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Serine/threonine-protein kinase PINK1, mitochondrial (EC 2.7.11.1) (BRPK) (PTEN-induced putative kinase protein 1)

 PINK1_HUMAN             Reviewed;         581 AA.
Q9BXM7; Q8N6T9; Q8NBU3; Q96DE4;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 169.
RecName: Full=Serine/threonine-protein kinase PINK1, mitochondrial;
EC=2.7.11.1 {ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582};
AltName: Full=BRPK;
AltName: Full=PTEN-induced putative kinase protein 1;
Flags: Precursor;
Name=PINK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAK28062.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Endometrium {ECO:0000269|PubMed:11494141};
PubMed=11494141; DOI=10.1038/sj.onc.1204608;
Unoki M., Nakamura Y.;
"Growth-suppressive effects of BPOZ and EGR2, two genes involved in
the PTEN signaling pathway.";
Oncogene 20:4457-4465(2001).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND
AUTOPHOSPHORYLATION.
TISSUE=Placenta {ECO:0000312|EMBL:AAK28062.1};
PubMed=14607334; DOI=10.1016/S0304-3835(03)00443-9;
Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.;
"BRPK, a novel protein kinase showing increased expression in mouse
cancer cell lines with higher metastatic potential.";
Cancer Lett. 201:195-201(2003).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
THR-340 AND THR-521.
TISSUE=Placenta {ECO:0000312|EMBL:BAC11484.1};
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] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Leukocyte {ECO:0000312|EMBL:AAH28215.1}, and
Lung {ECO:0000312|EMBL:AAH09534.1};
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).
[6]
SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
PubMed=18687899; DOI=10.1073/pnas.0802814105;
Zhou C., Huang Y., Shao Y., May J., Prou D., Perier C., Dauer W.,
Schon E.A., Przedborski S.;
"The kinase domain of mitochondrial PINK1 faces the cytoplasm.";
Proc. Natl. Acad. Sci. U.S.A. 105:12022-12027(2008).
[7]
FUNCTION, COMPONENT OF A COMPLEX COMPOSED OF PRKN; PARK7 AND PINK1,
SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, CHARACTERIZATION OF
VARIANTS PARK6 ASP-309 AND MET-313, AND CHARACTERIZATION OF VARIANT
LEU-399.
PubMed=19229105; DOI=10.1172/JCI37617;
Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K.,
Jiang W., Ronai Z., Zhuang X., Zhang Z.;
"Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting
unfolded protein degradation.";
J. Clin. Invest. 119:650-660(2009).
[8]
FUNCTION IN MITOCHONDRIAL AUTOPHAGY, SUBCELLULAR LOCATION, INTERACTION
WITH PRKN, AND CHARACTERIZATION OF VARIANTS PARK6 PRO-126; ASP-309 AND
PRO-347.
PubMed=20798600; DOI=10.4161/auto.6.7.13286;
Geisler S., Holmstrom K.M., Treis A., Skujat D., Weber S.S.,
Fiesel F.C., Kahle P.J., Springer W.;
"The PINK1/Parkin-mediated mitophagy is compromised by PD-associated
mutations.";
Autophagy 6:871-878(2010).
[9]
FUNCTION IN MITOCHONDRIAL AUTOPHAGY.
PubMed=20404107; DOI=10.1083/jcb.200910140;
Matsuda N., Sato S., Shiba K., Okatsu K., Saisho K., Gautier C.A.,
Sou Y.S., Saiki S., Kawajiri S., Sato F., Kimura M., Komatsu M.,
Hattori N., Tanaka K.;
"PINK1 stabilized by mitochondrial depolarization recruits Parkin to
damaged mitochondria and activates latent Parkin for mitophagy.";
J. Cell Biol. 189:211-221(2010).
[10]
FUNCTION IN MITOCHONDRIAL AUTOPHAGY, AND INTERACTION WITH PRKN.
PubMed=19966284; DOI=10.1073/pnas.0911187107;
Vives-Bauza C., Zhou C., Huang Y., Cui M., de Vries R.L., Kim J.,
May J., Tocilescu M.A., Liu W., Ko H.S., Magrane J., Moore D.J.,
Dawson V.L., Grailhe R., Dawson T.M., Li C., Tieu K., Przedborski S.;
"PINK1-dependent recruitment of Parkin to mitochondria in mitophagy.";
Proc. Natl. Acad. Sci. U.S.A. 107:378-383(2010).
[11]
INVOLVEMENT IN PARK6.
PubMed=22043288; DOI=10.1371/journal.pone.0025622;
Abramov A.Y., Gegg M., Grunewald A., Wood N.W., Klein C.,
Schapira A.H.;
"Bioenergetic consequences of PINK1 mutations in Parkinson disease.";
PLoS ONE 6:E25622-E25622(2011).
[12]
PHOSPHORYLATION AT SER-228 AND SER-402.
PubMed=22910362; DOI=10.1038/ncomms2016;
Okatsu K., Oka T., Iguchi M., Imamura K., Kosako H., Tani N.,
Kimura M., Go E., Koyano F., Funayama M., Shiba-Fukushima K., Sato S.,
Shimizu H., Fukunaga Y., Taniguchi H., Komatsu M., Hattori N.,
Mihara K., Tanaka K., Matsuda N.;
"PINK1 autophosphorylation upon membrane potential dissipation is
essential for Parkin recruitment to damaged mitochondria.";
Nat. Commun. 3:1016-1016(2012).
[13]
FUNCTION.
