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Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]

 NOTC1_MOUSE             Reviewed;        2531 AA.
Q01705; Q06007; Q3TZW2; Q3U3Y2; Q61905; Q7TQ50; Q7TQ51; Q7TQ52;
Q8K428; Q99JC2; Q9QW58; Q9R0X7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
18-APR-2012, sequence version 3.
22-NOV-2017, entry version 200.
RecName: Full=Neurogenic locus notch homolog protein 1;
Short=Notch 1;
AltName: Full=Motch A;
AltName: Full=mT14;
AltName: Full=p300;
Contains:
RecName: Full=Notch 1 extracellular truncation;
Short=NEXT;
Contains:
RecName: Full=Notch 1 intracellular domain;
Short=NICD;
Flags: Precursor;
Name=Notch1; Synonyms=Motch;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=8449489; DOI=10.1006/geno.1993.1055;
Franco del Amo F., Gendron-Maguire M., Swiatek P.J., Jenkins N.A.,
Copeland N.G., Gridley T.;
"Cloning, analysis, and chromosomal localization of Notch-1, a mouse
homolog of Drosophila Notch.";
Genomics 15:259-264(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Thymus;
PubMed=7956822;
Nye J.S., Kopan R., Axel R.;
"An activated Notch suppresses neurogenesis and myogenesis but not
gliogenesis in mammalian cells.";
Development 120:2421-2430(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Thymus;
PubMed=12123574; DOI=10.1016/S0960-9822(02)00888-6;
Foltz D.R., Santiago M.C., Berechid B.E., Nye J.S.;
"Glycogen synthase kinase-3beta modulates notch signaling and
stability.";
Curr. Biol. 12:1006-1011(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CB-17/SCID; TISSUE=Thymus;
PubMed=12807718; DOI=10.1093/carcin/bgg071;
Tsuji H., Ishii-Ohba H., Ukai H., Katsube T., Ogiu T.;
"Radiation-induced deletions in the 5' end region of Notch1 lead to
the formation of truncated proteins and are involved in the
development of mouse thymic lymphomas.";
Carcinogenesis 24:1257-1268(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 731-1899 (ISOFORM 2), AND DEVELOPMENTAL
STAGE.
STRAIN=CD-1; TISSUE=Embryo;
PubMed=1426644; DOI=10.1016/0012-1606(92)90076-S;
Reaume A.G., Conlon R.A., Zirngibl R., Yamaguchi T.P., Rossant J.;
"Expression analysis of a Notch homologue in the mouse embryo.";
Dev. Biol. 154:377-387(1992).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1547.
STRAIN=C57BL/6 X CBA; TISSUE=Embryo;
PubMed=8440332; DOI=10.1006/excr.1993.1044;
Lardelli M., Lendahl U.;
"Motch A and Motch B-two mouse Notch homologues coexpressed in a wide
variety of tissues.";
Exp. Cell Res. 204:364-372(1993).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1373-2531.
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1551-1647 (ISOFORM 1), AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=1425352;
Franco del Amo F., Smith D.E., Swiatek P.J., Gendron-Maguire M.,
Greenspan R.J., McMahon A.P., Gridley T.;
"Expression pattern of Motch, a mouse homolog of Drosophila Notch,
suggests an important role in early postimplantation mouse
development.";
Development 115:737-744(1992).
[12]
PROTEIN SEQUENCE OF 1655-1659, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND
MUTAGENESIS OF 1651-ARG--ARG-1654.
PubMed=9653148; DOI=10.1073/pnas.95.14.8108;
Logeat F., Bessia C., Brou C., LeBail O., Jarriault S., Seidah N.G.,
Israel A.;
"The Notch1 receptor is cleaved constitutively by a furin-like
convertase.";
Proc. Natl. Acad. Sci. U.S.A. 95:8108-8112(1998).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1659-1673.
PubMed=10437788; DOI=10.1016/S0014-5793(99)00901-1;
Lee J.S., Ishimoto A., Yanagawa S.;
"Murine leukemia provirus-mediated activation of the Notch1 gene leads
to induction of HES-1 in a mouse T lymphoma cell line, DL-3.";
FEBS Lett. 455:276-280(1999).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1865-2076, AND DEVELOPMENTAL STAGE IN
HAIR FOLLICLES.
PubMed=8486742; DOI=10.1083/jcb.121.3.631;
Kopan R., Weintraub H.;
"Mouse notch: expression in hair follicles correlates with cell fate
determination.";
J. Cell Biol. 121:631-641(1993).
[15]
PROTEIN SEQUENCE OF 1937-1952 AND 1995-2019, FUNCTION, INTERACTION
WITH HIF1AN, HYDROXYLATION AT ASN-1945 AND ASN-2012 BY HIF1AN,
MUTAGENESIS OF ASN-1945 AND ASN-2012, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18299578; DOI=10.1073/pnas.0711591105;
Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P.,
Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L.,
Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J.,
Peet D.J., Lendahl U., Poellinger L.;
"Interaction with factor inhibiting HIF-1 defines an additional mode
of cross-coupling between the Notch and hypoxia signaling pathways.";
Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1951-2201.
PubMed=9384671;
Messerle M., Follo M., Nehls M., Eggert H., Boehm T.;
"Dynamic changes in gene expression during in vitro differentiation of
mouse embryonic stem cells.";
Cytokines Cell. Mol. Ther. 1:139-143(1995).
[17]
PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING.
PubMed=11518718; DOI=10.1074/jbc.M107234200;
Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R.;
"Murine notch homologs (N1-4) undergo presenilin-dependent
proteolysis.";
J. Biol. Chem. 276:40268-40273(2001).
[18]
PROTEOLYTIC PROCESSING.
PubMed=11459941; DOI=10.1073/pnas.161269998;
Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T.;
"Conservation of the biochemical mechanisms of signal transduction
among mammalian Notch family members.";
Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001).
[19]
INTERACTION WITH DTX1 AND DTX2.
PubMed=11226752; DOI=10.1016/S0736-5748(00)00071-X;
Kishi N., Tang Z., Maeda Y., Hirai A., Mo R., Ito M., Suzuki S.,
Nakao K., Kinoshita T., Kadesch T., Hui C.-C., Artavanis-Tsakonas S.,
Okano H., Matsuno K.;
"Murine homologs of deltex define a novel gene family involved in
vertebrate Notch signaling and neurogenesis.";
Int. J. Dev. Neurosci. 19:21-35(2001).
