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Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi432Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi435Calcium 1; via amide nitrogenBy similarity1
Metal bindingi452Calcium 2By similarity1
Metal bindingi453Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi455Calcium 2By similarity1
Metal bindingi469Calcium 2By similarity1
Metal bindingi470Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi490Calcium 3By similarity1
Metal bindingi491Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi493Calcium 3By similarity1
Metal bindingi507Calcium 3By similarity1
Metal bindingi508Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1457Calcium 4; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi1460Calcium 4PROSITE-ProRule annotation1
Metal bindingi1475Calcium 4PROSITE-ProRule annotation1
Metal bindingi1478Calcium 4PROSITE-ProRule annotation1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • chromatin binding Source: MGI
  • chromatin DNA binding Source: MGI
  • core promoter binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • enzyme inhibitor activity Source: UniProtKB
  • Notch binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • receptor activity Source: InterPro
  • sequence-specific DNA binding Source: MGI
  • transcriptional activator activity, RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: MGI

GO - Biological processi

  • animal organ regeneration Source: Ensembl
  • aortic valve morphogenesis Source: BHF-UCL
  • apoptotic process involved in embryonic digit morphogenesis Source: MGI
  • arterial endothelial cell differentiation Source: BHF-UCL
  • astrocyte differentiation Source: Ensembl
  • atrioventricular node development Source: BHF-UCL
  • atrioventricular valve morphogenesis Source: BHF-UCL
  • auditory receptor cell fate commitment Source: MGI
  • axonogenesis Source: MGI
  • branching morphogenesis of an epithelial tube Source: MGI
  • cardiac atrium morphogenesis Source: BHF-UCL
  • cardiac chamber formation Source: BHF-UCL
  • cardiac epithelial to mesenchymal transition Source: BHF-UCL
  • cardiac left ventricle morphogenesis Source: BHF-UCL
  • cardiac muscle cell proliferation Source: BHF-UCL
  • cardiac muscle tissue morphogenesis Source: BHF-UCL
  • cardiac right atrium morphogenesis Source: BHF-UCL
  • cardiac right ventricle formation Source: MGI
  • cardiac septum morphogenesis Source: BHF-UCL
  • cardiac vascular smooth muscle cell development Source: BHF-UCL
  • cardiac ventricle morphogenesis Source: BHF-UCL
  • cell differentiation Source: MGI
  • cell differentiation in spinal cord Source: Ensembl
  • cell fate commitment Source: MGI
  • cell fate specification Source: MGI
  • cell migration involved in endocardial cushion formation Source: BHF-UCL
  • cellular response to follicle-stimulating hormone stimulus Source: MGI
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • cilium morphogenesis Source: UniProtKB
  • collecting duct development Source: UniProtKB
  • compartment pattern specification Source: MGI
  • coronary artery morphogenesis Source: BHF-UCL
  • coronary vein morphogenesis Source: BHF-UCL
  • determination of left/right symmetry Source: MGI
  • distal tubule development Source: UniProtKB
  • embryonic hindlimb morphogenesis Source: MGI
  • embryonic limb morphogenesis Source: MGI
  • endocardial cell differentiation Source: BHF-UCL
  • endocardial cushion development Source: MGI
  • endocardial cushion morphogenesis Source: BHF-UCL
  • endocardium development Source: BHF-UCL
  • endocardium morphogenesis Source: BHF-UCL
  • endoderm development Source: MGI
  • epidermis development Source: MGI
  • epithelial to mesenchymal transition Source: MGI
  • epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  • forebrain development Source: MGI
  • foregut morphogenesis Source: MGI
  • glial cell differentiation Source: MGI
  • glomerular mesangial cell development Source: UniProtKB
  • growth involved in heart morphogenesis Source: BHF-UCL
  • hair follicle morphogenesis Source: MGI
  • heart development Source: MGI
  • heart looping Source: BHF-UCL
  • heart trabecula morphogenesis Source: BHF-UCL
  • humoral immune response Source: MGI
  • inflammatory response to antigenic stimulus Source: MGI
  • interleukin-4 secretion Source: MGI
  • in utero embryonic development Source: MGI
  • keratinocyte differentiation Source: MGI
  • left/right axis specification Source: BHF-UCL
  • liver development Source: MGI
  • lung development Source: MGI
  • mesenchymal cell development Source: BHF-UCL
  • mitral valve formation Source: MGI
  • negative regulation of anoikis Source: MGI
  • negative regulation of auditory receptor cell differentiation Source: MGI