PubMed=23754282; DOI=10.1074/jbc.M113.467530;
Iguchi M., Kujuro Y., Okatsu K., Koyano F., Kosako H., Kimura M.,
Suzuki N., Uchiyama S., Tanaka K., Matsuda N.;
"Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-
dependent phosphorylation.";
J. Biol. Chem. 288:22019-22032(2013).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FBXO7.
PubMed=23933751; DOI=10.1038/nn.3489;
Burchell V.S., Nelson D.E., Sanchez-Martinez A., Delgado-Camprubi M.,
Ivatt R.M., Pogson J.H., Randle S.J., Wray S., Lewis P.A., Houlden H.,
Abramov A.Y., Hardy J., Wood N.W., Whitworth A.J., Laman H.,
Plun-Favreau H.;
"The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to
mediate mitophagy.";
Nat. Neurosci. 16:1257-1265(2013).
[15]
FUNCTION IN MITOPHAGY, AND MUTAGENESIS OF LYS-219; ASP-362 AND
ASP-384.
PubMed=23620051; DOI=10.1126/science.1231031;
Chen Y., Dorn G.W. II;
"PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling
damaged mitochondria.";
Science 340:471-475(2013).
[16]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24660806; DOI=10.1042/BJ20140334;
Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G.,
Ritorto M.S., Hofmann K., Alessi D.R., Knebel A., Trost M.,
Muqit M.M.;
"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin
at Ser65.";
Biochem. J. 460:127-139(2014).
[17]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24751536; DOI=10.1083/jcb.201402104;
Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
Banerjee S., Youle R.J.;
"PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
activity.";
J. Cell Biol. 205:143-153(2014).
[18]
FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS PARK6
PRO-168 AND ALA-386.
PubMed=24784582; DOI=10.1038/nature13392;
Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M.,
Kimura Y., Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A.,
Trempe J.F., Saeki Y., Tanaka K., Matsuda N.;
"Ubiquitin is phosphorylated by PINK1 to activate parkin.";
Nature 510:162-166(2014).
[19]
FUNCTION.
PubMed=24896179; DOI=10.1038/nature13418;
Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q.,
Foreman O., Kirkpatrick D.S., Sheng M.;
"The mitochondrial deubiquitinase USP30 opposes parkin-mediated
mitophagy.";
Nature 510:370-375(2014).
[20]
VARIANTS PARK6 GLY-170 AND 456-GLN--LEU-581 DEL.
PubMed=24652937; DOI=10.1126/science.1249161;
Morais V.A., Haddad D., Craessaerts K., De Bock P.J., Swerts J.,
Vilain S., Aerts L., Overbergh L., Gruenewald A., Seibler P.,
Klein C., Gevaert K., Verstreken P., De Strooper B.;
"PINK1 loss-of-function mutations affect mitochondrial complex I
activity via NdufA10 ubiquinone uncoupling.";
Science 344:203-207(2014).
[21]
FUNCTION.
PubMed=25527291; DOI=10.15252/embj.201489847;
Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
"Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
assembly and hydrolysis.";
EMBO J. 34:307-325(2015).
[22]
VARIANTS PARK6 PHE-92; PRO-168 AND HIS-464, AND VARIANTS LEU-296;
THR-340; THR-442; LYS-476; THR-521 AND ASN-525.
PubMed=15349860; DOI=10.1002/ana.20256;
Valente E.M., Salvi S., Ialongo T., Marongiu R., Elia A.E., Caputo V.,
Romito L., Albanese A., Dallapiccola B., Bentivoglio A.R.;
"PINK1 mutations are associated with sporadic early-onset
parkinsonism.";
Ann. Neurol. 56:336-341(2004).
[23]
VARIANTS PARK6 GLN-271; PRO-347 AND GLY-417.
PubMed=15349870; DOI=10.1002/ana.20251;
Hatano Y., Li Y., Sato K., Asakawa S., Yamamura Y., Tomiyama H.,
Yoshino H., Asahina M., Kobayashi S., Hassin-Baer S., Lu C.-S.,
Ng A.R., Rosales R.L., Shimizu N., Toda T., Mizuno Y., Hattori N.;
"Novel PINK1 mutations in early-onset parkinsonism.";
Ann. Neurol. 56:424-427(2004).
[24]
ERRATUM.
Hatano Y., Li Y., Sato K., Asakawa S., Yamamura Y., Tomiyama H.,
Yoshino H., Asahina M., Kobayashi S., Hassin-Baer S., Lu C.-S.,
Ng A.R., Rosales R.L., Shimizu N., Toda T., Mizuno Y., Hattori N.;
Ann. Neurol. 56:603-603(2004).
[25]
VARIANTS PARK6 LYS-240; PRO-347 AND PRO-489, AND VARIANTS GLY-231;
ILE-235; GLY-263; LEU-318; THR-339; THR-340; HIS-362; SER-425; LYS-476
AND THR-521.
PubMed=15596610; DOI=10.1001/archneur.61.12.1898;
Rogaeva E., Johnson J., Lang A.E., Gulick C., Gwinn-Hardy K.,
Kawarai T., Sato C., Morgan A., Werner J., Nussbaum R., Petit A.,
Okun M.S., McInerney A., Mandel R., Groen J.L., Fernandez H.H.,
Postuma R., Foote K.D., Salehi-Rad S., Liang Y., Reimsnider S.,
Tandon A., Hardy J., St George-Hyslop P., Singleton A.B.;
"Analysis of the PINK1 gene in a large cohort of cases with Parkinson
disease.";
Arch. Neurol. 61:1898-1904(2004).
[26]
VARIANT PARK6 HIS-147.
PubMed=15505171; DOI=10.1212/01.WNL.0000142089.38301.8E;
Healy D.G., Abou-Sleiman P.M., Gibson J.M., Ross O.A., Jain S.,
Gandhi S., Gosal D., Muqit M.M.K., Wood N.W., Lynch T.;
"PINK1 (PARK6) associated Parkinson disease in Ireland.";
Neurology 63:1486-1488(2004).
