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Neurogenic locus Notch protein [Cleaved into: Processed neurogenic locus Notch protein]

 NOTCH_DROME             Reviewed;        2703 AA.
P07207; O97458; P04154; Q9W4T8;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 3.
30-AUG-2017, entry version 218.
RecName: Full=Neurogenic locus Notch protein;
Contains:
RecName: Full=Processed neurogenic locus Notch protein;
Flags: Precursor;
Name=N; ORFNames=CG3936;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=3935325; DOI=10.1016/0092-8674(85)90229-6;
Wharton K.A., Johansen K.M., Xu T., Artavanis-Tsakonas S.;
"Nucleotide sequence from the neurogenic locus notch implies a gene
product that shares homology with proteins containing EGF-like
repeats.";
Cell 43:567-581(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
PubMed=3097517; DOI=10.1128/MCB.6.9.3094;
Kidd S., Kelley M.R., Young M.W.;
"Sequence of the notch locus of Drosophila melanogaster: relationship
of the encoded protein to mammalian clotting and growth factors.";
Mol. Cell. Biol. 6:3094-3108(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
PubMed=3037327; DOI=10.1128/MCB.7.4.1545;
Kelley M.R., Kidd S., Berg R.L., Young M.W.;
"Restriction of P-element insertions at the Notch locus of Drosophila
melanogaster.";
Mol. Cell. Biol. 7:1545-1548(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2611.
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=2981631; DOI=10.1016/0092-8674(85)90308-3;
Wharton K.A., Yedvobnick B., Finnerty V.G., Artavanis-Tsakonas S.;
"opa: a novel family of transcribed repeats shared by the Notch locus
and other developmentally regulated loci in D. melanogaster.";
Cell 40:55-62(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2604.
PubMed=2780284; DOI=10.1093/nar/17.16.6463;
Tautz D.;
"Hypervariability of simple sequences as a general source for
polymorphic DNA markers.";
Nucleic Acids Res. 17:6463-6471(1989).
[9]
INTERACTION WITH DX, AND MUTANT SU42C.
PubMed=8162848;
Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.;
"Cytosolic interaction between deltex and Notch ankyrin repeats
implicates deltex in the Notch signaling pathway.";
Development 120:473-481(1994).
[10]
INTERACTION WITH DX.
PubMed=7671825;
Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M.,
Artavanis-Tsakonas S.;
"Deltex acts as a positive regulator of Notch signaling through
interactions with the Notch ankyrin repeats.";
Development 121:2633-2644(1995).
[11]
S3 CLEAVAGE BY PSN.
PubMed=10206646; DOI=10.1038/19091;
Struhl G., Greenwald I.;
"Presenilin is required for activity and nuclear access of Notch in
Drosophila.";
Nature 398:522-525(1999).
[12]
S3 CLEAVAGE BY PSN.
PubMed=10206647; DOI=10.1038/19096;
Ye Y., Lukinova N., Fortini M.E.;
"Neurogenic phenotypes and altered Notch processing in Drosophila
Presenilin mutants.";
Nature 398:525-529(1999).
[13]
FUNCTION, AND INTERACTION WITH DL.
PubMed=10935637; DOI=10.1038/35019075;
Bruckner K., Perez L., Clausen H., Cohen S.;
"Glycosyltransferase activity of Fringe modulates Notch-Delta
interactions.";
Nature 406:411-415(2000).
[14]
MUTANT MCD5.
PubMed=11719214; DOI=10.1016/S0960-9822(01)00562-0;
Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C.,
Heitzler P.;
"Novel Notch alleles reveal a Deltex-dependent pathway repressing
neural fate.";
Curr. Biol. 11:1729-1738(2001).
[15]
S2 CLEAVAGE BY KUZ.
PubMed=11799064; DOI=10.1101/gad.942302;
Lieber T., Kidd S., Young M.W.;
"Kuzbanian-mediated cleavage of Drosophila Notch.";
Genes Dev. 16:209-221(2002).