  • negative regulation of BMP signaling pathway Source: BHF-UCL
  • negative regulation of calcium ion-dependent exocytosis Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of catalytic activity Source: UniProtKB
  • negative regulation of cell death Source: MGI
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cell-substrate adhesion Source: MGI
  • negative regulation of endothelial cell chemotaxis Source: UniProtKB
  • negative regulation of glial cell proliferation Source: UniProtKB
  • negative regulation of myoblast differentiation Source: MGI
  • negative regulation of myotube differentiation Source: UniProtKB
  • negative regulation of neurogenesis Source: UniProtKB
  • negative regulation of neuron differentiation Source: MGI
  • negative regulation of oligodendrocyte differentiation Source: UniProtKB
  • negative regulation of ossification Source: BHF-UCL
  • negative regulation of osteoblast differentiation Source: BHF-UCL
  • negative regulation of photoreceptor cell differentiation Source: MGI
  • negative regulation of pro-B cell differentiation Source: UniProtKB
  • negative regulation of stem cell differentiation Source: MGI
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neural tube development Source: MGI
  • neuronal stem cell population maintenance Source: Ensembl
  • neuron differentiation Source: MGI
  • neuron fate commitment Source: MGI
  • Notch receptor processing Source: Reactome
  • Notch signaling involved in heart development Source: BHF-UCL
  • Notch signaling pathway Source: UniProtKB
  • Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation Source: MGI
  • oligodendrocyte differentiation Source: Ensembl
  • osteoblast fate commitment Source: BHF-UCL
  • pericardium morphogenesis Source: BHF-UCL
  • positive regulation of aorta morphogenesis Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of astrocyte differentiation Source: UniProtKB
  • positive regulation of BMP signaling pathway Source: UniProtKB
  • positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of endothelial cell differentiation Source: Ensembl
  • positive regulation of ephrin receptor signaling pathway Source: BHF-UCL
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • positive regulation of JAK-STAT cascade Source: UniProtKB
  • positive regulation of keratinocyte differentiation Source: MGI
  • positive regulation of neuroblast proliferation Source: Ensembl
  • positive regulation of Notch signaling pathway Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  • positive regulation of transcription of Notch receptor target Source: MGI
  • positive regulation of viral genome replication Source: AgBase
  • positive regulation of viral transcription Source: AgBase
  • prostate gland epithelium morphogenesis Source: MGI
  • pulmonary valve morphogenesis Source: MGI
  • regulation of auditory receptor cell differentiation Source: MGI
  • regulation of cell adhesion involved in heart morphogenesis Source: BHF-UCL
  • regulation of cell migration Source: BHF-UCL
  • regulation of cell proliferation Source: MGI
  • regulation of epithelial cell proliferation Source: MGI
  • regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
  • regulation of extracellular matrix assembly Source: BHF-UCL
  • regulation of gene expression Source: MGI
  • regulation of neurogenesis Source: MGI
  • regulation of Notch signaling pathway Source: MGI
  • regulation of somitogenesis Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
  • response to corticosteroid Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to muramyl dipeptide Source: BHF-UCL
  • secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: MGI
  • skeletal muscle cell differentiation Source: MGI
  • somatic stem cell division Source: MGI
  • spermatogenesis Source: Ensembl
  • sprouting angiogenesis Source: MGI
  • tissue regeneration Source: Ensembl
  • tube formation Source: UniProtKB
  • vasculogenesis involved in coronary vascular morphogenesis Source: BHF-UCL
  • venous blood vessel morphogenesis Source: MGI
  • venous endothelial cell differentiation Source: BHF-UCL
  • ventricular septum morphogenesis Source: MGI
  • ventricular trabecula myocardium morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-1912420. Pre-NOTCH Processing in Golgi.
R-MMU-210744. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
R-MMU-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-350054. Notch-HLH transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 1
Short name:
Notch 1
Alternative name(s):
Motch A
mT14
p300
Cleaved into the following 2 chains:
Gene namesi
Name:Notch1
Synonyms:Motch
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97363. Notch1.