[20]
INTERACTION WITH NOV.
PubMed=12050162; DOI=10.1074/jbc.M203727200;
Sakamoto K., Yamaguchi S., Ando R., Miyawaki A., Kabasawa Y.,
Takagi M., Li C.L., Perbal B., Katsube K.;
"The nephroblastoma overexpressed gene (NOV/ccn3) protein associates
with Notch1 extracellular domain and inhibits myoblast differentiation
via Notch signaling pathway.";
J. Biol. Chem. 277:29399-29405(2002).
[21]
INTERACTION WITH MAML1.
PubMed=15019995; DOI=10.1016/j.gene.2003.12.007;
Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E.,
Mukhopadhyay N.K., Griffin J.D.;
"Cloning and functional characterization of the murine mastermind-like
1 (Maml1) gene.";
Gene 328:153-165(2004).
[22]
UBIQUITINATION AT LYS-1749, AND ENDOCYTOSIS.
PubMed=15240571; DOI=10.1083/jcb.200310098;
Gupta-Rossi N., Six E., LeBail O., Logeat F., Chastagner P., Olry A.,
Israel A., Brou C.;
"Monoubiquitination and endocytosis direct gamma-secretase cleavage of
activated Notch receptor.";
J. Cell Biol. 166:73-83(2004).
[23]
INTERACTION WITH DNER, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15965470; DOI=10.1038/nn1492;
Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T.,
Kengaku M.;
"DNER acts as a neuron-specific Notch ligand during Bergmann glial
development.";
Nat. Neurosci. 8:873-880(2005).
[24]
UBIQUITINATION BY ITCH.
PubMed=18628966; DOI=10.1371/journal.pone.0002735;
Chastagner P., Israel A., Brou C.;
"AIP4/Itch regulates Notch receptor degradation in the absence of
ligand.";
PLoS ONE 3:E2735-E2735(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1851, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[26]
INTERACTION WITH AAK1.
PubMed=21464124; DOI=10.1074/jbc.M110.190769;
Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
Olivo-Marin J.C., Israel A.;
"The adaptor-associated kinase 1, AAK1, is a positive regulator of the
Notch pathway.";
J. Biol. Chem. 286:18720-18730(2011).
[27]
GLYCOSYLATION AT SER-65; THR-73; THR-116; SER-146; THR-194; SER-341;
SER-378; SER-458; THR-466; SER-496; SER-534; SER-609; SER-647;
SER-722; SER-759; THR-767; SER-797; THR-805; SER-951; SER-1027;
THR-1035; SER-1065; SER-1189; THR-1197; SER-1273 AND THR-1362, AND
MUTAGENESIS OF SER-65; SER-146; SER-341; SER-378; SER-458; SER-496;
SER-534; SER-609; SER-647; SER-722; SER-759; SER-797; SER-951;
SER-1027; SER-1065; SER-1189 AND SER-1273.
PubMed=21757702; DOI=10.1074/jbc.M111.268243;
Rana N.A., Nita-Lazar A., Takeuchi H., Kakuda S., Luther K.B.,
Haltiwanger R.S.;
"O-glucose trisaccharide is present at high but variable stoichiometry
at multiple sites on mouse Notch1.";
J. Biol. Chem. 286:31623-31637(2011).
[28]
FUNCTION AS NEUROGENESIS REPRESSOR, AND INTERACTION WITH BCL6.
PubMed=23160044; DOI=10.1038/nn.3264;
Tiberi L., van den Ameele J., Dimidschstein J., Piccirilli J.,
Gall D., Herpoel A., Bilheu A., Bonnefont J., Iacovino M., Kyba M.,
Bouschet T., Vanderhaeghen P.;
"BCL6 controls neurogenesis through Sirt1-dependent epigenetic
repression of selective Notch targets.";
Nat. Neurosci. 15:1627-1635(2012).
[29]
UBIQUITINATION BY ITCH.
PubMed=23886940; DOI=10.1242/jcs.130500;
Puca L., Chastagner P., Meas-Yedid V., Israel A., Brou C.;
"Alpha-arrestin 1 (ARRDC1) and beta-arrestins cooperate to mediate
Notch degradation in mammals.";
J. Cell Sci. 126:4457-4468(2013).
[30]
FUNCTION, AND INTERACTION WITH THBS4.
PubMed=23615612; DOI=10.1038/nature12069;
Benner E.J., Luciano D., Jo R., Abdi K., Paez-Gonzalez P., Sheng H.,
Warner D.S., Liu C., Eroglu C., Kuo C.T.;
"Protective astrogenesis from the SVZ niche after injury is controlled
by Notch modulator Thbs4.";
Nature 497:369-373(2013).
[31]
GLYCOSYLATION AT THR-73; THR-116; THR-194; THR-232; THR-311; THR-349;
SER-458; THR-466; THR-617; THR-692; SER-759; THR-767; SER-784;
SER-797; THR-805; THR-900; SER-921; THR-997; THR-1035; THR-1159;
THR-1197; THR-1362; THR-1379 AND THR-1402, MUTAGENESIS OF THR-232;
THR-311; THR-349; THR-466; THR-997; THR-1035; THR-1159; THR-1362 AND
THR-1402, AND INTERACTION WITH DLL1 AND JAG1.
PubMed=28089369; DOI=10.1016/j.devcel.2016.12.013;
Kakuda S., Haltiwanger R.S.;
"Deciphering the fringe-mediated notch code: identification of
activating and inhibiting sites allowing discrimination between
ligands.";
Dev. Cell 40:193-201(2017).
[32]
SUBCELLULAR LOCATION, AND INTERACTION WITH MEGF10.
PubMed=28498977; DOI=10.1093/hmg/ddx189;
Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
Cho K.A., Pacak C.A., Draper I., Kang P.B.;
"Consequences of MEGF10 deficiency on myoblast function and Notch1
interactions.";
Hum. Mol. Genet. 26:2984-3000(2017).
[33]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1971-2104.
PubMed=15802643; DOI=10.1110/ps.041184105;
Lubman O.Y., Kopan R., Waksman G., Korolev S.;
"The crystal structure of a partial mouse Notch-1 ankyrin domain:
repeats 4 through 7 preserve an ankyrin fold.";
Protein Sci. 14:1274-1281(2005).
