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Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p135) (p150-glued)

 DCTN1_HUMAN             Reviewed;        1278 AA.
Q14203; A8MY36; B4DM45; E9PFS5; E9PGE1; G5E9H4; O95296; Q6IQ37;
Q9BRM9; Q9UIU1; Q9UIU2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 3.
25-OCT-2017, entry version 181.
RecName: Full=Dynactin subunit 1;
AltName: Full=150 kDa dynein-associated polypeptide;
AltName: Full=DAP-150;
Short=DP-150;
AltName: Full=p135;
AltName: Full=p150-glued;
Name=DCTN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=9799602; DOI=10.1006/geno.1998.5542;
Collin G.B., Nishina P.M., Marshall J.D., Naggert J.K.;
"Human DCTN1: genomic structure and evaluation as a candidate for
Alstrom syndrome.";
Genomics 53:359-364(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain, and Trachea;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-1278.
TISSUE=Brain;
PubMed=8838327; DOI=10.1006/geno.1996.0068;
Holzbaur E.L.F., Tokito M.K.;
"Localization of the DCTN1 gene encoding p150Glued to human chromosome
2p13 by fluorescence in situ hybridization.";
Genomics 31:398-399(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-1278 (ISOFORM 6), AND ALTERNATIVE
SPLICING.
TISSUE=Brain;
PubMed=8856662; DOI=10.1091/mbc.7.8.1167;
Tokito M.K., Howland D.S., Lee V.M.-Y., Holzbaur E.L.F.;
"Functionally distinct isoforms of dynactin are expressed in human
neurons.";
Mol. Biol. Cell 7:1167-1180(1996).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-1278.
PubMed=9805007; DOI=10.1016/S0167-4781(98)00195-X;
Tokito M.K., Holzbaur E.L.F.;
"The genomic structure of DCTN1, a candidate gene for limb-girdle
muscular dystrophy.";
Biochim. Biophys. Acta 1442:432-436(1998).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1081-1278.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
PubMed=14514668; DOI=10.1074/jbc.M306194200;
Bu W., Su L.-K.;
"Characterization of functional domains of human EB1 family
proteins.";
J. Biol. Chem. 278:49721-49731(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
UBIQUITINATION, AND INTERACTION WITH FBXL5.
PubMed=17532294; DOI=10.1016/j.bbrc.2007.05.068;
Zhang N., Liu J., Ding X., Aikhionbare F., Jin C., Yao X.;
"FBXL5 interacts with p150Glued and regulates its ubiquitination.";
Biochem. Biophys. Res. Commun. 359:34-39(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH SNX6.
PubMed=19935774; DOI=10.1038/cr.2009.130;
Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
"The retromer component SNX6 interacts with dynactin p150(Glued) and
mediates endosome-to-TGN transport.";
Cell Res. 19:1334-1349(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
INTERACTION WITH ECM29.
PubMed=20682791; DOI=10.1074/jbc.M110.154120;
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
Hughes R.E., Rechsteiner M.;
"A protein interaction network for Ecm29 links the 26 S proteasome to
molecular motors and endosomal components.";
J. Biol. Chem. 285:31616-31633(2010).
[17]
INTERACTION WITH PARD6A, AND SUBCELLULAR LOCATION.
PubMed=20719959; DOI=10.1091/mbc.E10-05-0430;
Kodani A., Tonthat V., Wu B., Suetterlin C.;
"Par6 alpha interacts with the dynactin subunit p150 Glued and is a
critical regulator of centrosomal protein recruitment.";
Mol. Biol. Cell 21:3376-3385(2010).
[18]
INTERACTION WITH DYNAP.
PubMed=20978158; DOI=10.1158/1535-7163.MCT-10-0730;
Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K.,
Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S.,
Sasaki R., Mizukami T.;
"A novel human dynactin-associated protein, dynAP, promotes activation
of Akt, and ergosterol-related compounds induce dynAP-dependent
apoptosis of human cancer cells.";
Mol. Cancer Ther. 9:2934-2942(2010).
[19]
PHOSPHORYLATION AT SER-179 AND SER-212, MUTAGENESIS OF SER-179 AND
SER-212, INTERACTION WITH PLK1 AND CLIP1, AND SUBCELLULAR LOCATION.
PubMed=20679239; DOI=10.1073/pnas.1006615107;
Li H., Liu X.S., Yang X., Song B., Wang Y., Liu X.;
"Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear
envelope breakdown during prophase.";
Proc. Natl. Acad. Sci. U.S.A. 107:14633-14638(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
INTERACTION WITH CLN3.
PubMed=22261744; DOI=10.1007/s00018-011-0913-1;
Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K.,
Neefjes J., Olkkonen V.M., Jalanko A.;
"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor
proteins and modifies location of late endosomal compartments.";
Cell. Mol. Life Sci. 69:2075-2089(2012).
[22]
INTERACTION WITH CEP131.
PubMed=22797915; DOI=10.1242/jcs.104059;
Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J.,
Swanton C., Howell M., Boulton S.J., Collis S.J.;
"The centriolar satellite protein Cep131 is important for genome
stability.";
J. Cell Sci. 125:4770-4779(2012).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22327364; DOI=10.1038/ncb2440;
Kiyomitsu T., Cheeseman I.M.;
"Chromosome- and spindle-pole-derived signals generate an intrinsic
code for spindle position and orientation.";
Nat. Cell Biol. 14:311-317(2012).