Subcellular locationi

Notch 1 intracellular domain :
  • Nucleus

  • Note: Following proteolytical processing NICD is translocated to the nucleus.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 1725ExtracellularSequence analysisAdd BLAST1707
Transmembranei1726 – 1746HelicalSequence analysisAdd BLAST21
Topological domaini1747 – 2531CytoplasmicSequence analysisAdd BLAST785

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • cell periphery Source: MGI
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle Source: MGI
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: Reactome
  • extracellular region Source: Reactome
  • Golgi membrane Source: Reactome
  • integral component of plasma membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • MAML1-RBP-Jkappa- ICN1 complex Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: AgBase
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65S → A: No effect. 1 Publication1
Mutagenesisi146S → A: No effect. 1 Publication1
Mutagenesisi341S → A: No effect. 1 Publication1
Mutagenesisi378S → A: No effect. 1 Publication1
Mutagenesisi458S → A: No effect. 1 Publication1
Mutagenesisi496S → A: No effect. 1 Publication1
Mutagenesisi534S → A: No effect. 1 Publication1
Mutagenesisi609S → A: No effect. 1 Publication1
Mutagenesisi647S → A: No effect. 1 Publication1
Mutagenesisi722S → A: No effect. 1 Publication1
Mutagenesisi759S → A: No effect. 1 Publication1
Mutagenesisi797S → A: No effect. 1 Publication1
Mutagenesisi951S → A: No effect. 1 Publication1
Mutagenesisi1027S → A: No effect. 1 Publication1
Mutagenesisi1065S → A: Reduced activity. 1 Publication1
Mutagenesisi1189S → A: No effect. 1 Publication1
Mutagenesisi1273S → A: No effect. 1 Publication1
Mutagenesisi1651 – 1654RQRR → AAAA: Processing by furin-like convertase abolished. 1 Publication4
Mutagenesisi1744V → L: NICD processing severely reduced. 1
Mutagenesisi1945N → 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. 2 Publications1
Mutagenesisi2012N → 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. 2 Publications1
Mutagenesisi2012N → G: Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with A-1945. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000767719 – 2531Neurogenic locus notch homolog protein 1Add BLAST2513
ChainiPRO_00000076781711 – 2531Notch 1 extracellular truncationAdd BLAST821
ChainiPRO_00000076791744 – 2531Notch 1 intracellular domainAdd BLAST788