[34]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1899-2106 IN COMPLEX WITH
HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT ASN-1945 AND
ASN-2012, MUTAGENESIS OF ASN-1945 AND ASN-2012, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=17573339; DOI=10.1074/jbc.M704102200;
Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
Oldham N.J., Ratcliffe P.J., Schofield C.J.;
"Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
factor inhibiting hypoxia-inducible factor.";
J. Biol. Chem. 282:24027-24038(2007).
-!- FUNCTION: Functions as a receptor for membrane-bound ligands
Jagged1, Jagged2 and Delta1 to regulate cell-fate determination.
Upon ligand activation through the released notch intracellular
domain (NICD) it forms a transcriptional activator complex with
RBPJ/RBPSUH and activates genes of the enhancer of split locus.
Affects the implementation of differentiation, proliferation and
apoptotic programs. Involved in angiogenesis; negatively regulates
endothelial cell proliferation and migration and angiogenic
sprouting. Involved in the maturation of both CD4+ and CD8+ cells
in the thymus. Important for follicular differentiation and
possibly cell fate selection within the follicle. During
cerebellar development, functions as a receptor for neuronal DNER
and is involved in the differentiation of Bergmann glia. Represses
neuronal and myogenic differentiation. May play an essential role
in postimplantation development, probably in some aspect of cell
specification and/or differentiation. May be involved in mesoderm
development, somite formation and neurogenesis. May enhance HIF1A
function by sequestering HIF1AN away from HIF1A. Required for the
THBS4 function in regulating protective astrogenesis from the
subventricular zone (SVZ) niche after injury. Involved in
determination of left/right symmetry by modulating the balance
between motile and immotile (sensory) cilia at the left-right
organiser (LRO). {ECO:0000269|PubMed:15965470,
ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:23160044,
ECO:0000269|PubMed:23615612}.
-!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
terminal fragment N(EC) which are probably linked by disulfide
bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also
interacts with MAML1, MAML2 and MAML3 which act as transcriptional
coactivators for NOTCH1. Notch 1 intracellular domain interacts
with SNW1; the interaction involves multimerized NOTCH1 NICD and
is implicated in a formation of an intermediate preactivation
complex which associates with DNA-bound CBF-1/RBPJ. The activated
membrane-bound form interacts with AAK1 which promotes NOTCH1
stabilization. Forms a trimeric complex with FBXW7 and SGK1.
Interacts with HIF1AN. HIF1AN negatively regulates the function of
notch intracellular domain (NICD), accelerating myogenic
differentiation. Interacts (via NICD) with SNAI1 (via zinc
fingers); the interaction induces SNAI1 degradation via MDM2-
mediated ubiquitination and inhibits SNAI1-induced cell invasion.
Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6;
the interaction decreases MAML1 recruitment by NOTCH1 NICD on
target genes DNA and inhibits NOTCH1 transcractivation activity.
Interacts with THBS4. Interacts (via the EGF-like repeat region)
with NOV (via CTCK domain) (PubMed:12050162). Interacts (via EGF-
like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By
similarity). Interacts with ZMIZ1. Interacts (via NICD domain)
with MEGF10 (via the cytoplasmic domain) (PubMed:28498977).
Interacts with DLL1 and JAG1 (PubMed:28089369).
{ECO:0000250|UniProtKB:Q07008, ECO:0000269|PubMed:11226752,
ECO:0000269|PubMed:12050162, ECO:0000269|PubMed:15019995,
ECO:0000269|PubMed:15965470, ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:21464124,
ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:23615612,
ECO:0000269|PubMed:28089369, ECO:0000269|PubMed:28498977}.
-!- INTERACTION:
Q77CA8:LRORF2 (xeno); NbExp=3; IntAct=EBI-11292892, EBI-11292862;
Q06330:RBPJ (xeno); NbExp=3; IntAct=EBI-1392707, EBI-632552;
P31266:Rbpj; NbExp=8; IntAct=EBI-1392707, EBI-1392666;
Q3TKT4:Smarca4; NbExp=2; IntAct=EBI-1392707, EBI-1210244;
Q6P9Z1:Smarcd3; NbExp=2; IntAct=EBI-1392707, EBI-7525857;
P28159:Su(H) (xeno); NbExp=3; IntAct=EBI-1392707, EBI-92180;
P62991:Ubc; NbExp=3; IntAct=EBI-1392707, EBI-413074;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28498977};
Single-pass type I membrane protein.
-!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
{ECO:0000269|PubMed:28498977}. Note=Following proteolytical
processing NICD is translocated to the nucleus. Nuclear location
may require MEGF10. {ECO:0000269|PubMed:28498977}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q01705-1; Sequence=Displayed;
Name=2;
IsoId=Q01705-2; Sequence=VSP_001402, VSP_001403, VSP_001404;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q01705-3; Sequence=VSP_043064;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q01705-4; Sequence=VSP_043065;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in the brain, lung and
thymus. Expressed at lower levels in the spleen, bone-marrow,
spinal cord, eyes, mammary gland, liver, intestine, skeletal
muscle, kidney and heart. In the hair follicle, highly expressed
exclusively in the epithelial compartment.
{ECO:0000269|PubMed:15965470}.
-!- DEVELOPMENTAL STAGE: First detected in the mesoderm at 7.5 dpc By
8.5 dpc highly expressed in presomitic mesoderm, mesenchyme and
endothelial cells, while much lower levels are seen in the
neuroepithelium. Between 9.5-10.5 dpc expressed at high levels in
the neuroepithelium. At 13.5 dpc expressed in the surface
ectoderm, eye and developing whisker follicles. Hair follicle
matrix cells expression starts as different cell types become
distinguishable in the developing follicle. Expression persists
throughout the growth phase of the follicle and maintains the same
expression profile in the second hair cycle. The cells in the
follicle that undergo a phase of high level expression are in
transition from mitotic precursors to several discrete,
differentiating cell types. Specifically expressed in cerebellar
Bergmann glial cells during postnatal development.
{ECO:0000269|PubMed:1425352, ECO:0000269|PubMed:1426644,
ECO:0000269|PubMed:8486742}.
-!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
which is proteolytically cleaved by a furin-like convertase in the
trans-Golgi network before it reaches the plasma membrane to yield
an active, ligand-accessible form. Cleavage results in a C-
terminal fragment N(TM) and a N-terminal fragment N(EC). Following
ligand binding, it is cleaved by ADAM17 to yield a membrane-
associated intermediate fragment called notch extracellular
truncation (NEXT). Following endocytosis, this fragment is then
cleaved by presenilin dependent gamma-secretase to release a
notch-derived peptide containing the intracellular domain (NICD)
from the membrane.
