Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Emerin

 EMD_HUMAN               Reviewed;         254 AA.
P50402; Q6FI02;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
30-AUG-2017, entry version 190.
RecName: Full=Emerin;
Name=EMD; Synonyms=EDMD, STA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Teratocarcinoma;
PubMed=7894480; DOI=10.1038/ng1294-323;
Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G.,
Toniolo D.;
"Identification of a novel X-linked gene responsible for Emery-
Dreifuss muscular dystrophy.";
Nat. Genet. 8:323-327(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8733135; DOI=10.1093/hmg/5.5.659;
Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N.,
Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
D'Urso M.;
"Long-range sequence analysis in Xq28: thirteen known and six
candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
G6PD loci.";
Hum. Mol. Genet. 5:659-668(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8655156; DOI=10.1007/BF02281886;
Yamada T., Kobayashi T.;
"A novel emerin mutation in a Japanese patient with Emery-Dreifuss
muscular dystrophy.";
Hum. Genet. 97:693-694(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8595407; DOI=10.1093/hmg/4.10.1859;
Bione S., Small K., Aksmanovic M.A., D'Urso M., Ciccodicola A.,
Merlini L., Morandi L., Kress W., Yates J.R.W., Warren S.T.,
Toniolo D.;
"Identification of new mutations in the Emery-Dreifuss muscular
dystrophy gene and evidence for genetic heterogeneity of the
disease.";
Hum. Mol. Genet. 4:1859-1863(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[10]
PROTEIN SEQUENCE OF 1-17.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 1-31; 37-45; 48-115 AND 158-203, ACETYLATION AT
MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, and Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[12]
SUBCELLULAR LOCATION.
PubMed=9673989; DOI=10.1016/S0960-8966(98)00031-5;
Squarzoni S., Sabatelli P., Ognibene A., Toniolo D., Cartegni L.,
Cobianchi F., Petrini S., Merlini L., Maraldi N.M.;
"Immunocytochemical detection of emerin within the nuclear matrix.";
Neuromuscul. Disord. 8:338-344(1998).
[13]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=9472006;
Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.;
"Aberrant intracellular targeting and cell cycle-dependent
phosphorylation of emerin contribute to the Emery-Dreifuss muscular
dystrophy phenotype.";
J. Cell Sci. 111:781-792(1998).
[14]
INTERACTION WITH BANF1.
PubMed=11792822;
Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y.,
Yoneda Y., Wilson K.L., Hiraoka Y.;
"BAF is required for emerin assembly into the reforming nuclear
envelope.";
J. Cell Sci. 114:4575-4585(2001).
[15]
INTERACTION WITH YTHDC1.
PubMed=12755701; DOI=10.1046/j.1432-1033.2003.03617.x;
Wilkinson F.L., Holaska J.M., Zhang Z., Sharma A., Manilal S.,
Holt I., Stamm S., Wilson K.L., Morris G.E.;
"Emerin interacts in vitro with the splicing-associated factor, YT521-
B.";
Eur. J. Biochem. 270:2459-2466(2003).
[16]
INTERACTION WITH GMCL.
PubMed=12493765; DOI=10.1074/jbc.M208811200;
Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L.;
"Transcriptional repressor germ cell-less (GCL) and barrier to
autointegration factor (BAF) compete for binding to emerin in vitro.";
J. Biol. Chem. 278:6969-6975(2003).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[18]
INTERACTION WITH BCLAF1, AND CHARACTERIZATION OF VARIANT EDMD1 PHE-54.
PubMed=15009215; DOI=10.1111/j.1432-1033.2004.04007.x;
Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N.,
Mori C., Wilson K.L., Hiraoka Y.;
"Emerin binding to Btf, a death-promoting transcriptional repressor,
is disrupted by a missense mutation that causes Emery-Dreifuss
muscular dystrophy.";
Eur. J. Biochem. 271:1035-1045(2004).
[19]
FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF
SER-196 AND SER-197, AND CHARACTERIZATION OF VARIANTS EDMD1 PHE-54;
HIS-133 AND HIS-183.
PubMed=15328537; DOI=10.1371/journal.pbio.0020231;
Holaska J.M., Kowalski A.K., Wilson K.L.;
"Emerin caps the pointed end of actin filaments: evidence for an actin
cortical network at the nuclear inner membrane.";
PLoS Biol. 2:1354-1362(2004).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
FUNCTION, AND INTERACTION WITH CTNNB1.
PubMed=16858403; DOI=10.1038/sj.emboj.7601230;
Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H.,
Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S.,
Broers J.L.V., Blankesteijn W.M., Salpingidou G., Wilson R.G.,
Ellis J.A., Hutchison C.J.;
"The inner nuclear membrane protein emerin regulates beta-catenin
activity by restricting its accumulation in the nucleus.";
EMBO J. 25:3275-3285(2006).
