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

14-3-3 protein epsilon (14-3-3E)

 1433E_HUMAN             Reviewed;         255 AA.
P62258; B3KY71; D3DTH5; P29360; P42655; Q4VJB6; Q53XZ5; Q63631;
Q7M4R4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 167.
RecName: Full=14-3-3 protein epsilon;
Short=14-3-3E;
Name=YWHAE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7644510; DOI=10.1073/pnas.92.17.7892;
Conklin D.S., Galaktionov K., Beach D.;
"14-3-3 proteins associate with cdc25 phosphatases.";
Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8858348; DOI=10.1101/gr.6.8.735;
Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
"14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on
chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome
region.";
Genome Res. 6:735-741(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8684458; DOI=10.1038/382308a0;
Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
"Function of 14-3-3 proteins.";
Nature 382:308-308(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=20417184; DOI=10.1016/j.bbrc.2010.04.104;
Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.;
"Functional identification of a novel 14-3-3 epsilon splicing variant
suggests dimerization is not necessary for 14-3-3 epsilon to inhibit
UV-induced apoptosis.";
Biochem. Biophys. Res. Commun. 396:401-406(2010).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Luk S.C.W., Lee C.Y., Waye M.M.Y.;
"Sequence determination of human epsilon 14-3-3 protein.";
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tanigami A., Chong S.S., Ledbetter D.H.;
"14-3-3 epsilon genomic sequence.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND SV).
TISSUE=Caudate nucleus, Heart, and Subthalamic nucleus;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[11]
PROTEIN SEQUENCE OF 1-19.
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).
[12]
PROTEIN SEQUENCE OF 1-56; 62-73; 95-118; 131-193 AND 197-255,
INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[13]
PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAY-2005) to UniProtKB.
[14]
PROTEIN SEQUENCE OF 50-60, AND INTERACTION WITH KSR1.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[15]
PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
TISSUE=Histiocytic lymphoma;
PubMed=2026444;
Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.;
"Isolation and partial characterization of the structures of
fibroblast activating factor-related proteins from U937 cells.";
Immunology 72:350-354(1991).
[16]
PROTEIN SEQUENCE OF 131-141 AND 154-190, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[17]
INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
PubMed=10644344; DOI=10.1128/JVI.74.4.1736-1741.2000;
Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.;
"Hepatitis C virus core protein interacts with 14-3-3 protein and
activates the kinase Raf-1.";
J. Virol. 74:1736-1741(2000).
[18]
INTERACTION WITH AANAT.
PubMed=11427721; DOI=10.1073/pnas.141118798;
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
3-3-binding switch in melatonin synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
[19]
INTERACTION WITH CDKN1B, AND SUBCELLULAR LOCATION.
PubMed=12042314; DOI=10.1074/jbc.M203668200;
Fujita N., Sato S., Katayama K., Tsuruo T.;
"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3
and cytoplasmic localization.";
J. Biol. Chem. 277:28706-28713(2002).
[20]
FUNCTION, INTERACTION WITH HSF1, AND SUBCELLULAR LOCATION.
PubMed=12917326; DOI=10.1128/MCB.23.17.6013-6026.2003;
Wang X., Grammatikakis N., Siganou A., Calderwood S.K.;
"Regulation of molecular chaperone gene transcription involves the
serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic
sequestration of heat shock factor 1.";
Mol. Cell. Biol. 23:6013-6026(2003).
[21]
INTERACTION WITH GRB10.
PubMed=15722337; DOI=10.1074/jbc.M501477200;
Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
"Phosphorylation of grb10 regulates its interaction with 14-3-3.";
J. Biol. Chem. 280:16987-16993(2005).
[22]
INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15696159; DOI=10.1038/ncb1228;
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[23]
INTERACTION WITH YWHAZ.
PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
"Protein kinase A phosphorylates and regulates dimerization of 14-3-3
epsilon.";
FEBS Lett. 580:305-310(2006).
[24]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[25]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[27]
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).
[28]
INTERACTION WITH SLITRK1.
PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
Kajiwara Y., Buxbaum J.D., Grice D.E.;
"SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a
phosphorylation-dependent manner.";
Biol. Psychiatry 66:918-925(2009).