-!- PTM: Phosphorylated.
-!- PTM: O-linked glycosylation by GALNT11 is involved in
determination of left/right symmetry: glycosylation promotes
activation of NOTCH1, possibly by promoting cleavage by ADAM17,
modulating the balance between motile and immotile (sensory) cilia
at the left-right organiser (LRO) (By similarity). O-glycosylated
on the EGF-like domains (PubMed:21757702). Contains both O-linked
fucose and O-linked glucose in the EGF-like domains 11, 12 and 13,
which are interacting with the residues on DLL4 (By similarity).
O-glycosylation at Ser-1027 is only partial (PubMed:21757702).
MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues
at specific EGF-like domains results in inhibition of its
activation by JAG1 and enhancement of its activation by DLL1 via
an increased binding to DLL1 (PubMed:28089369).
{ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q07008,
ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369}.
-!- PTM: Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination
by ITCH; promotes the lysosomal degradation of non-activated
internalized NOTCH1 (PubMed:18628966, PubMed:23886940).
Monoubiquitination at Lys-1749 is required for activation by
gamma-secretase cleavage, it promotes interaction with AAK1, which
stabilizes it. Deubiquitination by EIF3F is necessary for nuclear
import of activated Notch (PubMed:15240571).
{ECO:0000269|PubMed:15240571, ECO:0000269|PubMed:18628966,
ECO:0000269|PubMed:23886940}.
-!- PTM: Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN.
Hydroxylation reduces affinity for HI1AN and may thus indirectly
modulate negative regulation of NICD.
{ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578}.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z11886; CAA77941.1; -; mRNA.
EMBL; AF508809; AAM28905.1; -; mRNA.
EMBL; AB100603; BAC77038.1; -; Genomic_DNA.
EMBL; AB100603; BAC77039.1; -; Genomic_DNA.
EMBL; AB100603; BAC77040.1; -; Genomic_DNA.
EMBL; AL732541; CAM20304.1; -; Genomic_DNA.
EMBL; CH466542; EDL08321.1; -; Genomic_DNA.
EMBL; BC138441; AAI38442.1; -; mRNA.
EMBL; BC138442; AAI38443.1; -; mRNA.
EMBL; L02613; AAK14898.1; -; mRNA.
EMBL; X68278; CAA48339.1; -; mRNA.
EMBL; AK154528; BAE32653.1; -; mRNA.
EMBL; AK157475; BAE34095.1; -; mRNA.
EMBL; AJ238029; CAB40733.1; -; mRNA.
EMBL; X82562; CAA57909.1; -; mRNA.
CCDS; CCDS15806.1; -. [Q01705-1]
PIR; A46438; A46438.
PIR; B49175; B49175.
RefSeq; NP_032740.3; NM_008714.3. [Q01705-1]
UniGene; Mm.290610; -.
PDB; 1YMP; X-ray; 2.20 A; A/B=1971-2105.
PDB; 2QC9; X-ray; 2.35 A; A/B=1899-2106.
PDB; 2RQZ; NMR; -; A=452-489.
PDB; 2RR0; NMR; -; A=452-489.
PDB; 2RR2; NMR; -; A=452-489.
PDB; 3P3N; X-ray; 2.40 A; B=1930-1949.
PDB; 3P3P; X-ray; 2.60 A; B=1999-2016.
PDB; 5KY0; X-ray; 1.53 A; B=452-491.
PDB; 5KY4; X-ray; 1.47 A; B=983-1022.
PDB; 5KY8; X-ray; 1.65 A; B=452-491.
PDB; 5KY9; X-ray; 1.83 A; B=452-491.
PDBsum; 1YMP; -.
PDBsum; 2QC9; -.
PDBsum; 2RQZ; -.
PDBsum; 2RR0; -.
PDBsum; 2RR2; -.
PDBsum; 3P3N; -.
PDBsum; 3P3P; -.
PDBsum; 5KY0; -.
PDBsum; 5KY4; -.
PDBsum; 5KY8; -.
PDBsum; 5KY9; -.
ProteinModelPortal; Q01705; -.
SMR; Q01705; -.
BioGrid; 201808; 21.
CORUM; Q01705; -.
DIP; DIP-214N; -.
IntAct; Q01705; 11.
MINT; MINT-142586; -.
STRING; 10090.ENSMUSP00000028288; -.
iPTMnet; Q01705; -.
PhosphoSitePlus; Q01705; -.
PaxDb; Q01705; -.
PeptideAtlas; Q01705; -.
PRIDE; Q01705; -.
Ensembl; ENSMUST00000028288; ENSMUSP00000028288; ENSMUSG00000026923. [Q01705-1]
GeneID; 18128; -.
KEGG; mmu:18128; -.
UCSC; uc008ivl.2; mouse. [Q01705-1]
CTD; 4851; -.
MGI; MGI:97363; Notch1.
eggNOG; ENOG410IR7G; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00810000125346; -.
HOGENOM; HOG000234369; -.
HOVERGEN; HBG052650; -.
InParanoid; Q01705; -.
KO; K02599; -.
OMA; QYVNSYT; -.
OrthoDB; EOG091G01NU; -.
TreeFam; TF351641; -.
Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-MMU-350054; Notch-HLH transcription pathway.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
EvolutionaryTrace; Q01705; -.
PRO; PR:Q01705; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026923; -.
CleanEx; MM_NOTCH1; -.
ExpressionAtlas; Q01705; baseline and differential.
Genevisible; Q01705; MM.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
GO; GO:0005112; F:Notch binding; IPI:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IMP:MGI.
GO; GO:0060842; P:arterial endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
GO; GO:0003162; P:atrioventricular node development; IMP:BHF-UCL.
GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IDA:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:BHF-UCL.
GO; GO:0003207; P:cardiac chamber formation; IMP:BHF-UCL.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0003213; P:cardiac right atrium morphogenesis; IMP:BHF-UCL.
GO; GO:0003219; P:cardiac right ventricle formation; IMP:MGI.
GO; GO:0060411; P:cardiac septum morphogenesis; IMP:BHF-UCL.
GO; GO:0060948; P:cardiac vascular smooth muscle cell development; IMP:BHF-UCL.
GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0021515; P:cell differentiation in spinal cord; IEA:Ensembl.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0001708; P:cell fate specification; IMP:MGI.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISO:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0072044; P:collecting duct development; IEP:UniProtKB.
