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

 NOTC1_RAT               Reviewed;        2531 AA.
Q07008; F1M9E7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 3.
30-AUG-2017, entry version 184.
RecName: Full=Neurogenic locus notch homolog protein 1;
Short=Notch 1;
Contains:
RecName: Full=Notch 1 extracellular truncation;
Short=NEXT;
Contains:
RecName: Full=Notch 1 intracellular domain;
Short=NICD;
Flags: Precursor;
Name=Notch1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Schwann cell;
PubMed=1764995;
Weinmaster G., Roberts V.J., Lemke G.;
"A homolog of Drosophila Notch expressed during mammalian
development.";
Development 113:199-205(1991).
[2]
SEQUENCE REVISION TO 1652-1653.
Weinmaster G.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
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.
[5]
FUNCTION.
PubMed=11182080; DOI=10.1016/S0896-6273(01)00179-9;
Tanigaki K., Nogaki F., Takahashi J., Tashiro K., Kurooka H.,
Honjo T.;
"Notch1 and Notch3 instructively restrict bFGF-responsive multipotent
neural progenitor cells to an astroglial fate.";
Neuron 29:45-55(2001).
[6]
TISSUE SPECIFICITY.
PubMed=1295745;
Weinmaster G., Roberts V.J., Lemke G.;
"Notch2: a second mammalian Notch gene.";
Development 116:931-941(1992).
[7]
TISSUE SPECIFICITY.
PubMed=11438922; DOI=10.1002/cne.1059.abs;
Irvin D.K., Zurcher S.D., Nguyen T., Weinmaster G., Kornblum H.I.;
"Expression patterns of Notch1, Notch2, and Notch3 suggest multiple
functional roles for the Notch-DSL signaling system during brain
development.";
J. Comp. Neurol. 436:167-181(2001).
[8] {ECO:0000244|PDB:4XL1, ECO:0000244|PDB:4XLW}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 412-526 IN COMPLEX WITH DLL4
AND CALCIUM, GLYCOSYLATION AT SER-435; SER-458; THR-466 AND SER-496,
AND DISULFIDE BONDS.
PubMed=25700513; DOI=10.1126/science.1261093;
Luca V.C., Jude K.M., Pierce N.W., Nachury M.V., Fischer S.,
Garcia K.C.;
"Structural biology. Structural basis for Notch1 engagement of Delta-
like 4.";
Science 347:847-853(2015).
-!- 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) (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11182080}.
-!- 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
(By similarity). Interacts with THBS4 (By similarity). Interacts
(via the EGF-like repeat region) with NOV (via CTCK domain) (By
similarity). Interacts (via EGF-like domains) with DLL4 (via N-
terminal DSL and MNNL domains) (PubMed:25700513). Interacts with
ZMIZ1 (By similarity). Interacts (via NICD domain) with MEGF10
(via the cytoplasmic domain) (By similarity).
{ECO:0000250|UniProtKB:Q01705, ECO:0000269|PubMed:25700513}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q01705}.
-!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
{ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical
processing NICD is translocated to the nucleus. Nuclear location
may require MEGF10. {ECO:0000250|UniProtKB:Q01705}.
-!- TISSUE SPECIFICITY: Expressed in the brain, kidney and spleen.
Expressed in postnatal central nervous system (CNS) germinal zones
and, in early postnatal life, within numerous cells throughout the
CNS. Found in both subventricular and ventricular germinal zones.
{ECO:0000269|PubMed:11438922, ECO:0000269|PubMed:1295745}.
-!- DEVELOPMENTAL STAGE: In the embryo, highest levels occur between
days 12 and 14 and decrease rapidly to much lower levels in the
adult.
-!- 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. {ECO:0000250|UniProtKB:Q01705}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- PTM: O-glycosylated on the EGF-like domains. 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
(PubMed:25700513). 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). {ECO:0000250,
ECO:0000269|PubMed:25700513}.
-!- PTM: Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination
catalyzed by ITCH. 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 (By similarity).
{ECO:0000250}.
-!- PTM: Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN.
Hydroxylation reduces affinity for HI1AN and may thus indirectly
modulate negative regulation of NICD (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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EMBL; X57405; CAA40667.1; -; mRNA.
EMBL; AABR06021907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06021908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474001; EDL93491.1; -; Genomic_DNA.
PIR; S18188; S18188.
RefSeq; NP_001099191.1; NM_001105721.1.
UniGene; Rn.25046; -.
PDB; 4XL1; X-ray; 2.30 A; A/D=412-526.
PDB; 4XLW; X-ray; 3.39 A; A/C/E/G=412-526.
PDB; 5UK5; X-ray; 2.51 A; A=295-488.
PDBsum; 4XL1; -.
PDBsum; 4XLW; -.
PDBsum; 5UK5; -.
ProteinModelPortal; Q07008; -.
SMR; Q07008; -.
IntAct; Q07008; 3.
STRING; 10116.ENSRNOP00000026212; -.