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 37By similarity
Disulfide bondi31 ↔ 46By similarity
Disulfide bondi63 ↔ 74By similarity
Glycosylationi65O-linked (Glc...)1 Publication1
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73O-linked (Fuc...)1 Publication1
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116O-linked (Fuc...)1 Publication1
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146O-linked (Glc...)1 Publication1
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194O-linked (Fuc...)1 Publication1
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232O-linked (Fuc...); alternateBy similarity1
Glycosylationi232O-linked (GalNAc...); alternateBy similarity1
Disulfide bondi245 ↔ 254By similarity
Disulfide bondi261 ↔ 272By similarity
Disulfide bondi266 ↔ 281By similarity
Disulfide bondi283 ↔ 292By similarity
Disulfide bondi299 ↔ 312By similarity
Disulfide bondi306 ↔ 321By similarity
Disulfide bondi323 ↔ 332By similarity
Disulfide bondi339 ↔ 350By similarity
Glycosylationi341O-linked (Glc...)1 Publication1
Disulfide bondi344 ↔ 359By similarity
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378O-linked (Glc...)1 Publication1
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Glycosylationi435O-linked (Glc...)By similarity1
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458O-linked (Glc...)1 Publication1
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466O-linked (Fuc...)1 Publication1
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496O-linked (Glc...)1 Publication1
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534O-linked (Glc...)1 Publication1
Disulfide bondi537 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi570 ↔ 580By similarity
Disulfide bondi575 ↔ 589By similarity
Disulfide bondi591 ↔ 600By similarity
Disulfide bondi607 ↔ 618By similarity
Glycosylationi609O-linked (Glc...)1 Publication1
Disulfide bondi612 ↔ 627By similarity
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647O-linked (Glc...)1 Publication1
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722O-linked (Glc...)1 Publication1
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759O-linked (Glc...)1 Publication1
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767O-linked (Fuc...)1 Publication1
Disulfide bondi779 ↔ 788By similarity
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797O-linked (Glc...)1 Publication1
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805O-linked (Fuc...)1 Publication1
Disulfide bondi817 ↔ 826By similarity
Disulfide bondi833 ↔ 844By similarity
Disulfide bondi838 ↔ 855By similarity
Disulfide bondi857 ↔ 866By similarity
Disulfide bondi873 ↔ 884By similarity
Disulfide bondi878 ↔ 893By similarity
Glycosylationi888N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi895 ↔ 904By similarity
Disulfide bondi911 ↔ 922By similarity
Disulfide bondi916 ↔ 931By similarity
Disulfide bondi933 ↔ 942By similarity
Disulfide bondi949 ↔ 960By similarity
Glycosylationi951O-linked (Glc...)1 Publication1
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027O-linked (Glc...)1 Publication1
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035O-linked (Fuc...)1 Publication1
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065O-linked (Glc...)1 Publication1
Disulfide bondi1068 ↔ 1083By similarity
Disulfide bondi1085 ↔ 1094By similarity
Disulfide bondi1101 ↔ 1122By similarity
Disulfide bondi1116 ↔ 1131By similarity
Disulfide bondi1133 ↔ 1142By similarity
Disulfide bondi1149 ↔ 1160By similarity
Disulfide bondi1154 ↔ 1169By similarity
Disulfide bondi1171 ↔ 1180By similarity
Glycosylationi1179N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189O-linked (Glc...)1 Publication1
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197O-linked (Fuc...)1 Publication1
Disulfide bondi1209 ↔ 1218By similarity
Disulfide bondi1225 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1253By similarity
Glycosylationi1241N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1255 ↔ 1264By similarity
Disulfide bondi1271 ↔ 1284By similarity
Glycosylationi1273O-linked (Glc...)1 Publication1
Disulfide bondi1276 ↔ 1293By similarity
Disulfide bondi1295 ↔ 1304By similarity
Disulfide bondi1311 ↔ 1322By similarity
Disulfide bondi1316 ↔ 1334By similarity
Disulfide bondi1336 ↔ 1345By similarity
Disulfide bondi1352 ↔ 1363By similarity
Disulfide bondi1357 ↔ 1372By similarity
Glycosylationi1362O-linked (Fuc...)1 Publication1
Disulfide bondi1374 ↔ 1383By similarity
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402O-linked (Fuc...); alternateBy similarity1
Glycosylationi1402O-linked (GalNAc...); alternateBy similarity1
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 1472By similarity
Disulfide bondi1454 ↔ 1467By similarity
Disulfide bondi1463 ↔ 1479By similarity
Glycosylationi1489N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1490 ↔ 1514By similarity
Disulfide bondi1496 ↔ 1509By similarity
Disulfide bondi1505 ↔ 1521By similarity
Disulfide bondi1536 ↔ 1549By similarity
Disulfide bondi1545 ↔ 1561By similarity
Glycosylationi1587N-linked (GlcNAc...)Sequence analysis1
Cross-linki1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1851PhosphothreonineCombined sources1
Modified residuei1945(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications1
Modified residuei2012(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications1

Post-translational modificationi

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.
Phosphorylated.
O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). O-glycosylated on the EGF-like domains (PubMed:21757702). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4 (By similarity). O-glycosylation at Ser-1027 is only partial (PubMed:21757702).By similarity1 Publication
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.2 Publications
Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1654 – 1655Cleavage; by furin-like protease2
Sitei1710 – 1711Cleavage; by ADAM17By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ01705.
PeptideAtlasiQ01705.
PRIDEiQ01705.

PTM databases

iPTMnetiQ01705.
PhosphoSitePlusiQ01705.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.3 Publications

Gene expression databases

BgeeiENSMUSG00000026923.
CleanExiMM_NOTCH1.
ExpressionAtlasiQ01705. baseline and differential.
GenevisibleiQ01705. MM.