GO; GO:0007386; P:compartment pattern specification; IMP:MGI.
GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL.
GO; GO:0003169; P:coronary vein morphogenesis; IMP:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0072017; P:distal tubule development; IEP:UniProtKB.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
GO; GO:0060956; P:endocardial cell differentiation; IMP:BHF-UCL.
GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
GO; GO:0003157; P:endocardium development; IMP:BHF-UCL.
GO; GO:0003160; P:endocardium morphogenesis; IMP:BHF-UCL.
GO; GO:0007492; P:endoderm development; IMP:MGI.
GO; GO:0008544; P:epidermis development; IGI:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0007440; P:foregut morphogenesis; IMP:MGI.
GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
GO; GO:0072144; P:glomerular mesangial cell development; IEP:UniProtKB.
GO; GO:0003241; P:growth involved in heart morphogenesis; IMP:BHF-UCL.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0007507; P:heart development; ISO:MGI.
GO; GO:0001947; P:heart looping; IGI:BHF-UCL.
GO; GO:0061384; P:heart trabecula morphogenesis; IMP:BHF-UCL.
GO; GO:0006959; P:humoral immune response; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IGI:MGI.
GO; GO:0072602; P:interleukin-4 secretion; IGI:MGI.
GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
GO; GO:0070986; P:left/right axis specification; IGI:BHF-UCL.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0014031; P:mesenchymal cell development; IMP:BHF-UCL.
GO; GO:0003192; P:mitral valve formation; ISO:MGI.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0045608; P:negative regulation of auditory receptor cell differentiation; IMP:MGI.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IMP:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISS:UniProtKB.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IDA:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:MGI.
GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; IDA:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IDA:UniProtKB.
GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IMP:MGI.
GO; GO:2000974; P:negative regulation of pro-B cell differentiation; IMP:UniProtKB.
GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0048663; P:neuron fate commitment; IGI:MGI.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IMP:MGI.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0002051; P:osteoblast fate commitment; NAS:BHF-UCL.
GO; GO:0003344; P:pericardium morphogenesis; IMP:BHF-UCL.
GO; GO:1903849; P:positive regulation of aorta morphogenesis; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; IC:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IDA:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IDA:MGI.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
GO; GO:0050434; P:positive regulation of viral transcription; IMP:AgBase.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:MGI.
GO; GO:0045607; P:regulation of auditory receptor cell differentiation; IMP:MGI.
GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IC:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; IMP:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:1901201; P:regulation of extracellular matrix assembly; IMP:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
GO; GO:0008593; P:regulation of Notch signaling pathway; IGI:MGI.
GO; GO:0014807; P:regulation of somitogenesis; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; IMP:BHF-UCL.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IMP:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0048103; P:somatic stem cell division; IDA:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; IMP:MGI.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
GO; GO:0035148; P:tube formation; ISS:UniProtKB.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL.
GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:MGI.
GO; GO:0060843; P:venous endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISO:MGI.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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_cys_sf.
InterPro; IPR008297; Notch.
InterPro; IPR035993; Notch-like_dom_sf.
InterPro; IPR022362; Notch_1.
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; 21.
Pfam; PF07645; EGF_CA; 5.
Pfam; PF12661; hEGF; 3.
Pfam; PF06816; NOD; 1.
Pfam; PF07684; NODP; 1.
Pfam; PF00066; Notch; 3.
PIRSF; PIRSF002279; Notch; 1.
PRINTS; PR01452; LNOTCHREPEAT.
PRINTS; PR01984; NOTCH1.
SMART; SM00248; ANK; 6.
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; 6.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS00010; ASX_HYDROXYL; 22.
PROSITE; PS00022; EGF_1; 35.
PROSITE; PS01186; EGF_2; 27.
PROSITE; PS50026; EGF_3; 36.
PROSITE; PS01187; EGF_CA; 21.
PROSITE; PS50258; LNR; 3.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Angiogenesis;
ANK repeat; Calcium; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation;
Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway;
Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 2531 Neurogenic locus notch homolog protein 1.
/FTId=PRO_0000007677.
CHAIN 1711 2531 Notch 1 extracellular truncation.
/FTId=PRO_0000007678.
CHAIN 1744 2531 Notch 1 intracellular domain.
/FTId=PRO_0000007679.
TOPO_DOM 19 1725 Extracellular. {ECO:0000255}.
TRANSMEM 1726 1746 Helical. {ECO:0000255}.
TOPO_DOM 1747 2531 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 58 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 59 99 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 102 139 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 140 176 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 178 216 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 218 255 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 257 293 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 295 333 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 335 371 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 372 410 EGF-like 10; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 412 450 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 452 488 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 490 526 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 528 564 EGF-like 14; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 566 601 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 603 639 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 641 676 EGF-like 17; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 678 714 EGF-like 18; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 716 751 EGF-like 19; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 753 789 EGF-like 20; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 791 827 EGF-like 21; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 829 867 EGF-like 22. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 869 905 EGF-like 23; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 907 943 EGF-like 24. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 945 981 EGF-like 25; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 983 1019 EGF-like 26. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1021 1057 EGF-like 27; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1059 1095 EGF-like 28. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1097 1143 EGF-like 29. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1145 1181 EGF-like 30; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1183 1219 EGF-like 31; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1221 1265 EGF-like 32; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1267 1305 EGF-like 33. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1307 1346 EGF-like 34. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1348 1384 EGF-like 35. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1387 1426 EGF-like 36. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1449 1489 LNR 1.
REPEAT 1490 1531 LNR 2.
REPEAT 1532 1571 LNR 3.
REPEAT 1917 1946 ANK 1.
REPEAT 1950 1980 ANK 2.
REPEAT 1984 2013 ANK 3.
REPEAT 2017 2046 ANK 4.
REPEAT 2050 2079 ANK 5.
REGION 420 421 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 448 452 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
REGION 1937 1945 HIF1AN-binding.
REGION 2004 2012 HIF1AN-binding.
METAL 432 432 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 435 435 Calcium 1; via amide nitrogen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 452 452 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 453 453 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 455 455 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 469 469 Calcium 2.
{ECO:0000250|UniProtKB:Q07008}.
METAL 470 470 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 490 490 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 491 491 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 493 493 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 507 507 Calcium 3.
{ECO:0000250|UniProtKB:Q07008}.
METAL 508 508 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q07008}.
METAL 1457 1457 Calcium 4; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00525}.
