasome; novel location to endoplasmic
reticulum; loss of lysosomal membrane
location; dbSNP:rs121918227).
{ECO:0000269|PubMed:17485642,
ECO:0000269|PubMed:22768177}.
/FTId=VAR_058455.
VARIANT 517 517 T -> I (in SPG78; no effect on protein
stability; loss of autophosphorylation;
loss of lysosomal location).
{ECO:0000269|PubMed:28137957}.
/FTId=VAR_078055.
VARIANT 522 522 G -> V (in KRS; unknown pathological
significance).
{ECO:0000269|PubMed:22296644}.
/FTId=VAR_078056.
VARIANT 533 533 G -> R (in a patient with early onset
Parkinson disease and KRS; decreased
ATPase activity; no effect on
autophosphorylation; no effect on
stability; no effect on location).
{ECO:0000269|PubMed:17485642,
ECO:0000269|PubMed:22768177,
ECO:0000269|PubMed:28137957}.
/FTId=VAR_058456.
VARIANT 578 578 V -> G (in dbSNP:rs56186751).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058457.
VARIANT 746 746 A -> T (in KRS; decreased ATPase
activity; no effect on stability; no
effect on location; dbSNP:rs147277743).
{ECO:0000269|PubMed:19015489,
ECO:0000269|PubMed:22768177}.
/FTId=VAR_058458.
VARIANT 762 762 R -> W (in dbSNP:rs55635527).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058459.
VARIANT 776 776 V -> I (in dbSNP:rs56170027).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058460.
VARIANT 854 854 M -> R (in KRS; some patients manifest
neuropathologic findings suggestive of
neuronal ceroid lipofuscinosis;
dbSNP:rs587777053).
{ECO:0000269|PubMed:22388936}.
/FTId=VAR_070194.
VARIANT 877 877 G -> R (in KRS; found in two affected
brothers also carrying C-481 in FBXO7;
decreased protein stability; increased
degradation by proteasome; novel location
to endoplasmic reticulum;
dbSNP:rs144701072).
{ECO:0000269|PubMed:20853184,
ECO:0000269|PubMed:22768177}.
/FTId=VAR_066020.
VARIANT 946 946 I -> F (in dbSNP:rs55708915).
{ECO:0000269|PubMed:19085912}.
/FTId=VAR_058461.
VARIANT 1059 1059 L -> R (in KRS; the mutant protein is
retained in the endoplasmic reticulum;
dbSNP:rs137853967).
{ECO:0000269|PubMed:21542062}.
/FTId=VAR_066021.
MUTAGEN 513 513 D->N: Loss of ATPase function.
{ECO:0000269|PubMed:28137957}.
CONFLICT 322 322 Q -> R (in Ref. 6; AAH30267).
{ECO:0000305}.
CONFLICT 855 858 APEQ -> IPRA (in Ref. 8; CAA08912).
{ECO:0000305}.
CONFLICT 861 861 E -> V (in Ref. 8; CAA08912).
{ECO:0000305}.
SEQUENCE 1180 AA; 128794 MW; 98D13745D3B615BE CRC64;
MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY HVVVWMMAGI
PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW QLFTVQVQTE AIGEGSLEPS
PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK SEEAVSVGQK RVLRYYLFQG QRYIWIETQQ
AFYQVSLLDH GRSCDDVHRS RHGLSLQDQM VRKAIYGPNV ISIPVKSYPQ LLVDEALNPY
YGFQAFSIAL WLADHYYWYA LCIFLISSIS ICLSLYKTRK QSQTLRDMVK LSMRVCVCRP
GGEEEWVDSS ELVPGDCLVL PQEGGLMPCD AALVAGECMV NESSLTGESI PVLKTALPEG
LGPYCAETHR RHTLFCGTLI LQARAYVGPH VLAVVTRTGF CTAKGGLVSS ILHPRPINFK
FYKHSMKFVA ALSVLALLGT IYSIFILYRN RVPLNEIVIR ALDLVTVVVP PALPAAMTVC
TLYAQSRLRR QGIFCIHPLR INLGGKLQLV CFDKTGTLTE DGLDVMGVVP LKGQAFLPLV
PEPRRLPVGP LLRALATCHA LSRLQDTPVG DPMDLKMVES TGWVLEEEPA ADSAFGTQVL
AVMRPPLWEP QLQAMEEPPV PVSVLHRFPF SSALQRMSVV VAWPGATQPE AYVKGSPELV
AGLCNPETVP TDFAQMLQSY TAAGYRVVAL ASKPLPTVPS LEAAQQLTRD TVEGDLSLLG
LLVMRNLLKP QTTPVIQALR RTRIRAVMVT GDNLQTAVTV ARGCGMVAPQ EHLIIVHATH
PERGQPASLE FLPMESPTAV NGVKDPDQAA SYTVEPDPRS RHLALSGPTF GIIVKHFPKL
LPKVLVQGTV FARMAPEQKT ELVCELQKLQ YCVGMCGDGA NDCGALKAAD VGISLSQAEA
SVVSPFTSSM ASIECVPMVI REGRCSLDTS FSVFKYMALY SLTQFISVLI LYTINTNLGD
LQFLAIDLVI TTTVAVLMSR TGPALVLGRV RPPGALLSVP VLSSLLLQMV LVTGVQLGGY
FLTLAQPWFV PLNRTVAAPD NLPNYENTVV FSLSSFQYLI LAAAVSKGAP FRRPLYTNVP
FLVALALLSS VLVGLVLVPG LLQGPLALRN ITDTGFKLLL LGLVTLNFVG AFMLESVLDQ
CLPACLRRLR PKRASKKRFK QLERELAEQP WPPLPAGPLR


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