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Q01705 (NOTC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic locus notch homolog protein 1
Short name=Notch 1
Alternative name(s):
Motch A
mT14
p300

Cleaved into the following 2 chains:

  1. Notch 1 extracellular truncation
  2. Notch 1 intracellular domain
    Short name=NICD
Gene names
Name:Notch1
Synonyms:Motch
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length2531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. 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 enhance HIF1A function by sequestering HIF1AN away from HIF1A. Ref.15 Ref.22

Subunit structure

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 By similarity. 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 By similarity. Ref.15 Ref.19 Ref.20 Ref.22 Ref.24

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Notch 1 intracellular domain: Nucleus. Note: Following proteolytical processing NICD is translocated to the nucleus.

Tissue specificity

Highly expressed in the brain, lung and thymus. Expressed at lower levels in the spleen, bone-marrow, spinal cord, eyes, mammary gland, liver, intestine, skeletal muscle, kidney and heart. In the hair follicle, highly expressed exclusively in the epithelial compartment. Ref.22

Developmental stage

First detected in the mesoderm at 7.5 dpc By 8.5 dpc highly expressed in presomitic mesoderm, mesenchyme and endothelial cells, while much lower levels are seen in the neuroepithelium. Between 9.5-10.5 dpc expressed at high levels in the neuroepithelium. At 13.5 dpc expressed in the surface ectoderm, eye and developing whisker follicles. Hair follicle matrix cells expression starts as different cell types become distinguishable in the developing follicle. Expression persists throughout the growth phase of the follicle and maintains the same expression profile in the second hair cycle. The cells in the follicle that undergo a phase of high level expression are in transition from mitotic precursors to several discrete, differentiating cell types. Specifically expressed in cerebellar Bergmann glial cells during postnatal development. Ref.8 Ref.11 Ref.14

Post-translational modification

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). 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. Ref.12 Ref.17 Ref.18

Phosphorylated.

O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose By similarity.

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. Ref.21 Ref.23

Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD.

Sequence similarities

Belongs to the NOTCH family.

Contains 5 ANK repeats.

Contains 36 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Ontologies

Keywords
   Biological processDifferentiation
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentCell membrane
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionActivator
Developmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway involved in regulation of secondary heart field cardioblast proliferation

Inferred from mutant phenotype PubMed 19620969. Source: MGI

anagen

Inferred from mutant phenotype PubMed 15978571. Source: MGI

aortic valve morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

arterial endothelial cell differentiation

Inferred from mutant phenotype PubMed 15107403. Source: BHF-UCL

atrioventricular node development

Inferred from mutant phenotype PubMed 21266778. Source: BHF-UCL

atrioventricular valve morphogenesis

Inferred from mutant phenotype PubMed 14701881PubMed 21266778. Source: BHF-UCL

auditory receptor cell fate commitment

Inferred from mutant phenotype PubMed 19154718. Source: MGI

axonogenesis

Inferred from direct assay PubMed 15598981. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from mutant phenotype PubMed 15064243. Source: MGI

cardiac left ventricle morphogenesis

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

cardiac right atrium morphogenesis

Inferred from mutant phenotype PubMed 20007915. Source: BHF-UCL

cardiac right ventricle formation

Inferred from mutant phenotype PubMed 19620969. Source: MGI

cardiac septum morphogenesis

Inferred from mutant phenotype PubMed 20007915. Source: BHF-UCL

cardiac vascular smooth muscle cell development

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

cell fate specification

Inferred from mutant phenotype PubMed 15068794. Source: MGI

cell migration involved in endocardial cushion formation

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Compara

collecting duct development

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

compartment pattern specification

Inferred from mutant phenotype PubMed 12001066. Source: MGI

coronary artery morphogenesis

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

coronary vein morphogenesis

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

distal tubule development

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

embryonic hindlimb morphogenesis

Inferred from mutant phenotype PubMed 16245338. Source: MGI

endocardial cell differentiation

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

endocardium morphogenesis

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

endoderm development

Inferred from mutant phenotype PubMed 14657333. Source: MGI

epithelial to mesenchymal transition involved in endocardial cushion formation

Inferred from mutant phenotype PubMed 14701881. Source: BHF-UCL

forebrain development

Inferred from mutant phenotype PubMed 16120638. Source: MGI

foregut morphogenesis

Inferred from mutant phenotype PubMed 16107537. Source: MGI

glial cell differentiation

Inferred from mutant phenotype Ref.22. Source: MGI

glomerular mesangial cell development

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

growth involved in heart morphogenesis

Inferred from mutant phenotype PubMed 20007915. Source: BHF-UCL

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 15525534PubMed 15978571. Source: MGI