[29]
INTERACTION WITH SRPK2.
PubMed=19592491; DOI=10.1074/jbc.M109.026237;
Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
cycle and cell death in neurons.";
J. Biol. Chem. 284:24512-24525(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 AND
LYS-123, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, 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).
[32]
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, 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).
[36]
INTERACTION WITH DAPK2.
PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
"Suppression of death-associated protein kinase 2 by interaction with
14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 464:70-75(2015).
[37]
INTERACTION WITH DENND1A.
PubMed=26055712; DOI=10.1074/jbc.M115.636712;
Kulasekaran G., Nossova N., Marat A.L., Lund I., Cremer C.,
Ioannou M.S., McPherson P.S.;
"Phosphorylation-dependent regulation of Connecdenn/DENND1 guanine
nucleotide exchange factors.";
J. Biol. Chem. 290:17999-18008(2015).
[38]
INTERACTION WITH RIPOR2.
PubMed=25588844; DOI=10.1242/jcs.161497;
Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
"Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
leading edges polarizes neutrophils.";
J. Cell Sci. 128:992-1000(2015).
[39]
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).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[41]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, IDENTIFICATION BY
MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
PubMed=17085597; DOI=10.1073/pnas.0605779103;
Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
"Structural basis for protein-protein interactions in the 14-3-3
protein family.";
Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner (By
similarity). Positively regulates phosphorylated protein HSF1
nuclear export to the cytoplasm (PubMed:12917326).
{ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:12917326}.
-!- SUBUNIT: Homodimer (PubMed:17085597). Heterodimerizes with YWHAZ
(PubMed:16376338). Interacts with PKA-phosphorylated AANAT
(PubMed:11427721). Interacts with ABL1 (phosphorylated form); the
interaction retains it in the cytoplasm (PubMed:15696159).
Interacts with ARHGEF28 (By similarity). Interacts with BEX3 (By
similarity). Weakly interacts with CDKN1B (PubMed:12042314).
Interacts with the 'Thr-369' phosphorylated form of DAPK2
(PubMed:26047703). Interacts with DENND1A (PubMed:26055712).
Interacts with GAB2 (PubMed:19172738). Interacts with
phosphorylated GRB10 (PubMed:15722337). Interacts with KSR1
(PubMed:10409742). Interacts with NDEL1 (By similarity). Interacts
with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts
with the phosphorylated (by AKT1) form of SRPK2 (PubMed:19592491).
Interacts with TIAM2. Interacts with the 'Ser-1134' and 'Ser-1161'
phosphorylated form of SOS1 (By similarity). Interacts with ZFP36
(via phosphorylated form) (By similarity). Interacts with SLITRK1
(PubMed:19640509). Interacts with HSF1 (via phosphorylated form);
this interaction promotes HSF1 sequestration in the cytoplasm in a
ERK-dependent manner (PubMed:12917326). Interacts with RIPOR2
isoform 2 (PubMed:25588844). {ECO:0000250|UniProtKB:P62259,
ECO:0000250|UniProtKB:P62260, ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15696159,
ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:16376338,
ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:19172738,
ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:19640509,
ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:26055712}.