METAL 1460 1460 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 1475 1475 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 1478 1478 Calcium 4. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
SITE 469 469 Interaction with DLL4.
{ECO:0000250|UniProtKB:Q07008}.
SITE 1654 1655 Cleavage; by furin-like protease.
SITE 1710 1711 Cleavage; by ADAM17. {ECO:0000250}.
MOD_RES 1851 1851 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1945 1945 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578}.
MOD_RES 2012 2012 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578}.
CARBOHYD 65 65 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 73 73 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 116 116 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 146 146 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 194 194 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 232 232 O-linked (Fuc...) threonine; alternate.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 232 232 O-linked (GalNAc...) threonine;
alternate.
{ECO:0000250|UniProtKB:P46531}.
CARBOHYD 311 311 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 341 341 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 349 349 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 378 378 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 435 435 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q07008}.
CARBOHYD 458 458 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 466 466 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 496 496 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 534 534 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 609 609 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 617 617 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 647 647 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 692 692 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 722 722 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 759 759 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 767 767 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 784 784 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 797 797 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 805 805 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 888 888 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 900 900 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 921 921 O-linked (Fuc) serine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 951 951 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 959 959 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 997 997 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 1027 1027 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 1035 1035 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 1065 1065 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 1159 1159 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 1179 1179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1189 1189 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 1197 1197 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 1241 1241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1273 1273 O-linked (Glc...) serine.
{ECO:0000269|PubMed:21757702}.
CARBOHYD 1362 1362 O-linked (Fuc...) threonine.
{ECO:0000269|PubMed:21757702,
ECO:0000269|PubMed:28089369}.
CARBOHYD 1379 1379 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 1402 1402 O-linked (Fuc...) threonine; alternate.
{ECO:0000269|PubMed:28089369}.
CARBOHYD 1402 1402 O-linked (GalNAc...) threonine;
alternate. {ECO:0000269|PubMed:28089369}.
CARBOHYD 1489 1489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1587 1587 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 24 37 {ECO:0000250}.
DISULFID 31 46 {ECO:0000250}.
DISULFID 63 74 {ECO:0000250}.
DISULFID 68 87 {ECO:0000250}.
DISULFID 89 98 {ECO:0000250}.
DISULFID 106 117 {ECO:0000250}.
DISULFID 111 127 {ECO:0000250}.
DISULFID 129 138 {ECO:0000250}.
DISULFID 144 155 {ECO:0000250}.
DISULFID 149 164 {ECO:0000250}.
DISULFID 166 175 {ECO:0000250}.
DISULFID 182 195 {ECO:0000250}.
DISULFID 189 204 {ECO:0000250}.
DISULFID 206 215 {ECO:0000250}.
DISULFID 222 233 {ECO:0000250}.
DISULFID 227 243 {ECO:0000250}.
DISULFID 245 254 {ECO:0000250}.
DISULFID 261 272 {ECO:0000250}.
DISULFID 266 281 {ECO:0000250}.
DISULFID 283 292 {ECO:0000250}.
DISULFID 299 312 {ECO:0000250}.
DISULFID 306 321 {ECO:0000250}.
DISULFID 323 332 {ECO:0000250}.
DISULFID 339 350 {ECO:0000250}.
DISULFID 344 359 {ECO:0000250}.
DISULFID 361 370 {ECO:0000250}.
DISULFID 376 387 {ECO:0000250}.
DISULFID 381 398 {ECO:0000250}.
DISULFID 400 409 {ECO:0000250}.
DISULFID 416 429 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 423 438 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 440 449 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 456 467 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 461 476 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 478 487 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 494 505 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 499 514 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 516 525 {ECO:0000250|UniProtKB:Q07008}.
DISULFID 532 543 {ECO:0000250}.
DISULFID 537 552 {ECO:0000250}.
DISULFID 554 563 {ECO:0000250}.
DISULFID 570 580 {ECO:0000250}.
DISULFID 575 589 {ECO:0000250}.
DISULFID 591 600 {ECO:0000250}.
DISULFID 607 618 {ECO:0000250}.
DISULFID 612 627 {ECO:0000250}.
DISULFID 629 638 {ECO:0000250}.
DISULFID 645 655 {ECO:0000250}.
DISULFID 650 664 {ECO:0000250}.
DISULFID 666 675 {ECO:0000250}.
DISULFID 682 693 {ECO:0000250}.
DISULFID 687 702 {ECO:0000250}.
DISULFID 704 713 {ECO:0000250}.
DISULFID 720 730 {ECO:0000250}.
DISULFID 725 739 {ECO:0000250}.
DISULFID 741 750 {ECO:0000250}.
DISULFID 757 768 {ECO:0000250}.
DISULFID 762 777 {ECO:0000250}.
DISULFID 779 788 {ECO:0000250}.
DISULFID 795 806 {ECO:0000250}.
DISULFID 800 815 {ECO:0000250}.
DISULFID 817 826 {ECO:0000250}.
DISULFID 833 844 {ECO:0000250}.
DISULFID 838 855 {ECO:0000250}.
DISULFID 857 866 {ECO:0000250}.
DISULFID 873 884 {ECO:0000250}.
DISULFID 878 893 {ECO:0000250}.
DISULFID 895 904 {ECO:0000250}.
DISULFID 911 922 {ECO:0000250}.
DISULFID 916 931 {ECO:0000250}.
DISULFID 933 942 {ECO:0000250}.
DISULFID 949 960 {ECO:0000250}.
DISULFID 954 969 {ECO:0000250}.
DISULFID 971 980 {ECO:0000250}.
DISULFID 987 998 {ECO:0000250}.
DISULFID 992 1007 {ECO:0000250}.
DISULFID 1009 1018 {ECO:0000250}.
DISULFID 1025 1036 {ECO:0000250}.
DISULFID 1030 1045 {ECO:0000250}.
DISULFID 1047 1056 {ECO:0000250}.
DISULFID 1063 1074 {ECO:0000250}.
DISULFID 1068 1083 {ECO:0000250}.
DISULFID 1085 1094 {ECO:0000250}.
DISULFID 1101 1122 {ECO:0000250}.
DISULFID 1116 1131 {ECO:0000250}.
DISULFID 1133 1142 {ECO:0000250}.
DISULFID 1149 1160 {ECO:0000250}.
DISULFID 1154 1169 {ECO:0000250}.
DISULFID 1171 1180 {ECO:0000250}.