heart looping

Inferred from genetic interaction PubMed 12730124. Source: BHF-UCL

humoral immune response

Inferred from genetic interaction PubMed 17658279. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 7789282. Source: MGI

inflammatory response to antigenic stimulus

Inferred from genetic interaction PubMed 17658279. Source: MGI

interleukin-4 secretion

Inferred from genetic interaction PubMed 17658279. Source: MGI

keratinocyte differentiation

Inferred from mutant phenotype PubMed 15068794. Source: MGI

left/right axis specification

Inferred from genetic interaction PubMed 12730124. Source: BHF-UCL

liver development

Inferred from mutant phenotype PubMed 15226394. Source: MGI

lung development

Inferred from mutant phenotype PubMed 15064243. Source: MGI

mitral valve formation

Inferred from electronic annotation. Source: Compara

negative regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 19695258. Source: BHF-UCL

negative regulation of anoikis

Inferred from electronic annotation. Source: Compara

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16245338. Source: MGI

negative regulation of calcium ion-dependent exocytosis

Inferred from mutant phenotype PubMed 19251639. Source: MGI

negative regulation of canonical Wnt receptor signaling pathway

Inferred from mutant phenotype PubMed 19620969. Source: MGI

negative regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Compara

negative regulation of glial cell proliferation

Inferred from direct assay PubMed 12666205. Source: UniProtKB

negative regulation of myoblast differentiation

Inferred from electronic annotation. Source: Compara

negative regulation of myotube differentiation

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of oligodendrocyte differentiation

Inferred from direct assay PubMed 12666205. Source: UniProtKB

negative regulation of ossification

Inferred from mutant phenotype PubMed 21493891. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 19695258. Source: BHF-UCL

negative regulation of photoreceptor cell differentiation

Inferred from mutant phenotype PubMed 16452096. Source: MGI

negative regulation of pro-B cell differentiation

Inferred from mutant phenotype PubMed 12032823. Source: UniProtKB

negative regulation of stem cell differentiation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12032823. Source: UniProtKB

neural tube development

Inferred from mutant phenotype PubMed 7789282. Source: MGI

neuronal stem cell maintenance

Inferred from electronic annotation. Source: Compara

osteoblast fate commitment

Non-traceable author statement PubMed 16025100. Source: BHF-UCL

pericardium morphogenesis

Inferred from mutant phenotype PubMed 14701881PubMed 20890042PubMed 21311046. Source: BHF-UCL

positive regulation of BMP signaling pathway

Inferred from direct assay PubMed 20547764. Source: UniProtKB

positive regulation of JAK-STAT cascade

Inferred from direct assay PubMed 15156153. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 15081359. Source: MGI

positive regulation of astrocyte differentiation

Inferred from direct assay PubMed 12666205. Source: UniProtKB

positive regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 20007915. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

positive regulation of ephrin receptor signaling pathway

Inferred by curator PubMed 17336907. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from genetic interaction PubMed 19251639. Source: MGI

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

positive regulation of keratinocyte differentiation

Inferred from direct assay PubMed 17079689. Source: MGI

positive regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of transcription of Notch receptor target

Inferred from genetic interaction PubMed 12794108. Source: MGI

prostate gland epithelium morphogenesis

Inferred from mutant phenotype PubMed 16360140. Source: MGI

pulmonary valve morphogenesis

Inferred from electronic annotation. Source: Compara

regulation of cell adhesion involved in heart morphogenesis

Inferred by curator PubMed 14701881. Source: BHF-UCL

regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 16360140. Source: MGI

regulation of extracellular matrix assembly

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

regulation of somitogenesis

Inferred from mutant phenotype PubMed 7789282. Source: MGI

regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation

Inferred from mutant phenotype PubMed 20007915. Source: BHF-UCL

response to muramyl dipeptide

Inferred from direct assay PubMed 21156799. Source: BHF-UCL

secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development

Inferred from mutant phenotype PubMed 16360140. Source: MGI

skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 22147266. Source: MGI

somatic stem cell division

Inferred from direct assay PubMed 12717450. Source: MGI

sprouting angiogenesis

Inferred from mutant phenotype PubMed 15809373. Source: MGI

vasculogenesis involved in coronary vascular morphogenesis

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

venous endothelial cell differentiation

Inferred from mutant phenotype PubMed 20890042. Source: BHF-UCL

ventricular septum morphogenesis

Inferred from electronic annotation. Source: Compara

ventricular trabecula myocardium morphogenesis

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

MAML1-RBP-Jkappa- ICN1 complex

Inferred from electronic annotation. Source: Compara

cell surface

Inferred from direct assay PubMed 15574878. Source: MGI

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

integral to plasma membrane

Inferred by curator PubMed 10551863. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 17336907. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

chromatin DNA binding

Inferred from direct assay PubMed 17658278. Source: MGI

core promoter binding

Inferred from direct assay PubMed 20547764. Source: UniProtKB

enzyme inhibitor activity

Inferred from direct assay Ref.26. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from direct assay PubMed 17658278. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17658278PubMed 9111338. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RbpjP312665EBI-1392707,EBI-1392666
Su(H)P281592EBI-1392707,EBI-92180From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01705-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q01705-2)