Interactioni

Subunit structurei

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization. Forms a trimeric complex with FBXW7 and SGK1. Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation. Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity. Interacts with THBS4. Interacts (via the EGF-like repeat region) with NOV (via CTCK domain) (PubMed:12050162). Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By similarity).By similarity9 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei469Interaction with DLL4By similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
LRORF2Q77CA83EBI-11292892,EBI-11292862From a different organism.
RBPJQ063303EBI-1392707,EBI-632552From a different organism.
RbpjP312666EBI-1392707,EBI-1392666
Su(H)P281593EBI-1392707,EBI-92180From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Notch binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi201808. 21 interactors.
DIPiDIP-214N.
IntActiQ01705. 6 interactors.
MINTiMINT-142586.
STRINGi10090.ENSMUSP00000028288.

Structurei

Secondary structure

12531
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni456 – 458Combined sources3
Beta strandi462 – 464Combined sources3
Beta strandi466 – 469Combined sources4
Beta strandi471 – 477Combined sources7
Turni484 – 487Combined sources4
Helixi1921 – 1927Combined sources7
Helixi1931 – 1939Combined sources9
Helixi1954 – 1961Combined sources8
Helixi1964 – 1972Combined sources9
Helixi1975 – 1977Combined sources3
Helixi1988 – 1995Combined sources8
Helixi2000 – 2006Combined sources7
Helixi2021 – 2027Combined sources7
Helixi2031 – 2039Combined sources9
Helixi2054 – 2061Combined sources8
Helixi2064 – 2072Combined sources9
Helixi2087 – 2093Combined sources7
Helixi2097 – 2103Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ01705.
SMRiQ01705.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01705.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 58EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini59 – 99EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini102 – 139EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini140 – 176EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini178 – 216EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini218 – 255EGF-like 6PROSITE-ProRule annotationAdd BLAST38
Domaini257 – 293EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini295 – 333EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini335 – 371EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini372 – 410EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini412 – 450EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini452 – 488EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini490 – 526EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini528 – 564EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini566 – 601EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini603 – 639EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini641 – 676EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini678 – 714EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini716 – 751EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini753 – 789EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini791 – 827EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini829 – 867EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini869 – 905EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini907 – 943EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini945 – 981EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini983 – 1019EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1021 – 1057EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1059 – 1095EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1097 – 1143EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1145 – 1181EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1183 – 1219EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1221 – 1265EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1267 – 1305EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1307 – 1346EGF-like 34PROSITE-ProRule annotationAdd BLAST40
Domaini1348 – 1384EGF-like 35PROSITE-ProRule annotationAdd BLAST37
Domaini1387 – 1426EGF-like 36PROSITE-ProRule annotationAdd BLAST40
Repeati1449 – 1489LNR 1Add BLAST41
Repeati1490 – 1531LNR 2Add BLAST42
Repeati1532 – 1571LNR 3Add BLAST40
Repeati1917 – 1946ANK 1Add BLAST30
Repeati1950 – 1980ANK 2Add BLAST31
Repeati1984 – 2013ANK 3Add BLAST30
Repeati2017 – 2046ANK 4Add BLAST30
Repeati2050 – 2079ANK 5Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni420 – 421Interaction with DLL4By similarity2
Regioni448 – 452Interaction with DLL4By similarity5
Regioni1937 – 1945HIF1AN-binding9
Regioni2004 – 2012HIF1AN-binding9