[16]
REVIEW.
PubMed=12369105; DOI=10.1034/j.1601-5223.2002.1360201.x;
Portin P.;
"General outlines of the molecular genetics of the Notch signalling
pathway in Drosophila melanogaster: a review.";
Hereditas 136:89-96(2002).
[17]
GLYCOSYLATION, AND LIGAND-BINDING.
PubMed=12909620; DOI=10.1074/jbc.M308687200;
Okajima T., Xu A., Irvine K.D.;
"Modulation of notch-ligand binding by protein O-fucosyltransferase 1
and fringe.";
J. Biol. Chem. 278:42340-42345(2003).
[18]
INTERACTION WITH NEDD4, UBIQUITINATION, AND MUTAGENESIS OF TYR-2328.
PubMed=15620649; DOI=10.1016/j.cub.2004.12.028;
Sakata T., Sakaguchi H., Tsuda L., Higashitani A., Aigaki T.,
Matsuno K., Hayashi S.;
"Drosophila Nedd4 regulates endocytosis of notch and suppresses its
ligand-independent activation.";
Curr. Biol. 14:2228-2236(2004).
[19]
INTERACTION WITH SU(DX).
PubMed=15620650; DOI=10.1016/j.cub.2004.11.030;
Wilkin M.B., Carbery A.-M., Fostier M., Aslam H., Mazaleyrat S.L.,
Higgs J., Myat A., Evans D.A.P., Cornell M., Baron M.;
"Regulation of notch endosomal sorting and signaling by Drosophila
Nedd4 family proteins.";
Curr. Biol. 14:2237-2244(2004).
[20]
SUBCELLULAR LOCATION, AND INTERACTION WITH O-FUT1.
PubMed=17329366; DOI=10.1242/dev.02811;
Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S.,
Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.;
"The O-fucosyltransferase O-fut1 is an extracellular component that is
essential for the constitutive endocytic trafficking of Notch in
Drosophila.";
Development 134:1347-1356(2007).
[21]
FUNCTION.
PubMed=18243100; DOI=10.1016/j.cell.2007.12.016;
Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A.,
Pan H., Haltiwanger R.S., Bellen H.J.;
"Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is
required for Notch signaling.";
Cell 132:247-258(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2447, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[23]
GLYCOSYLATION AT THR-72; THR-110; THR-153; SER-183; THR-191; THR-210;
SER-223; THR-231; THR-307; THR-348; THR-386; SER-427; THR-481;
SER-494; SER-502; THR-519; SER-532; SER-570; THR-595; SER-608;
SER-645; SER-683; THR-691; SER-721; SER-759; SER-797; THR-805;
THR-822; THR-843; SER-922; SER-952; THR-960; SER-990; THR-998;
SER-1036; SER-1066; THR-1074; THR-1112; SER-1189; THR-1197; THR-1235;
SER-1273; SER-1303 AND SER-1381.
PubMed=27268051; DOI=10.1074/jbc.M116.732537;
Harvey B.M., Rana N.A., Moss H., Leonardi J., Jafar-Nejad H.,
Haltiwanger R.S.;
"Mapping sites of O-glycosylation and fringe elongation on Drosophila
Notch.";
J. Biol. Chem. 291:16348-16360(2016).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1901-2139, DOMAIN ANK
REPEATS, AND SUBUNIT.
PubMed=14573873; DOI=10.1110/ps.03279003;
Zweifel M.E., Leahy D.J., Hughson F.M., Barrick D.;
"Structure and stability of the ankyrin domain of the Drosophila Notch
receptor.";
Protein Sci. 12:2622-2632(2003).