DISULFID 1187 1198 {ECO:0000250}.
DISULFID 1192 1207 {ECO:0000250}.
DISULFID 1209 1218 {ECO:0000250}.
DISULFID 1225 1244 {ECO:0000250}.
DISULFID 1238 1253 {ECO:0000250}.
DISULFID 1255 1264 {ECO:0000250}.
DISULFID 1271 1284 {ECO:0000250}.
DISULFID 1276 1293 {ECO:0000250}.
DISULFID 1295 1304 {ECO:0000250}.
DISULFID 1311 1322 {ECO:0000250}.
DISULFID 1316 1334 {ECO:0000250}.
DISULFID 1336 1345 {ECO:0000250}.
DISULFID 1352 1363 {ECO:0000250}.
DISULFID 1357 1372 {ECO:0000250}.
DISULFID 1374 1383 {ECO:0000250}.
DISULFID 1391 1403 {ECO:0000250}.
DISULFID 1397 1414 {ECO:0000250}.
DISULFID 1416 1425 {ECO:0000250}.
DISULFID 1449 1472 {ECO:0000250}.
DISULFID 1454 1467 {ECO:0000250}.
DISULFID 1463 1479 {ECO:0000250}.
DISULFID 1490 1514 {ECO:0000250}.
DISULFID 1496 1509 {ECO:0000250}.
DISULFID 1505 1521 {ECO:0000250}.
DISULFID 1536 1549 {ECO:0000250}.
DISULFID 1545 1561 {ECO:0000250}.
CROSSLNK 1749 1749 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:15240571}.
VAR_SEQ 1 47 MPRLLTPLLCLTLLPALAARGLRCSQPSGTCLNGGRCEVAN
GTEACV -> MQTPLLSLAGATTELCFLPASVLASSLPGPS
L (in isoform 4). {ECO:0000305}.
/FTId=VSP_043065.
VAR_SEQ 1 21 MPRLLTPLLCLTLLPALAARG -> MKNSNTLTNKWRMEQC
(in isoform 3). {ECO:0000305}.
/FTId=VSP_043064.
VAR_SEQ 857 914 Missing (in isoform 2).
{ECO:0000303|PubMed:1426644}.
/FTId=VSP_001402.
VAR_SEQ 1329 1355 Missing (in isoform 2).
{ECO:0000303|PubMed:1426644}.
/FTId=VSP_001403.
VAR_SEQ 1636 1854 Missing (in isoform 2).
{ECO:0000303|PubMed:1426644}.
/FTId=VSP_001404.
MUTAGEN 65 65 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 146 146 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 232 232 T->V: No significant effect on its
binding and activation by DLL1 or JAG1.
No significant effect on RFNG-, LFNG- and
MFNG-mediated enhancement of its
activation by DLL1. Decrease in LFNG- and
MFNG-mediated inhibition of its
activation by JAG1. Significant decrease
in LFNG- and MFNG-mediated inhibition of
its activation by JAG1; when associated
with V-1402.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 311 311 T->V: Significant loss of binding and
activation by DLL1 or JAG1. Decrease in
RFNG-, LFNG- and MFNG-mediated
enhancement of its activation by DLL1.
Decrease in LFNG-mediated inhibition of
its activation by JAG1. Significant loss
of binding and activation by DLL1 or JAG1
and complete loss of RFNG- and LFNG-
mediated enhancement of its activation by
DLL1; when associated with V-466.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 341 341 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 349 349 T->V: Reduced binding and activation by
JAG1 but not DLL1. Decrease in MFNG-
mediated enhancement of its activation by
DLL1. {ECO:0000269|PubMed:28089369}.
MUTAGEN 378 378 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 458 458 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 466 466 T->V: Reduced binding and activation by
DLL1 but not JAG1. Decrease in RFNG- and
LFNG-mediated enhancement of its
activation by DLL1. Loss of RFNG-mediated
enhancement of its activation by JAG1.
Significant loss of binding and
activation by DLL1 or JAG1 and complete
loss of RFNG- and LFNG-mediated
enhancement of its activation by DLL1;
when associated with V-311.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 496 496 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 534 534 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 609 609 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 647 647 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 722 722 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 759 759 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 797 797 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 951 951 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 997 997 T->V: Reduced binding and activation by
DLL1 but not JAG1. No effect on RFNG-,
LFNG- and MFNG-mediated enhancement of
its activation by DLL1. No effect on
LFNG- and MFNG-mediated inhibition of its
activation by JAG1.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 1027 1027 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 1035 1035 T->V: Reduced binding and activation by
JAG1 but not DLL1. No effect on RFNG-,
LFNG- and MFNG-mediated enhancement of
its activation by DLL1. No effect on
LFNG- and MFNG-mediated inhibition of its
activation by JAG1.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 1065 1065 S->A: Reduced activity.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 1159 1159 T->V: No significant effect on its
binding and activation by DLL1 or JAG1.
No effect on RFNG-, LFNG- and MFNG-
mediated enhancement of its activation by
DLL1. No effect on LFNG- and MFNG-
mediated inhibition of its activation by
JAG1. {ECO:0000269|PubMed:28089369}.
MUTAGEN 1189 1189 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 1273 1273 S->A: No effect.
{ECO:0000269|PubMed:21757702}.
MUTAGEN 1362 1362 T->V: No significant effect on its
binding and activation by DLL1 or JAG1.
No effect on RFNG-, LFNG- and MFNG-
mediated enhancement of its activation by
DLL1. No effect on LFNG- and MFNG-
mediated inhibition of its activation by
JAG1. {ECO:0000269|PubMed:28089369}.
MUTAGEN 1402 1402 T->V: No significant effect on its
binding and activation by DLL1 or JAG1.
No effect on RFNG-, LFNG- and MFNG-
mediated enhancement of its activation by
DLL1. Decrease in LFNG- and MFNG-mediated
inhibition of its activation by JAG1.
Significant decrease in LFNG- and MFNG-
mediated inhibition of its activation by
JAG1; when associated with V-232.
{ECO:0000269|PubMed:28089369}.
MUTAGEN 1651 1654 RQRR->AAAA: Processing by furin-like
convertase abolished.
{ECO:0000269|PubMed:9653148}.
MUTAGEN 1744 1744 V->L: NICD processing severely reduced.