[27]
VARIANT PARK6 ASP-309, CHARACTERIZATION OF VARIANT PARK6 ASP-309,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15087508; DOI=10.1126/science.1096284;
Valente E.M., Abou-Sleiman P.M., Caputo V., Muqit M.M.K., Harvey K.,
Gispert S., Ali Z., Del Turco D., Bentivoglio A.R., Healy D.G.,
Albanese A., Nussbaum R., Gonzalez-Maldonado R., Deller T., Salvi S.,
Cortelli P., Gilks W.P., Latchman D.S., Harvey R.J., Dallapiccola B.,
Auburger G., Wood N.W.;
"Hereditary early-onset Parkinson's disease caused by mutations in
PINK1.";
Science 304:1158-1160(2004).
[28]
VARIANT PARK6 VAL-268.
PubMed=16207217; DOI=10.1111/j.1399-0004.2005.00500.x;
Tan E.K., Yew K., Chua E., Shen H., Jamora R.D., Lee E., Puong K.Y.,
Zhao Y., Pavanni R., Wong M.C., Puvan K., Yih Y., Tan L.C.S.;
"Analysis of PINK1 in Asian patients with familial parkinsonism.";
Clin. Genet. 68:468-470(2005).
[29]
VARIANTS PARK6 HIS-279 AND GLN-534 INS, AND VARIANT LEU-115.
PubMed=15970950; DOI=10.1038/sj.ejhg.5201455;
Klein C., Djarmati A., Hedrich K., Schaefer N., Scaglione C.,
Marchese R., Kock N., Schuele B., Hiller A., Lohnau T., Winkler S.,
Wiegers K., Hering R., Bauer P., Riess O., Abbruzzese G.,
Martinelli P., Pramstaller P.P.;
"PINK1, Parkin, and DJ-1 mutations in Italian patients with early-
onset parkinsonism.";
Eur. J. Hum. Genet. 13:1086-1093(2005).
[30]
CHARACTERIZATION OF VARIANTS PARK6 PRO-168 AND ASP-309.
PubMed=16207731; DOI=10.1093/hmg/ddi377;
Silvestri L., Caputo V., Bellacchio E., Atorino L., Dallapiccola B.,
Valente E.M., Casari G.;
"Mitochondrial import and enzymatic activity of PINK1 mutants
associated to recessive parkinsonism.";
Hum. Mol. Genet. 14:3477-3492(2005).
[31]
VARIANT PARK6 ARG-388.
PubMed=15955953; DOI=10.1212/01.WNL.0000164009.36740.4E;
Li Y., Tomiyama H., Sato K., Hatano Y., Yoshino H., Atsumi M.,
Kitaguchi M., Sasaki S., Kawaguchi S., Miyajima H., Toda T.,
Mizuno Y., Hattori N.;
"Clinicogenetic study of PINK1 mutations in autosomal recessive early-
onset parkinsonism.";
Neurology 64:1955-1957(2005).
[32]
VARIANTS PARK6 PRO-168 AND LEU-196, AND VARIANTS LEU-115; THR-340;
LYS-476 AND THR-521.
PubMed=16009891; DOI=10.1212/01.wnl.0000167546.39375.82;
The Italian Parkinson genetics network;
Bonifati V., Rohe C.F., Breedveld G.J., Fabrizio E., De Mari M.,
Tassorelli C., Tavella A., Marconi R., Nicholl D.J., Chien H.F.,
Fincati E., Abbruzzese G., Marini P., De Gaetano A., Horstink M.W.,
Maat-Kievit J.A., Sampaio C., Antonini A., Stocchi F., Montagna P.,
Toni V., Guidi M., Dalla Libera A., Tinazzi M., De Pandis F.,
Fabbrini G., Goldwurm S., de Klein A., Barbosa E., Lopiano L.,
Martignoni E., Lamberti P., Vanacore N., Meco G., Oostra B.A.;
"Early-onset parkinsonism associated with PINK1 mutations: frequency,
genotypes, and phenotypes.";
Neurology 65:87-95(2005).
[33]
VARIANTS ILE-317; THR-339; THR-383; SER-411; HIS-431; SER-451;
SER-461; LYS-476; PRO-501 AND ARG-575, AND CHARACTERIZATION OF
VARIANTS HIS-431; SER-451; LYS-476; PRO-501 AND ARG-575.
PubMed=16969854; DOI=10.1002/ana.20960;
Abou-Sleiman P.M., Muqit M.M.K., McDonald N.Q., Yang Y.X., Gandhi S.,
Healy D.G., Harvey K., Harvey R.J., Deas E., Bhatia K., Quinn N.,
Lees A., Latchman D.S., Wood N.W.;
"A heterozygous effect for PINK1 mutations in Parkinson's disease?";
Ann. Neurol. 60:414-419(2006).
[34]
VARIANT PARK6 ASP-217.
PubMed=16966503; DOI=10.1001/archneur.63.9.1257;
Leutenegger A.-L., Salih M.A.M., Ibanez P., Mukhtar M.M., Lesage S.,
Arabi A., Lohmann E., Duerr A., Ahmed A.E.M., Brice A.;
"Juvenile-onset Parkinsonism as a result of the first mutation in the
adenosine triphosphate orientation domain of PINK1.";
Arch. Neurol. 63:1257-1261(2006).
[35]
VARIANT PARK6 MET-313.
PubMed=17030667; DOI=10.1001/archneur.63.10.1483;
Chishti M.A., Bohlega S., Ahmed M., Loualich A., Carroll P., Sato C.,
St George-Hyslop P., Westaway D., Rogaeva E.;
"T313M PINK1 mutation in an extended highly consanguineous Saudi
family with early-onset Parkinson disease.";
Arch. Neurol. 63:1483-1485(2006).