[24]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23386061; DOI=10.1038/emboj.2013.3;
Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
Reiter J.F.;
"Kif3a interacts with Dynactin subunit p150 Glued to organize
centriole subdistal appendages.";
EMBO J. 32:597-607(2013).
[25]
INTERACTION WITH MISP.
PubMed=23509069; DOI=10.1083/jcb.201207050;
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L.,
Ponting C.P., Goenczy P., Hoffmann I.;
"MISP is a novel Plk1 substrate required for proper spindle
orientation and mitotic progression.";
J. Cell Biol. 200:773-787(2013).
[26]
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).
[27]
PHOSPHORYLATION AT THR-145; THR-146 AND THR-147, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF THR-145; THR-146 AND THR-147.
PubMed=23985322; DOI=10.1091/mbc.E13-03-0137;
Zhapparova O.N., Fokin A.I., Vorobyeva N.E., Bryantseva S.A.,
Nadezhdina E.S.;
"Ste20-like protein kinase SLK (LOSK) regulates microtubule
organization by targeting dynactin to the centrosome.";
Mol. Biol. Cell 24:3205-3214(2013).
[28]
INTERACTION WITH CEP126.
PubMed=24867236; DOI=10.1111/boc.201300087;
Bonavita R., Walas D., Brown A.K., Luini A., Stephens D.J.,
Colanzi A.;
"Cep126 is required for pericentriolar satellite localisation to the
centrosome and for primary cilium formation.";
Biol. Cell 106:254-267(2014).
[29]
INTERACTION WITH HPS6.
PubMed=25189619; DOI=10.1242/jcs.141978;
Li K., Yang L., Zhang C., Niu Y., Li W., Liu J.J.;
"HPS6 interacts with dynactin p150Glued to mediate retrograde
trafficking and maturation of lysosomes.";
J. Cell Sci. 127:4574-4588(2014).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25774020; DOI=10.1002/jcb.25160;
Chen T.Y., Syu J.S., Han T.Y., Cheng H.L., Lu F.I., Wang C.Y.;
"Cell cycle-dependent localization of dynactin subunit p150 glued at
centrosome.";
J. Cell. Biochem. 116:2049-2060(2015).
[32]
ASSOCIATION WITH MICROTUBULES, AND DOMAIN CAP-GLY.
PubMed=26968983; DOI=10.15252/embj.201593071;
McKenney R.J., Huynh W., Vale R.D., Sirajuddin M.;
"Tyrosination of alpha-tubulin controls the initiation of processive
dynein-dynactin motility.";
EMBO J. 35:1175-1185(2016).
[33]
INTERACTION WITH BCCIP.
PubMed=28394342; DOI=10.1038/onc.2017.92;
Huhn S.C., Liu J., Ye C., Lu H., Jiang X., Feng X., Ganesan S.,
White E., Shen Z.;
"Regulation of spindle integrity and mitotic fidelity by BCCIP.";
Oncogene 36:4750-4766(2017).
[34]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-107 IN COMPLEX WITH
MAPRE1, AND INTERACTION WITH MAPRE1.
PubMed=16109370; DOI=10.1016/j.molcel.2005.06.034;
Hayashi I., Wilde A., Mal T.K., Ikura M.;
"Structural basis for the activation of microtubule assembly by the
EB1 and p150Glued complex.";
Mol. Cell 19:449-460(2005).
[35]
STRUCTURE BY NMR OF 1-99.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the CAP-Gly domain in human dynactin 1.";
Submitted (NOV-2005) to the PDB data bank.
[36]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 18-111 IN COMPLEX WITH
MAPRE1, AND INTERACTION WITH MAPRE1.
PubMed=16949363; DOI=10.1016/j.molcel.2006.07.013;
Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I.,
Winkler F.K., Steinmetz M.O.;
"Key interaction modes of dynamic +TIP networks.";
Mol. Cell 23:663-671(2006).
[37]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 15-111 IN COMPLEX WITH
CLIP1, SUBCELLULAR LOCATION, AND INTERACTION WITH CLIP1.
PubMed=17828277; DOI=10.1038/nsmb1291;
Weisbrich A., Honnappa S., Jaussi R., Okhrimenko O., Frey D.,
Jelesarov I., Akhmanova A., Steinmetz M.O.;
"Structure-function relationship of CAP-Gly domains.";
Nat. Struct. Mol. Biol. 14:959-967(2007).
[38]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-107 IN COMPLEX WITH
CLIP1, INTERACTION WITH CLIP1, AND MUTAGENESIS OF LYS-68 AND ARG-90.
PubMed=17828275; DOI=10.1038/nsmb1299;
Hayashi I., Plevin M.J., Ikura M.;
"CLIP170 autoinhibition mimics intermolecular interactions with
p150Glued or EB1.";
Nat. Struct. Mol. Biol. 14:980-981(2007).
[39]
VARIANT HMN7B SER-59.
PubMed=12627231; DOI=10.1038/ng1123;
Puls I., Jonnakuty C., LaMonte B.H., Holzbaur E.L., Tokito M.,
Mann E., Floeter M.K., Bidus K., Drayna D., Oh S.J., Brown R.H. Jr.,
Ludlow C.L., Fischbeck K.H.;
"Mutant dynactin in motor neuron disease.";
Nat. Genet. 33:455-456(2003).
[40]
INVOLVEMENT IN ALS, AND VARIANTS ALS THR-571; TRP-785 AND ILE-1249.