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 36 EGF-like domains.PROSITE-ProRule annotation
Contains 3 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ01705.
KOiK02599.
OMAiILDYSFV.
OrthoDBiEOG091G01NU.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 21 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 3 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 36 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. 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]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01705-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG
60 70 80 90 100
AFVGQRCQDS NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT
110 120 130 140 150
PLDNACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA
160 170 180 190 200
NGGQCLPFES SYICRCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG
210 220 230 240 250
SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA
260 270 280 290 300
GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
310 320 330 340 350
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC
360 370 380 390 400
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC
410 420 430 440 450
PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE
460 470 480 490 500
IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL
510 520 530 540 550
HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG AKCLDGPNTY
560 570 580 590 600
TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC
610 620 630 640 650
ETNINECHSQ PCRHGGTCQD RDNSYLCLCL KGTTGPNCEI NLDDCASNPC
660 670 680 690 700
DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF
710 720 730 740 750
TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC
760 770 780 790 800
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC
810 820 830 840 850
LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY
860 870 880 890 900
ESFSCVCPTG WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
910 920 930 940 950
GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA
960 970 980 990 1000
SNPCQNGANC TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD
1010 1020 1030 1040 1050
GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG
1060 1070 1080 1090 1100
YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ YHCECRSGWT GVNCDVLSVS
1110 1120 1130 1140 1150
CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS YCEDEVDECS
1160 1170 1180 1190 1200
PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
1210 1220 1230 1240 1250
LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG
1260 1270 1280 1290 1300
YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT
1310 1320 1330 1340 1350
GRRCESVING CRGKPCKNGG VCAVASNTAR GFICRCPAGF EGATCENDAR
1360 1370 1380 1390 1400
TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ
1410 1420 1430 1440 1450
GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE
1460 1470 1480 1490 1500
LPECQVDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
1510 1520 1530 1540 1550
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN
1560 1570 1580 1590 1600
SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL
1610 1620 1630 1640 1650
HTNVVFKRDA QGQQMIFPYY GHEEELRKHP IKRSTVGWAT SSLLPGTSGG
1660 1670 1680 1690 1700
RQRRELDPMD IRGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG
1710 1720 1730 1740 1750
SLNIPYKIEA VKSEPVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR
1760 1770 1780 1790 1800
RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ
1810 1820 1830 1840 1850
NEWGDEDLET KKFRFEEPVV LPDLSDQTDH RQWTQQHLDA ADLRMSAMAP
1860 1870 1880 1890 1900
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI
1910 1920 1930 1940 1950
SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM
1960 1970 1980 1990 2000
GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM
2010 2020 2030 2040 2050
LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK
2060 2070 2080 2090 2100
EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV
2110 2120 2130 2140 2150
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK
2160 2170 2180 2190 2200
PSTKGLACGS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL
2210 2220 2230 2240 2250
SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG
2260 2270 2280 2290 2300
GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW
2310 2320 2330 2340 2350
LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHSMMGPL HSSLSTNTLS
2360 2370 2380 2390 2400
PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ LQPQNLQPPS QPHLSVSSAA
2410 2420 2430 2440 2450
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP
2460 2470 2480 2490 2500
MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS
2510 2520 2530
PHSNISDWSE GISSPPTTMP SQITHIPEAF K
Length:2,531
Mass (Da):270,835
Last modified:April 18, 2012 - v3
Checksum:i97C91F69BABF02BF
GO
Isoform 2 (identifier: Q01705-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:2,227
Mass (Da):237,414
Checksum:iE36CEB947C4464C4
GO
Isoform 3 (identifier: Q01705-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MPRLLTPLLCLTLLPALAARG → MKNSNTLTNKWRMEQC

Note: No experimental confirmation available.
Show »
Length:2,526
Mass (Da):270,585
Checksum:i017563FCE9703264
GO
Isoform 4 (identifier: Q01705-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MPRLLTPLLC...EVANGTEACV → MQTPLLSLAGATTELCFLPASVLASSLPGPSL