[36]
VARIANTS PARK6 GLY-125; LYS-240; PRO-369; ALA-386 AND VAL-409.
PubMed=16401616; DOI=10.1093/brain/awl005;
The French Parkinson's disease genetics study group;
Ibanez P., Lesage S., Lohmann E., Thobois S., De Michele G., Borg M.,
Agid Y., Durr A., Brice A.;
"Mutational analysis of the PINK1 gene in early-onset parkinsonism in
Europe and North Africa.";
Brain 129:686-694(2006).
[37]
VARIANT LEU-399.
PubMed=16632486; DOI=10.1093/hmg/ddl104;
Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H.,
Pan Q., Xia J.-H., Xia K., Zhang Z.;
"Association of PINK1 and DJ-1 confers digenic inheritance of early-
onset Parkinson's disease.";
Hum. Mol. Genet. 15:1816-1825(2006).
[38]
VARIANT PARK6 THR-280, AND VARIANTS THR-340 AND THR-521.
PubMed=16482571; DOI=10.1002/mds.20810;
Tan E.-K., Yew K., Chua E., Puvan K., Shen H., Lee E., Puong K.-Y.,
Zhao Y., Pavanni R., Wong M.-C., Jamora D., de Silva D., Moe K.-T.,
Woon F.-P., Yuen Y., Tan L.;
"PINK1 mutations in sporadic early-onset Parkinson's disease.";
Mov. Disord. 21:789-793(2006).
[39]
VARIANT PARK6 GLN-407, AND VARIANTS THR-340 AND THR-521.
PubMed=16257123; DOI=10.1016/j.neulet.2005.10.005;
Fung H.-C., Chen C.-M., Hardy J., Singleton A.B., Lee-Chen G.-J.,
Wu Y.-R.;
"Analysis of the PINK1 gene in a cohort of patients with sporadic
early-onset parkinsonism in Taiwan.";
Neurosci. Lett. 394:33-36(2006).
[40]
VARIANTS [LARGE SCALE ANALYSIS] TRP-148; SER-196; LEU-209; LEU-215;
THR-339; THR-340; ILE-341; PHE-377; THR-477 AND THR-521.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[41]
VARIANTS PHE-67; PRO-68; TRP-98; SER-111; VAL-124; MET-145; ASN-186;
ILE-257 VAL-268; GLN-276; LEU-296; ILE-317; LEU-322; THR-339; THR-383;
VAL-395; THR-442; LYS-476; ASN-525 AND THR-537.
PubMed=18330912; DOI=10.1002/humu.20719;
The Italian PD study group;
Marongiu R., Ferraris A., Ialongo T., Michiorri S., Soleti F.,
Ferrari F., Elia A.E., Ghezzi D., Albanese A., Altavista M.C.,
Antonini A., Barone P., Brusa L., Cortelli P., Martinelli P.,
Pellecchia M.T., Pezzoli G., Scaglione C., Stanzione P., Tinazzi M.,
Zecchinelli A., Zeviani M., Cassetta E., Garavaglia B.,
Dallapiccola B., Bentivoglio A.R., Valente E.M.;
"PINK1 heterozygous rare variants: prevalence, significance and
phenotypic spectrum.";
Hum. Mutat. 29:565-565(2008).
[42]
VARIANT PARK6 PRO-126.
PubMed=18286320; DOI=10.1007/s00415-008-0763-4;
Prestel J., Gempel K., Hauser T.K., Schweitzer K., Prokisch H.,
Ahting U., Freudenstein D., Bueltmann E., Naegele T., Berg D.,
Klopstock T., Gasser T.;
"Clinical and molecular characterisation of a Parkinson family with a
novel PINK1 mutation.";
J. Neurol. 255:643-648(2008).
[43]
VARIANT PARK6 PRO-347.
PubMed=22956510; DOI=10.1002/mds.25132;
Kilarski L.L., Pearson J.P., Newsway V., Majounie E., Knipe M.D.,
Misbahuddin A., Chinnery P.F., Burn D.J., Clarke C.E., Marion M.H.,
Lewthwaite A.J., Nicholl D.J., Wood N.W., Morrison K.E.,
Williams-Gray C.H., Evans J.R., Sawcer S.J., Barker R.A.,
Wickremaratchi M.M., Ben-Shlomo Y., Williams N.M., Morris H.R.;
"Systematic review and UK-based study of PARK2 (parkin), PINK1, PARK7
(DJ-1) and LRRK2 in early-onset Parkinson's disease.";
Mov. Disord. 27:1522-1529(2012).
-!- FUNCTION: Protects against mitochondrial dysfunction during
cellular stress by phosphorylating mitochondrial proteins.
Involved in the clearance of damaged mitochondria via selective
autophagy (mitophagy) by mediating activation and translocation of
PRKN (PubMed:14607334, PubMed:15087508, PubMed:19229105,
PubMed:19966284, PubMed:20404107, PubMed:20798600,
PubMed:23620051, PubMed:23754282, PubMed:23933751,
PubMed:24660806, PubMed:24751536, PubMed:24784582,
PubMed:24896179, PubMed:25527291). Targets PRKN to dysfunctional
depolarized mitochondria through the phosphorylation of MFN2
(PubMed:23620051). Activates PRKN in 2 steps: (1) by mediating
phosphorylation at 'Ser-65' of PRKN and (2) mediating
phosphorylation of ubiquitin, converting PRKN to its fully-active
form (PubMed:24660806, PubMed:24751536, PubMed:24784582,
PubMed:25527291). Required for ubiquinone reduction by
mitochondrial complex I by mediating phosphorylation of complex I
subunit NDUFA10 (By similarity). {ECO:0000250|UniProtKB:Q99MQ3,
ECO:0000269|PubMed:14607334, ECO:0000269|PubMed:15087508,
ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284,
ECO:0000269|PubMed:20404107, ECO:0000269|PubMed:20798600,
ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282,
ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806,
ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Interacts with PRKN. Interacts with FBXO7. Forms a
complex with PRKN and PARK7 (PubMed:19229105).
{ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284,
ECO:0000269|PubMed:20798600, ECO:0000269|PubMed:23933751}.
-!- INTERACTION:
Q9Y3I1:FBXO7; NbExp=8; IntAct=EBI-2846068, EBI-1161222;
Q9Y3I1-1:FBXO7; NbExp=2; IntAct=EBI-2846068, EBI-9102965;
Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-2846068, EBI-373144;
O60260:PRKN; NbExp=7; IntAct=EBI-2846068, EBI-716346;
Q8IXI2:RHOT1; NbExp=3; IntAct=EBI-2846068, EBI-1396430;
Q8WXH5:SOCS4; NbExp=3; IntAct=EBI-2846068, EBI-3942425;
Q12931:TRAP1; NbExp=4; IntAct=EBI-15643376, EBI-1055869;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:15087508, ECO:0000269|PubMed:18687899,
ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20798600,
ECO:0000269|PubMed:23933751}; Single-pass membrane protein
{ECO:0000255}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q99MQ3}; Single-pass membrane protein
{ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:19229105,
ECO:0000269|PubMed:20798600}. Note=Localizes mostly in
mitochondrion and the 2 proteolytic processed fragments of 55 kDa
and 48 kDa localize mainly in cytosol.
{ECO:0000269|PubMed:19229105}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:14607334};
IsoId=Q9BXM7-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q9BXM7-2; Sequence=VSP_050754, VSP_050755;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
testis, and at lower levels in brain, placenta, liver, kidney,
pancreas, prostate, ovary and small intestine. Present in the
embryonic testis from an early stage of development.
{ECO:0000269|PubMed:11494141}.
-!- PTM: Autophosphorylation at Ser-228 and Ser-402 is essential for
Parkin/PRKN recruitment to depolarized mitochondria.
{ECO:0000269|PubMed:22910362}.
-!- PTM: Two shorter forms of 55 kDa and 48 kDa seem to be produced by
proteolytic cleavage and localize mainly in cytosol.
{ECO:0000269|PubMed:19229105}.
-!- DISEASE: Parkinson disease 6 (PARK6) [MIM:605909]: An early-onset
form of Parkinson disease, a neurodegenerative disorder
characterized by parkinsonian signs such as rigidity, resting
tremor and bradykinesia. A subset of patients manifest additional
symptoms including hyperreflexia, autonomic instability, dementia
and psychiatric disturbances. Symptoms show diurnal fluctuation
and can improve after sleep. PARK6 pathogenesis involves
respiratory complex I deficiency causing mitochondrial
depolarization and dysfunction. Inheritance is autosomal
recessive. {ECO:0000269|PubMed:15087508,
ECO:0000269|PubMed:15349860, ECO:0000269|PubMed:15349870,
ECO:0000269|PubMed:15505171, ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:15955953, ECO:0000269|PubMed:15970950,
ECO:0000269|PubMed:16009891, ECO:0000269|PubMed:16207217,
ECO:0000269|PubMed:16207731, ECO:0000269|PubMed:16257123,
ECO:0000269|PubMed:16401616, ECO:0000269|PubMed:16482571,
ECO:0000269|PubMed:16632486, ECO:0000269|PubMed:16966503,
ECO:0000269|PubMed:17030667, ECO:0000269|PubMed:18286320,
ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20798600,
ECO:0000269|PubMed:22043288, ECO:0000269|PubMed:22956510,
ECO:0000269|PubMed:24652937, ECO:0000269|PubMed:24784582}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AB053323; BAB55647.1; -; mRNA.
EMBL; AF316873; AAK28062.1; -; mRNA.
EMBL; AK075225; BAC11484.1; -; mRNA.
EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009534; AAH09534.1; -; mRNA.
EMBL; BC028215; AAH28215.1; -; mRNA.
CCDS; CCDS211.1; -. [Q9BXM7-1]
RefSeq; NP_115785.1; NM_032409.2. [Q9BXM7-1]
UniGene; Hs.389171; -.
ProteinModelPortal; Q9BXM7; -.
SMR; Q9BXM7; -.
BioGrid; 122376; 63.
CORUM; Q9BXM7; -.
DIP; DIP-29427N; -.
IntAct; Q9BXM7; 16.
MINT; Q9BXM7; -.
STRING; 9606.ENSP00000364204; -.
ChEMBL; CHEMBL3337330; -.
CarbonylDB; Q9BXM7; -.
iPTMnet; Q9BXM7; -.
PhosphoSitePlus; Q9BXM7; -.
BioMuta; PINK1; -.
DMDM; 48428484; -.
EPD; Q9BXM7; -.
PaxDb; Q9BXM7; -.
PeptideAtlas; Q9BXM7; -.
PRIDE; Q9BXM7; -.
ProteomicsDB; 79455; -.
ProteomicsDB; 79456; -. [Q9BXM7-2]
DNASU; 65018; -.
Ensembl; ENST00000321556; ENSP00000364204; ENSG00000158828. [Q9BXM7-1]
GeneID; 65018; -.
KEGG; hsa:65018; -.
UCSC; uc001bdm.3; human. [Q9BXM7-1]
CTD; 65018; -.
DisGeNET; 65018; -.
EuPathDB; HostDB:ENSG00000158828.5; -.