-!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
{ECO:0000269|PubMed:10644344}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-356498, EBI-356498;
O92972:- (xeno); NbExp=5; IntAct=EBI-356498, EBI-9213553;
Q96AP0:ACD; NbExp=2; IntAct=EBI-356498, EBI-717666;
O14727:APAF1; NbExp=2; IntAct=EBI-356498, EBI-446492;
P10398:ARAF; NbExp=3; IntAct=EBI-356498, EBI-365961;
O00257-3:CBX4; NbExp=2; IntAct=EBI-356498, EBI-4392727;
Q9Y3M2:CBY1; NbExp=3; IntAct=EBI-356498, EBI-947308;
Q86Z20:CCDC125; NbExp=4; IntAct=EBI-356498, EBI-11977221;
O94921:CDK14; NbExp=3; IntAct=EBI-356498, EBI-1043945;
Q9UKT5:FBXO4; NbExp=5; IntAct=EBI-356498, EBI-960409;
P56524:HDAC4; NbExp=4; IntAct=EBI-356498, EBI-308629;
Q14678-2:KANK1; NbExp=3; IntAct=EBI-356498, EBI-6173812;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-356498, EBI-5323863;
Q99759:MAP3K3; NbExp=3; IntAct=EBI-356498, EBI-307281;
O15151:MDM4; NbExp=3; IntAct=EBI-356498, EBI-398437;
P58340:MLF1; NbExp=3; IntAct=EBI-356498, EBI-721328;
O35244:Prdx6 (xeno); NbExp=2; IntAct=EBI-356498, EBI-915490;
P04049:RAF1; NbExp=3; IntAct=EBI-356498, EBI-365996;
P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-356498, EBI-6930266;
Q99469:STAC; NbExp=2; IntAct=EBI-356498, EBI-2652799;
Q9GZV5:WWTR1; NbExp=3; IntAct=EBI-356498, EBI-747743;
P46937:YAP1; NbExp=5; IntAct=EBI-356498, EBI-1044059;
P31946:YWHAB; NbExp=4; IntAct=EBI-356498, EBI-359815;
P61981:YWHAG; NbExp=5; IntAct=EBI-356498, EBI-359832;
P27348:YWHAQ; NbExp=4; IntAct=EBI-356498, EBI-359854;
P63104:YWHAZ; NbExp=6; IntAct=EBI-356498, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12917326}.
Cytoplasm {ECO:0000269|PubMed:12917326}. Melanosome
{ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV. {ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:17081065}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62258-1; Sequence=Displayed;
Name=SV;
IsoId=P62258-2; Sequence=VSP_040621;
Note=Unable to dimerize with YWHAZ.;
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U20972; AAC50175.1; -; mRNA.
EMBL; U54778; AAC50710.1; -; mRNA.
EMBL; U43399; AAC50625.1; -; mRNA.
EMBL; U43430; AAD00026.1; -; mRNA.
EMBL; U28936; AAA75301.1; -; mRNA.
EMBL; AB017103; BAA32538.1; -; Genomic_DNA.
EMBL; AY883089; AAX68683.1; -; mRNA.
EMBL; AK128785; BAG54733.1; -; mRNA.
EMBL; AK295260; BAG58249.1; -; mRNA.
EMBL; AK316185; BAH14556.1; -; mRNA.
EMBL; BT007161; AAP35825.1; -; mRNA.
EMBL; CH471108; EAW90628.1; -; Genomic_DNA.
EMBL; CH471108; EAW90629.1; -; Genomic_DNA.
EMBL; BC000179; AAH00179.1; -; mRNA.
EMBL; BC001440; AAH01440.1; -; mRNA.
CCDS; CCDS11001.1; -. [P62258-1]
PIR; A61235; A61235.
PIR; I38947; I38947.
RefSeq; NP_006752.1; NM_006761.4. [P62258-1]
UniGene; Hs.513851; -.
PDB; 2BR9; X-ray; 1.75 A; A=1-233.
PDB; 3UAL; X-ray; 1.80 A; A=1-232.
PDB; 3UBW; X-ray; 1.90 A; A=1-234.
PDB; 6EIH; X-ray; 2.70 A; A=3-232.
PDBsum; 2BR9; -.
PDBsum; 3UAL; -.
PDBsum; 3UBW; -.
PDBsum; 6EIH; -.
ProteinModelPortal; P62258; -.
SMR; P62258; -.
BioGrid; 113363; 430.
CORUM; P62258; -.
DIP; DIP-36676N; -.
ELM; P62258; -.
IntAct; P62258; 179.
MINT; P62258; -.
STRING; 9606.ENSP00000264335; -.
ChEMBL; CHEMBL3329082; -.
DrugBank; DB01780; Fusicoccin.
iPTMnet; P62258; -.
PhosphoSitePlus; P62258; -.
SwissPalm; P62258; -.
BioMuta; YWHAE; -.
DMDM; 51702210; -.
OGP; P42655; -.
UCD-2DPAGE; P62258; -.
EPD; P62258; -.
PaxDb; P62258; -.
PeptideAtlas; P62258; -.
PRIDE; P62258; -.
TopDownProteomics; P62258-1; -. [P62258-1]
DNASU; 7531; -.
Ensembl; ENST00000264335; ENSP00000264335; ENSG00000108953. [P62258-1]
Ensembl; ENST00000571732; ENSP00000461762; ENSG00000108953. [P62258-2]
Ensembl; ENST00000616643; ENSP00000481059; ENSG00000274474. [P62258-2]
Ensembl; ENST00000627231; ENSP00000487356; ENSG00000274474. [P62258-1]
GeneID; 7531; -.
KEGG; hsa:7531; -.
UCSC; uc002fsk.4; human. [P62258-1]
CTD; 7531; -.
DisGeNET; 7531; -.
EuPathDB; HostDB:ENSG00000108953.16; -.
GeneCards; YWHAE; -.
H-InvDB; HIX0013751; -.
H-InvDB; HIX0030006; -.
HGNC; HGNC:12851; YWHAE.
HPA; CAB016200; -.
HPA; CAB021109; -.
HPA; CAB047350; -.
HPA; HPA008445; -.
MalaCards; YWHAE; -.
MIM; 605066; gene.
neXtProt; NX_P62258; -.
OpenTargets; ENSG00000108953; -.
Orphanet; 217385; 17p13.3 microduplication syndrome.
Orphanet; 261257; Distal 17p13.3 microdeletion syndrome.
Orphanet; 531; Miller-Dieker syndrome.
PharmGKB; PA37440; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
HOVERGEN; HBG050423; -.
InParanoid; P62258; -.
KO; K06630; -.
OMA; IPCATTG; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; P62258; -.
TreeFam; TF102003; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-2028269; Signaling by Hippo.
Reactome; R-HSA-205025; NADE modulates death signalling.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-3371511; HSF1 activation.
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-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
SignaLink; P62258; -.
SIGNOR; P62258; -.
ChiTaRS; YWHAE; human.
EvolutionaryTrace; P62258; -.
GeneWiki; YWHAE; -.
GenomeRNAi; 7531; -.
PMAP-CutDB; P62258; -.
PRO; PR:P62258; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108953; -.
CleanEx; HS_YWHAE; -.
ExpressionAtlas; P62258; baseline and differential.
Genevisible; P62258; HS.
GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005246; F:calcium channel regulator activity; IDA:SynGO-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
GO; GO:0050815; F:phosphoserine residue binding; IPI:BHF-UCL.
GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0035329; P:hippo signaling; TAS:Reactome.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IDA:SynGO-UCL.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:SynGO-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:SynGO-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IC:BHF-UCL.
GO; GO:0003064; P:regulation of heart rate by hormone; NAS:BHF-UCL.
GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Host-virus interaction;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
CHAIN 1 255 14-3-3 protein epsilon.
/FTId=PRO_0000058618.
SITE 57 57 Interaction with phosphoserine on
interacting protein.
SITE 130 130 Interaction with phosphoserine on
interacting protein.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.13}.
MOD_RES 50 50 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:P62260}.
MOD_RES 69 69 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 118 118 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 131 131 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62260}.
MOD_RES 137 137 Phosphothreonine.
{ECO:0000250|UniProtKB:P62260}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 232 232 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 22 Missing (in isoform SV).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:20417184}.
/FTId=VSP_040621.
CONFLICT 106 107 KH -> NY (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 143 143 E -> F (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 148 148 S -> T (in Ref. 15; AA sequence).
{ECO:0000305}.
HELIX 4 17 {ECO:0000244|PDB:2BR9}.
HELIX 20 31 {ECO:0000244|PDB:2BR9}.
HELIX 39 73 {ECO:0000244|PDB:2BR9}.
HELIX 76 106 {ECO:0000244|PDB:2BR9}.
HELIX 108 111 {ECO:0000244|PDB:2BR9}.
HELIX 115 135 {ECO:0000244|PDB:2BR9}.
HELIX 138 162 {ECO:0000244|PDB:2BR9}.
HELIX 168 183 {ECO:0000244|PDB:2BR9}.
HELIX 188 204 {ECO:0000244|PDB:2BR9}.
HELIX 205 208 {ECO:0000244|PDB:2BR9}.
TURN 211 213 {ECO:0000244|PDB:2BR9}.
HELIX 214 231 {ECO:0000244|PDB:2BR9}.
SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64;
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
EQNKEALQDV EDENQ


Related products :

Catalog number Product name Quantity
EIAAB41754 Cct5,Ccte,CCT-epsilon,Kiaa0098,Mouse,Mus musculus,T-complex protein 1 subunit epsilon,TCP-1-epsilon
EIAAB08609 Bos taurus,Bovine,Coatomer subunit epsilon,COPE,COPE1,Epsilon-coat protein,Epsilon-COP
EIAAB08607 Coatomer subunit epsilon,COPE,Epsilon-coat protein,Epsilon-COP,Homo sapiens,Human
EIAAB08606 Coatomer subunit epsilon,Cope,Cope1,Epsilon-coat protein,Epsilon-COP,Mouse,Mus musculus
18-003-44146 Transcription factor AP-2 epsilon - AP2-epsilon; Activating enhancer-binding protein 2 epsilon Polyclonal 0.1 mg Protein A
EIAAB41756 CCT5,CCTE,CCT-epsilon,Homo sapiens,Human,KIAA0098,T-complex protein 1 subunit epsilon,TCP-1-epsilon
EIAAB41755 Cct5,CCT-epsilon,Rat,Rattus norvegicus,T-complex protein 1 subunit epsilon,TCP-1-epsilon
15-288-22834 T-complex protein 1 subunit epsilon - TCP-1-epsilon; CCT-epsilon Polyclonal 0.05 mg
15-288-22834 T-complex protein 1 subunit epsilon - TCP-1-epsilon; CCT-epsilon Polyclonal 0.1 mg
EIAAB08608 Chicken,Coatomer subunit epsilon,COPE,Epsilon-coat protein,Epsilon-COP,Gallus gallus,RCJMB04_25f12
EIAAB33082 Homo sapiens,Human,Protein-tyrosine phosphatase epsilon,PTPRE,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon
EIAAB33081 Mouse,Mus musculus,Protein-tyrosine phosphatase epsilon,Ptpe,Ptpre,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon
EIAAB33083 Protein-tyrosine phosphatase epsilon,Ptpe,Ptpre,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon
EIAAB31453 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1,Kiaa1516,Mouse,Mus musculus,Phosphoinositide phospholipase C-epsilon-1,Phospholipase C-epsilon-1,Plce,Plce1,PLC-epsilon-1
EIAAB31455 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1,Phosphoinositide phospholipase C-epsilon-1,Phospholipase C-epsilon-1,Plce,Plce1,PLC-epsilon-1,Rat,Rattus norvegicus
15-288-21468 Receptor-type tyrosine-protein phosphatase epsilon - EC 3.1.3.48; Protein-tyrosine phosphatase epsilon; R-PTP-epsilon Polyclonal 0.1 mg
18-461-10237 Receptor-type tyrosine-protein phosphatase epsilon - EC 3.1.3.48; Protein-tyrosine phosphatase epsilon; R-PTP-epsilon Polyclonal 0.05 ml
18-461-10236 Receptor-type tyrosine-protein phosphatase epsilon - EC 3.1.3.48; Protein-tyrosine phosphatase epsilon; R-PTP-epsilon Polyclonal 0.05 ml
15-288-21468 Receptor-type tyrosine-protein phosphatase epsilon - EC 3.1.3.48; Protein-tyrosine phosphatase epsilon; R-PTP-epsilon Polyclonal 0.05 mg
18-461-10235 Receptor-type tyrosine-protein phosphatase epsilon - EC 3.1.3.48; Protein-tyrosine phosphatase epsilon; R-PTP-epsilon Polyclonal 0.05 ml
EIAAB11066 DAG kinase epsilon,DAGK5,DGKE,DGK-epsilon,Diacylglycerol kinase epsilon,Diglyceride kinase epsilon,Homo sapiens,Human
Z8050093 Rabbit Polyclonal Anti-Protein Kinase C Epsilon (PKC-epsilon) 100
EIAAB33689 Mouse,Mus musculus,RAE-1-epsilon,Raet1e,Retinoic acid early-inducible protein 1-epsilon
10-782-55101 Protein kinase C epsilon type - EC 2.7.11.13; nPKC-epsilon N_A 0.01 mg
10-663-45565 Protein Kinase C epsilon (PKC-e) Human - EC 2.7.11.13; nPKC-epsilon N_A 1 mg


 

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