[23]
PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITH
LMNA, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-49.
PubMed=16972941; DOI=10.1111/j.1742-4658.2006.05464.x;
Roberts R.C., Sutherland-Smith A.J., Wheeler M.A., Jensen O.N.,
Emerson L.J., Spiliotis I.I., Tate C.G., Kendrick-Jones J.,
Ellis J.A.;
"The Emery-Dreifuss muscular dystrophy associated-protein emerin is
phosphorylated on serine 49 by protein kinase A.";
FEBS J. 273:4562-4575(2006).
[24]
FUNCTION.
PubMed=16680152; DOI=10.1038/nature04682;
Jacque J.-M., Stevenson M.;
"The inner-nuclear-envelope protein emerin regulates HIV-1
infectivity.";
Nature 441:641-645(2006).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BETA-TUBULIN.
PubMed=17785515; DOI=10.1083/jcb.200702026;
Salpingidou G., Smertenko A., Hausmanowa-Petrucewicz I., Hussey P.J.,
Hutchison C.J.;
"A novel role for the nuclear membrane protein emerin in association
of the centrosome to the outer nuclear membrane.";
J. Cell Biol. 178:897-904(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; SER-60 AND
SER-87, AND 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).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LMNA.
PubMed=19323649; DOI=10.1042/BC20080175;
Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M.,
Schena E., Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.;
"Emerin-prelamin A interplay in human fibroblasts.";
Biol. Cell 101:541-554(2009).
[31]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=19167377; DOI=10.1016/j.ydbio.2008.12.038;
Mamada H., Takahashi N., Taira M.;
"Involvement of an inner nuclear membrane protein, Nemp1, in Xenopus
neural development through an interaction with the chromatin protein
BAF.";
Dev. Biol. 327:497-507(2009).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, 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).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-8 AND SER-171, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
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).
[36]
INTERACTION WITH TMEM201.
PubMed=21610090; DOI=10.1242/jcs.078923;
Gudise S., Figueroa R.A., Lindberg R., Larsson V., Hallberg E.;
"Samp1 is functionally associated with the LINC complex and A-type
lamina networks.";
J. Cell Sci. 124:2077-2085(2011).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-29; SER-49;
SER-60; SER-87; SER-98; SER-171 AND SER-173, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND 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).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[43]
STRUCTURE BY NMR OF 2-54.
PubMed=11470279; DOI=10.1016/S0014-5793(01)02649-7;
Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J.,
Zinn-Justin S.;
"Structural analysis of emerin, an inner nuclear membrane protein
mutated in X-linked Emery-Dreifuss muscular dystrophy.";
FEBS Lett. 501:171-176(2001).
[44]
STRUCTURE BY NMR OF 2-54.
PubMed=11435115; DOI=10.1016/S0969-2126(01)00611-6;
Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K.,
Callebaut I., Worman H.J., Zinn-Justin S.;
"Structural characterization of the LEM motif common to three human
inner nuclear membrane proteins.";
Structure 9:503-511(2001).
[45]
VARIANTS EDMD1 HIS-183 AND THR-183.
PubMed=10323252; DOI=10.1007/s004390050946;
Ellis J.A., Yates J.R.W., Kendrick-Jones J., Brown C.A.;
"Changes at P183 of emerin weaken its protein-protein interactions
resulting in X-linked Emery-Dreifuss muscular dystrophy.";
Hum. Genet. 104:262-268(1999).
[46]
VARIANT EDMD1 HIS-133.
PubMed=11587540; DOI=10.1006/bbrc.2001.5708;
Holt I., Clements L., Manilal S., Morris G.E.;
"How does a g993t mutation in the emerin gene cause Emery-Dreifuss
muscular dystrophy?";
Biochem. Biophys. Res. Commun. 287:1129-1133(2001).
-!- FUNCTION: Stabilizes and promotes the formation of a nuclear actin
cortical network. Stimulates actin polymerization in vitro by
binding and stabilizing the pointed end of growing filaments.
Inhibits beta-catenin activity by preventing its accumulation in
the nucleus. Acts by influencing the nuclear accumulation of beta-
catenin through a CRM1-dependent export pathway. Links centrosomes
to the nuclear envelope via a microtubule association. EMD and BAF
are cooperative cofactors of HIV-1 infection. Association of EMD
with the viral DNA requires the presence of BAF and viral
integrase. The association of viral DNA with chromatin requires
the presence of BAF and EMD. Required for proper localization of
non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537,
ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403,
ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}.