GeneCards; PINK1; -.
GeneReviews; PINK1; -.
HGNC; HGNC:14581; PINK1.
HPA; CAB026191; -.
HPA; HPA001931; -.
MalaCards; PINK1; -.
MIM; 168600; phenotype.
MIM; 605909; phenotype.
MIM; 608309; gene.
neXtProt; NX_Q9BXM7; -.
OpenTargets; ENSG00000158828; -.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA33325; -.
eggNOG; KOG4158; Eukaryota.
eggNOG; ENOG410YE6P; LUCA.
GeneTree; ENSGT00390000001206; -.
HOGENOM; HOG000231649; -.
HOVERGEN; HBG053601; -.
InParanoid; Q9BXM7; -.
KO; K05688; -.
OMA; FLVMKNY; -.
OrthoDB; EOG091G03V6; -.
PhylomeDB; Q9BXM7; -.
TreeFam; TF313183; -.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
SignaLink; Q9BXM7; -.
SIGNOR; Q9BXM7; -.
ChiTaRS; PINK1; human.
GeneWiki; PINK1; -.
GenomeRNAi; 65018; -.
PRO; PR:Q9BXM7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158828; -.
CleanEx; HS_PINK1; -.
Genevisible; Q9BXM7; HS.
GO; GO:0097449; C:astrocyte projection; IDA:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0097413; C:Lewy body; TAS:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ParkinsonsUK-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
GO; GO:0010857; F:calcium-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0016504; F:peptidase activator activity; TAS:ParkinsonsUK-UCL.
GO; GO:0002020; F:protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004672; F:protein kinase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0043422; F:protein kinase B binding; IDA:ParkinsonsUK-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IC:ParkinsonsUK-UCL.
GO; GO:0000422; P:autophagy of mitochondrion; IMP:UniProtKB.
GO; GO:1904881; P:cellular response to hydrogen sulfide; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IMP:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0097237; P:cellular response to toxic substance; TAS:ParkinsonsUK-UCL.
GO; GO:0072655; P:establishment of protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0072656; P:maintenance of protein location in mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0099074; P:mitochondrion to lysosome transport; IMP:ParkinsonsUK-UCL.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:ParkinsonsUK-UCL.
GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; ISS:ParkinsonsUK-UCL.
GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IDA:ParkinsonsUK-UCL.
GO; GO:0046329; P:negative regulation of JNK cascade; TAS:ParkinsonsUK-UCL.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:ParkinsonsUK-UCL.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; TAS:ParkinsonsUK-UCL.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; TAS:ParkinsonsUK-UCL.
GO; GO:1903852; P:positive regulation of cristae formation; IMP:ParkinsonsUK-UCL.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0033603; P:positive regulation of dopamine secretion; IEA:Ensembl.
GO; GO:1904544; P:positive regulation of free ubiquitin chain polymerization; ISS:ParkinsonsUK-UCL.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; TAS:ParkinsonsUK-UCL.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IEA:Ensembl.
GO; GO:0010952; P:positive regulation of peptidase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IC:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:AgBase.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:BHF-UCL.
GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:1900407; P:regulation of cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0002082; P:regulation of oxidative phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; NAS:ParkinsonsUK-UCL.
GO; GO:0043254; P:regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IDA:AgBase.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1902803; P:regulation of synaptic vesicle transport; TAS:ParkinsonsUK-UCL.
GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IGI:ParkinsonsUK-UCL.
GO; GO:0038203; P:TORC2 signaling; IC:ParkinsonsUK-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ParkinsonsUK-UCL.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Autophagy; Complete proteome;
Cytoplasm; Disease mutation; Kinase; Magnesium; Membrane;
Metal-binding; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Neurodegeneration; Nucleotide-binding;
Parkinson disease; Parkinsonism; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transit peptide;
Transmembrane; Transmembrane helix.
TRANSIT 1 77 Mitochondrion. {ECO:0000255}.
CHAIN 78 581 Serine/threonine-protein kinase PINK1,
mitochondrial.
/FTId=PRO_0000024369.
TOPO_DOM 78 93 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 94 110 Helical. {ECO:0000255}.
TOPO_DOM 111 581 Cytoplasmic. {ECO:0000255}.
DOMAIN 156 511 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000305}.
NP_BIND 162 170 ATP. {ECO:0000250|UniProtKB:Q02750,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 362 362 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 186 186 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 228 228 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:22910362}.
MOD_RES 402 402 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:22910362}.
VAR_SEQ 1 307 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_050754.
VAR_SEQ 308 320 LGHGRTLFLVMKN -> MCGSQRPSPLSTS (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_050755.
VARIANT 67 67 L -> F (in dbSNP:rs763142730).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046566.
VARIANT 68 68 R -> P. {ECO:0000269|PubMed:18330912}.
/FTId=VAR_046567.
VARIANT 92 92 C -> F (in PARK6).
{ECO:0000269|PubMed:15349860}.
/FTId=VAR_046568.
VARIANT 98 98 R -> W (in dbSNP:rs575668171).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046569.
VARIANT 111 111 I -> S. {ECO:0000269|PubMed:18330912}.
/FTId=VAR_046570.
VARIANT 115 115 Q -> L (in dbSNP:rs148871409).
{ECO:0000269|PubMed:15970950,
ECO:0000269|PubMed:16009891}.
/FTId=VAR_046571.
VARIANT 124 124 A -> V. {ECO:0000269|PubMed:18330912}.
/FTId=VAR_046572.
VARIANT 125 125 C -> G (in PARK6).
{ECO:0000269|PubMed:16401616}.
/FTId=VAR_062773.
VARIANT 126 126 Q -> P (in PARK6; strongly reduces
interaction with PRKN).