PubMed=15326253; DOI=10.1212/01.WNL.0000134608.83927.B1;
Muench C., Sedlmeier R., Meyer T., Homberg V., Sperfeld A.D., Kurt A.,
Prudlo J., Peraus G., Hanemann C.O., Stumm G., Ludolph A.C.;
"Point mutations of the p150 subunit of dynactin (DCTN1) gene in
ALS.";
Neurology 63:724-726(2004).
[41]
VARIANT ALS LYS-1101.
PubMed=16240349; DOI=10.1002/ana.20631;
Muench C., Rosenbohm A., Sperfeld A.-D., Uttner I., Reske S.,
Krause B.J., Sedlmeier R., Meyer T., Hanemann C.O., Stumm G.,
Ludolph A.C.;
"Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS
and FTD.";
Ann. Neurol. 58:777-780(2005).
[42]
CHARACTERIZATION OF VARIANT HMN7B SER-59, AND INTERACTION WITH MAPRE1.
PubMed=16505168; DOI=10.1083/jcb.200511068;
Levy J.R., Sumner C.J., Caviston J.P., Tokito M.K., Ranganathan S.,
Ligon L.A., Wallace K.E., LaMonte B.H., Harmison G.G., Puls I.,
Fischbeck K.H., Holzbaur E.L.F.;
"A motor neuron disease-associated mutation in p150Glued perturbs
dynactin function and induces protein aggregation.";
J. Cell Biol. 172:733-745(2006).
[43]
VARIANTS VAL-196; GLN-495 AND ILE-1249.
PubMed=17824900; DOI=10.1111/j.1600-0404.2007.00884.x;
Muench C., Meyer R., Linke P., Meyer T., Ludolph A.C., Haas J.,
Hemmer B.;
"The p150 subunit of dynactin (DCTN1) gene in multiple sclerosis.";
Acta Neurol. Scand. 116:231-234(2007).
[44]
VARIANTS PERRYS ARG-71; GLU-71; ALA-71; PRO-72 AND PRO-74,
CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND PRO-74, AND
CHARACTERIZATION OF VARIANT HMN7B SER-59.
PubMed=19136952; DOI=10.1038/ng.293;
Farrer M.J., Hulihan M.M., Kachergus J.M., Daechsel J.C.,
Stoessl A.J., Grantier L.L., Calne S., Calne D.B., Lechevalier B.,
Chapon F., Tsuboi Y., Yamada T., Gutmann L., Elibol B., Bhatia K.P.,
Wider C., Vilarino-Gueell C., Ross O.A., Brown L.A.,
Castanedes-Casey M., Dickson D.W., Wszolek Z.K.;
"DCTN1 mutations in Perry syndrome.";
Nat. Genet. 41:163-165(2009).
[45]
VARIANT ILE-1249.
PubMed=19506225; DOI=10.1212/WNL.0b013e3181a92c4c;
Vilarino-Gueell C., Wider C., Soto-Ortolaza A.I., Cobb S.A.,
Kachergus J.M., Keeling B.H., Dachsel J.C., Hulihan M.M.,
Dickson D.W., Wszolek Z.K., Uitti R.J., Graff-Radford N.R.,
Boeve B.F., Josephs K.A., Miller B., Boylan K.B., Gwinn K.,
Adler C.H., Aasly J.O., Hentati F., Destee A., Krygowska-Wajs A.,
Chartier-Harlin M.-C., Ross O.A., Rademakers R., Farrer M.J.;
"Characterization of DCTN1 genetic variability in neurodegeneration.";
Neurology 72:2024-2028(2009).
[46]
CHARACTERIZATION OF VARIANT HMN7B SER-59.
PubMed=19279216; DOI=10.1073/pnas.0810828106;
Moore J.K., Sept D., Cooper J.A.;
"Neurodegeneration mutations in dynactin impair dynein-dependent
nuclear migration.";
Proc. Natl. Acad. Sci. U.S.A. 106:5147-5152(2009).
[47]
CHARACTERIZATION OF VARIANT HMN7B SER-59, CHARACTERIZATION OF VARIANT
196-ILE, INTERACTION WITH TBCB, AND SUBCELLULAR LOCATION.
PubMed=22777741; DOI=10.1007/s00441-012-1463-z;
Kuh G.F., Stockmann M., Meyer-Ohlendorf M., Linta L., Proepper C.,
Ludolph A.C., Bockmann J., Boeckers T.M., Liebau S.;
"Tubulin-binding cofactor B is a direct interaction partner of the
dynactin subunit p150(Glued).";
Cell Tissue Res. 350:13-26(2012).
[48]
CHARACTERIZATION OF VARIANT PERRYS PRO-74, FUNCTION, SUBUNIT, AND
INTERACTION WITH MAPRE1.
PubMed=23874158; DOI=10.1371/journal.pbio.1001611;
Lazarus J.E., Moughamian A.J., Tokito M.K., Holzbaur E.L.;
"Dynactin subunit p150(Glued) is a neuron-specific anti-catastrophe
factor.";
PLoS Biol. 11:E1001611-E1001611(2013).
[49]
VARIANT PHE-670.
PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R.,
Erwa W., Trajanoski S., Strom T.M., Auer-Grumbach M.;
"Whole-exome sequencing in patients with inherited neuropathies:
outcome and challenges.";
J. Neurol. 261:970-982(2014).
[50]
VARIANT PERRYS LEU-52.
PubMed=24676999; DOI=10.1002/mds.25833;
Araki E., Tsuboi Y., Daechsel J., Milnerwood A., Vilarino-Guell C.,
Fujii N., Mishima T., Oka T., Hara H., Fukae J., Farrer M.J.;
"A Novel DCTN1 mutation with late-onset parkinsonism and
frontotemporal atrophy.";
Mov. Disord. 29:1201-1204(2014).