-!- FUNCTION: Signaling protein, which regulates, with both positive
and negative signals, the differentiation of at least central and
peripheral nervous system and eye, wing disk, oogenesis, segmental
appendages such as antennae and legs, and muscles, through lateral
inhibition or induction. Functions as a receptor for membrane-
bound ligands Delta and Serrate to regulate cell-fate
determination. Upon ligand activation, and releasing from the cell
membrane, the Notch intracellular domain (NICD) forms a
transcriptional activator complex with Su(H) (Suppressor of
hairless) and activates genes of the E(spl) complex. Essential for
proper differentiation of ectoderm. Fringe (fng) acts in the Golgi
to determine the type of O-linked fucose on the EGF modules in N,
altering the ability of N to bind with Delta (Dl). O-fut1 also has
a role in modulating the interaction. Rumi acts in the endoplasmic
reticulum to glucosylate the EGF modules in N, this is required
for correct folding and cleavage of N.
{ECO:0000269|PubMed:10935637, ECO:0000269|PubMed:18243100}.
-!- SUBUNIT: Homomer. Interacts with Su(H) when activated. Interacts
with Dx via its ANK repeats. Interacts with Dl via the EGF repeats
and the Dl EGF repeats. Interacts with Nedd4 and Su(dx). Interacts
with O-fut1; the interaction glycosylates N and transports N to
early endosomes. {ECO:0000269|PubMed:10935637,
ECO:0000269|PubMed:14573873, ECO:0000269|PubMed:15620649,
ECO:0000269|PubMed:15620650, ECO:0000269|PubMed:17329366,
ECO:0000269|PubMed:7671825, ECO:0000269|PubMed:8162848}.
-!- INTERACTION:
Q24279:cno; NbExp=3; IntAct=EBI-103438, EBI-868783;
P10041:Dl; NbExp=2; IntAct=EBI-103438, EBI-115346;
P28159:Su(H); NbExp=4; IntAct=EBI-103438, EBI-92180;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17329366};
Single-pass type I membrane protein {ECO:0000269|PubMed:17329366}.
Endosome {ECO:0000269|PubMed:17329366}. Note=Transported to early
endosomes by O-fut1 (PubMed:17329366).
-!- SUBCELLULAR LOCATION: Processed neurogenic locus Notch protein:
Nucleus. Note=Upon activation and S3 cleavage, it is released from
the cell membrane and enters into the nucleus in conjunction with
Su(H).
-!- DOMAIN: Crystal structure of the ANK repeat domain shows that
there are 7 repeats and the stabilizing C-terminal repeat enhances
the protein stability by extending the ankyrin domain.
{ECO:0000269|PubMed:14573873}.
-!- PTM: Upon binding its ligands such as Delta or Serrate, it is
cleaved (S2 cleavage) in its extracellular domain, close to the
transmembrane domain. S2 cleavage is probably mediated by Kuz. It
is then cleaved (S3 cleavage) downstream of its transmembrane
domain, releasing it from the cell membrane. S3 cleavage requires
Psn.
-!- PTM: O-glycosylated (PubMed:12909620, PubMed:27268051). Three
forms of O-glycosylation, O-fucosylation, O-glucosylation and O-
GlcNAcylation, are detected (PubMed:27268051). O-fucosylated by O-
fut1 in the EGF repeat domain which inhibits both Serrate/Ser- and
Delta/Dl-binding (PubMed:12909620). {ECO:0000269|PubMed:12909620,
ECO:0000269|PubMed:27268051}.
-!- PTM: Ubiquitinated by Nedd4; which promotes ligand-independent
endocytosis and proteasomal degradation. May also be ubiquitinated
by Su(dx). {ECO:0000269|PubMed:15620649}.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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EMBL; M16152; AAB59220.1; -; Genomic_DNA.
EMBL; M16153; AAB59220.1; JOINED; Genomic_DNA.
EMBL; M16149; AAB59220.1; JOINED; Genomic_DNA.
EMBL; M16150; AAB59220.1; JOINED; Genomic_DNA.
EMBL; M16151; AAB59220.1; JOINED; Genomic_DNA.
EMBL; K03508; AAA28725.1; -; Genomic_DNA.
EMBL; M13689; AAA28725.1; JOINED; Genomic_DNA.
EMBL; K03507; AAA28725.1; JOINED; Genomic_DNA.
EMBL; AE014298; AAF45848.2; -; Genomic_DNA.
EMBL; AL035436; CAB37610.1; -; Genomic_DNA.
EMBL; AL035395; CAB37610.1; JOINED; Genomic_DNA.
EMBL; M16025; AAA28726.1; -; Genomic_DNA.
EMBL; M12175; AAA74496.1; -; Genomic_DNA.
PIR; A24420; A24420.
RefSeq; NP_001245510.1; NM_001258581.2.
RefSeq; NP_476859.2; NM_057511.4.
PDB; 1OT8; X-ray; 2.00 A; A/B/C=1902-2139.
PDB; 2JMF; NMR; -; B=2318-2333.
PDBsum; 1OT8; -.
PDBsum; 2JMF; -.
ProteinModelPortal; P07207; -.
SMR; P07207; -.
BioGrid; 57823; 139.
DIP; DIP-5N; -.
IntAct; P07207; 231.
MINT; MINT-133064; -.
STRING; 7227.FBpp0070483; -.
iPTMnet; P07207; -.
PaxDb; P07207; -.
PRIDE; P07207; -.
EnsemblMetazoa; FBtr0070507; FBpp0070483; FBgn0004647.
EnsemblMetazoa; FBtr0304659; FBpp0293201; FBgn0004647.
GeneID; 31293; -.
KEGG; dme:Dmel_CG3936; -.
CTD; 109544; -.
FlyBase; FBgn0004647; N.
eggNOG; ENOG410IR7G; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00810000125346; -.
InParanoid; P07207; -.
KO; K02599; -.
OMA; QYVNSYT; -.
OrthoDB; EOG091G01NU; -.
PhylomeDB; P07207; -.
Reactome; R-DME-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-DME-1980148; Signaling by NOTCH3.
Reactome; R-DME-1980150; Signaling by NOTCH4.
Reactome; R-DME-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-DME-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
Reactome; R-DME-8941856; RUNX3 regulates NOTCH signaling.
SignaLink; P07207; -.
ChiTaRS; N; fly.
EvolutionaryTrace; P07207; -.
GenomeRNAi; 31293; -.
PRO; PR:P07207; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004647; -.
ExpressionAtlas; P07207; differential.
Genevisible; P07207; DM.
GO; GO:0005912; C:adherens junction; IDA:FlyBase.
GO; GO:0009986; C:cell surface; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; IDA:FlyBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:FlyBase.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:FlyBase.
GO; GO:0005622; C:intracellular; IDA:FlyBase.
GO; GO:0005770; C:late endosome; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0043234; C:protein complex; IPI:FlyBase.
GO; GO:0035003; C:subapical complex; IDA:FlyBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
GO; GO:0004872; F:receptor activity; TAS:FlyBase.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0009952; P:anterior/posterior pattern specification; TAS:FlyBase.
GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0007155; P:cell adhesion; TAS:FlyBase.
GO; GO:0001708; P:cell fate specification; TAS:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
GO; GO:0042676; P:compound eye cone cell fate commitment; TAS:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
GO; GO:0046667; P:compound eye retinal cell programmed cell death; TAS:FlyBase.
GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase.
GO; GO:0002213; P:defense response to insect; IDA:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
GO; GO:0007451; P:dorsal/ventral lineage restriction, imaginal disc; TAS:FlyBase.
GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; TAS:FlyBase.
GO; GO:0007398; P:ectoderm development; TAS:FlyBase.
GO; GO:0035165; P:embryonic crystal cell differentiation; TAS:FlyBase.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:FlyBase.
GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
GO; GO:0035153; P:epithelial cell type specification, open tracheal system; IMP:FlyBase.
GO; GO:0060429; P:epithelium development; IMP:FlyBase.
GO; GO:0042067; P:establishment of ommatidial planar polarity; TAS:FlyBase.
GO; GO:0035214; P:eye-antennal disc development; IMP:FlyBase.
GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
GO; GO:0060288; P:formation of a compartment boundary; IMP:FlyBase.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; TAS:FlyBase.
GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
GO; GO:0007403; P:glial cell fate determination; IMP:FlyBase.
GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
GO; GO:0035172; P:hemocyte proliferation; IMP:FlyBase.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:FlyBase.
GO; GO:0007446; P:imaginal disc growth; TAS:FlyBase.
GO; GO:0007447; P:imaginal disc pattern formation; TAS:FlyBase.
GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IMP:FlyBase.
GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
GO; GO:0035171; P:lamellocyte differentiation; IMP:FlyBase.
GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
GO; GO:0007478; P:leg disc morphogenesis; TAS:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0035170; P:lymph gland crystal cell differentiation; TAS:FlyBase.
GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
GO; GO:0061382; P:Malpighian tubule tip cell differentiation; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
GO; GO:0016333; P:morphogenesis of follicular epithelium; NAS:FlyBase.
GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
GO; GO:0007521; P:muscle cell fate determination; IMP:FlyBase.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IMP:FlyBase.
GO; GO:0045316; P:negative regulation of compound eye photoreceptor development; IMP:FlyBase.
GO; GO:0035157; P:negative regulation of fusion cell fate specification; TAS:FlyBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
GO; GO:0046329; P:negative regulation of JNK cascade; NAS:FlyBase.
GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
GO; GO:0050768; P:negative regulation of neurogenesis; IMP:FlyBase.
GO; GO:0035155; P:negative regulation of terminal cell fate specification, open tracheal system; TAS:FlyBase.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:FlyBase.
GO; GO:0007400; P:neuroblast fate determination; IDA:FlyBase.
GO; GO:0050877; P:neurological system process; IMP:FlyBase.
GO; GO:0048666; P:neuron development; IMP:FlyBase.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0007314; P:oocyte anterior/posterior axis specification; TAS:FlyBase.
GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; TAS:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0007297; P:ovarian follicle cell migration; IMP:FlyBase.
GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0042691; P:positive regulation of crystal cell differentiation; IMP:FlyBase.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0048052; P:R1/R6 cell differentiation; IMP:FlyBase.
GO; GO:0007464; P:R3/R4 cell fate commitment; NAS:FlyBase.
GO; GO:0045466; P:R7 cell differentiation; IMP:FlyBase.
GO; GO:0045463; P:R8 cell development; TAS:FlyBase.
GO; GO:0045465; P:R8 cell differentiation; NAS:FlyBase.
GO; GO:0007460; P:R8 cell fate commitment; TAS:FlyBase.
GO; GO:0042686; P:regulation of cardioblast cell fate specification; IMP:FlyBase.
GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
GO; GO:0042689; P:regulation of crystal cell differentiation; TAS:FlyBase.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
GO; GO:0006110; P:regulation of glycolytic process; IMP:FlyBase.
GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
GO; GO:0007346; P:regulation of mitotic cell cycle; TAS:FlyBase.
GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
GO; GO:0045468; P:regulation of R8 cell spacing in compound eye; NAS:FlyBase.
GO; GO:0009608; P:response to symbiont; IMP:FlyBase.
GO; GO:0046666; P:retinal cell programmed cell death; TAS:FlyBase.
GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:FlyBase.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:FlyBase.
GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007419; P:ventral cord development; NAS:FlyBase.
GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
GO; GO:0007473; P:wing disc proximal/distal pattern formation; TAS:FlyBase.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR024600; DUF3454_notch.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR008297; Notch.
InterPro; IPR000800; Notch_dom.
InterPro; IPR010660; Notch_NOD_dom.
InterPro; IPR011656; Notch_NODP_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF11936; DUF3454; 1.
Pfam; PF00008; EGF; 24.
Pfam; PF07645; EGF_CA; 4.
Pfam; PF12661; hEGF; 2.
Pfam; PF06816; NOD; 1.
Pfam; PF07684; NODP; 1.