-!- SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and
YTHDC1/YT521. Interacts with TMEM43; the interaction retains
emerin in the nuclear inner membrane. Interacts with SUN1 and SUN2
(By similarity). Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and
beta-tubulin. Interacts with TMEM201. {ECO:0000250,
ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12493765,
ECO:0000269|PubMed:12755701, ECO:0000269|PubMed:15009215,
ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16858403,
ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:17785515,
ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:21610090}.
-!- INTERACTION:
Q9ULW3:ABT1; NbExp=5; IntAct=EBI-489887, EBI-2602396;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-489887, EBI-8637627;
O75531:BANF1; NbExp=6; IntAct=EBI-489887, EBI-1055977;
Q9NYF8:BCLAF1; NbExp=3; IntAct=EBI-489887, EBI-437804;
Q8N7W2-2:BEND7; NbExp=8; IntAct=EBI-489887, EBI-10181188;
Q13895:BYSL; NbExp=3; IntAct=EBI-489887, EBI-358049;
Q8NEC5:CATSPER1; NbExp=8; IntAct=EBI-489887, EBI-744545;
Q8N6L0:CCDC155; NbExp=7; IntAct=EBI-489887, EBI-749265;
Q8NHQ1:CEP70; NbExp=6; IntAct=EBI-489887, EBI-739624;
O43889-2:CREB3; NbExp=3; IntAct=EBI-489887, EBI-625022;
P35222:CTNNB1; NbExp=3; IntAct=EBI-489887, EBI-491549;
Q5JST6:EFHC2; NbExp=3; IntAct=EBI-489887, EBI-2349927;
Q969F0:FATE1; NbExp=9; IntAct=EBI-489887, EBI-743099;
Q9P127:LUZP4; NbExp=8; IntAct=EBI-489887, EBI-10198848;
Q8N8X9:MAB21L3; NbExp=3; IntAct=EBI-489887, EBI-10268010;
P50222:MEOX2; NbExp=5; IntAct=EBI-489887, EBI-748397;
Q8TB93:PAK7; NbExp=3; IntAct=EBI-489887, EBI-741896;
Q99962:SH3GL2; NbExp=2; IntAct=EBI-489887, EBI-77938;
Q12846:STX4; NbExp=3; IntAct=EBI-489887, EBI-744942;
Q9D666:Sun1 (xeno); NbExp=4; IntAct=EBI-489887, EBI-6752574;
Q9UH99:SUN2; NbExp=3; IntAct=EBI-489887, EBI-1044964;
Q8NF91-11:SYNE1; NbExp=3; IntAct=EBI-489887, EBI-10758913;
Q8NF91-3:SYNE1; NbExp=5; IntAct=EBI-489887, EBI-10760352;
Q8WXH0-3:SYNE2; NbExp=5; IntAct=EBI-489887, EBI-10760388;
Q5SNT2-2:TMEM201; NbExp=5; IntAct=EBI-489887, EBI-11994282;
Q9Y228:TRAF3IP3; NbExp=10; IntAct=EBI-489887, EBI-765817;
Q8IWZ5:TRIM42; NbExp=6; IntAct=EBI-489887, EBI-5235829;
O95292:VAPB; NbExp=5; IntAct=EBI-489887, EBI-1188298;
Q9NTW7:ZFP64; NbExp=3; IntAct=EBI-489887, EBI-745730;
P49910:ZNF165; NbExp=3; IntAct=EBI-489887, EBI-741694;
Q53Z40:ZNF165; NbExp=3; IntAct=EBI-489887, EBI-10186058;
Q9UNY5:ZNF232; NbExp=3; IntAct=EBI-489887, EBI-749023;
Q9BYN7:ZNF341; NbExp=4; IntAct=EBI-489887, EBI-9089622;
Q6P9A3:ZNF549; NbExp=4; IntAct=EBI-489887, EBI-13046342;
-!- SUBCELLULAR LOCATION: Nucleus inner membrane
{ECO:0000269|PubMed:19167377}; Single-pass membrane protein;
Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer
membrane. Note=Colocalized with BANF1 at the central region of the
assembling nuclear rim, near spindle-attachment sites. The
accumulation of different intermediates of prelamin-A/C (non-
farnesylated or carboxymethylated farnesylated prelamin-A/C) in
fibroblasts modify its localization in the nucleus.
-!- TISSUE SPECIFICITY: Skeletal muscle, heart, colon, testis, ovary
and pancreas.
-!- PTM: Found in four different phosphorylated forms, three of which
appear to be associated with the cell cycle.
{ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:9472006}.