[51]
CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND PRO-74, FUNCTION,
INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DYNEIN HEAVY CHAIN, AND
DOMAIN CAP-GLY.
PubMed=25185702; DOI=10.1038/ncomms5807;
Ayloo S., Lazarus J.E., Dodda A., Tokito M., Ostap E.M.,
Holzbaur E.L.;
"Dynactin functions as both a dynamic tether and brake during dynein-
driven motility.";
Nat. Commun. 5:4807-4807(2014).
[52]
VARIANTS PERRYS ARG-71 AND CYS-78, AND CHARACTERIZATION OF VARIANTS
PERRYS ARG-71 AND CYS-78.
PubMed=24881494; DOI=10.1016/j.parkreldis.2014.05.004;
Tacik P., Fiesel F.C., Fujioka S., Ross O.A., Pretelt F.,
Castaneda Cardona C., Kidd A., Hlavac M., Raizis A., Okun M.S.,
Traynor S., Strongosky A.J., Springer W., Wszolek Z.K.;
"Three families with Perry syndrome from distinct parts of the
world.";
Parkinsonism Relat. Disord. 20:884-888(2014).
[53]
CHARACTERIZATION OF VARIANT PERRYS ARG-71, SUBCELLULAR LOCATION,
DOMAIN CAP-GLY, INTERACTION WITH CLIP1, AND ASSOCIATION WITH
MICROTUBULES.
PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
"Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
initiation of dynein-driven transport in neurons.";
Cell Rep. 14:2637-2652(2016).
-!- FUNCTION: Plays a key role in dynein-mediated retrograde transport
of vesicles and organelles along microtubules by recruiting and
tethering dynein to microtubules. Binds to both dynein and
microtubules providing a link between specific cargos,
microtubules and dynein. Essential for targeting dynein to
microtubule plus ends, recruiting dynein to membranous cargos and
enhancing dynein processivity (the ability to move along a
microtubule for a long distance without falling off the track).
Can also act as a brake to slow the dynein motor during motility
along the microtubule (PubMed:25185702). Can regulate microtubule
stability by promoting microtubule formation, nucleation and
polymerization and by inhibiting microtubule catastrophe in
neurons. Inhibits microtubule catastrophe by binding both to
microtubules and to tubulin, leading to enhanced microtubule
stability along the axon (PubMed:23874158). Plays a role in
metaphase spindle orientation (PubMed:22327364). Plays a role in
centriole cohesion and subdistal appendage organization and
function. Its recruitement to the centriole in a KIF3A-dependent
manner is essential for the maintenance of centriole cohesion and
the formation of subdistal appendage. Also required for
microtubule anchoring at the mother centriole (PubMed:23386061).
Plays a role in primary cilia formation (PubMed:25774020).
{ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23386061,
ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:25185702,
ECO:0000269|PubMed:25774020}.
-!- SUBUNIT: Monomer and homodimer (PubMed:23874158). Dynactin is a
large macromolecular complex of at least 10 components;
p150(glued) binds directly to microtubules and to cytoplasmic
dynein. Interacts with the C-terminus of MAPRE1, MAPRE2 and
MAPRE3. Interacts (via C-terminus) with SNX6. Interacts with CLN3,
DYNAP, ECM29 and FBXL5. Interacts with MISP; this interaction
regulates its distribution at the cell cortex. Interacts with
CEP131. Interacts with CEP126 (PubMed:24867236). Interacts with
CLIP1 (PubMed:17828275, PubMed:17828277, PubMed:26972003,
PubMed:20679239). Interacts with dynein intermediate chain and
dynein heavy chain (PubMed:25185702). Interacts with PLK1 (via
POLO-box domain) (PubMed:20679239). Interacts with TBCB
(PubMed:22777741). Binds preferentially to tyrosinated
microtubules than to detyrosinated microtubules (PubMed:26972003,
PubMed:26968983). Interacts with PARD6A (PubMed:20719959).
Interacts with HPS6 (PubMed:25189619). Interacts with KIF3A.
Interacts with BICD2 (By similarity). Interacts with DST (isoform
9) (By similarity). Interacts with DST (isoform 1) (By
similarity). Interacts with BCCIP (isoform 2/alpha)
(PubMed:28394342). {ECO:0000250|UniProtKB:O08788,
ECO:0000269|PubMed:14514668, ECO:0000269|PubMed:16109370,
ECO:0000269|PubMed:16505168, ECO:0000269|PubMed:16949363,
ECO:0000269|PubMed:17532294, ECO:0000269|PubMed:17828275,
ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:19935774,
ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:20682791,
ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:20978158,
ECO:0000269|PubMed:22261744, ECO:0000269|PubMed:22777741,
ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:23509069,
ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:24867236,
ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:25189619,
ECO:0000269|PubMed:26968983, ECO:0000269|PubMed:26972003,
ECO:0000269|PubMed:28394342}.