{ECO:0000269|PubMed:18286320,
ECO:0000269|PubMed:20798600}.
/FTId=VAR_064344.
VARIANT 145 145 T -> M (in dbSNP:rs45604240).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046573.
VARIANT 147 147 R -> H (in PARK6; unknown pathological
significance; dbSNP:rs138050841).
{ECO:0000269|PubMed:15505171}.
/FTId=VAR_046574.
VARIANT 148 148 L -> W (in dbSNP:rs56297806).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041010.
VARIANT 168 168 A -> P (in PARK6; no effect on
autophosphorylation; localizes to the
mitochondria and immunogold experiments
reveal that both wild-type and mutant
proteins face the mitochondrial
intermembrane space; dbSNP:rs768091663).
{ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:16009891,
ECO:0000269|PubMed:16207731,
ECO:0000269|PubMed:24784582}.
/FTId=VAR_046575.
VARIANT 170 170 V -> G (in PARK6).
{ECO:0000269|PubMed:24652937}.
/FTId=VAR_078934.
VARIANT 186 186 K -> N (in dbSNP:rs143204084).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046576.
VARIANT 196 196 P -> L (in PARK6; dbSNP:rs138302371).
{ECO:0000269|PubMed:16009891}.
/FTId=VAR_046577.
VARIANT 196 196 P -> S (in dbSNP:rs35802484).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041011.
VARIANT 209 209 P -> L (in dbSNP:rs34677717).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041012.
VARIANT 215 215 P -> L (in a glioblastoma multiforme
sample; somatic mutation;
dbSNP:rs371854396).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041013.
VARIANT 217 217 A -> D (in PARK6; dbSNP:rs74315360).
{ECO:0000269|PubMed:16966503}.
/FTId=VAR_046578.
VARIANT 231 231 E -> G. {ECO:0000269|PubMed:15596610}.
/FTId=VAR_046579.
VARIANT 235 235 N -> I. {ECO:0000269|PubMed:15596610}.
/FTId=VAR_046580.
VARIANT 240 240 E -> K (in PARK6; dbSNP:rs573931674).
{ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:16401616}.
/FTId=VAR_046581.
VARIANT 257 257 T -> I (in dbSNP:rs370906995).
/FTId=VAR_046582.
VARIANT 263 263 R -> G. {ECO:0000269|PubMed:15596610}.
/FTId=VAR_046583.
VARIANT 268 268 L -> V (in PARK6; dbSNP:rs372280083).
{ECO:0000269|PubMed:16207217,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046584.
VARIANT 271 271 H -> Q (in PARK6; dbSNP:rs28940284).
{ECO:0000269|PubMed:15349870}.
/FTId=VAR_046585.
VARIANT 276 276 R -> Q (in dbSNP:rs548506734).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046586.
VARIANT 279 279 R -> H (in PARK6; dbSNP:rs74315358).
{ECO:0000269|PubMed:15970950}.
/FTId=VAR_046587.
VARIANT 280 280 A -> T (in PARK6; early-onset;
dbSNP:rs772510148).
{ECO:0000269|PubMed:16482571}.
/FTId=VAR_062774.
VARIANT 296 296 P -> L (in dbSNP:rs779060308).
{ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046588.
VARIANT 305 305 P -> L (in dbSNP:rs7349186).
/FTId=VAR_018993.
VARIANT 309 309 G -> D (in PARK6; fails to maintain
mitochondrial membrane potential; full-
length mutant has no effect on
autophosphorylation; strongly reduces
interaction with PRKN; decreases PRKN and
SNCAIP ubiquitination and degradation;
dbSNP:rs74315355).
{ECO:0000269|PubMed:15087508,
ECO:0000269|PubMed:16207731,
ECO:0000269|PubMed:19229105,
ECO:0000269|PubMed:20798600}.
/FTId=VAR_018994.
VARIANT 313 313 T -> M (in PARK6; decreases PRKN and
SNCAIP ubiquitination and degradation;
dbSNP:rs74315359).
{ECO:0000269|PubMed:17030667,
ECO:0000269|PubMed:19229105}.
/FTId=VAR_046589.
VARIANT 317 317 V -> I (in dbSNP:rs200949139).
{ECO:0000269|PubMed:16969854,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046590.
VARIANT 318 318 M -> L (in dbSNP:rs139226733).
{ECO:0000269|PubMed:15596610}.
/FTId=VAR_046591.
VARIANT 322 322 P -> L (in dbSNP:rs768019187).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046592.
VARIANT 339 339 A -> T (in dbSNP:rs55831733).
{ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:16969854,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_041014.
VARIANT 340 340 A -> T (in dbSNP:rs3738136).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:16009891,
ECO:0000269|PubMed:16257123,
ECO:0000269|PubMed:16482571,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018995.
VARIANT 341 341 M -> I (in dbSNP:rs35813094).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041015.
VARIANT 347 347 L -> P (in PARK6; strongly reduces
interaction with PRKN; dbSNP:rs28940285).
{ECO:0000269|PubMed:15349870,
ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:20798600,
ECO:0000269|PubMed:22956510}.
/FTId=VAR_046593.
VARIANT 362 362 D -> H. {ECO:0000269|PubMed:15596610}.
/FTId=VAR_046594.
VARIANT 369 369 L -> P (in PARK6).
{ECO:0000269|PubMed:16401616}.
/FTId=VAR_062775.
VARIANT 377 377 C -> F (in dbSNP:rs34203620).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041016.
VARIANT 383 383 A -> T (in dbSNP:rs45515602).
{ECO:0000269|PubMed:16969854,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046595.
VARIANT 386 386 G -> A (in PARK6; abolishes kinase
activity). {ECO:0000269|PubMed:16401616,
ECO:0000269|PubMed:24784582}.