PhosphoSitePlus; Q07008; -.
PaxDb; Q07008; -.
PRIDE; Q07008; -.
Ensembl; ENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322.
GeneID; 25496; -.
KEGG; rno:25496; -.
UCSC; RGD:3187; rat.
CTD; 4851; -.
RGD; 3187; Notch1.
eggNOG; ENOG410IR7G; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00810000125346; -.
HOGENOM; HOG000234369; -.
HOVERGEN; HBG052650; -.
InParanoid; Q07008; -.
KO; K02599; -.
OMA; QYVNSYT; -.
OrthoDB; EOG091G01NU; -.
TreeFam; TF351641; -.
Reactome; R-RNO-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-RNO-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-RNO-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-RNO-350054; Notch-HLH transcription pathway.
Reactome; R-RNO-8941856; RUNX3 regulates NOTCH signaling.
PRO; PR:Q07008; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000019322; -.
Genevisible; Q07008; RN.
GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
GO; GO:0005112; F:Notch binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0060842; P:arterial endothelial cell differentiation; IEA:Ensembl.
GO; GO:0048708; P:astrocyte differentiation; IDA:RGD.
GO; GO:0003162; P:atrioventricular node development; IEA:Ensembl.
GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0003213; P:cardiac right atrium morphogenesis; IEA:Ensembl.
GO; GO:0003219; P:cardiac right ventricle formation; IEA:Ensembl.
GO; GO:0060948; P:cardiac vascular smooth muscle cell development; IEA:Ensembl.
GO; GO:0021515; P:cell differentiation in spinal cord; IEP:RGD.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0007386; P:compartment pattern specification; IEA:Ensembl.
GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
GO; GO:0003169; P:coronary vein morphogenesis; IEA:Ensembl.
GO; GO:0072017; P:distal tubule development; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0060956; P:endocardial cell differentiation; IEA:Ensembl.
GO; GO:0003160; P:endocardium morphogenesis; IEA:Ensembl.
GO; GO:0007492; P:endoderm development; IEA:Ensembl.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0007440; P:foregut morphogenesis; IEA:Ensembl.
GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
GO; GO:0003241; P:growth involved in heart morphogenesis; IEA:Ensembl.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0014031; P:mesenchymal cell development; IEA:Ensembl.
GO; GO:0003192; P:mitral valve formation; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
GO; GO:0045608; P:negative regulation of auditory receptor cell differentiation; IEA:Ensembl.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISS:UniProtKB.
GO; GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IEA:Ensembl.
GO; GO:2000974; P:negative regulation of pro-B cell differentiation; ISS:UniProtKB.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0061314; P:Notch signaling involved in heart development; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IMP:RGD.
GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
GO; GO:0003344; P:pericardium morphogenesis; IEA:Ensembl.
GO; GO:1903849; P:positive regulation of aorta morphogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:RGD.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0045687; P:positive regulation of glial cell differentiation; IMP:RGD.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
GO; GO:0003184; P:pulmonary valve morphogenesis; IEA:Ensembl.
GO; GO:0003264; P:regulation of cardioblast proliferation; IMP:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IMP:RGD.
GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:1901201; P:regulation of extracellular matrix assembly; IEA:Ensembl.
GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; IEA:Ensembl.
GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IMP:RGD.
GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
GO; GO:0042246; P:tissue regeneration; IEP:RGD.
GO; GO:0035148; P:tube formation; ISS:UniProtKB.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; IEA:Ensembl.
GO; GO:0060843; P:venous endothelial cell differentiation; IEA:Ensembl.
GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR024600; DUF3454_notch.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR008297; Notch.
InterPro; 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; 20.
Pfam; PF07645; EGF_CA; 5.
Pfam; PF12661; hEGF; 4.
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; 32.
SMART; SM00004; NL; 3.
SMART; SM01338; NOD; 1.
SMART; SM01339; NODP; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF90193; SSF90193; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 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; Angiogenesis; ANK repeat; Calcium;
Cell membrane; Complete proteome; Developmental protein;
Differentiation; 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_0000007680.
CHAIN 1711 2531 Notch 1 extracellular truncation.
{ECO:0000250}.
/FTId=PRO_0000007681.
CHAIN 1744 2531 Notch 1 intracellular domain.
{ECO:0000250}.
/FTId=PRO_0000007682.
TOPO_DOM 19 1723 Extracellular. {ECO:0000255}.
TRANSMEM 1724 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. {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:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
REGION 448 452 Interaction with DLL4.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
REGION 1937 1945 HIF1AN-binding. {ECO:0000250}.
REGION 2004 2012 HIF1AN-binding. {ECO:0000250}.
COMPBIAS 1730 1733 Poly-Ala.
COMPBIAS 1891 1894 Poly-Glu.
COMPBIAS 2258 2261 Poly-Pro.
COMPBIAS 2497 2500 Poly-Ser.