-!- INTERACTION:
P42025:ACTR1B; NbExp=3; IntAct=EBI-724352, EBI-367493;
Q96RK4:BBS4; NbExp=3; IntAct=EBI-724352, EBI-1805814;
P30622-1:CLIP1; NbExp=7; IntAct=EBI-724352, EBI-9640673;
P54256:Hap1 (xeno); NbExp=4; IntAct=EBI-724352, EBI-994539;
Q15691:MAPRE1; NbExp=7; IntAct=EBI-724352, EBI-1004115;
P10636-8:MAPT; NbExp=8; IntAct=EBI-724352, EBI-366233;
Q9UNH7:SNX6; NbExp=2; IntAct=EBI-724352, EBI-949294;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17828277}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17828277,
ECO:0000269|PubMed:22777741, ECO:0000269|PubMed:25774020,
ECO:0000269|PubMed:26972003}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:20719959,
ECO:0000269|PubMed:23985322, ECO:0000269|PubMed:25774020}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000269|PubMed:23386061,
ECO:0000269|PubMed:25774020}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:25774020}. Nucleus envelope
{ECO:0000269|PubMed:20679239}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:22327364}. Note=Localizes to microtubule plus
ends (PubMed:17828277, PubMed:22777741, PubMed:25774020).
Localizes preferentially to the ends of tyrosinated microtubules
(PubMed:26972003). Localization at centrosome is regulated by SLK-
dependent phosphorylation (PubMed:23985322). Localizes to
centrosome in a PARKDA-dependent manner (PubMed:20719959).
Localizes to the subdistal appendage region of the centriole in a
KIF3A-dependent manner (PubMed:23386061). PLK1-mediated
phosphorylation at Ser-179 is essential for its localization in
the nuclear envelope (PubMed:20679239).
{ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:20679239,
ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:22777741,
ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23985322,
ECO:0000269|PubMed:25774020, ECO:0000269|PubMed:26972003}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=p150;
IsoId=Q14203-1; Sequence=Displayed;
Name=p135;
IsoId=Q14203-2; Sequence=VSP_000760;
Name=3;
IsoId=Q14203-3; Sequence=VSP_045392, VSP_045393, VSP_045394;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q14203-4; Sequence=VSP_045393, VSP_045394;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q14203-5; Sequence=VSP_000760, VSP_045394;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q14203-6; Sequence=VSP_047174;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain.
-!- DOMAIN: The CAP-Gly domain is essential for interactions with
microtubules and its binding partners and for its motion along the
microtubules. Essential for its preferential binding to
tyrosinated microtubules and for promoting the sustained
interaction of the dynein motor with microtubules.
{ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:26968983,
ECO:0000269|PubMed:26972003}.
-!- PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to
its degradation by the proteasome. {ECO:0000269|PubMed:17532294}.
-!- PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147
targets DCTN1 to the centrosome. It is uncertain if SLK
phosphorylates all three threonines or one or two of them. PLK1-
mediated phosphorylation at Ser-179 is essential for its
localization in the nuclear envelope, promotes its dissociation
from microtubules during early mitosis and positively regulates
nuclear envelope breakdown during prophase.
{ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:23985322}.
-!- DISEASE: Neuronopathy, distal hereditary motor, 7B (HMN7B)
[MIM:607641]: A neuromuscular disorder. Distal hereditary motor
neuronopathies constitute a heterogeneous group of neuromuscular
disorders caused by selective degeneration of motor neurons in the
anterior horn of the spinal cord, without sensory deficit in the
posterior horn. The overall clinical picture consists of a
classical distal muscular atrophy syndrome in the legs without
clinical sensory loss. The disease starts with weakness and
wasting of distal muscles of the anterior tibial and peroneal
compartments of the legs. Later on, weakness and atrophy may
expand to the proximal muscles of the lower limbs and/or to the
distal upper limbs. {ECO:0000269|PubMed:12627231,
ECO:0000269|PubMed:16505168, ECO:0000269|PubMed:19136952,
ECO:0000269|PubMed:19279216, ECO:0000269|PubMed:22777741}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A
neurodegenerative disorder affecting upper motor neurons in the
brain and lower motor neurons in the brain stem and spinal cord,
resulting in fatal paralysis. Sensory abnormalities are absent.
The pathologic hallmarks of the disease include pallor of the
corticospinal tract due to loss of motor neurons, presence of
ubiquitin-positive inclusions within surviving motor neurons, and
deposition of pathologic aggregates. The etiology of amyotrophic
lateral sclerosis is likely to be multifactorial, involving both
genetic and environmental factors. The disease is inherited in 5-
10% of the cases. {ECO:0000269|PubMed:15326253,
ECO:0000269|PubMed:16240349}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Perry syndrome (PERRYS) [MIM:168605]: A neuropsychiatric
disorder characterized by mental depression not responsive to
antidepressant drugs or electroconvulsive therapy, sleep
disturbances, exhaustion and marked weight loss. Parkinsonism
develops later and respiratory failure occurred terminally.
{ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:23874158,
ECO:0000269|PubMed:24676999, ECO:0000269|PubMed:24881494,
ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:26972003}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF064205; AAD55811.1; -; Genomic_DNA.
EMBL; AF064203; AAD55811.1; JOINED; Genomic_DNA.
EMBL; AF064204; AAD55811.1; JOINED; Genomic_DNA.
EMBL; AF064205; AAD55812.1; -; Genomic_DNA.
EMBL; AF064204; AAD55812.1; JOINED; Genomic_DNA.
EMBL; AK297286; BAG59757.1; -; mRNA.
EMBL; AK314352; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAW99684.1; -; Genomic_DNA.
EMBL; BC071583; AAH71583.1; -; mRNA.
EMBL; X98801; CAA67333.1; -; mRNA.
EMBL; AF086947; AAD03694.1; -; Genomic_DNA.
EMBL; AF086927; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086928; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086929; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086930; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086931; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086932; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086933; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086934; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086935; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086936; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086937; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086938; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086939; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086940; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086941; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086942; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086943; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086944; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086945; AAD03694.1; JOINED; Genomic_DNA.