-!- DISEASE: Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1)
[MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a
degenerative myopathy characterized by weakness and atrophy of
muscle without involvement of the nervous system, early
contractures of the elbows, Achilles tendons and spine, and
cardiomyopathy associated with cardiac conduction defects.
{ECO:0000269|PubMed:10323252, ECO:0000269|PubMed:11587540,
ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=EMD db; Note="EMD mutation database";
URL="http://www.dmd.nl/nmdb/index.php?select_db=EMD";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X82434; CAA57817.1; -; mRNA.
EMBL; L44140; AAA92645.1; -; Genomic_DNA.
EMBL; D64111; BAA10972.1; -; Genomic_DNA.
EMBL; X86810; CAA60500.1; -; Genomic_DNA.
EMBL; BT007401; AAP36065.1; -; mRNA.
EMBL; CR536536; CAG38773.1; -; mRNA.
EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471172; EAW72742.1; -; Genomic_DNA.
EMBL; BC000738; AAH00738.1; -; mRNA.
CCDS; CCDS14745.1; -.
PIR; S50834; S50834.
RefSeq; NP_000108.1; NM_000117.2.
UniGene; Hs.522823; -.
PDB; 1JEI; NMR; -; A=2-54.
PDB; 2ODC; NMR; -; I=2-47.
PDB; 2ODG; NMR; -; C=2-47.
PDBsum; 1JEI; -.
PDBsum; 2ODC; -.
PDBsum; 2ODG; -.
ProteinModelPortal; P50402; -.
SMR; P50402; -.
BioGrid; 108325; 172.
DIP; DIP-34638N; -.
IntAct; P50402; 110.
MINT; MINT-266014; -.
STRING; 9606.ENSP00000358857; -.
iPTMnet; P50402; -.
PhosphoSitePlus; P50402; -.
BioMuta; EMD; -.
DMDM; 1706639; -.
EPD; P50402; -.
PaxDb; P50402; -.
PeptideAtlas; P50402; -.
PRIDE; P50402; -.
TopDownProteomics; P50402; -.
DNASU; 2010; -.
Ensembl; ENST00000369842; ENSP00000358857; ENSG00000102119.
GeneID; 2010; -.
KEGG; hsa:2010; -.
UCSC; uc004fkl.4; human.
CTD; 2010; -.
DisGeNET; 2010; -.
GeneCards; EMD; -.
GeneReviews; EMD; -.
HGNC; HGNC:3331; EMD.
HPA; CAB001545; -.
HPA; CAB002029; -.
HPA; CAB062552; -.
HPA; HPA000609; -.
MalaCards; EMD; -.
MIM; 300384; gene.
MIM; 310300; phenotype.
neXtProt; NX_P50402; -.
OpenTargets; ENSG00000102119; -.
Orphanet; 98863; X-linked Emery-Dreifuss muscular dystrophy.
PharmGKB; PA27766; -.
eggNOG; ENOG410IJ10; Eukaryota.
eggNOG; ENOG410ZEWX; LUCA.
GeneTree; ENSGT00390000002034; -.
HOGENOM; HOG000081509; -.
HOVERGEN; HBG001099; -.
InParanoid; P50402; -.
KO; K12569; -.
OMA; SVDSDMY; -.
OrthoDB; EOG091G0M7U; -.
PhylomeDB; P50402; -.
TreeFam; TF337236; -.
Reactome; R-HSA-2993913; Clearance of Nuclear Envelope Membranes from Chromatin.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope Reformation.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
SIGNOR; P50402; -.
EvolutionaryTrace; P50402; -.
GeneWiki; Emerin; -.
GenomeRNAi; 2010; -.
PRO; PR:P50402; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102119; -.
CleanEx; HS_EMD; -.
ExpressionAtlas; P50402; baseline and differential.
Genevisible; P50402; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005635; C:nuclear envelope; IDA:LIFEdb.
GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:BHF-UCL.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
CDD; cd12939; LEM_emerin; 1.
Gene3D; 1.10.720.40; -; 1.
InterPro; IPR035004; Emerin.
InterPro; IPR011015; LEM/LEM-like_dom.
InterPro; IPR003887; LEM_dom.
InterPro; IPR034989; LEM_emerin.
PANTHER; PTHR15171:SF3; PTHR15171:SF3; 1.
Pfam; PF03020; LEM; 1.
SMART; SM00540; LEM; 1.
SUPFAM; SSF63451; SSF63451; 1.
PROSITE; PS50954; LEM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Cardiomyopathy;
Complete proteome; Direct protein sequencing; Disease mutation;
Emery-Dreifuss muscular dystrophy; Membrane; Microtubule; Nucleus;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 254 Emerin.