The sequence of this isoform differs from the canonical sequence as follows:
     857-914: Missing.
     1329-1355: Missing.
     1636-1854: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q01705-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MPRLLTPLLCLTLLPALAARG → MKNSNTLTNKWRMEQC
Note: No experimental confirmation available.
Isoform 4 (identifier: Q01705-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MPRLLTPLLC...EVANGTEACV → MQTPLLSLAGATTELCFLPASVLASSLPGPSL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 25312513Neurogenic locus notch homolog protein 1
PRO_0000007677
Chain1711 – 2531821Notch 1 extracellular truncation
PRO_0000007678
Chain1744 – 2531788Notch 1 intracellular domain
PRO_0000007679

Regions

Topological domain19 – 17251707Extracellular Potential
Transmembrane1726 – 174621Helical; Potential
Topological domain1747 – 2531785Cytoplasmic Potential
Domain20 – 5839EGF-like 1
Domain59 – 9941EGF-like 2
Domain102 – 13938EGF-like 3
Domain140 – 17637EGF-like 4
Domain178 – 21639EGF-like 5; calcium-binding Potential
Domain218 – 25538EGF-like 6
Domain257 – 29337EGF-like 7; calcium-binding Potential
Domain295 – 33339EGF-like 8; calcium-binding Potential
Domain335 – 37137EGF-like 9; calcium-binding Potential
Domain372 – 41039EGF-like 10; calcium-binding Potential
Domain412 – 45039EGF-like 11; calcium-binding Potential
Domain452 – 48837EGF-like 12; calcium-binding Potential
Domain490 – 52637EGF-like 13; calcium-binding Potential
Domain528 – 56437EGF-like 14; calcium-binding Potential
Domain566 – 60136EGF-like 15; calcium-binding Potential
Domain603 – 63937EGF-like 16; calcium-binding Potential
Domain641 – 67636EGF-like 17; calcium-binding Potential
Domain678 – 71437EGF-like 18; calcium-binding Potential
Domain716 – 75136EGF-like 19; calcium-binding Potential
Domain753 – 78937EGF-like 20; calcium-binding Potential
Domain791 – 82737EGF-like 21; calcium-binding Potential
Domain829 – 86739EGF-like 22
Domain869 – 90537EGF-like 23; calcium-binding Potential
Domain907 – 94337EGF-like 24
Domain945 – 98137EGF-like 25; calcium-binding Potential
Domain983 – 101937EGF-like 26
Domain1021 – 105737EGF-like 27; calcium-binding Potential
Domain1059 – 109537EGF-like 28
Domain1097 – 114347EGF-like 29
Domain1145 – 118137EGF-like 30; calcium-binding Potential
Domain1183 – 121937EGF-like 31; calcium-binding Potential
Domain1221 – 126545EGF-like 32; calcium-binding Potential
Domain1267 – 130539EGF-like 33
Domain1307 – 134640EGF-like 34
Domain1348 – 138437EGF-like 35
Domain1387 – 142640EGF-like 36
Repeat1449 – 148941LNR 1
Repeat1490 – 153142LNR 2
Repeat1532 – 157140LNR 3
Repeat1917 – 194630ANK 1
Repeat1950 – 198031ANK 2
Repeat1984 – 201330ANK 3
Repeat2017 – 204630ANK 4
Repeat2050 – 207930ANK 5
Region1937 – 19459HIF1AN-binding
Region2004 – 20129HIF1AN-binding

Sites

Metal binding14571Calcium; via carbonyl oxygen By similarity
Metal binding14601Calcium By similarity
Metal binding14751Calcium By similarity
Metal binding14781Calcium By similarity
Site1654 – 16552Cleavage; by furin-like protease

Amino acid modifications

Modified residue19451(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.15 Ref.26
Modified residue20121(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.15 Ref.26
Glycosylation8881N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation11791N-linked (GlcNAc...) Potential
Glycosylation12411N-linked (GlcNAc...) Potential
Glycosylation14891N-linked (GlcNAc...) Potential
Glycosylation15871N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 37 By similarity
Disulfide bond31 ↔ 46 By similarity
Disulfide bond63 ↔ 74 By similarity
Disulfide bond68 ↔ 87 By similarity
Disulfide bond89 ↔ 98 By similarity
Disulfide bond106 ↔ 117 By similarity
Disulfide bond111 ↔ 127 By similarity
Disulfide bond129 ↔ 138 By similarity
Disulfide bond144 ↔ 155 By similarity
Disulfide bond149 ↔ 164 By similarity
Disulfide bond166 ↔ 175 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond189 ↔ 204 By similarity
Disulfide bond206 ↔ 215 By similarity
Disulfide bond222 ↔ 233 By similarity
Disulfide bond227 ↔ 243 By similarity
Disulfide bond245 ↔ 254 By similarity
Disulfide bond261 ↔ 272 By similarity
Disulfide bond266 ↔ 281 By similarity
Disulfide bond283 ↔ 292 By similarity
Disulfide bond299 ↔ 312 By similarity
Disulfide bond306 ↔ 321 By similarity
Disulfide bond323 ↔ 332 By similarity
Disulfide bond339 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond361 ↔ 370 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 398 By similarity
Disulfide bond400 ↔ 409 By similarity
Disulfide bond416 ↔ 429 By similarity
Disulfide bond423 ↔ 438 By similarity
Disulfide bond440 ↔ 449 By similarity
Disulfide bond456 ↔ 467 By similarity
Disulfide bond461 ↔ 476 By similarity
Disulfide bond478 ↔ 487 By similarity
Disulfide bond494 ↔ 505 By similarity
Disulfide bond499 ↔ 514 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond532 ↔ 543 By similarity
Disulfide bond537 ↔ 552 By similarity
Disulfide bond554 ↔ 563 By similarity
Disulfide bond570 ↔ 580 By similarity
Disulfide bond575 ↔ 589 By similarity
Disulfide bond591 ↔ 600 By similarity
Disulfide bond607 ↔ 618 By similarity
Disulfide bond612 ↔ 627 By similarity
Disulfide bond629 ↔ 638 By similarity
Disulfide bond645 ↔ 655 By similarity
Disulfide bond650 ↔ 664 By similarity
Disulfide bond666 ↔ 675 By similarity
Disulfide bond682 ↔ 693 By similarity
Disulfide bond687 ↔ 702 By similarity
Disulfide bond704 ↔ 713 By similarity
Disulfide bond720 ↔ 730 By similarity
Disulfide bond725 ↔ 739 By similarity
Disulfide bond741 ↔ 750 By similarity
Disulfide bond757 ↔ 768 By similarity
Disulfide bond762 ↔ 777 By similarity
Disulfide bond779 ↔ 788 By similarity
Disulfide bond795 ↔ 806 By similarity
Disulfide bond800 ↔ 815 By similarity
Disulfide bond817 ↔ 826 By similarity
Disulfide bond833 ↔ 844 By similarity
Disulfide bond838 ↔ 855 By similarity
Disulfide bond857 ↔ 866 By similarity
Disulfide bond873 ↔ 884 By similarity
Disulfide bond878 ↔ 893 By similarity
Disulfide bond895 ↔ 904 By similarity
Disulfide bond911 ↔ 922 By similarity
Disulfide bond916 ↔ 931 By similarity
Disulfide bond933 ↔ 942 By similarity
Disulfide bond949 ↔ 960 By similarity
Disulfide bond954 ↔ 969 By similarity
Disulfide bond971 ↔ 980 By similarity
Disulfide bond987 ↔ 998 By similarity
Disulfide bond992 ↔ 1007 By similarity
Disulfide bond1009 ↔ 1018 By similarity
Disulfide bond1025 ↔ 1036 By similarity
Disulfide bond1030 ↔ 1045 By similarity
Disulfide bond1047 ↔ 1056 By similarity
Disulfide bond1063 ↔ 1074 By similarity
Disulfide bond1068 ↔ 1083 By similarity
Disulfide bond1085 ↔ 1094 By similarity
Disulfide bond1101 ↔ 1122 By similarity
Disulfide bond1116 ↔ 1131 By similarity
Disulfide bond1133 ↔ 1142 By similarity
Disulfide bond1149 ↔ 1160 By similarity
Disulfide bond1154 ↔ 1169 By similarity
Disulfide bond1171 ↔ 1180 By similarity
Disulfide bond1187 ↔ 1198 By similarity
Disulfide bond1192 ↔ 1207 By similarity
Disulfide bond1209 ↔ 1218 By similarity
Disulfide bond1225 ↔ 1244 By similarity
Disulfide bond1238 ↔ 1253 By similarity
Disulfide bond1255 ↔ 1264 By similarity
Disulfide bond1271 ↔ 1284 By similarity
Disulfide bond1276 ↔ 1293 By similarity
Disulfide bond1295 ↔ 1304 By similarity
Disulfide bond1311 ↔ 1322 By similarity
Disulfide bond1316 ↔ 1334 By similarity
Disulfide bond1336 ↔ 1345 By similarity
Disulfide bond1352 ↔ 1363 By similarity
Disulfide bond1357 ↔ 1372 By similarity
Disulfide bond1374 ↔ 1383 By similarity
Disulfide bond1391 ↔ 1403 By similarity
Disulfide bond1397 ↔ 1414 By similarity
Disulfide bond1416 ↔ 1425 By similarity
Disulfide bond1449 ↔ 1472 By similarity
Disulfide bond1454 ↔ 1467 By similarity
Disulfide bond1463 ↔ 1479 By similarity
Disulfide bond1490 ↔ 1514 By similarity
Disulfide bond1496 ↔ 1509 By similarity
Disulfide bond1505 ↔ 1521 By similarity
Disulfide bond1536 ↔ 1549 By similarity
Disulfide bond1545 ↔ 1561 By similarity
Cross-link1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Natural variations