METAL 432 432 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 435 435 Calcium 1; via amide nitrogen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 452 452 Calcium 2. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 453 453 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 455 455 Calcium 2. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 469 469 Calcium 2. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 470 470 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 490 490 Calcium 3. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 491 491 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 493 493 Calcium 3. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 507 507 Calcium 3. {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
METAL 508 508 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
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:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
SITE 1654 1655 Cleavage; by furin-like protease.
{ECO:0000250}.
SITE 1710 1711 Cleavage; by ADAM17. {ECO:0000250}.
MOD_RES 1851 1851 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01705}.
MOD_RES 1945 1945 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 2012 2012 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 73 73 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 116 116 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 146 146 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 194 194 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 232 232 O-linked (Fuc...) threonine; alternate.
{ECO:0000250}.
CARBOHYD 232 232 O-linked (GalNAc...) threonine;
alternate. {ECO:0000250}.
CARBOHYD 341 341 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 378 378 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 435 435 O-linked (Glc...) serine.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
CARBOHYD 458 458 O-linked (Glc...) serine.
{ECO:0000269|PubMed:25700513}.
CARBOHYD 466 466 O-linked (Fuc...) threonine.
{ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
CARBOHYD 496 496 O-linked (Glc...) serine.
{ECO:0000269|PubMed:25700513}.
CARBOHYD 534 534 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 609 609 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 647 647 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 722 722 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 759 759 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 767 767 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 797 797 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 805 805 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 888 888 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 951 951 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 959 959 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1027 1027 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1035 1035 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1065 1065 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1179 1179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1189 1189 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1197 1197 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1241 1241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1273 1273 O-linked (Glc...) serine. {ECO:0000250}.
CARBOHYD 1362 1362 O-linked (Fuc...) threonine.
{ECO:0000250}.
CARBOHYD 1402 1402 O-linked (Fuc...) threonine; alternate.
{ECO:0000250}.
CARBOHYD 1402 1402 O-linked (GalNAc...) threonine;
alternate. {ECO:0000250}.
CARBOHYD 1489 1489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1587 1587 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1715 1715 O-linked (GalNAc...) threonine.
{ECO:0000250}.
DISULFID 24 37 {ECO:0000250}.
DISULFID 31 46 {ECO:0000250}.
DISULFID 48 57 {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:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 423 438 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 440 449 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 456 467 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 461 476 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 478 487 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 494 505 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 499 514 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
DISULFID 516 525 {ECO:0000244|PDB:4XL1,
ECO:0000269|PubMed:25700513}.
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:0000250|UniProtKB:Q01705}.
CONFLICT 309 309 G -> A (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 334 334 E -> D (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 402 402 S -> R (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 577 577 Y -> I (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 951 951 S -> T (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 1339 1339 G -> R (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 1435 1435 G -> A (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 1595 1596 EL -> DV (in Ref. 1; CAA40667).
{ECO:0000305}.
CONFLICT 2501 2501 P -> R (in Ref. 1; CAA40667).
{ECO:0000305}.
HELIX 415 418 {ECO:0000244|PDB:4XL1}.
TURN 424 426 {ECO:0000244|PDB:4XL1}.
STRAND 428 432 {ECO:0000244|PDB:4XL1}.
STRAND 435 439 {ECO:0000244|PDB:4XL1}.
STRAND 444 446 {ECO:0000244|PDB:4XL1}.
TURN 455 458 {ECO:0000244|PDB:4XL1}.
STRAND 466 470 {ECO:0000244|PDB:4XL1}.
STRAND 473 477 {ECO:0000244|PDB:4XL1}.
STRAND 482 484 {ECO:0000244|PDB:4XL1}.
TURN 493 496 {ECO:0000244|PDB:4XL1}.
STRAND 504 507 {ECO:0000244|PDB:4XL1}.
STRAND 512 515 {ECO:0000244|PDB:4XL1}.
TURN 522 525 {ECO:0000244|PDB:4XL1}.
SEQUENCE 2531 AA; 270822 MW; 3E61AE863AA237F2 CRC64;
MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDP
SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT PLANACLANP CRNGGTCDLL
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICGCPPGF HGPTCRQDVN
ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT
HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC HDRVASFYCE
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECALGA
NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP
GYEGVYCEIN TDECASSPCL HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID
GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC
NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN
SGVCKESEDY ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA SNPCQNGANC
TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY
DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ
YHCECRSGWT GFNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS
YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV
GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCRNGG
VCAVASNTAR GFICRCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG
PECQFPASSP CVGSNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI
PPPQIEEACE LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD
CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL HTNVVFKRDA QGQQMIFPYY
GREEELRKHP IKRSAVGWAT TSLLPGTNGG RQRRELDPMD IHGSIVYLEI DNRQCVQSSS
QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP 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 PSTKGLACSS
KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP
LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG
TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI
HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP
SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS PHSNISDWSE GISSPPTSMP
SQITHIPEAF K


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