/FTId=PRO_0000206140.
TRANSMEM 223 243 Helical. {ECO:0000255}.
DOMAIN 1 45 LEM. {ECO:0000255|PROSITE-
ProRule:PRU00313}.
REGION 46 222 Interaction with F-actin. {ECO:0000305}.
REGION 168 186 Interaction with CTNNB1.
{ECO:0000269|PubMed:16858403}.
COMPBIAS 192 199 Poly-Ser.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.11}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 49 49 Phosphoserine; by PKA.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16972941}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:Q63190}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:Q63190}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:Q63190}.
MOD_RES 161 161 Phosphotyrosine.
{ECO:0000250|UniProtKB:O08579}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000250|UniProtKB:O08579}.
VARIANT 54 54 S -> F (in EDMD1; no loss of binding to
F-actin, enhanced rate of actin
polymerization and loss of binding to
BCLAF1). {ECO:0000269|PubMed:15009215,
ECO:0000269|PubMed:15328537}.
/FTId=VAR_005198.
VARIANT 133 133 Q -> H (in EDMD1; loss of binding to F-
actin). {ECO:0000269|PubMed:11587540,
ECO:0000269|PubMed:15328537}.
/FTId=VAR_016016.
VARIANT 149 149 D -> H (in dbSNP:rs2070818).
/FTId=VAR_038433.
VARIANT 183 183 P -> H (in EDMD1; no loss of binding to
F-actin and enhanced rate of actin
polymerization; dbSNP:rs104894805).
{ECO:0000269|PubMed:10323252,
ECO:0000269|PubMed:15328537}.
/FTId=VAR_005199.
VARIANT 183 183 P -> T (in EDMD1; dbSNP:rs104894806).
{ECO:0000269|PubMed:10323252}.
/FTId=VAR_005200.
MUTAGEN 49 49 S->A: Abolishes phosphorylation. No
effect on targeting to nuclear envelope
nor on interaction with LMNA.
{ECO:0000269|PubMed:16972941}.
MUTAGEN 49 49 S->E: Mimics phosphorylation. No effect
on targeting to nuclear envelope nor on
interaction with LMNA.
{ECO:0000269|PubMed:16972941}.
MUTAGEN 196 196 S->A: No loss of binding to F-actin; when
associated with A-197.
{ECO:0000269|PubMed:15328537}.
MUTAGEN 197 197 S->A: No loss of binding to F-actin; when
associated with A-196.
{ECO:0000269|PubMed:15328537}.
TURN 4 6 {ECO:0000244|PDB:1JEI}.
HELIX 9 16 {ECO:0000244|PDB:1JEI}.
STRAND 17 19 {ECO:0000244|PDB:1JEI}.
HELIX 29 31 {ECO:0000244|PDB:1JEI}.
HELIX 32 37 {ECO:0000244|PDB:1JEI}.
HELIX 40 42 {ECO:0000244|PDB:1JEI}.
SEQUENCE 254 AA; 28994 MW; EB62EDD59B7A044F CRC64;
MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS
FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS
VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS
YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF
FIYHFMQAEE GNPF


Related products :

Catalog number Product name Quantity
IQ567 Mouse Anti-Emerin Target Antigen Emerin Host Isotype Mouse IgG1 Application WB, IF 0.1ml (1mg/ml)
LF-MA10097 anti-emerin (3B9), Mouse monoclonal to emerin, Isotype IgG2a, Host Mouse 100 ug
LF-PA40380 anti-Emerin (EMD) , Rabbit polyclonal to Emerin (EMD) , Isotype IgG, Host Rabbit 50 ug
MO20027-100 Emerin 0.1 ml
Z5100048 Emerin 14 nmole
MO20027-100 Emerin 0.1 ml
BP4518 Emerin 20 µl
AP01160PU-S Emerin 50 µl
AP01159PU-S Emerin 50 µl
AP30313PU-N Emerin 0.1 mg
BP4518 Emerin 20 µl
BP4518 Emerin 20 µl
AM00583SU-N Emerin 0.5 ml
ABP-Ri-VAsiD31 emerin 5OD (12.5nmol)
AM00583SU-N Emerin 0.5 ml
AP01159PU-S Emerin 50 µl
Z5100048 Emerin 14 nmole
AP01160PU-S Emerin 50 µl
AP07749PU-N Emerin 50 µg
AP07749PU-N Emerin 50 µg
orb76617 Emerin antibody 50 ul
orb74797 Emerin antibody 100 ug
orb76618 Emerin antibody 0.1 ml
orb76619 Emerin antibody 20 ul(Trial Size)
orb76620 Emerin antibody 50 ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur