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Neurogenic locus notch homolog protein 3 (Notch 3) [Cleaved into: Notch 3 extracellular truncation; Notch 3 intracellular domain]

 NOTC3_HUMAN             Reviewed;        2321 AA.
Q9UM47; Q9UEB3; Q9UPL3; Q9Y6L8;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
22-NOV-2017, entry version 186.
RecName: Full=Neurogenic locus notch homolog protein 3;
Short=Notch 3;
Contains:
RecName: Full=Notch 3 extracellular truncation;
Contains:
RecName: Full=Notch 3 intracellular domain;
Flags: Precursor;
Name=NOTCH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-2223.
PubMed=8878478; DOI=10.1038/383707a0;
Joutel A., Corpechot C., Ducros A., Vahedi K., Chabriat H., Mouton P.,
Alamowitch S., Domenga V., Cecillion M., Marechal E., Maciazek J.,
Vayssiere C., Cruaud C., Cabanis E.-A., Ruchoux M.M., Weissenbach J.,
Bach J.-F., Bousser M.-G., Tournier-Lasserve E.;
"Notch3 mutations in CADASIL, a hereditary adult-onset condition
causing stroke and dementia.";
Nature 383:707-710(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Gunel M., Artavanis-Tsakonas S.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
IDENTIFICATION OF LIGANDS.
PubMed=10079256; DOI=10.1016/S0002-9440(10)65325-4;
Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L.,
Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.;
"Human ligands of the Notch receptor.";
Am. J. Pathol. 154:785-794(1999).
[5]
INTERACTION WITH MAML1.
PubMed=11101851; DOI=10.1038/82644;
Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S.,
Griffin J.D.;
"MAML1, a human homologue of Drosophila mastermind, is a
transcriptional co-activator for NOTCH receptors.";
Nat. Genet. 26:484-489(2000).
[6]
INTERACTION WITH MAML2 AND MAML3.
PubMed=12370315; DOI=10.1128/MCB.22.21.7688-7700.2002;
Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.;
"Identification of a family of mastermind-like transcriptional
coactivators for mammalian notch receptors.";
Mol. Cell. Biol. 22:7688-7700(2002).
[7]
INTERACTION WITH PSMA1.
PubMed=17292860; DOI=10.1016/j.bbrc.2007.01.151;
Zhang Y., Jia L., Lee S.J., Wang M.M.;
"Conserved signal peptide of Notch3 inhibits interaction with
proteasome.";
Biochem. Biophys. Res. Commun. 355:245-251(2007).
[8]
INTERACTION WITH HIF1AN.
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).
[9]
HYDROXYLATION BY HIF1AN.
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).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2174, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
INVOLVEMENT IN LMNS.
PubMed=25394726; DOI=10.1002/ajmg.a.36863;
Gripp K.W., Robbins K.M., Sobreira N.L., Witmer P.D., Bird L.M.,
Avela K., Makitie O., Alves D., Hogue J.S., Zackai E.H., Doheny K.F.,
Stabley D.L., Sol-Church K.;
"Truncating mutations in the last exon of NOTCH3 cause lateral
meningocele syndrome.";
Am. J. Med. Genet. A 167A:271-281(2015).
[12]
VARIANTS CADASIL1 TYR-49; CYS-71; CYS-90; CYS-110; CYS-133; CYS-141;
ARG-146; CYS-153; CYS-169; CYS-171; CYS-182; ARG-185; SER-212;
GLY-222; TYR-224; CYS-258; TYR-542; CYS-558; CYS-578; CYS-728;
CYS-985; CYS-1006; CYS-1031; CYS-1231 AND ARG-1261, AND VARIANTS
ARG-170; LEU-496; GLN-1133; MET-1183 AND VAL-2223.
PubMed=9388399; DOI=10.1016/S0140-6736(97)08083-5;
Joutel A., Vahedi K., Corpechot C., Troesch A., Chabriat H.,
Vayssiere C., Cruaud C., Maciazek J., Weissenbach J., Bousser M.-G.,
Bach J.-F., Tournier-Lasserve E.;
"Strong clustering and stereotyped nature of Notch3 mutations in
CADASIL patients.";
Lancet 350:1511-1515(1997).
[13]
VARIANTS CADASIL1 CYS-90; PHE-117; CYS-133; CYS-141; CYS-169; TYR-174;
CYS-182 AND ARG-183.
PubMed=10227618; DOI=10.1212/WNL.52.7.1361;
Dichgans M., Filippi M., Bruening R., Iannucci G., Berchtenbreiter C.,
Minicucci L., Uttner I., Crispin A., Ludwig H., Gasser T.,
Yousry T.A.;
"Quantitative MRI in CADASIL: correlation with disability and
cognitive performance.";
Neurology 52:1361-1367(1999).
[14]
VARIANTS CADASIL1 CYS-133; CYS-141; CYS-153; CYS-182; CYS-207; CYS-544
AND ARG-1015.
PubMed=10371548; DOI=10.1212/WNL.52.9.1913;
Dutch CADASIL research group;
Lesnik Oberstein S.A.J., Ferrari M.D., Bakker E., van Gestel J.,
Kneppers A.L.J., Frants R.R., Breuning M.H., Haan J.;
"Diagnostic Notch3 sequence analysis in CADASIL: three new mutations
in Dutch patients. Dutch CADASIL Research Group.";
Neurology 52:1913-1915(1999).
[15]
VARIANTS CADASIL1 80-ASP--SER-84 DEL; CYS-90; PHE-93; CYS-110;
PHE-117; PHE-123; CYS-133; CYS-141; SER-144; TYR-144; CYS-150;
153-ARG--CYS-155 DEL; CYS-153; CYS-169; TYR-174; CYS-182; ARG-183;
SER-183; ARG-185 AND PHE-194.
PubMed=10854111; DOI=10.1038/sj.ejhg.5200460;
Dichgans M., Ludwig H., Mueller-Hoecker J., Messerschmidt A.,
Gasser T.;
"Small in-frame deletions and missense mutations in CADASIL: 3D models
predict misfolding of Notch3 EGF-like repeat domains.";
Eur. J. Hum. Genet. 8:280-285(2000).
[16]
VARIANT CADASIL1 PHE-144.
PubMed=11058919;
DOI=10.1002/1098-1004(200011)16:5<449::AID-HUMU26>3.3.CO;2-9;
Grigg R., Lea R., Sullivan A.A., Curtain R., MacMillian J.,
Griffiths L.;
"Identification of a novel mutation C144F in the Notch3 gene in an
Australian CADASIL pedigree.";
Hum. Mutat. 16:449-450(2000).
[17]
VARIANTS CADASIL1 TYR-49; CYS-54; CYS-90; CYS-110; 114-GLY--PRO-120
DEL; TYR-123; CYS-133; CYS-141; ARG-146; CYS-153; SER-162; CYS-169;
TYR-174; CYS-180; CYS-182; ARG-185; TYR-194; TYR-206; CYS-207;
SER-212; GLY-222; TYR-224; CYS-258; TYR-542; CYS-558; CYS-578;
CYS-607; CYS-728; CYS-984; CYS-985; CYS-1006; CYS-1031; CYS-1231 AND
ARG-1261.
PubMed=11102981;
DOI=10.1002/1098-1004(200012)16:6<518::AID-HUMU9>3.3.CO;2-H;
Escary J.-L., Cecillon M., Maciazek J., Lathrop M.,
Tournier-Lasserve E., Joutel A.;
"Evaluation of DHPLC analysis in mutational scanning of Notch3, a gene
with a high G-C content.";
Hum. Mutat. 16:518-526(2000).
[18]
VARIANT CADASIL1 114-GLY--PRO-120 DEL.
PubMed=10802807; DOI=10.1212/WNL.54.9.1874;
Joutel A., Chabriat H., Vahedi K., Domenga V., Vayssiere C.,
Ruchoux M.M., Lucas C., Leys D., Bousser M.-G., Tournier-Lasserve E.;
"Splice site mutation causing a seven amino acid Notch3 in-frame
deletion in CADASIL.";
Neurology 54:1874-1875(2000).
[19]
VARIANT CADASIL1 CYS-332.
PubMed=11559313; DOI=10.1001/archneur.58.9.1418;
Oliveri R.L., Muglia M., De Stefano N., Mazzei R., Labate A.,
Conforti F.L., Patitucci A., Gabriele A.L., Tagarelli G.,
Magariello A., Zappia M., Gambardella A., Federico A., Quattrone A.;
"A novel mutation in the Notch3 gene in an Italian family with
cerebral autosomal dominant arteriopathy with subcortical infarcts and
leukoencephalopathy: genetic and magnetic resonance spectroscopic
findings.";
Arch. Neurol. 58:1418-1422(2001).
[20]
VARIANTS CADASIL1 CYS-110; CYS-133; TRP-134; CYS-141; CYS-153;
CYS-182; GLY-185; CYS-207; SER-212; GLY-222; SER-428; CYS-558; CYS-985
AND CYS-1063.
PubMed=11755616; DOI=10.1016/S0140-6736(01)07142-2;
Joutel A., Favrole P., Labauge P., Chabriat H., Lescoat C.,
Andreux F., Domenga V., Cecillon M., Vahedi K., Ducros A.,
Cave-Riant F., Bousser M.G., Tournier-Lasserve E.;
"Skin biopsy immunostaining with a Notch3 monoclonal antibody for
CADASIL diagnosis.";
Lancet 358:2049-2051(2001).
[21]
VARIANT CADASIL1 TRP-134.
PubMed=11810186; DOI=10.1007/s004010100439;
Feuerhake F., Volk B., Ostertag C.B., Jungling F.D., Kassubek J.,
Orszagh M., Dichgans M.;
"Reversible coma with raised intracranial pressure: an unusual
clinical manifestation of CADASIL.";
Acta Neuropathol. 103:188-192(2002).
[22]
VARIANTS CADASIL1 ARG-76; TYR-93; TYR-128; CYS-142; ARG-194; TYR-222;
SER-233; ARG-251; CYS-420; GLY-440; CYS-449; CYS-953 AND CYS-1021.
PubMed=12146805;
Kalimo H., Ruchoux M.-M., Viitanen M., Kalaria R.N.;
"CADASIL: a common form of hereditary arteriopathy causing brain
infarcts and dementia.";
Brain Pathol. 12:371-384(2002).
[23]
VARIANT CADASIL1 ARG-455.
PubMed=12136071; DOI=10.1212/WNL.59.2.277;
Arboleda-Velasquez J.F., Lopera F., Lopez E., Frosch M.P.,
Sepulveda-Falla D., Gutierrez J.E., Vargas S., Medina M.,
Martinez De Arrieta C., Lebo R.V., Slaugenhaupt S.A., Betensky R.A.,
Villegas A., Arcos-Burgos M., Rivera D., Restrepo J.C., Kosik K.S.;
"C455R notch3 mutation in a Colombian CADASIL kindred with early onset
of stroke.";
Neurology 59:277-279(2002).
[24]
VARIANT CADASIL1 TYR-67.
PubMed=12589106;
Moon S.-Y., Kim H.-Y., Seok J.-I., Kwon J.-C., Ki C.-S., Kim J.-W.,
Suh Y.-L., Na D.L.;
"A novel mutation (C67Y)in the NOTCH3 gene in a Korean CADASIL
patient.";
J. Korean Med. Sci. 18:141-144(2003).
[25]
VARIANTS CADASIL1 CYS-90; CYS-133; CYS-169; ARG-174; PHE-174 AND
LYS-213.
PubMed=12810003; DOI=10.1016/S0022-510X(03)00109-6;
Santa Y., Uyama E., Chui D.H., Arima M., Kotorii S., Takahashi K.,
Tabira T.;
"Genetic, clinical and pathological studies of CADASIL in Japan: a
partial contribution of Notch3 mutations and implications of smooth
muscle cell degeneration for the pathogenesis.";
J. Neurol. Sci. 212:79-84(2003).
[26]
VARIANTS CADASIL1 ARG-76; CYS-90; CYS-110; CYS-141; CYS-153; CYS-169;
CYS-182; ARG-183; CYS-189; SER-194; CYS-207; ARG-251; CYS-332;
GLY-440; CYS-607; CYS-953 AND CYS-1231.
PubMed=15229130; DOI=10.1093/brain/awh223;
Singhal S., Bevan S., Barrick T., Rich P., Markus H.S.;
"The influence of genetic and cardiovascular risk factors on the
CADASIL phenotype.";
Brain 127:2031-2038(2004).
[27]
VARIANTS CADASIL1 GLY-43; PHE-49; CYS-60; SER-65; TRP-76;
77-GLN--CYS-82 DEL; 80-ASP--SER-84 DEL; ARG-87; TYR-87; CYS-90;
PHE-93; TRP-106; TYR-108; CYS-110; PHE-117; PHE-123; CYS-133; TRP-134;
CYS-141; SER-144; TYR-144; CYS-145; CYS-149; CYS-150; 153-ARG--155-CYS
DEL; CYS-153; SER-155; CYS-169; ARG-174; TYR-174; CYS-182; ARG-183;
SER-183; PHE-183; ARG-185; PHE-194; TYR-201; CYS-207; TYR-233;
239-ASP--ASP-253 DEL; SER-240; ARG-245; TYR-260; CYS-332; CYS-335;
CYS-337; SER-379; ARG-395; CYS-421; TYR-428; ARG-440; SER-446;
TYR-484; TYR-495; ARG-511; TYR-549; CYS-558; CYS-985 AND TYR-1261.
PubMed=15364702; DOI=10.1093/brain/awh282;
Opherk C., Peters N., Herzog J., Luedtke R., Dichgans M.;
"Long-term prognosis and causes of death in CADASIL: a retrospective
study in 411 patients.";
Brain 127:2533-2539(2004).
[28]
VARIANT CADASIL1 CYS-133.
PubMed=15378071; DOI=10.1038/sj.ejhg.5201221;
Mykkaenen K., Savontaus M.L., Juvonen V., Sistonen P., Tuisku S.,
Tuominen S., Penttinen M., Lundkvist J., Viitanen M., Kalimo H.,
Peoyhoenen M.;
"Detection of the founder effect in Finnish CADASIL families.";
Eur. J. Hum. Genet. 12:813-819(2004).
[29]
VARIANT CADASIL1 TRP-108.
PubMed=15300988;
Rojas-Marcos I., Encarnacion M., Martinez-Yelamos S., Ferrer I.,
Arbizu T., Gil-Peralta A., Garcia-Lozano J.R.;
"Gene symbol: NOTCH3. Disease: CADASIL.";
Hum. Genet. 115:175-175(2004).
[30]
VARIANTS CADASIL1 GLY-43; PHE-49; CYS-60; SER-65; TRP-76;
80-ASP--SER-84 DEL; ARG-87; CYS-90; PHE-93; TYR-108; CYS-110; PHE-117;
PHE-123; CYS-133; TRP-134; CYS-141; SER-144; TYR-144; CYS-149;
CYS-150; CYS-153; 153-ARG--CYS-155 DEL; CYS-169; ARG-174; TYR-174;
CYS-182; SER-183; PHE-183; ARG-185; PHE-194; CYS-207; TYR-233;
SER-240; ARG-245; TYR-260; 239-ASP--ASP-253 DEL; CYS-319; CYS-332;
CYS-335; CYS-337; SER-379; ARG-395; CYS-421; TYR-428; ARG-440;
PHE-484; TYR-495; ARG-511; TYR-549; CYS-558; CYS-728; SER-775; CYS-985
AND TYR-1261.
PubMed=16009764; DOI=10.1001/archneur.62.7.1091;
Peters N., Opherk C., Bergmann T., Castro M., Herzog J., Dichgans M.;
"Spectrum of mutations in biopsy-proven CADASIL: implications for
diagnostic strategies.";
Arch. Neurol. 62:1091-1094(2005).
[31]
VARIANT CADASIL1 CYS-118.
PubMed=15818833;
Soong B.W., Lee Y.-C., Lu Y.-C.;
"Gene symbol: NOTCH3. Disease: cerebral autosomal dominant
arteriopathy with subcortical infarcts and leukoencephalopathy.";
Hum. Genet. 116:242-242(2005).
[32]
VARIANT BRAIN SMALL-VESSEL-DISEASE PRO-1515.
PubMed=18273901; DOI=10.1002/humu.9527;
Fouillade C., Chabriat H., Riant F., Mine M., Arnoud M., Magy L.,
Bousser M.G., Tournier-Lasserve E., Joutel A.;
"Activating NOTCH3 mutation in a patient with small-vessel-disease of
the brain.";
Hum. Mutat. 29:452-452(2008).
[33]
VARIANT IMF2 PRO-1519.
PubMed=23731542; DOI=10.1016/j.ajhg.2013.04.024;
Martignetti J.A., Tian L., Li D., Ramirez M.C., Camacho-Vanegas O.,
Camacho S.C., Guo Y., Zand D.J., Bernstein A.M., Masur S.K., Kim C.E.,
Otieno F.G., Hou C., Abdel-Magid N., Tweddale B., Metry D.,
Fournet J.C., Papp E., McPherson E.W., Zabel C., Vaksmann G.,
Morisot C., Keating B., Sleiman P.M., Cleveland J.A., Everman D.B.,
Zackai E., Hakonarson H.;
"Mutations in PDGFRB cause autosomal-dominant infantile
myofibromatosis.";
Am. J. Hum. Genet. 92:1001-1007(2013).
[34]
VARIANT CADASIL1 CYS-710.
PubMed=24000151; DOI=10.1002/humu.22432;
Rutten J.W., Boon E.M., Liem M.K., Dauwerse J.G., Pont M.J.,
Vollebregt E., Maat-Kievit A.J., Ginjaar H.B., Lakeman P.,
van Duinen S.G., Terwindt G.M., Lesnik Oberstein S.A.;
"Hypomorphic NOTCH3 alleles do not cause CADASIL in humans.";
Hum. Mutat. 34:1486-1489(2013).
-!- 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 (By similarity). {ECO:0007001}.
-!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and a N-
terminal fragment N(EC) which are probably linked by disulfide
bonds (By similarity). Interacts with MAML1, MAML2 and MAML3 which
act as transcriptional coactivators for NOTCH3. Interacts with
PSMA1. Interacts with HIF1AN. {ECO:0000269|PubMed:11101851,
ECO:0000269|PubMed:12370315, ECO:0000269|PubMed:17292860,
ECO:0000269|PubMed:17573339, ECO:0007001}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1236377, EBI-1236377;
Q9R1P4:Psma1 (xeno); NbExp=2; IntAct=EBI-1236377, EBI-991653;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Notch 3 intracellular domain: Nucleus.
Note=Following proteolytical processing NICD is translocated to
the nucleus.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult
tissues.
-!- 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 TNF-alpha converting enzyme
(TACE) to yield a membrane-associated intermediate fragment called
notch extracellular truncation (NEXT). This fragment is then
cleaved by presenilin dependent gamma-secretase to release a
notch-derived peptide containing the intracellular domain (NICD)
from the membrane (By similarity). {ECO:0007001}.
-!- PTM: Phosphorylated. {ECO:0007001}.
-!- PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}.
-!- DISEASE: Cerebral arteriopathy, autosomal dominant, with
subcortical infarcts and leukoencephalopathy, 1 (CADASIL1)
[MIM:125310]: A cerebrovascular disease characterized by multiple
subcortical infarcts, pseudobulbar palsy, dementia, and the
presence of granular deposits in small cerebral arteries producing
ischemic stroke. {ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10371548, ECO:0000269|PubMed:10802807,
ECO:0000269|PubMed:10854111, ECO:0000269|PubMed:11058919,
ECO:0000269|PubMed:11102981, ECO:0000269|PubMed:11559313,
ECO:0000269|PubMed:11755616, ECO:0000269|PubMed:11810186,
ECO:0000269|PubMed:12136071, ECO:0000269|PubMed:12146805,
ECO:0000269|PubMed:12589106, ECO:0000269|PubMed:12810003,
ECO:0000269|PubMed:15229130, ECO:0000269|PubMed:15300988,
ECO:0000269|PubMed:15364702, ECO:0000269|PubMed:15378071,
ECO:0000269|PubMed:15818833, ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:24000151, ECO:0000269|PubMed:9388399}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myofibromatosis, infantile 2 (IMF2) [MIM:615293]: A rare
mesenchymal disorder characterized by the development of benign
tumors in the skin, striated muscles, bones, and, more rarely,
visceral organs. Subcutaneous or soft tissue nodules commonly
involve the skin of the head, neck, and trunk. Skeletal and
muscular lesions occur in about half of the patients. Lesions may
be solitary or multicentric, and they may be present at birth or
become apparent in early infancy or occasionally in adult life.