Pfam; PF00066; Notch; 3.
PIRSF; PIRSF002279; Notch; 1.
PRINTS; PR01452; LNOTCHREPEAT.
SMART; SM00248; ANK; 7.
SMART; SM01334; DUF3454; 1.
SMART; SM00181; EGF; 36.
SMART; SM00179; EGF_CA; 33.
SMART; SM00004; NL; 3.
SMART; SM01338; NOD; 1.
SMART; SM01339; NODP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS00010; ASX_HYDROXYL; 22.
PROSITE; PS00022; EGF_1; 34.
PROSITE; PS01186; EGF_2; 28.
PROSITE; PS50026; EGF_3; 36.
PROSITE; PS01187; EGF_CA; 21.
PROSITE; PS50258; LNR; 3.
1: Evidence at protein level;
3D-structure; Activator; ANK repeat; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Endosome; Glycoprotein; Membrane; Neurogenesis;
Notch signaling pathway; Nucleus; Oogenesis; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 52 {ECO:0000255}.
CHAIN 53 2703 Neurogenic locus Notch protein.
/FTId=PRO_0000007673.
CHAIN ? 2703 Processed neurogenic locus Notch protein.
/FTId=PRO_0000296234.
TOPO_DOM 53 1745 Extracellular. {ECO:0000255}.
TRANSMEM 1746 1766 Helical. {ECO:0000255}.
TOPO_DOM 1767 2703 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 95 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 96 136 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 139 176 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 177 215 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 217 253 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 255 291 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 293 329 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 331 370 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 372 408 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 409 447 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 449 486 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 488 524 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 526 562 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 564 600 EGF-like 14; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 602 637 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 639 675 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 677 713 EGF-like 17; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 715 751 EGF-like 18; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 753 789 EGF-like 19; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 791 827 EGF-like 20; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 829 865 EGF-like 21; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 867 905 EGF-like 22. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 907 944 EGF-like 23; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 946 982 EGF-like 24; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 984 1020 EGF-like 25. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1022 1058 EGF-like 26; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1060 1096 EGF-like 27. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1098 1134 EGF-like 28. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1136 1181 EGF-like 29. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1183 1219 EGF-like 30; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1221 1257 EGF-like 31; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1259 1295 EGF-like 32; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1297 1335 EGF-like 33. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1337 1373 EGF-like 34. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1375 1412 EGF-like 35. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1415 1451 EGF-like 36. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1482 1521 LNR 1. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
REPEAT 1522 1557 LNR 2. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
REPEAT 1559 1599 LNR 3. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
REPEAT 1901 1945 ANK 1. {ECO:0000255}.
REPEAT 1950 1979 ANK 2. {ECO:0000255}.
REPEAT 1983 2013 ANK 3. {ECO:0000255}.
REPEAT 2017 2046 ANK 4. {ECO:0000255}.
REPEAT 2050 2079 ANK 5. {ECO:0000255}.
REPEAT 2083 2112 ANK 6. {ECO:0000255}.
REPEAT 2116 2139 ANK 7. {ECO:0000255}.
REGION 2325 2328 Interaction with Nedd4.
COMPBIAS 2264 2277 Ala-rich. {ECO:0000255|PROSITE-
ProRule:PRU00001}.
COMPBIAS 2369 2498 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 2533 2568 Gln-rich. {ECO:0000255|PROSITE-
ProRule:PRU00006}.
COMPBIAS 2587 2675 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
MOD_RES 2447 2447 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CARBOHYD 72 72 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 110 110 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 153 153 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 183 183 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 191 191 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 210 210 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 223 223 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 231 231 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 307 307 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 427 427 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 494 494 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 502 502 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 519 519 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 532 532 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 570 570 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 595 595 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 608 608 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 645 645 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 683 683 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 691 691 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 721 721 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 759 759 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 797 797 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 805 805 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 822 822 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 843 843 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 922 922 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 952 952 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 960 960 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 990 990 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 998 998 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1036 1036 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1045 1045 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1066 1066 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1074 1074 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1112 1112 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1157 1157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1189 1189 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1197 1197 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1235 1235 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1242 1242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1271 1271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1273 1273 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1303 1303 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1381 1381 O-linked (Glc...) serine.