EMBL; AF086946; AAD03694.1; JOINED; Genomic_DNA.
EMBL; BT006758; AAP35404.1; -; mRNA.
CCDS; CCDS1939.1; -. [Q14203-1]
CCDS; CCDS46341.1; -. [Q14203-4]
CCDS; CCDS46342.1; -. [Q14203-5]
CCDS; CCDS46343.1; -. [Q14203-2]
CCDS; CCDS54368.1; -. [Q14203-3]
CCDS; CCDS54369.1; -. [Q14203-6]
RefSeq; NP_001128512.1; NM_001135040.2. [Q14203-4]
RefSeq; NP_001128513.1; NM_001135041.2. [Q14203-5]
RefSeq; NP_001177765.1; NM_001190836.1. [Q14203-3]
RefSeq; NP_001177766.1; NM_001190837.1. [Q14203-6]
RefSeq; NP_004073.2; NM_004082.4. [Q14203-1]
RefSeq; NP_075408.1; NM_023019.3. [Q14203-2]
UniGene; Hs.516111; -.
PDB; 1TXQ; X-ray; 1.80 A; A=15-107.
PDB; 2COY; NMR; -; A=1-99.
PDB; 2HKN; X-ray; 1.87 A; A/B=18-111.
PDB; 2HKQ; X-ray; 1.86 A; B=18-111.
PDB; 2HL3; X-ray; 2.03 A; A/B=18-111.
PDB; 2HL5; X-ray; 1.93 A; C/D=18-111.
PDB; 2HQH; X-ray; 1.80 A; A/B/C/D=15-107.
PDB; 3E2U; X-ray; 2.60 A; A/B/C/D=18-111.
PDB; 3TQ7; X-ray; 2.30 A; P/Q=27-97.
PDBsum; 1TXQ; -.
PDBsum; 2COY; -.
PDBsum; 2HKN; -.
PDBsum; 2HKQ; -.
PDBsum; 2HL3; -.
PDBsum; 2HL5; -.
PDBsum; 2HQH; -.
PDBsum; 3E2U; -.
PDBsum; 3TQ7; -.
ProteinModelPortal; Q14203; -.
SMR; Q14203; -.
BioGrid; 108007; 246.
CORUM; Q14203; -.
DIP; DIP-31365N; -.
IntAct; Q14203; 202.
MINT; MINT-5004548; -.
STRING; 9606.ENSP00000354791; -.
iPTMnet; Q14203; -.
PhosphoSitePlus; Q14203; -.
SwissPalm; Q14203; -.
BioMuta; DCTN1; -.
DMDM; 17375490; -.
OGP; Q14203; -.
EPD; Q14203; -.
MaxQB; Q14203; -.
PaxDb; Q14203; -.
PeptideAtlas; Q14203; -.
PRIDE; Q14203; -.
DNASU; 1639; -.
Ensembl; ENST00000361874; ENSP00000354791; ENSG00000204843. [Q14203-1]
Ensembl; ENST00000394003; ENSP00000377571; ENSG00000204843. [Q14203-6]
Ensembl; ENST00000409240; ENSP00000386406; ENSG00000204843. [Q14203-3]
Ensembl; ENST00000409438; ENSP00000387270; ENSG00000204843. [Q14203-5]
Ensembl; ENST00000409567; ENSP00000386843; ENSG00000204843. [Q14203-4]
Ensembl; ENST00000633691; ENSP00000487724; ENSG00000204843. [Q14203-2]
GeneID; 1639; -.
KEGG; hsa:1639; -.
UCSC; uc002sku.4; human. [Q14203-1]
CTD; 1639; -.
DisGeNET; 1639; -.
EuPathDB; HostDB:ENSG00000204843.12; -.
GeneCards; DCTN1; -.
GeneReviews; DCTN1; -.
H-InvDB; HIX0204314; -.
HGNC; HGNC:2711; DCTN1.
HPA; CAB009108; -.
HPA; HPA034635; -.
MalaCards; DCTN1; -.
MIM; 105400; phenotype.
MIM; 168605; phenotype.
MIM; 601143; gene.
MIM; 607641; phenotype.
neXtProt; NX_Q14203; -.
OpenTargets; ENSG00000204843; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
Orphanet; 139589; Distal hereditary motor neuropathy type 7.
Orphanet; 178509; Perry syndrome.
PharmGKB; PA27180; -.
eggNOG; KOG0971; Eukaryota.
eggNOG; COG5244; LUCA.
GeneTree; ENSGT00760000119173; -.
HOGENOM; HOG000015352; -.
HOVERGEN; HBG004956; -.
InParanoid; Q14203; -.
KO; K04648; -.
OMA; CLRQSCN; -.
OrthoDB; EOG091G0WO0; -.
PhylomeDB; Q14203; -.
TreeFam; TF105246; -.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; Q14203; -.
ChiTaRS; DCTN1; human.
EvolutionaryTrace; Q14203; -.
GeneWiki; DCTN1; -.
GenomeRNAi; 1639; -.
PMAP-CutDB; Q14203; -.
PRO; PR:Q14203; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000204843; -.
CleanEx; HS_DCTN1; -.
ExpressionAtlas; Q14203; baseline and differential.
Genevisible; Q14203; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0099738; C:cell cortex region; IDA:UniProtKB.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005869; C:dynactin complex; IEA:InterPro.
GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; NAS:ProtInc.
GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
GO; GO:1905515; P:non-motile cilium assembly; IMP:UniProtKB.