Visceral lesions are associated with high morbidity and mortality.
{ECO:0000269|PubMed:23731542}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Lateral meningocele syndrome (LMNS) [MIM:130720]: A very
rare skeletal disorder with facial anomalies, hypotonia and
neurologic dysfunction due to meningocele, a protrusion of the
meninges, unaccompanied by neural tissue, through a bony defect in
the skull or vertebral column. LMNS facial features include
hypertelorism and telecanthus, high arched eyebrows, ptosis, mid-
facial hypoplasia, micrognathia, high and narrow palate, low-set
ears and a hypotonic appearance. Additional variable features are
connective tissue abnormalities, aortic dilation, a high-pitched
nasal voice, wormian bones and osteolysis.
{ECO:0000269|PubMed:25394726}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000320}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NOTCH3ID41557ch19p13.html";
-----------------------------------------------------------------------
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EMBL; U97669; AAB91371.1; -; mRNA.
EMBL; AF058900; AAC14346.1; -; Genomic_DNA.
EMBL; AF058881; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058882; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058883; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058884; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058885; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058886; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058887; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058888; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058889; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058890; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058891; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058892; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058893; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058894; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058895; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058896; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058897; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058898; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AF058899; AAC14346.1; JOINED; Genomic_DNA.
EMBL; AC004257; AAC04897.1; -; Genomic_DNA.
EMBL; AC004663; AAC15789.1; -; Genomic_DNA.
CCDS; CCDS12326.1; -.
PIR; S78549; S78549.
RefSeq; NP_000426.2; NM_000435.2.
UniGene; Hs.8546; -.
PDB; 4ZLP; X-ray; 2.48 A; A/B=1378-1640.
PDB; 5CZV; X-ray; 3.19 A; A=1378-1640.
PDB; 5CZX; X-ray; 2.10 A; A/B=1378-1640.
PDBsum; 4ZLP; -.
PDBsum; 5CZV; -.
PDBsum; 5CZX; -.
ProteinModelPortal; Q9UM47; -.
SMR; Q9UM47; -.
BioGrid; 110916; 65.
DIP; DIP-39827N; -.
ELM; Q9UM47; -.
IntAct; Q9UM47; 19.
MINT; MINT-2822317; -.
STRING; 9606.ENSP00000263388; -.
BindingDB; Q9UM47; -.
ChEMBL; CHEMBL3407319; -.
GuidetoPHARMACOLOGY; 2860; -.
iPTMnet; Q9UM47; -.
PhosphoSitePlus; Q9UM47; -.
BioMuta; NOTCH3; -.
DMDM; 322510053; -.
EPD; Q9UM47; -.
MaxQB; Q9UM47; -.
PaxDb; Q9UM47; -.
PeptideAtlas; Q9UM47; -.
PRIDE; Q9UM47; -.
Ensembl; ENST00000263388; ENSP00000263388; ENSG00000074181.
GeneID; 4854; -.
KEGG; hsa:4854; -.
UCSC; uc002nan.4; human.
CTD; 4854; -.
DisGeNET; 4854; -.
EuPathDB; HostDB:ENSG00000074181.8; -.
GeneCards; NOTCH3; -.
GeneReviews; NOTCH3; -.
H-InvDB; HIX0040142; -.
H-InvDB; HIX0174419; -.
HGNC; HGNC:7883; NOTCH3.
HPA; CAB005393; -.
HPA; HPA044392; -.
MalaCards; NOTCH3; -.
MIM; 125310; phenotype.
MIM; 130720; phenotype.
MIM; 600276; gene.
MIM; 615293; phenotype.
neXtProt; NX_Q9UM47; -.
OpenTargets; ENSG00000074181; -.
Orphanet; 136; CADASIL.
Orphanet; 2591; Infantile myofibromatosis.
PharmGKB; PA31685; -.
eggNOG; ENOG410IR7G; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00810000125346; -.
HOGENOM; HOG000234369; -.
HOVERGEN; HBG052650; -.
InParanoid; Q9UM47; -.
KO; K20995; -.
OMA; ADHFADG; -.
OrthoDB; EOG091G01NU; -.
PhylomeDB; Q9UM47; -.
TreeFam; TF351641; -.
Reactome; R-HSA-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-1980148; Signaling by NOTCH3.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-5083630; Defective LFNG causes SCDO3.
SignaLink; Q9UM47; -.
SIGNOR; Q9UM47; -.
ChiTaRS; NOTCH3; human.
GeneWiki; Notch_3; -.
GenomeRNAi; 4854; -.
PRO; PR:Q9UM47; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000074181; -.
CleanEx; HS_NOTCH3; -.
ExpressionAtlas; Q9UM47; baseline and differential.
Genevisible; Q9UM47; HS.
GO; GO:0015629; C:actin cytoskeleton; HTP:HPA.
GO; GO:0005829; C:cytosol; HTP:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:Reactome.
GO; GO:0005576; C:extracellular region; IBA:Reactome.
GO; GO:0000139; C:Golgi membrane; IBA:Reactome.
GO; GO:0016021; C:integral component of membrane; RCA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; HTP:HPA.
GO; GO:0005886; C:plasma membrane; IBA:Reactome.
GO; GO:0043235; C:receptor complex; HTP:MGI.
GO; GO:0045296; F:cadherin binding; HTP:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; RCA:InterPro.
GO; GO:0019899; F:enzyme binding; RCA:Ensembl.
GO; GO:0042802; F:identical protein binding; IDA:IntAct.
GO; GO:0004872; F:receptor activity; RCA:InterPro.
GO; GO:0048844; P:artery morphogenesis; RCA:Ensembl.
GO; GO:0030900; P:forebrain development; RCA:Ensembl.
GO; GO:0072104; P:glomerular capillary formation; RCA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; RCA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; RCA:Ensembl.
GO; GO:0048663; P:neuron fate commitment; RCA:Ensembl.
GO; GO:0007220; P:Notch receptor processing; IBA:Reactome.
GO; GO:0007219; P:Notch signaling pathway; IBA:Reactome.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; RCA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; RCA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:Reactome.
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; IPR022331; Notch_3.
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; 19.
Pfam; PF07645; EGF_CA; 6.
Pfam; PF12661; hEGF; 3.
Pfam; PF06816; NOD; 1.
Pfam; PF07684; NODP; 1.
Pfam; PF00066; Notch; 3.
PIRSF; PIRSF002279; Notch; 1.
PRINTS; PR01452; LNOTCHREPEAT.
PRINTS; PR01986; NOTCH3.
SMART; SM00248; ANK; 6.
SMART; SM01334; DUF3454; 1.
SMART; SM00181; EGF; 34.
SMART; SM00179; EGF_CA; 31.
SMART; SM00004; NL; 3.
SMART; SM01338; NOD; 1.
SMART; SM01339; NODP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57184; SSF57184; 4.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS00010; ASX_HYDROXYL; 18.