{ECO:0000269|PubMed:27268051}.
CARBOHYD 1521 1521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1594 1594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1627 1627 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 73 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 67 83 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 85 94 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 100 111 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 105 124 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 126 135 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 143 154 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 148 164 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 166 175 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 181 192 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 186 203 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 205 214 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 221 232 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 226 241 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 243 252 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 259 270 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 264 279 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 281 290 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 297 308 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 302 317 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 319 328 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 335 349 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 343 358 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 360 369 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 376 387 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 381 396 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 398 407 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 413 424 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 418 435 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 437 446 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 453 465 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 459 474 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 476 485 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 492 503 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 497 512 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 514 523 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 530 541 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 535 550 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 552 561 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 568 579 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 573 588 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 590 599 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 606 616 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 611 625 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 627 636 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 643 654 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 648 663 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 665 674 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 681 692 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 686 701 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 703 712 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 719 730 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 724 739 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 741 750 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 757 768 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 762 777 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 779 788 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 795 806 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 800 815 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 817 826 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 833 844 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 838 853 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 855 864 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 871 882 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 876 893 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 895 904 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 911 923 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 917 932 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 934 943 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 950 961 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 955 970 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 972 981 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 988 999 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 993 1008 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1010 1019 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1026 1037 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1031 1046 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1048 1057 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1064 1075 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1069 1084 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1086 1095 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1102 1113 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1107 1122 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1124 1133 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1155 1160 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1171 1180 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1187 1198 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1192 1207 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1209 1218 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1225 1236 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1230 1245 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1247 1256 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1263 1274 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1268 1283 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1285 1294 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1301 1314 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1306 1323 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1325 1334 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1341 1352 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1346 1361 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1363 1372 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1379 1389 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1384 1400 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1402 1411 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1419 1430 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1424 1439 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1441 1450 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1482 1505 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1487 1500 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1496 1512 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1522 1545 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1527 1540 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1536 1552 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1559 1585 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1567 1580 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 1576 1592 {ECO:0000255|PROSITE-ProRule:PRU00525}.
VARIANT 578 578 I -> T.
VARIANT 2044 2044 I -> R.
VARIANT 2265 2265 A -> V.
VARIANT 2407 2407 H -> R.
VARIANT 2445 2445 R -> L.
VARIANT 2568 2568 Q -> QQQQQ.
MUTAGEN 739 739 C->Y: In mcd5; induces loss of
microchaetae sensory precursors.
MUTAGEN 2060 2060 A->V: In su42c; deltex-like mutation that
induces outstreched wings and
variability-fused ocelli.
MUTAGEN 2328 2328 Y->F: Abolishes interaction with Nedd4
and reduces ubiquitination.
{ECO:0000269|PubMed:15620649}.
CONFLICT 9 9 R -> G (in Ref. 5; CAB37610).
{ECO:0000305}.
CONFLICT 84 84 A -> G (in Ref. 5; CAB37610).
{ECO:0000305}.
CONFLICT 103 103 M -> I (in Ref. 1; AAB59220).
{ECO:0000305}.
CONFLICT 119 119 R -> H (in Ref. 2; AAA28725).
{ECO:0000305}.
CONFLICT 231 231 T -> I (in Ref. 1; AAB59220).
{ECO:0000305}.
CONFLICT 240 240 Q -> R (in Ref. 5; CAB37610).
{ECO:0000305}.
CONFLICT 267 267 G -> A (in Ref. 1; AAB59220).
{ECO:0000305}.
CONFLICT 1561 1561 S -> T (in Ref. 1; AAB59220 and 2;
AAA28725). {ECO:0000305}.
CONFLICT 2257 2257 G -> S (in Ref. 2; AAA28725).