GO; GO:0051081; P:nuclear envelope disassembly; IMP:UniProtKB.
GO; GO:0090063; P:positive regulation of microtubule nucleation; IDA:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
GO; GO:0010970; P:transport along microtubule; IEA:InterPro.
Gene3D; 2.30.30.190; -; 1.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR027663; DCTN1.
InterPro; IPR022157; Dynactin.
PANTHER; PTHR18916:SF40; PTHR18916:SF40; 1.
Pfam; PF01302; CAP_GLY; 1.
Pfam; PF12455; Dynactin; 1.
SMART; SM01052; CAP_GLY; 1.
SUPFAM; SSF74924; SSF74924; 1.
PROSITE; PS00845; CAP_GLY_1; 1.
PROSITE; PS50245; CAP_GLY_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amyotrophic lateral sclerosis;
Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Dynein; Microtubule; Mitosis; Neurodegeneration;
Nucleus; Parkinsonism; Phosphoprotein; Polymorphism;
Reference proteome; Transport; Ubl conjugation.
CHAIN 1 1278 Dynactin subunit 1.
/FTId=PRO_0000083518.
DOMAIN 48 90 CAP-Gly. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
REGION 911 1278 Interaction with HPS6.
{ECO:0000269|PubMed:25189619}.
COILED 213 547 {ECO:0000255}.
COILED 943 1049 {ECO:0000255}.
COILED 1182 1211 {ECO:0000255}.
COMPBIAS 164 191 Ser-rich.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 145 145 Phosphothreonine; by SLK.
{ECO:0000269|PubMed:23985322}.
MOD_RES 146 146 Phosphothreonine; by SLK.
{ECO:0000269|PubMed:23985322}.
MOD_RES 147 147 Phosphothreonine; by SLK.
{ECO:0000269|PubMed:23985322}.
MOD_RES 179 179 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:20679239}.
MOD_RES 212 212 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:20679239}.
VAR_SEQ 1 138 MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHR
GTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCD
EGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTD
TTAKTSKLRGLKPKK -> MMRQ (in isoform p135
and isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000760.
VAR_SEQ 1 17 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045392.
VAR_SEQ 132 151 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045393.
VAR_SEQ 132 138 Missing (in isoform 6).
{ECO:0000303|PubMed:8856662}.
/FTId=VSP_047174.
VAR_SEQ 1066 1070 Missing (in isoform 3, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_045394.
VARIANT 52 52 F -> L (in PERRYS; mutation carriers
either do not develop depression or they
do develop it late in the disease
course). {ECO:0000269|PubMed:24676999}.
/FTId=VAR_071452.
VARIANT 59 59 G -> S (in HMN7B; reduced affinity for
microtubules which has been suggested to
impair axonal transport; the effect is
identical to that of complete loss of the
CAP-Gly domain; decreased interaction
with MAPRE1; no effect on its interaction
with TBCB; dbSNP:rs121909342).
{ECO:0000269|PubMed:12627231,
ECO:0000269|PubMed:16505168,
ECO:0000269|PubMed:19136952,
ECO:0000269|PubMed:19279216,
ECO:0000269|PubMed:22777741}.
/FTId=VAR_015850.
VARIANT 71 71 G -> A (in PERRYS; dbSNP:rs67586389).
{ECO:0000269|PubMed:19136952}.
/FTId=VAR_063867.
VARIANT 71 71 G -> E (in PERRYS; dbSNP:rs67586389).
{ECO:0000269|PubMed:19136952}.
/FTId=VAR_063868.
VARIANT 71 71 G -> R (in PERRYS; reduced microtubule
binding; results in the accumulation of
intracytoplasmic inclusions; loss of
interaction with CLIP1; significant
decrease in motility of dynein-dynactin
complex along microtubules;
dbSNP:rs72466485).
{ECO:0000269|PubMed:19136952,
ECO:0000269|PubMed:24881494,
ECO:0000269|PubMed:25185702,
ECO:0000269|PubMed:26972003}.
/FTId=VAR_063869.
VARIANT 72 72 T -> P (in PERRYS; dbSNP:rs72466486).
{ECO:0000269|PubMed:19136952}.
/FTId=VAR_063870.
VARIANT 74 74 Q -> P (in PERRYS; diminishes microtubule
binding and lead to intracytoplasmic
inclusions; significant decrease in
motility of dynein-dynactin complex along
microtubules; defective in inhibiting
microtubule catastrophe in neurons;
dbSNP:rs72466487).
{ECO:0000269|PubMed:19136952,
ECO:0000269|PubMed:23874158,
ECO:0000269|PubMed:25185702}.
/FTId=VAR_063871.
VARIANT 78 78 Y -> C (in PERRYS; significantly reduced
microtubule binding).
{ECO:0000269|PubMed:24881494}.
/FTId=VAR_071453.
VARIANT 163 163 A -> P.
/FTId=VAR_001373.
VARIANT 196 196 I -> V (no effect of its interaction with
TBCB; no loss of localization to
microtubules; dbSNP:rs55862001).
{ECO:0000269|PubMed:17824900,
ECO:0000269|PubMed:22777741}.
/FTId=VAR_076920.
VARIANT 287 287 L -> M (in dbSNP:rs13420401).
/FTId=VAR_048677.
VARIANT 495 495 R -> Q (in dbSNP:rs17721059).
{ECO:0000269|PubMed:17824900}.
/FTId=VAR_048678.
VARIANT 571 571 M -> T (in ALS; associated with disease
susceptibility; dbSNP:rs121909343).