PROSITE; PS00022; EGF_1; 33.
PROSITE; PS01186; EGF_2; 25.
PROSITE; PS50026; EGF_3; 34.
PROSITE; PS01187; EGF_CA; 16.
PROSITE; PS50258; LNR; 3.
1: Evidence at protein level;
3D-structure; Activator; ANK repeat; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Methylation;
Notch signaling pathway; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix.
SIGNAL 1 39 {ECO:0000270}.
CHAIN 40 2321 Neurogenic locus notch homolog protein 3.
/FTId=PRO_0000007692.
CHAIN 1629 2321 Notch 3 extracellular truncation.
{ECO:0007001}.
/FTId=PRO_0000007693.
CHAIN 1662 2321 Notch 3 intracellular domain.
{ECO:0007001}.
/FTId=PRO_0000007694.
TOPO_DOM 40 1643 Extracellular. {ECO:0000270}.
TRANSMEM 1644 1664 Helical. {ECO:0000270}.
TOPO_DOM 1665 2321 Cytoplasmic. {ECO:0000270}.
DOMAIN 40 77 EGF-like 1. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 78 118 EGF-like 2. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 119 156 EGF-like 3. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 158 195 EGF-like 4; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 197 234 EGF-like 5. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 236 272 EGF-like 6; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 274 312 EGF-like 7. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 314 350 EGF-like 8; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 351 389 EGF-like 9. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 391 429 EGF-like 10; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 431 467 EGF-like 11; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 469 505 EGF-like 12; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 507 543 EGF-like 13; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 545 580 EGF-like 14; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 582 618 EGF-like 15; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 620 655 EGF-like 16; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 657 693 EGF-like 17; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 695 730 EGF-like 18. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 734 770 EGF-like 19. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 771 808 EGF-like 20. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 810 847 EGF-like 21; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 849 885 EGF-like 22; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 887 922 EGF-like 23; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 924 960 EGF-like 24. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 962 998 EGF-like 25. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1000 1034 EGF-like 26. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1047 1082 EGF-like 27. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1084 1120 EGF-like 28. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1122 1158 EGF-like 29; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 1160 1203 EGF-like 30; calcium-binding.
{ECO:0000270|PROSITE-ProRule:PRU00076}.
DOMAIN 1205 1244 EGF-like 31. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1246 1287 EGF-like 32. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1289 1325 EGF-like 33. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
DOMAIN 1335 1373 EGF-like 34. {ECO:0000270|PROSITE-
ProRule:PRU00076}.
REPEAT 1387 1427 LNR 1.
REPEAT 1428 1458 LNR 2.
REPEAT 1467 1505 LNR 3.
REPEAT 1838 1867 ANK 1.
REPEAT 1871 1901 ANK 2.
REPEAT 1905 1934 ANK 3.
REPEAT 1938 1967 ANK 4.
REPEAT 1971 2000 ANK 5.
SITE 1571 1572 Cleavage; by furin-like protease.
{ECO:0007001}.
MOD_RES 2174 2174 Omega-N-methylarginine.
{ECO:0000307|PubMed:24129315}.
CARBOHYD 1179 1179 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
CARBOHYD 1336 1336 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
CARBOHYD 1438 1438 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
DISULFID 43 55 {ECO:0007001}.
DISULFID 49 65 {ECO:0007001}.
DISULFID 67 76 {ECO:0007001}.
DISULFID 82 93 {ECO:0007001}.
DISULFID 87 106 {ECO:0007001}.
DISULFID 108 117 {ECO:0007001}.
DISULFID 123 134 {ECO:0007001}.
DISULFID 128 144 {ECO:0007001}.
DISULFID 146 155 {ECO:0007001}.
DISULFID 162 174 {ECO:0007001}.
DISULFID 168 183 {ECO:0007001}.
DISULFID 185 194 {ECO:0007001}.
DISULFID 201 212 {ECO:0007001}.
DISULFID 206 222 {ECO:0007001}.
DISULFID 224 233 {ECO:0007001}.
DISULFID 240 251 {ECO:0007001}.
DISULFID 245 260 {ECO:0007001}.
DISULFID 262 271 {ECO:0007001}.
DISULFID 278 291 {ECO:0007001}.
DISULFID 285 300 {ECO:0007001}.
DISULFID 302 311 {ECO:0007001}.
DISULFID 318 329 {ECO:0007001}.
DISULFID 323 338 {ECO:0007001}.
DISULFID 340 349 {ECO:0007001}.
DISULFID 355 366 {ECO:0007001}.
DISULFID 360 377 {ECO:0007001}.
DISULFID 379 388 {ECO:0007001}.
DISULFID 395 408 {ECO:0007001}.
DISULFID 402 417 {ECO:0007001}.
DISULFID 419 428 {ECO:0007001}.
DISULFID 435 446 {ECO:0007001}.
DISULFID 440 455 {ECO:0007001}.
DISULFID 457 466 {ECO:0007001}.
DISULFID 473 484 {ECO:0007001}.
DISULFID 478 493 {ECO:0007001}.
DISULFID 495 504 {ECO:0007001}.
DISULFID 511 522 {ECO:0007001}.
DISULFID 516 531 {ECO:0007001}.
DISULFID 533 542 {ECO:0007001}.
DISULFID 549 559 {ECO:0007001}.
DISULFID 554 568 {ECO:0007001}.
DISULFID 570 579 {ECO:0007001}.
DISULFID 586 597 {ECO:0007001}.
DISULFID 591 606 {ECO:0007001}.
DISULFID 608 617 {ECO:0007001}.
DISULFID 624 634 {ECO:0007001}.
DISULFID 629 643 {ECO:0007001}.
DISULFID 645 654 {ECO:0007001}.
DISULFID 661 672 {ECO:0007001}.
DISULFID 666 681 {ECO:0007001}.
DISULFID 683 692 {ECO:0007001}.
DISULFID 699 709 {ECO:0007001}.
DISULFID 704 718 {ECO:0007001}.
DISULFID 720 729 {ECO:0007001}.
DISULFID 738 749 {ECO:0007001}.
DISULFID 743 758 {ECO:0007001}.
DISULFID 760 769 {ECO:0007001}.
DISULFID 775 786 {ECO:0007001}.
DISULFID 780 796 {ECO:0007001}.
DISULFID 798 807 {ECO:0007001}.
DISULFID 814 826 {ECO:0007001}.
DISULFID 820 835 {ECO:0007001}.
DISULFID 837 846 {ECO:0007001}.
DISULFID 853 864 {ECO:0007001}.
DISULFID 858 873 {ECO:0007001}.
DISULFID 875 884 {ECO:0007001}.
DISULFID 891 901 {ECO:0007001}.
DISULFID 896 910 {ECO:0007001}.
DISULFID 912 921 {ECO:0007001}.
DISULFID 928 939 {ECO:0007001}.
DISULFID 933 948 {ECO:0007001}.
DISULFID 950 959 {ECO:0007001}.
DISULFID 966 977 {ECO:0007001}.
DISULFID 971 986 {ECO:0007001}.
DISULFID 988 997 {ECO:0007001}.
DISULFID 1004 1015 {ECO:0007001}.
DISULFID 1009 1022 {ECO:0007001}.
DISULFID 1024 1033 {ECO:0007001}.
DISULFID 1040 1061 {ECO:0007001}.
DISULFID 1055 1070 {ECO:0007001}.
DISULFID 1072 1081 {ECO:0007001}.
DISULFID 1088 1099 {ECO:0007001}.
DISULFID 1093 1108 {ECO:0007001}.
DISULFID 1110 1119 {ECO:0007001}.
DISULFID 1126 1137 {ECO:0007001}.
DISULFID 1131 1146 {ECO:0007001}.
DISULFID 1148 1157 {ECO:0007001}.
DISULFID 1164 1182 {ECO:0007001}.
DISULFID 1176 1191 {ECO:0007001}.
DISULFID 1193 1202 {ECO:0007001}.
DISULFID 1209 1222 {ECO:0007001}.
DISULFID 1214 1232 {ECO:0007001}.
DISULFID 1234 1243 {ECO:0007001}.
DISULFID 1250 1261 {ECO:0007001}.
DISULFID 1255 1275 {ECO:0007001}.
DISULFID 1277 1286 {ECO:0007001}.
DISULFID 1293 1304 {ECO:0007001}.
DISULFID 1298 1313 {ECO:0007001}.
DISULFID 1315 1324 {ECO:0007001}.
DISULFID 1339 1350 {ECO:0007001}.
DISULFID 1344 1361 {ECO:0007001}.
DISULFID 1363 1372 {ECO:0007001}.
DISULFID 1387 1410 {ECO:0007001}.
DISULFID 1392 1405 {ECO:0007001}.
DISULFID 1401 1417 {ECO:0007001}.
DISULFID 1428 1451 {ECO:0007001}.
DISULFID 1433 1446 {ECO:0007001}.
DISULFID 1442 1458 {ECO:0007001}.
DISULFID 1467 1493 {ECO:0007001}.
DISULFID 1475 1488 {ECO:0007001}.
DISULFID 1484 1500 {ECO:0007001}.
VARIANT 43 43 C -> G (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044230.
VARIANT 49 49 C -> F (in CADASIL1; dbSNP:rs193921045).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044231.
VARIANT 49 49 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012871.
VARIANT 54 54 R -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044232.
VARIANT 60 60 S -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044233.
VARIANT 65 65 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044234.
VARIANT 67 67 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:12589106}.
/FTId=VAR_044235.
VARIANT 71 71 W -> C (in CADASIL1; dbSNP:rs28937321).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012872.
VARIANT 76 76 C -> R (in CADASIL1).
{ECO:0000269|PubMed:12146805,
ECO:0000269|PubMed:15229130}.
/FTId=VAR_044236.
VARIANT 76 76 C -> W (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044237.
VARIANT 77 82 Missing (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044238.
VARIANT 80 84 Missing (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044239.
VARIANT 87 87 C -> R (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044240.
VARIANT 87 87 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044241.
VARIANT 90 90 R -> C (in CADASIL1).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:12810003,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012873.
VARIANT 93 93 C -> F (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044242.
VARIANT 93 93 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044243.
VARIANT 106 106 C -> W (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044244.
VARIANT 108 108 C -> W (in CADASIL1).
{ECO:0000269|PubMed:15300988}.
/FTId=VAR_044245.
VARIANT 108 108 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044246.
VARIANT 110 110 R -> C (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012874.
VARIANT 114 120 Missing (in CADASIL1).
{ECO:0000269|PubMed:10802807,
ECO:0000269|PubMed:11102981}.
/FTId=VAR_012875.
VARIANT 117 117 C -> F (in CADASIL1; dbSNP:rs773539041).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044247.
VARIANT 118 118 S -> C (in CADASIL1).
{ECO:0000269|PubMed:15818833}.
/FTId=VAR_044248.
VARIANT 123 123 C -> F (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044249.
VARIANT 123 123 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044250.
VARIANT 128 128 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044251.
VARIANT 133 133 R -> C (in CADASIL1; dbSNP:rs137852642).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10371548,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:12810003,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:15378071,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012876.
VARIANT 134 134 C -> W (in CADASIL1).
{ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:11810186,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044252.
VARIANT 141 141 R -> C (in CADASIL1).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10371548,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012877.
VARIANT 142 142 F -> C (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044253.
VARIANT 144 144 C -> F (in CADASIL1).
{ECO:0000269|PubMed:11058919}.
/FTId=VAR_044254.
VARIANT 144 144 C -> S (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044255.
VARIANT 144 144 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044256.
VARIANT 145 145 S -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044257.
VARIANT 146 146 C -> R (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012878.
VARIANT 149 149 G -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044258.
VARIANT 150 150 Y -> C (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044259.
VARIANT 153 155 Missing (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044260.
VARIANT 153 153 R -> C (in CADASIL1; dbSNP:rs797045014).
{ECO:0000269|PubMed:10371548,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012879.
VARIANT 155 155 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044261.
VARIANT 162 162 C -> S (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044262.
VARIANT 169 169 R -> C (in CADASIL1; dbSNP:rs28933696).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:12810003,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012880.
VARIANT 170 170 H -> R (in dbSNP:rs147373451).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012881.
VARIANT 171 171 G -> C (in CADASIL1).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012882.
VARIANT 174 174 C -> F (in CADASIL1).
{ECO:0000269|PubMed:12810003}.
/FTId=VAR_044263.
VARIANT 174 174 C -> R (in CADASIL1).
{ECO:0000269|PubMed:12810003,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044264.
VARIANT 174 174 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044265.
VARIANT 180 180 S -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044266.
VARIANT 182 182 R -> C (in CADASIL1; dbSNP:rs28933697).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10371548,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012883.
VARIANT 183 183 C -> F (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044267.
VARIANT 183 183 C -> R (in CADASIL1).
{ECO:0000269|PubMed:10227618,
ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702}.
/FTId=VAR_044268.
VARIANT 183 183 C -> S (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044269.
VARIANT 185 185 C -> G (in CADASIL1).
{ECO:0000269|PubMed:11755616}.
/FTId=VAR_044270.
VARIANT 185 185 C -> R (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012884.
VARIANT 189 189 Y -> C (in CADASIL1).
{ECO:0000269|PubMed:15229130}.
/FTId=VAR_044271.
VARIANT 194 194 C -> F (in CADASIL1).
{ECO:0000269|PubMed:10854111,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044272.
VARIANT 194 194 C -> R (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044273.
VARIANT 194 194 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15229130}.
/FTId=VAR_044274.
VARIANT 194 194 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044275.
VARIANT 201 201 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044276.
VARIANT 206 206 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044277.
VARIANT 207 207 R -> C (in CADASIL1; dbSNP:rs775267348).
{ECO:0000269|PubMed:10371548,
ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044278.
VARIANT 212 212 C -> S (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012885.
VARIANT 213 213 R -> K (in CADASIL1).
{ECO:0000269|PubMed:12810003}.
/FTId=VAR_044279.
VARIANT 222 222 C -> G (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012886.
VARIANT 222 222 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044280.
VARIANT 224 224 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012887.
VARIANT 233 233 C -> S (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044281.
VARIANT 233 233 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044282.
VARIANT 239 253 Missing (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044283.
VARIANT 240 240 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044284.
VARIANT 245 245 C -> R (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044285.
VARIANT 251 251 C -> R (in CADASIL1).
{ECO:0000269|PubMed:12146805,
ECO:0000269|PubMed:15229130}.
/FTId=VAR_044286.
VARIANT 258 258 Y -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012888.
VARIANT 260 260 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044287.
VARIANT 319 319 A -> C (in CADASIL1; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:16009764}.
/FTId=VAR_044288.
VARIANT 332 332 R -> C (in CADASIL1; dbSNP:rs137852641).
{ECO:0000269|PubMed:11559313,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044289.
VARIANT 335 335 S -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044290.
VARIANT 337 337 Y -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044291.
VARIANT 379 379 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044292.
VARIANT 395 395 C -> R (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044293.
VARIANT 420 420 G -> C (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044294.
VARIANT 421 421 R -> C (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044295.
VARIANT 428 428 C -> S (in CADASIL1; dbSNP:rs267606915).
{ECO:0000269|PubMed:11755616}.
/FTId=VAR_044296.
VARIANT 428 428 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044297.
VARIANT 440 440 C -> G (in CADASIL1).
{ECO:0000269|PubMed:12146805,
ECO:0000269|PubMed:15229130}.
/FTId=VAR_044298.
VARIANT 440 440 C -> R (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044299.
VARIANT 446 446 C -> S (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044300.
VARIANT 449 449 R -> C (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044301.
VARIANT 455 455 C -> R (in CADASIL1; dbSNP:rs28933698).
{ECO:0000269|PubMed:12136071}.
/FTId=VAR_044302.
VARIANT 484 484 C -> F (in CADASIL1).
{ECO:0000269|PubMed:16009764}.
/FTId=VAR_044303.
VARIANT 484 484 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702}.
/FTId=VAR_044304.
VARIANT 495 495 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044305.
VARIANT 496 496 P -> L (in dbSNP:rs11670799).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012889.
VARIANT 511 511 C -> R (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044306.
VARIANT 542 542 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012890.
VARIANT 544 544 R -> C (in CADASIL1; dbSNP:rs201118034).
{ECO:0000269|PubMed:10371548}.
/FTId=VAR_044307.
VARIANT 549 549 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044308.
VARIANT 558 558 R -> C (in CADASIL1; dbSNP:rs75068032).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012891.
VARIANT 578 578 R -> C (in CADASIL1; dbSNP:rs769773673).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012892.
VARIANT 607 607 R -> C (in CADASIL1; dbSNP:rs777751303).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:15229130}.
/FTId=VAR_044309.
VARIANT 710 710 Y -> C (in CADASIL1; found in a compound
heterozygote also carrying an intragenic
frameshift deletion).
{ECO:0000269|PubMed:24000151}.
/FTId=VAR_072080.
VARIANT 728 728 R -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012893.
VARIANT 775 775 C -> S (in CADASIL1).
{ECO:0000269|PubMed:16009764}.
/FTId=VAR_044310.
VARIANT 953 953 G -> C (in CADASIL1).
{ECO:0000269|PubMed:12146805,
ECO:0000269|PubMed:15229130}.
/FTId=VAR_044311.
VARIANT 984 984 F -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981}.
/FTId=VAR_044312.
VARIANT 985 985 R -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:11755616,
ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012894.
VARIANT 1006 1006 R -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012895.
VARIANT 1015 1015 C -> R (in CADASIL1).
{ECO:0000269|PubMed:10371548}.
/FTId=VAR_044313.
VARIANT 1020 1020 A -> P (in dbSNP:rs35769976).
/FTId=VAR_044314.
VARIANT 1021 1021 Y -> C (in CADASIL1).
{ECO:0000269|PubMed:12146805}.
/FTId=VAR_044315.
VARIANT 1031 1031 R -> C (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012896.
VARIANT 1063 1063 D -> C (in CADASIL1; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:11755616}.
/FTId=VAR_044316.
VARIANT 1133 1133 H -> Q (in dbSNP:rs112197217).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012897.
VARIANT 1183 1183 V -> M (in dbSNP:rs10408676).
{ECO:0000269|PubMed:9388399}.
/FTId=VAR_012898.
VARIANT 1231 1231 R -> C (in CADASIL1; dbSNP:rs201680145).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:15229130,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012899.
VARIANT 1261 1261 C -> R (in CADASIL1).
{ECO:0000269|PubMed:11102981,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012900.
VARIANT 1261 1261 C -> Y (in CADASIL1).
{ECO:0000269|PubMed:15364702,
ECO:0000269|PubMed:16009764}.
/FTId=VAR_044317.
VARIANT 1515 1515 L -> P (in brain small-vessel-disease;
exhibits increased NOTCH3 signaling in a
ligand-independent fashion).
{ECO:0000269|PubMed:18273901}.
/FTId=VAR_044318.
VARIANT 1519 1519 L -> P (in IMF2; dbSNP:rs367543285).
{ECO:0000269|PubMed:23731542}.
/FTId=VAR_069927.
VARIANT 2223 2223 A -> V (in dbSNP:rs1044009).
{ECO:0000269|PubMed:8878478,
ECO:0000269|PubMed:9388399}.
/FTId=VAR_012901.
STRAND 1389 1391 {ECO:0000307|PDB:5CZX}.
HELIX 1393 1395 {ECO:0000307|PDB:5CZV}.
STRAND 1398 1400 {ECO:0000307|PDB:5CZX}.
HELIX 1403 1405 {ECO:0000307|PDB:4ZLP}.
TURN 1408 1410 {ECO:0000307|PDB:5CZX}.
HELIX 1411 1414 {ECO:0000307|PDB:5CZX}.
TURN 1415 1420 {ECO:0000307|PDB:5CZX}.
TURN 1424 1427 {ECO:0000307|PDB:5CZX}.
TURN 1431 1433 {ECO:0000307|PDB:5CZX}.
HELIX 1434 1437 {ECO:0000307|PDB:5CZX}.
STRAND 1439 1441 {ECO:0000307|PDB:5CZX}.
HELIX 1444 1446 {ECO:0000307|PDB:5CZX}.
TURN 1449 1451 {ECO:0000307|PDB:5CZX}.
HELIX 1452 1456 {ECO:0000307|PDB:5CZX}.
TURN 1457 1459 {ECO:0000307|PDB:5CZX}.
HELIX 1463 1465 {ECO:0000307|PDB:5CZX}.
HELIX 1469 1471 {ECO:0000307|PDB:5CZX}.