{ECO:0000305}.
CONFLICT 2577 2577 A -> E (in Ref. 7; AAA74496).
{ECO:0000305}.
HELIX 1930 1950 {ECO:0000244|PDB:1OT8}.
HELIX 1954 1960 {ECO:0000244|PDB:1OT8}.
HELIX 1964 1972 {ECO:0000244|PDB:1OT8}.
HELIX 1987 1993 {ECO:0000244|PDB:1OT8}.
HELIX 1997 2004 {ECO:0000244|PDB:1OT8}.
HELIX 2021 2027 {ECO:0000244|PDB:1OT8}.
HELIX 2033 2039 {ECO:0000244|PDB:1OT8}.
HELIX 2054 2060 {ECO:0000244|PDB:1OT8}.
HELIX 2064 2072 {ECO:0000244|PDB:1OT8}.
HELIX 2087 2093 {ECO:0000244|PDB:1OT8}.
HELIX 2097 2105 {ECO:0000244|PDB:1OT8}.
HELIX 2120 2126 {ECO:0000244|PDB:1OT8}.
HELIX 2130 2136 {ECO:0000244|PDB:1OT8}.
SEQUENCE 2703 AA; 288853 MW; 0EAE23F426FECD7B CRC64;
MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV RGTDTALVAA
SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC NSMRCQNGGT CQVTFRNGRP
GISCKCPLGF DESLCEIAVP NACDHVTCLN GGTCQLKTLE EYTCACANGY TGERCETKNL
CASSPCRNGA TCTALAGSSS FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ
CMCPTGYTGK DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH
LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT NTHGSYSCIC
VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK GKTGLLCHLD DACTSNPCHA
DAICDTSPIN GSYACSCATG YKGVDCSEDI DECDQGSPCE HNGICVNTPG SYRCNCSQGF
TGPRCETNIN ECESHPCQNE GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT
CHDKINGFKC SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE
ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF DGHCQDRVGS
YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK CQCVPGFTGQ HCEKNVDECI
SSPCANNGVC IDQVNGYKCE CPRGFYDAHC LSDVDECASN PCVNEGRCED GINEFICHCP
PGYTGKRCEL DIDECSSNPC QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN
GGTCIDKVNG YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT
GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC ASFPCQNGGT
CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS QYVNSYTCTC PLGFSGINCQ
TNDEDCTESS CLNGGSCIDG INGYNCSCLA GYSGANCQYK LNKCDSNPCL NGATCHEQNN
EYTCHCPSGF TGKQCSEYVD WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC
QDAADRKGLS LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD
LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG TMGIICEINK
DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE CLSNPCSNAG TLDCVQLVNN
YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG NCNIRQSGHH CICNNGFYGK NCELSGQDCD
SNPCRVGNCV VADEGFGYRC ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL
CPSKWKGKRC DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC
NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH DCERKLKSCD
SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV LAEGAMSVVM LMNVEAFREI
QAQFLRNMSH MLRTTVRLKK DALGHDIIIN WKDNVRVPEI EDTDFARKNK ILYTQQVHQT
GIQIYLEIDN RKCTECFTHA VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP
ANVKYVITGI ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM
RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY ASDHTMVSEY
EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP CGLTPLMIAA VRGGGLDTGE
DIENNEDSTA QVISDLLAQG AELNATMDKT GETSLHLAAR FARADAAKRL LDAGADANCQ
DNTGRTPLHA AVAADAMGVF QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA
DADINAADNS GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC
KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT PQAMIGSPPP
GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA AKKAKLIEGS PDNGLDATGS
LRRKASSKKT SAASKKAANL NGLNPGQLTG GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH
ELEGSPVGVG MGGNLPSPYD TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS
LQGNGLDMIK LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG
AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT SPTHIQAMRH
ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ NSPVSLGIIS PTGSDMGIML
APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD
LNGFCGSPDS FHSGQMNPPS IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH
TPQHLVQTLD SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA
IYI


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