{ECO:0000269|PubMed:15326253}.
/FTId=VAR_063872.
VARIANT 670 670 Y -> F (found in a patient with
hereditary motor and sensory neuropathy;
unknown pathological significance).
{ECO:0000269|PubMed:24627108}.
/FTId=VAR_073287.
VARIANT 785 785 R -> W (in ALS; associated with disease
susceptibility; dbSNP:rs121909344).
{ECO:0000269|PubMed:15326253}.
/FTId=VAR_063873.
VARIANT 1101 1101 R -> K (in ALS; associated with disease
susceptibility; dbSNP:rs121909345).
{ECO:0000269|PubMed:16240349}.
/FTId=VAR_063874.
VARIANT 1249 1249 T -> I (in ALS; unknown pathological
significance; dbSNP:rs72466496).
{ECO:0000269|PubMed:15326253,
ECO:0000269|PubMed:17824900,
ECO:0000269|PubMed:19506225}.
/FTId=VAR_063875.
MUTAGEN 68 68 K->A: Abolishes interaction with CLIP1.
{ECO:0000269|PubMed:17828275}.
MUTAGEN 90 90 R->E: Abolishes interaction with CLIP1.
{ECO:0000269|PubMed:17828275}.
MUTAGEN 145 145 T->A: Affects centrosomal localization;
when associated with A-146 and A-147.
{ECO:0000269|PubMed:23985322}.
MUTAGEN 146 146 T->A: Affects centrosomal localization;
when associated with A-145 and A-147.
{ECO:0000269|PubMed:23985322}.
MUTAGEN 147 147 T->A: Affects centrosomal localization;
when associated with A-145 and A-146.
{ECO:0000269|PubMed:23985322}.
MUTAGEN 179 179 S->A: Non-phosphorylatable by PLK1.
Decreased nuclear envelope localization.
No loss of microtubule-binding. No effect
on its interaction with CLIP1.
{ECO:0000269|PubMed:20679239}.
MUTAGEN 179 179 S->D: No loss of localization to nuclear
envelope. Decrease in microtubule-
binding. No effect on its interaction
with CLIP1.
{ECO:0000269|PubMed:20679239}.
MUTAGEN 212 212 S->A: No effect on its interaction with
CLIP1 and PLK1.
{ECO:0000269|PubMed:20679239}.
CONFLICT 10 10 S -> N (in Ref. 7; CAA67333).
{ECO:0000305}.
CONFLICT 257 257 Q -> R (in Ref. 2; BAG59757).
{ECO:0000305}.
CONFLICT 349 349 K -> R (in Ref. 2; AK314352).
{ECO:0000305}.
CONFLICT 368 368 A -> V (in Ref. 2; AK314352).
{ECO:0000305}.
CONFLICT 526 526 H -> N (in Ref. 5; AAH71583).
{ECO:0000305}.
CONFLICT 618 618 K -> R (in Ref. 5; AAH71583).
{ECO:0000305}.
CONFLICT 712 712 D -> V (in Ref. 7; CAA67333).
{ECO:0000305}.
CONFLICT 1081 1081 V -> M (in Ref. 9; AAP35404).
{ECO:0000305}.
CONFLICT 1261 1261 R -> Q (in Ref. 2; BAG59757).
{ECO:0000305}.
CONFLICT 1274 1274 S -> I (in Ref. 5; AAH71583).
{ECO:0000305}.
STRAND 17 19 {ECO:0000244|PDB:2COY}.
STRAND 32 35 {ECO:0000244|PDB:1TXQ}.
TURN 36 38 {ECO:0000244|PDB:1TXQ}.
STRAND 41 48 {ECO:0000244|PDB:1TXQ}.
STRAND 51 55 {ECO:0000244|PDB:1TXQ}.
STRAND 57 65 {ECO:0000244|PDB:1TXQ}.
STRAND 67 73 {ECO:0000244|PDB:1TXQ}.
STRAND 76 78 {ECO:0000244|PDB:1TXQ}.
TURN 83 85 {ECO:0000244|PDB:2HQH}.
STRAND 86 89 {ECO:0000244|PDB:1TXQ}.
HELIX 91 93 {ECO:0000244|PDB:1TXQ}.
STRAND 94 96 {ECO:0000244|PDB:1TXQ}.
SEQUENCE 1278 AA; 141695 MW; 6DCEA5E67856E4BC CRC64;
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE
GTDTTAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGASSSLGPS GSASAGELSS
SEPSTPAQTP LAAPIIPTPV LTSPGAVPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE
DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL
KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE
STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE
TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA
SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF ELSENCSERP GLRGAAGEQL SFAAGLVYSL
SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL
TKAIKYYQHL YSIHLAEQPE DCTMQLADHI KFTQSALDCM SVEVGRLRAF LQGGQEATDI
ALLLRDLETS CSDIRQFCKK IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV
LQEVAAAAAQ LIAPLAENEG LLVAALEELA FKASEQIYGT PSSSPYECLR QSCNILISTM
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK
IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLEE TQALLRKKEK EFEETMDALQ
ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEQQR GAIPGQAPGS
VPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILKGAQMK ASLASLPPLH VAKLSHEGPG
SELPAGALYR KTSQLLETLN QLSTHTHVVD ITRTSPAAKS PSAQLMEQVA QLKSLSDTVE
KLKDEVLKET VSQRPGATVP TDFATFPSSA FLRAKEEQQD DTVYMGKVTF SCAAGFGQRH
RLVLTQEQLH QLHSRLIS


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