HELIX 1472 1478 {ECO:0000307|PDB:5CZX}.
STRAND 1481 1483 {ECO:0000307|PDB:5CZX}.
HELIX 1486 1488 {ECO:0000307|PDB:5CZX}.
HELIX 1491 1493 {ECO:0000307|PDB:5CZX}.
HELIX 1495 1498 {ECO:0000307|PDB:5CZX}.
STRAND 1510 1519 {ECO:0000307|PDB:5CZX}.
HELIX 1521 1526 {ECO:0000307|PDB:5CZX}.
HELIX 1528 1539 {ECO:0000307|PDB:5CZX}.
STRAND 1541 1545 {ECO:0000307|PDB:5CZX}.
STRAND 1555 1558 {ECO:0000307|PDB:5CZX}.
STRAND 1579 1587 {ECO:0000307|PDB:5CZX}.
TURN 1589 1592 {ECO:0000307|PDB:5CZV}.
TURN 1595 1597 {ECO:0000307|PDB:4ZLP}.
STRAND 1598 1600 {ECO:0000307|PDB:5CZV}.
HELIX 1604 1616 {ECO:0000307|PDB:5CZX}.
STRAND 1626 1632 {ECO:0000307|PDB:5CZX}.
SEQUENCE 2321 AA; 243631 MW; 3E70EC12A59CD638 CRC64;
MGPGARGRRR RRRPMSPPPP PPPVRALPLL LLLAGPGAAA PPCLDGSPCA NGGRCTQLPS
REAACLCPPG WVGERCQLED PCHSGPCAGR GVCQSSVVAG TARFSCRCPR GFRGPDCSLP
DPCLSSPCAH GARCSVGPDG RFLCSCPPGY QGRSCRSDVD ECRVGEPCRH GGTCLNTPGS
FRCQCPAGYT GPLCENPAVP CAPSPCRNGG TCRQSGDLTY DCACLPGFEG QNCEVNVDDC
PGHRCLNGGT CVDGVNTYNC QCPPEWTGQF CTEDVDECQL QPNACHNGGT CFNTLGGHSC
VCVNGWTGES CSQNIDDCAT AVCFHGATCH DRVASFYCAC PMGKTGLLCH LDDACVSNPC
HEDAICDTNP VNGRAICTCP PGFTGGACDQ DVDECSIGAN PCEHLGRCVN TQGSFLCQCG
RGYTGPRCET DVNECLSGPC RNQATCLDRI GQFTCICMAG FTGTYCEVDI DECQSSPCVN
GGVCKDRVNG FSCTCPSGFS GSTCQLDVDE CASTPCRNGA KCVDQPDGYE CRCAEGFEGT
LCDRNVDDCS PDPCHHGRCV DGIASFSCAC APGYTGTRCE SQVDECRSQP CRHGGKCLDL
VDKYLCRCPS GTTGVNCEVN IDDCASNPCT FGVCRDGINR YDCVCQPGFT GPLCNVEINE
CASSPCGEGG SCVDGENGFR CLCPPGSLPP LCLPPSHPCA HEPCSHGICY DAPGGFRCVC
EPGWSGPRCS QSLARDACES QPCRAGGTCS SDGMGFHCTC PPGVQGRQCE LLSPCTPNPC
EHGGRCESAP GQLPVCSCPQ GWQGPRCQQD VDECAGPAPC GPHGICTNLA GSFSCTCHGG
YTGPSCDQDI NDCDPNPCLN GGSCQDGVGS FSCSCLPGFA GPRCARDVDE CLSNPCGPGT
CTDHVASFTC TCPPGYGGFH CEQDLPDCSP SSCFNGGTCV DGVNSFSCLC RPGYTGAHCQ
HEADPCLSRP CLHGGVCSAA HPGFRCTCLE SFTGPQCQTL VDWCSRQPCQ NGGRCVQTGA
YCLCPPGWSG RLCDIRSLPC REAAAQIGVR LEQLCQAGGQ CVDEDSSHYC VCPEGRTGSH
CEQEVDPCLA QPCQHGGTCR GYMGGYMCEC LPGYNGDNCE DDVDECASQP CQHGGSCIDL
VARYLCSCPP GTLGVLCEIN EDDCGPGPPL DSGPRCLHNG TCVDLVGGFR CTCPPGYTGL
RCEADINECR SGACHAAHTR DCLQDPGGGF RCLCHAGFSG PRCQTVLSPC ESQPCQHGGQ
CRPSPGPGGG LTFTCHCAQP FWGPRCERVA RSCRELQCPV GVPCQQTPRG PRCACPPGLS
GPSCRSFPGS PPGASNASCA AAPCLHGGSC RPAPLAPFFR CACAQGWTGP RCEAPAAAPE
VSEEPRCPRA ACQAKRGDQR CDRECNSPGC GWDGGDCSLS VGDPWRQCEA LQCWRLFNNS
RCDPACSSPA CLYDNFDCHA GGRERTCNPV YEKYCADHFA DGRCDQGCNT EECGWDGLDC
ASEVPALLAR GVLVLTVLLP PEELLRSSAD FLQRLSAILR TSLRFRLDAH GQAMVFPYHR
PSPGSEPRAR RELAPEVIGS VVMLEIDNRL CLQSPENDHC FPDAQSAADY LGALSAVERL
DFPYPLRDVR GEPLEPPEPS VPLLPLLVAG AVLLLVILVL GVMVARRKRE HSTLWFPEGF
SLHKDVASGH KGRREPVGQD ALGMKNMAKG ESLMGEVATD WMDTECPEAK RLKVEEPGMG
AEEAVDCRQW TQHHLVAADI RVAPAMALTP PQGDADADGM DVNVRGPDGF TPLMLASFCG
GALEPMPTEE DEADDTSASI ISDLICQGAQ LGARTDRTGE TALHLAARYA RADAAKRLLD
AGADTNAQDH SGRTPLHTAV TADAQGVFQI LIRNRSTDLD ARMADGSTAL ILAARLAVEG
MVEELIASHA DVNAVDELGK SALHWAAAVN NVEATLALLK NGANKDMQDS KEETPLFLAA
REGSYEAAKL LLDHFANREI TDHLDRLPRD VAQERLHQDI VRLLDQPSGP RSPPGPHGLG
PLLCPPGAFL PGLKAAQSGS KKSRRPPGKA GLGPQGPRGR GKKLTLACPG PLADSSVTLS
PVDSLDSPRP FGGPPASPGG FPLEGPYAAA TATAVSLAQL GGPGRAGLGR QPPGGCVLSL
GLLNPVAVPL DWARLPPPAP PGPSFLLPLA PGPQLLNPGT PVSPQERPPP YLAVPGHGEE
YPAAGAHSSP PKARFLRVPS EHPYLTPSPE SPEHWASPSP PSLSDWSEST PSPATATGAM
ATTTGALPAQ PLPLSVPSSL AQAQTQLGPQ PEVTPKRQVL A


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