Alternative sequence1 – 4747MPRLL…TEACV → MQTPLLSLAGATTELCFLPA SVLASSLPGPSL in isoform 4.
VSP_043065
Alternative sequence1 – 2121MPRLL…LAARG → MKNSNTLTNKWRMEQC in isoform 3.
VSP_043064
Alternative sequence857 – 91458Missing in isoform 2.
VSP_001402
Alternative sequence1329 – 135527Missing in isoform 2.
VSP_001403
Alternative sequence1636 – 1854219Missing in isoform 2.
VSP_001404

Experimental info

Mutagenesis1651 – 16544RQRR → AAAA: Processing by furin-like convertase abolished. Ref.12
Mutagenesis17441V → L: NICD processing severely reduced.
Mutagenesis19451N → A: Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and greatly reduced transactivation capacity. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with G-2012. Almost abolished transactivation capacity; when associated with A-2012. Ref.15 Ref.26
Mutagenesis20121N → A: Slightly reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and almost abolished transactivation capacity; when associated with A-1945. Ref.15 Ref.26
Mutagenesis20121N → G: Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with A-1945. Ref.15 Ref.26
Sequence conflict171L → R in CAA77941. Ref.1
Sequence conflict411N → S in CAA77941. Ref.1
Sequence conflict411N → S in AAM28905. Ref.3
Sequence conflict481C → A in CAA77941. Ref.1
Sequence conflict511A → S in CAA77941. Ref.1
Sequence conflict601S → P in CAA77941. Ref.1
Sequence conflict671P → R in CAA77941. Ref.1
Sequence conflict751H → Y in CAA77941. Ref.1
Sequence conflict821T → I in CAA77941. Ref.1
Sequence conflict104 – 1052NA → KP in CAA77941. Ref.1
Sequence conflict1301P → S in CAA77941. Ref.1
Sequence conflict1941T → H in CAA77941. Ref.1
Sequence conflict2071R → C in CAA77941. Ref.1
Sequence conflict2311G → A in CAA77941. Ref.1
Sequence conflict2871W → V in CAA77941. Ref.1
Sequence conflict3091G → A in CAA77941. Ref.1
Sequence conflict373 – 3742ND → KH in CAA77941. Ref.1
Sequence conflict3961A → R in CAA77941. Ref.1
Sequence conflict4171A → D in CAA77941. Ref.1
Sequence conflict4221P → R in CAA77941. Ref.1
Sequence conflict4481R → G in CAA77941. Ref.1
Sequence conflict5101N → H in CAA77941. Ref.1
Sequence conflict8351T → I in AAK14898. Ref.8
Sequence conflict933 – 9342CL → SV in AAK14898. Ref.8
Sequence conflict10501G → R in AAK14898. Ref.8
Sequence conflict1104 – 11063Missing in AAK14898. Ref.8
Sequence conflict11551Q → L in AAK14898. Ref.8
Sequence conflict12091C → W in AAK14898. Ref.8
Sequence conflict14381R → P in CAA77941. Ref.1
Sequence conflict15451C → S in AAK14898. Ref.8
Sequence conflict15561W → R in AAK14898. Ref.8
Sequence conflict15721G → R in AAK14898. Ref.8
Sequence conflict15761L → V in AAK14898. Ref.8
Sequence conflict16091D → H in AAK14898. Ref.8
Sequence conflict16611I → T in BAE32653. Ref.10
Sequence conflict18641V → D in AAK14898. Ref.8
Sequence conflict18901S → R in AAK14898. Ref.8
Sequence conflict1896 – 18983APA → RPG in AAK14898. Ref.8
Sequence conflict1933 – 19342AA → RR in CAA77941. Ref.1
Sequence conflict19381Missing in CAA77941. Ref.1
Sequence conflict19971V → L in AAM28905. Ref.3
Sequence conflict2046 – 20472MQ → IE in CAA77941. Ref.1
Sequence conflict20541P → S in CAA77941. Ref.1
Sequence conflict2058 – 20625AAREG → SIRRE in CAA77941. Ref.1
Sequence conflict20751A → G in CAA57909. Ref.16
Sequence conflict20861L → M in BAE34095. Ref.10
Sequence conflict21361L → P in CAA77941. Ref.1
Sequence conflict21721K → S in CAA77941. Ref.1
Sequence conflict21791C → W in CAA77941. Ref.1
Sequence conflict21851S → SS in CAA77941. Ref.1
Sequence conflict22061P → H in CAA77941. Ref.1
Sequence conflict22581P → H in CAA77941. Ref.1
Sequence conflict22731S → C in CAA77941. Ref.1
Sequence conflict23471N → S in BAE34095. Ref.10
Sequence conflict23801Q → P in CAA77941. Ref.1
Sequence conflict2483 – 24842HP → PT in CAA77941. Ref.1

Secondary structure

1 ..................................... 2531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 18, 2012. Version 3.
Checksum: 97C91F69BABF02BF

FASTA2,531270,835
        10         20         30         40         50         60 
MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDS 

        70         80         90        100        110        120 
NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT PLDNACLANP CRNGGTCDLL 

       130        140        150        160        170        180 
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICRCPPGF HGPTCRQDVN 

       190        200        210        220        230        240 
ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT 

       250        260        270        280        290        300 
HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 

       310        320        330        340        350        360 
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC HDRVASFYCE 

       370        380        390        400        410        420 
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECALGA 

       430        440        450        460        470        480 
NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP 

       490        500        510        520        530        540 
GYEGVYCEIN TDECASSPCL HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG 

       550        560        570        580        590        600 
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC 

       610        620        630        640        650        660 
ETNINECHSQ PCRHGGTCQD RDNSYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID 

       670        680        690        700        710        720 
GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC 

       730        740        750        760        770        780 
NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR 

       790        800        810        820        830        840 
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN 

       850        860        870        880        890        900 
SGVCKESEDY ESFSCVCPTG WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 

       910        920        930        940        950        960 
GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA SNPCQNGANC 

       970        980        990       1000       1010       1020 
TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY 

      1030       1040       1050       1060       1070       1080 
DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ 

      1090       1100       1110       1120       1130       1140 
YHCECRSGWT GVNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS 

      1150       1160       1170       1180       1190       1200 
YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 

      1210       1220       1230       1240       1250       1260 
LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV 

      1270       1280       1290       1300       1310       1320 
GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCKNGG 

      1330       1340       1350       1360       1370       1380 
VCAVASNTAR GFICRCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG 

      1390       1400       1410       1420       1430       1440 
PECQFPASSP CVGSNPCYNQ GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI 

      1450       1460       1470       1480       1490       1500 
PPPQIEEACE LPECQVDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 

      1510       1520       1530       1540       1550       1560 
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD 

      1570       1580       1590       1600       1610       1620 
CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL HTNVVFKRDA QGQQMIFPYY 

      1630       1640       1650       1660       1670       1680 
GHEEELRKHP IKRSTVGWAT SSLLPGTSGG RQRRELDPMD IRGSIVYLEI DNRQCVQSSS 

      1690       1700       1710       1720       1730       1740 
QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSEPVEPPL PSQLHLMYVA AAAFVLLFFV 

      1750       1760       1770       1780       1790       1800 
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 

      1810       1820       1830       1840       1850       1860 
NEWGDEDLET KKFRFEEPVV LPDLSDQTDH RQWTQQHLDA ADLRMSAMAP TPPQGEVDAD 

      1870       1880       1890       1900       1910       1920 
CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL HNQTDRTGET 

      1930       1940       1950       1960       1970       1980 
ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL LRNRATDLDA 

      1990       2000       2010       2020       2030       2040 
RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN 

      2050       2060       2070       2080       2090       2100 
GANKDMQNNK EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 

      2110       2120       2130       2140       2150       2160 
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK PSTKGLACGS 

      2170       2180       2190       2200       2210       2220 
KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP 

      2230       2240       2250       2260       2270       2280 
LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG 

      2290       2300       2310       2320       2330       2340 
TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHSMMGPL 

      2350       2360       2370       2380       2390       2400 
HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ LQPQNLQPPS QPHLSVSSAA 

      2410       2420       2430       2440       2450       2460 
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP 

      2470       2480       2490       2500       2510       2520 
SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS PHSNISDWSE GISSPPTTMP 

      2530 
SQITHIPEAF K

« Hide

Isoform 2 [UniParc].

Checksum: E36CEB947C4464C4
Show »

FASTA2,227237,414
Isoform 3 [UniParc].

Checksum: 017563FCE9703264
Show »

FASTA2,526270,585
Isoform 4 [UniParc].

Checksum: 17FD72740EBD6E35
Show »

FASTA2,516269,180

References

« Hide 'large scale' references
[1]"Cloning, analysis, and chromosomal localization of Notch-1, a mouse homolog of Drosophila Notch."
Franco del Amo F., Gendron-Maguire M., Swiatek P.J., Jenkins N.A., Copeland N.G., Gridley T.
Genomics 15:259-264(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[2]"An activated Notch suppresses neurogenesis and myogenesis but not gliogenesis in mammalian cells."
Nye J.S., Kopan R., Axel R.
Development 120:2421-2430(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Thymus.
[3]"Glycogen synthase kinase-3beta modulates notch signaling and stability."
Foltz D.R., Santiago M.C., Berechid B.E., Nye J.S.
Curr. Biol. 12:1006-1011(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Thymus.
[4]"Radiation-induced deletions in the 5' end region of Notch1 lead to the formation of truncated proteins and are involved in the development of mouse thymic lymphomas."
Tsuji H., Ishii-Ohba H., Ukai H., Katsube T., Ogiu T.
Carcinogenesis 24:1257-1268(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CB-17/SCID.
Tissue: Thymus.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]"Expression analysis of a Notch homologue in the mouse embryo."
Reaume A.G., Conlon R.A., Zirngibl R., Yamaguchi T.P., Rossant J.
Dev. Biol. 154:377-387(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 731-1899 (ISOFORM 2), DEVELOPMENTAL STAGE.
Strain: CD-1.
Tissue: Embryo.
[9]"Motch A and Motch B-two mouse Notch homologues coexpressed in a wide variety of tissues."
Lardelli M., Lendahl U.
Exp. Cell Res. 204:364-372(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1547.
Strain: C57BL/6 X CBA.
Tissue: Embryo.
[10]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1373-2531.
Strain: NOD.
[11]"Expression pattern of Motch, a mouse homolog of Drosophila Notch, suggests an important role in early postimplantation mouse development."
Franco del Amo F., Smith D.E., Swiatek P.J., Gendron-Maguire M., Greenspan R.J., McMahon A.P., Gridley T.
Development 115:737-744(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1551-1647 (ISOFORM 1), DEVELOPMENTAL STAGE.
Tissue: Embryo.
[12]"The Notch1 receptor is cleaved constitutively by a furin-like convertase."
Logeat F., Bessia C., Brou C., LeBail O., Jarriault S., Seidah N.G., Israel A.
Proc. Natl. Acad. Sci. U.S.A. 95:8108-8112(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1655-1659, CLEAVAGE BY FURIN-LIKE CONVERTASE, MUTAGENESIS OF 1651-ARG--ARG-1654.
[13]"Murine leukemia provirus-mediated activation of the Notch1 gene leads to induction of HES-1 in a mouse T lymphoma cell line, DL-3."
Lee J.S., Ishimoto A., Yanagawa S.
FEBS Lett. 455:276-280(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1659-1673.
[14]"Mouse notch: expression in hair follicles correlates with cell fate determination."
Kopan R., Weintraub H.
J. Cell Biol. 121:631-641(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1865-2076, DEVELOPMENTAL STAGE IN HAIR FOLLICLES.
[15]"Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways."
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.
Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1937-1952 AND 1995-2019, FUNCTION, INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-1945 AND ASN-2012 BY HIF1AN, MUTAGENESIS OF ASN-1945 AND ASN-2012, MASS SPECTROMETRY.
[16]"Dynamic changes in gene expression during in vitro differentiation of mouse embryonic stem cells."
Messerle M., Follo M., Nehls M., Eggert H., Boehm T.
Cytokines Cell. Mol. Ther. 1:139-143(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1951-2201.
[17]"Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis."
Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R.
J. Biol. Chem. 276:40268-40273(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING.
[18]"Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members."
Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T.
Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[19]"Murine homologs of deltex define a novel gene family involved in vertebrate Notch signaling and neurogenesis."
Kishi N., Tang Z., Maeda Y., Hirai A., Mo R., Ito M., Suzuki S., Nakao K., Kinoshita T., Kadesch T., Hui C.-C., Artavanis-Tsakonas S., Okano H., Matsuno K.
Int. J. Dev. Neurosci. 19:21-35(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DTX1 AND DTX2.
[20]"Cloning and functional characterization of the murine mastermind-like 1 (Maml1) gene."
Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E., Mukhopadhyay N.K., Griffin J.D.
Gene 328:153-165(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAML1.
[21]"Monoubiquitination and endocytosis direct gamma-secretase cleavage of activated Notch receptor."
Gupta-Rossi N., Six E., LeBail O., Logeat F., Chastagner P., Olry A., Israel A., Brou C.
J. Cell Biol. 166:73-83(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-1749, ENDOCYTOSIS.
[22]"DNER acts as a neuron-specific Notch ligand during Bergmann glial development."
Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T., Kengaku M.
Nat. Neurosci. 8:873-880(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNER, FUNCTION, TISSUE SPECIFICITY.
[23]"AIP4/Itch regulates Notch receptor degradation in the absence of ligand."
Chastagner P., Israel A., Brou C.
PLoS ONE 3:E2735-E2735(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY ITCH.
[24]"The adaptor-associated kinase 1, AAK1, is a positive regulator of the Notch pathway."
Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J., Olivo-Marin J.C., Israel A.
J. Biol. Chem. 286:18720-18730(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AAK1.
[25]"The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold."
Lubman O.Y., Kopan R., Waksman G., Korolev S.
Protein Sci. 14:1274-1281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1971-2104.
[26]"Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor."
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.
J. Biol. Chem. 282:24027-24038(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1899-2106 IN COMPLEX WITH HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT ASN-1945 AND ASN-2012, MUTAGENESIS OF ASN-1945 AND ASN-2012, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z11886 mRNA. Translation: CAA77941.1.
AF508809 mRNA. Translation: AAM28905.1.
AB100603 Genomic DNA. Translation: BAC77038.1.
AB100603 Genomic DNA. Translation: BAC77039.1.
AB100603 Genomic DNA. Translation: BAC77040.1.
AL732541 Genomic DNA. Translation: CAM20304.1.
CH466542 Genomic DNA. Translation: EDL08321.1.
BC138441 mRNA. Translation: AAI38442.1.
BC138442 mRNA. Translation: AAI38443.1.
L02613 mRNA. Translation: AAK14898.1.
X68278 mRNA. Translation: CAA48339.1.
AK154528 mRNA. Translation: BAE32653.1.
AK157475 mRNA. Translation: BAE34095.1.
AJ238029 mRNA. Translation: CAB40733.1.
X82562 mRNA. Translation: CAA57909.1.
IPIIPI00127186.
IPI00322561.
IPI00974755.
IPI00986769.
PIRA46438.
B49175.
RefSeqNP_032740.3. NM_008714.3.
UniGeneMm.290610.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YMPX-ray2.20A/B1971-2105[»]
2QC9X-ray2.35A/B1899-2106[»]
2RQZNMR-A452-489[»]
2RR0NMR-A452-489[»]
2RR2NMR-A452-489[»]
3P3NX-ray2.40B1930-1949[»]
3P3PX-ray2.60B1999-2016[»]
ProteinModelPortalQ01705.
SMRQ01705. Positions 411-526, 1446-1718, 1873-2112.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-214N.
IntActQ01705. 3 interactions.
MINTMINT-142586.