/FTId=VAR_062776.
VARIANT 388 388 C -> R (in PARK6).
{ECO:0000269|PubMed:15955953}.
/FTId=VAR_046596.
VARIANT 395 395 G -> V (in dbSNP:rs1035071310).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046597.
VARIANT 399 399 P -> L (probable disease-associated
mutation found in early-onset Parkinson
disease with digenic inheritance; found
in a patient also carrying mutation S-39
in PARK7; decreases PRKN and SNCAIP
ubiquitination and degradation;
dbSNP:rs119451946).
{ECO:0000269|PubMed:16632486,
ECO:0000269|PubMed:19229105}.
/FTId=VAR_062777.
VARIANT 407 407 R -> Q (in PARK6; early-onset;
dbSNP:rs556540177).
{ECO:0000269|PubMed:16257123}.
/FTId=VAR_062778.
VARIANT 409 409 G -> V (in PARK6).
{ECO:0000269|PubMed:16401616}.
/FTId=VAR_062779.
VARIANT 411 411 G -> S (in dbSNP:rs45478900).
{ECO:0000269|PubMed:16969854}.
/FTId=VAR_046598.
VARIANT 417 417 E -> G (in PARK6).
{ECO:0000269|PubMed:15349870}.
/FTId=VAR_046599.
VARIANT 425 425 P -> S (in dbSNP:rs554114655).
{ECO:0000269|PubMed:15596610}.
/FTId=VAR_046600.
VARIANT 431 431 Y -> H (may predispose to Parkinson
disease development; shows decreased
mitochondrial membrane potential under
stress conditions; dbSNP:rs74315361).
{ECO:0000269|PubMed:16969854}.
/FTId=VAR_046601.
VARIANT 442 442 I -> T. {ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046602.
VARIANT 451 451 N -> S (may predispose to Parkinson
disease development; shows decreased
mitochondrial membrane potential under
stress conditions; dbSNP:rs747400197).
{ECO:0000269|PubMed:16969854}.
/FTId=VAR_046603.
VARIANT 456 581 Missing (in PARK6).
{ECO:0000269|PubMed:24652937}.
/FTId=VAR_078935.
VARIANT 461 461 L -> S. {ECO:0000269|PubMed:16969854}.
/FTId=VAR_046604.
VARIANT 464 464 R -> H (in PARK6; dbSNP:rs764328076).
{ECO:0000269|PubMed:15349860}.
/FTId=VAR_046605.
VARIANT 476 476 E -> K (may predispose to Parkinson
disease development; shows decreased
mitochondrial membrane potential under
stress conditions; dbSNP:rs115477764).
{ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:16009891,
ECO:0000269|PubMed:16969854,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046606.
VARIANT 477 477 S -> T (in dbSNP:rs34416410).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041017.
VARIANT 489 489 L -> P (in PARK6).
{ECO:0000269|PubMed:15596610}.
/FTId=VAR_046607.
VARIANT 501 501 R -> P (may predispose to Parkinson
disease development; shows decreased
mitochondrial membrane potential under
stress conditions).
{ECO:0000269|PubMed:16969854}.
/FTId=VAR_046608.
VARIANT 521 521 N -> T (in dbSNP:rs1043424).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:15596610,
ECO:0000269|PubMed:16009891,
ECO:0000269|PubMed:16257123,
ECO:0000269|PubMed:16482571,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018996.
VARIANT 525 525 D -> N (in dbSNP:rs531477772).
{ECO:0000269|PubMed:15349860,
ECO:0000269|PubMed:18330912}.
/FTId=VAR_046609.
VARIANT 534 534 Q -> QQ (in PARK6).
{ECO:0000269|PubMed:15970950}.
/FTId=VAR_046610.
VARIANT 537 537 A -> T (in dbSNP:rs771032673).
{ECO:0000269|PubMed:18330912}.
/FTId=VAR_046611.
VARIANT 575 575 C -> R (may predispose to Parkinson
disease development; shows decreased
mitochondrial membrane potential under
stress conditions).
{ECO:0000269|PubMed:16969854}.
/FTId=VAR_046612.
MUTAGEN 219 219 K->A: Abolishes MFN2 phosphorylation and
interaction with PRKN; when associated
with ALA-362 and ALA-384.
{ECO:0000269|PubMed:23620051}.
MUTAGEN 362 362 D->A: Abolishes MFN2 phosphorylation and
interaction with PRKN; when associated
with ALA-219 and ALA-384.
{ECO:0000269|PubMed:23620051}.
MUTAGEN 384 384 D->A: Abolishes MFN2 phosphorylation and
interaction with PRKN; when associated
with ALA-219 and ALA-362.
{ECO:0000269|PubMed:23620051}.
CONFLICT 209 209 P -> A (in Ref. 5; AAH28215).
{ECO:0000305}.
CONFLICT 419 419 S -> P (in Ref. 3; BAC11484).
{ECO:0000305}.
SEQUENCE 581 AA; 62769 MW; 721FE01F63263A64 CRC64;
MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA GPGAEPRRVG
LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV FLAFGLGLGL IEEKQAESRR
AVSACQEIQA IFTQKSKPGP DPLDTRRLQG FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ
NLEVTKSTGL LPGRGPGTSA PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE
LVPASRVALA GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP
SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV DHLVQQGIAH
RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF SSWYVDRGGN GCLMAPEVST
ARPGPRAVID YSKADAWAVG AIAYEIFGLV NPFYGQGKAH LESRSYQEAQ LPALPESVPP
DVRQLVRALL QREASKRPSA RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL
ANRLTEKCCV ETKMKMLFLA NLECETLCQA ALLLCSWRAA L


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