Note: No experimental confirmation available.
Show »
Length:2,516
Mass (Da):269,180
Checksum:i17FD72740EBD6E35
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17L → R in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti41N → S in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti41N → S in AAM28905 (PubMed:12123574).Curated1
Sequence conflicti48C → A in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti51A → S in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti60S → P in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti67P → R in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti75H → Y in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti82T → I in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti104 – 105NA → KP in CAA77941 (PubMed:8449489).Curated2
Sequence conflicti130P → S in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti194T → H in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti207R → C in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti231G → A in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti287W → V in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti309G → A in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti373 – 374ND → KH in CAA77941 (PubMed:8449489).Curated2
Sequence conflicti396A → R in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti417A → D in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti422P → R in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti448R → G in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti510N → H in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti835T → I in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti933 – 934CL → SV in AAK14898 (PubMed:1426644).Curated2
Sequence conflicti1050G → R in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1104 – 1106Missing in AAK14898 (PubMed:1426644).Curated3
Sequence conflicti1155Q → L in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1209C → W in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1438R → P in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti1545C → S in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1556W → R in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1572G → R in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1576L → V in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1609D → H in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1661I → T in BAE32653 (PubMed:16141072).Curated1
Sequence conflicti1864V → D in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1890S → R in AAK14898 (PubMed:1426644).Curated1
Sequence conflicti1896 – 1898APA → RPG in AAK14898 (PubMed:1426644).Curated3
Sequence conflicti1933 – 1934AA → RR in CAA77941 (PubMed:8449489).Curated2
Sequence conflicti1938Missing in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti1997V → L in AAM28905 (PubMed:12123574).Curated1
Sequence conflicti2046 – 2047MQ → IE in CAA77941 (PubMed:8449489).Curated2
Sequence conflicti2054P → S in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2058 – 2062AAREG → SIRRE in CAA77941 (PubMed:8449489).Curated5
Sequence conflicti2075A → G in CAA57909 (PubMed:9384671).Curated1
Sequence conflicti2086L → M in BAE34095 (PubMed:16141072).Curated1
Sequence conflicti2136L → P in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2172K → S in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2179C → W in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2185S → SS in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2206P → H in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2258P → H in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2273S → C in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2347N → S in BAE34095 (PubMed:16141072).Curated1
Sequence conflicti2380Q → P in CAA77941 (PubMed:8449489).Curated1
Sequence conflicti2483 – 2484HP → PT in CAA77941 (PubMed:8449489).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0430651 – 47MPRLL…TEACV → MQTPLLSLAGATTELCFLPA SVLASSLPGPSL in isoform 4. CuratedAdd BLAST47
Alternative sequenceiVSP_0430641 – 21MPRLL…LAARG → MKNSNTLTNKWRMEQC in isoform 3. CuratedAdd BLAST21
Alternative sequenceiVSP_001402857 – 914Missing in isoform 2. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_0014031329 – 1355Missing in isoform 2. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_0014041636 – 1854Missing in isoform 2. 1 PublicationAdd BLAST219

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15806.1. [Q01705-1]
PIRiA46438.
B49175.
RefSeqiNP_032740.3. NM_008714.3. [Q01705-1]
UniGeneiMm.290610.

Genome annotation databases

EnsembliENSMUST00000028288; ENSMUSP00000028288; ENSMUSG00000026923. [Q01705-1]
GeneIDi18128.
KEGGimmu:18128.
UCSCiuc008ivl.2. mouse. [Q01705-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15806.1. [Q01705-1]
PIRiA46438.
B49175.
RefSeqiNP_032740.3. NM_008714.3. [Q01705-1]
UniGeneiMm.290610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ01705.
SMRiQ01705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201808. 21 interactors.
DIPiDIP-214N.
IntActiQ01705. 6 interactors.
MINTiMINT-142586.
STRINGi10090.ENSMUSP00000028288.

PTM databases

iPTMnetiQ01705.
PhosphoSitePlusiQ01705.

Proteomic databases

PaxDbiQ01705.
PeptideAtlasiQ01705.
PRIDEiQ01705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028288; ENSMUSP00000028288; ENSMUSG00000026923. [Q01705-1]
GeneIDi18128.
KEGGimmu:18128.
UCSCiuc008ivl.2. mouse. [Q01705-1]

Organism-specific databases

CTDi4851.
MGIiMGI:97363. Notch1.

Phylogenomic databases

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ01705.
KOiK02599.
OMAiILDYSFV.
OrthoDBiEOG091G01NU.
TreeFamiTF351641.

Enzyme and pathway databases

ReactomeiR-MMU-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-1912420. Pre-NOTCH Processing in Golgi.
R-MMU-210744. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
R-MMU-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-350054. Notch-HLH transcription pathway.

Miscellaneous databases

EvolutionaryTraceiQ01705.
PROiQ01705.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026923.
CleanExiMM_NOTCH1.
ExpressionAtlasiQ01705. baseline and differential.
GenevisibleiQ01705. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 21 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 3 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 36 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiNOTC1_MOUSE
AccessioniPrimary (citable) accession number: Q01705
Secondary accession number(s): Q06007
, Q3TZW2, Q3U3Y2, Q61905, Q7TQ50, Q7TQ51, Q7TQ52, Q8K428, Q99JC2, Q9QW58, Q9R0X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 18, 2012
Last modified: November 2, 2016
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.