Protein family/group databases

MEROPSI63.002.

PTM databases

PhosphoSiteQ01705.

Proteomic databases

PaxDbQ01705.
PRIDEQ01705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028288; ENSMUSP00000028288; ENSMUSG00000026923.
GeneID18128.
KEGGmmu:18128.

Organism-specific databases

CTD4851.
MGIMGI:97363. Notch1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00700000104305.
HOGENOMHOG000234369.
HOVERGENHBG052650.
InParanoidQ01705.
KOK02599.
OMAHGGYNCV.
OrthoDBEOG4HX504.

Enzyme and pathway databases

ReactomeREACT_115202. Signal Transduction.
REACT_81380. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_99130. A third proteolytic cleavage releases NICD.

Gene expression databases

ArrayExpressQ01705.
BgeeQ01705.
CleanExMM_NOTCH1.
GenevestigatorQ01705.
GermOnlineENSMUSG00000026923. Mus musculus.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 4 hits.
PF12661. hEGF. 3 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFPIRSF002279. Notch. 1 hit.
PRINTSPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
SSF90193. Notch_region. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 35 hits.
PS01186. EGF_2. 27 hits.
PS50026. EGF_3. 36 hits.
PS01187. EGF_CA. 21 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01705.
NextBio293356.
SOURCESearch...

Entry information

Entry nameNOTC1_MOUSE
AccessionPrimary (citable) accession number: Q01705
Secondary accession number(s): Q06007 expand/collapse secondary AC list , Q3TZW2, Q3U3Y2, Q61905, Q7TQ50, Q7TQ51, Q7TQ52, Q8K428, Q99JC2, Q9QW58, Q9R0X7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 18, 2012
Last modified: May 1, 2013
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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