MUTAGEN 1945 1945 N->A: Reduced ability to promote HIF1AN-
dependent 2-oxoglutarate decarboxylation
and greatly reduced transactivation
capacity. Abolished ability to promote
HIF1AN-dependent 2-oxoglutarate
decarboxylation; when associated with G-
2012. Almost abolished transactivation
capacity; when associated with A-2012.
{ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578}.
MUTAGEN 2012 2012 N->A: Slightly reduced ability to promote
HIF1AN-dependent 2-oxoglutarate
decarboxylation. Abolished ability to
promote HIF1AN-dependent 2-oxoglutarate
decarboxylation and almost abolished
transactivation capacity; when associated
with A-1945.
{ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578}.
MUTAGEN 2012 2012 N->G: Reduced ability to promote HIF1AN-
dependent 2-oxoglutarate decarboxylation.
Abolished ability to promote HIF1AN-
dependent 2-oxoglutarate decarboxylation;
when associated with A-1945.
{ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578}.
CONFLICT 17 17 L -> R (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 41 41 N -> S (in Ref. 1; CAA77941 and 3;
AAM28905). {ECO:0000305}.
CONFLICT 48 48 C -> A (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 51 51 A -> S (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 60 60 S -> P (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 67 67 P -> R (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 75 75 H -> Y (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 82 82 T -> I (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 104 105 NA -> KP (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 130 130 P -> S (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 194 194 T -> H (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 207 207 R -> C (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 231 231 G -> A (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 287 287 W -> V (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 309 309 G -> A (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 373 374 ND -> KH (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 396 396 A -> R (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 417 417 A -> D (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 422 422 P -> R (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 448 448 R -> G (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 510 510 N -> H (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 835 835 T -> I (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 933 934 CL -> SV (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1050 1050 G -> R (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1104 1106 Missing (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1155 1155 Q -> L (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1209 1209 C -> W (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1438 1438 R -> P (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 1545 1545 C -> S (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1556 1556 W -> R (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1572 1572 G -> R (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1576 1576 L -> V (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1609 1609 D -> H (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1661 1661 I -> T (in Ref. 10; BAE32653).
{ECO:0000305}.
CONFLICT 1864 1864 V -> D (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1890 1890 S -> R (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1896 1898 APA -> RPG (in Ref. 8; AAK14898).
{ECO:0000305}.
CONFLICT 1933 1934 AA -> RR (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 1938 1938 Missing (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 1997 1997 V -> L (in Ref. 3; AAM28905).
{ECO:0000305}.
CONFLICT 2046 2047 MQ -> IE (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2054 2054 P -> S (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2058 2062 AAREG -> SIRRE (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2075 2075 A -> G (in Ref. 16; CAA57909).
{ECO:0000305}.
CONFLICT 2086 2086 L -> M (in Ref. 10; BAE34095).
{ECO:0000305}.
CONFLICT 2136 2136 L -> P (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2172 2172 K -> S (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2179 2179 C -> W (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2185 2185 S -> SS (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2206 2206 P -> H (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2258 2258 P -> H (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2273 2273 S -> C (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2347 2347 N -> S (in Ref. 10; BAE34095).
{ECO:0000305}.
CONFLICT 2380 2380 Q -> P (in Ref. 1; CAA77941).
{ECO:0000305}.
CONFLICT 2483 2484 HP -> PT (in Ref. 1; CAA77941).
{ECO:0000305}.
HELIX 456 458 {ECO:0000244|PDB:5KY0}.
STRAND 462 464 {ECO:0000244|PDB:2RQZ}.
STRAND 466 469 {ECO:0000244|PDB:5KY0}.
STRAND 470 472 {ECO:0000244|PDB:2RR0}.
STRAND 474 477 {ECO:0000244|PDB:5KY0}.
STRAND 482 484 {ECO:0000244|PDB:5KY0}.
STRAND 997 1000 {ECO:0000244|PDB:5KY4}.
STRAND 1005 1008 {ECO:0000244|PDB:5KY4}.
STRAND 1013 1015 {ECO:0000244|PDB:5KY4}.
HELIX 1921 1927 {ECO:0000244|PDB:2QC9}.
HELIX 1931 1939 {ECO:0000244|PDB:2QC9}.
HELIX 1954 1961 {ECO:0000244|PDB:2QC9}.
HELIX 1964 1972 {ECO:0000244|PDB:2QC9}.
HELIX 1975 1977 {ECO:0000244|PDB:1YMP}.
HELIX 1988 1995 {ECO:0000244|PDB:1YMP}.
HELIX 2000 2006 {ECO:0000244|PDB:1YMP}.
HELIX 2021 2027 {ECO:0000244|PDB:1YMP}.
HELIX 2031 2039 {ECO:0000244|PDB:1YMP}.
HELIX 2054 2061 {ECO:0000244|PDB:1YMP}.
HELIX 2064 2072 {ECO:0000244|PDB:1YMP}.
HELIX 2087 2093 {ECO:0000244|PDB:1YMP}.
HELIX 2097 2103 {ECO:0000244|PDB:1YMP}.
SEQUENCE 2531 AA; 270835 MW; 97C91F69BABF02BF CRC64;
MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDS
NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT PLDNACLANP CRNGGTCDLL
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICRCPPGF HGPTCRQDVN
ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT
HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC HDRVASFYCE
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECALGA
NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP
GYEGVYCEIN TDECASSPCL HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC
ETNINECHSQ PCRHGGTCQD RDNSYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID
GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC
NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN
SGVCKESEDY ESFSCVCPTG WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA SNPCQNGANC
TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY
DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ
YHCECRSGWT GVNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS
YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV
GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCKNGG
VCAVASNTAR GFICRCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG
PECQFPASSP CVGSNPCYNQ GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI
PPPQIEEACE LPECQVDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD
CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL HTNVVFKRDA QGQQMIFPYY
GHEEELRKHP IKRSTVGWAT SSLLPGTSGG RQRRELDPMD IRGSIVYLEI DNRQCVQSSS
QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSEPVEPPL PSQLHLMYVA AAAFVLLFFV
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ
NEWGDEDLET KKFRFEEPVV LPDLSDQTDH RQWTQQHLDA ADLRMSAMAP TPPQGEVDAD
CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL HNQTDRTGET
ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL LRNRATDLDA
RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN
GANKDMQNNK EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK PSTKGLACGS
KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP
LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG
TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHSMMGPL
HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ LQPQNLQPPS QPHLSVSSAA
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP
SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS PHSNISDWSE GISSPPTTMP
SQITHIPEAF K


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