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Q01705

- NOTC1_MOUSE

UniProt

Q01705 - NOTC1_MOUSE

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Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1457 – 14571Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi1460 – 14601CalciumPROSITE-ProRule annotation
Metal bindingi1475 – 14751CalciumPROSITE-ProRule annotation
Metal bindingi1478 – 14781CalciumPROSITE-ProRule annotation
Sitei1654 – 16552Cleavage; by furin-like protease
Sitei1710 – 17112Cleavage; by ADAM17By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. chromatin binding Source: MGI
  3. chromatin DNA binding Source: MGI
  4. core promoter binding Source: UniProtKB
  5. enzyme binding Source: UniProtKB
  6. enzyme inhibitor activity Source: UniProtKB
  7. receptor activity Source: InterPro
  8. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  9. sequence-specific DNA binding Source: MGI
  10. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. anagen Source: MGI
  2. aortic valve morphogenesis Source: BHF-UCL
  3. apoptotic process involved in embryonic digit morphogenesis Source: MGI
  4. arterial endothelial cell differentiation Source: BHF-UCL
  5. atrioventricular node development Source: BHF-UCL
  6. atrioventricular valve morphogenesis Source: BHF-UCL
  7. auditory receptor cell fate commitment Source: MGI
  8. axonogenesis Source: MGI
  9. branching morphogenesis of an epithelial tube Source: MGI
  10. cardiac atrium morphogenesis Source: BHF-UCL
  11. cardiac chamber formation Source: BHF-UCL
  12. cardiac epithelial to mesenchymal transition Source: BHF-UCL
  13. cardiac left ventricle morphogenesis Source: BHF-UCL
  14. cardiac muscle cell proliferation Source: BHF-UCL
  15. cardiac muscle tissue morphogenesis Source: BHF-UCL
  16. cardiac right atrium morphogenesis Source: BHF-UCL
  17. cardiac right ventricle formation Source: MGI
  18. cardiac septum morphogenesis Source: BHF-UCL
  19. cardiac vascular smooth muscle cell development Source: BHF-UCL
  20. cardiac ventricle morphogenesis Source: BHF-UCL
  21. cell differentiation Source: MGI
  22. cell fate commitment Source: MGI
  23. cell fate specification Source: MGI
  24. cell migration involved in endocardial cushion formation Source: BHF-UCL
  25. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
  26. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  27. cilium morphogenesis Source: UniProtKB
  28. collecting duct development Source: UniProtKB
  29. compartment pattern specification Source: MGI
  30. coronary artery morphogenesis Source: BHF-UCL
  31. coronary vein morphogenesis Source: BHF-UCL
  32. determination of left/right symmetry Source: MGI
  33. distal tubule development Source: UniProtKB
  34. embryonic hindlimb morphogenesis Source: MGI
  35. embryonic limb morphogenesis Source: MGI
  36. endocardial cell differentiation Source: BHF-UCL
  37. endocardial cushion morphogenesis Source: BHF-UCL
  38. endocardium development Source: BHF-UCL
  39. endocardium morphogenesis Source: BHF-UCL
  40. endoderm development Source: MGI
  41. epidermis development Source: MGI
  42. epithelial to mesenchymal transition Source: MGI
  43. epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  44. forebrain development Source: MGI
  45. foregut morphogenesis Source: MGI
  46. glial cell differentiation Source: MGI
  47. glomerular mesangial cell development Source: UniProtKB
  48. growth involved in heart morphogenesis Source: BHF-UCL
  49. hair follicle morphogenesis Source: MGI
  50. heart development Source: MGI
  51. heart looping Source: BHF-UCL
  52. heart trabecula morphogenesis Source: BHF-UCL
  53. humoral immune response Source: MGI
  54. inflammatory response to antigenic stimulus Source: MGI
  55. interleukin-4 secretion Source: MGI
  56. in utero embryonic development Source: MGI
  57. keratinocyte differentiation Source: MGI
  58. left/right axis specification Source: BHF-UCL
  59. liver development Source: MGI
  60. lung development Source: MGI
  61. mesenchymal cell development Source: BHF-UCL
  62. mitral valve formation Source: Ensembl
  63. negative regulation of anoikis Source: Ensembl
  64. negative regulation of BMP signaling pathway Source: BHF-UCL
  65. negative regulation of calcium ion-dependent exocytosis Source: MGI
  66. negative regulation of canonical Wnt signaling pathway Source: MGI
  67. negative regulation of catalytic activity Source: UniProtKB
  68. negative regulation of cell death Source: MGI
  69. negative regulation of cell differentiation Source: MGI
  70. negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
  71. negative regulation of cell proliferation Source: UniProtKB
  72. negative regulation of cell-substrate adhesion Source: Ensembl
  73. negative regulation of endothelial cell chemotaxis Source: UniProtKB
  74. negative regulation of glial cell proliferation Source: UniProtKB
  75. negative regulation of myoblast differentiation Source: Ensembl
  76. negative regulation of myotube differentiation Source: UniProtKB
  77. negative regulation of neurogenesis Source: UniProtKB
  78. negative regulation of neuron differentiation Source: MGI
  79. negative regulation of oligodendrocyte differentiation Source: UniProtKB
  80. negative regulation of ossification Source: BHF-UCL
  81. negative regulation of osteoblast differentiation Source: BHF-UCL
  82. negative regulation of photoreceptor cell differentiation Source: MGI
  83. negative regulation of pro-B cell differentiation Source: UniProtKB
  84. negative regulation of stem cell differentiation Source: Ensembl
  85. negative regulation of transcription, DNA-templated Source: BHF-UCL
  86. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  87. neural tube development Source: MGI
  88. neuronal stem cell maintenance Source: Ensembl
  89. neuron differentiation Source: MGI
  90. neuron fate commitment Source: MGI
  91. Notch signaling involved in heart development Source: BHF-UCL
  92. Notch signaling pathway Source: UniProtKB
  93. Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation Source: MGI
  94. osteoblast fate commitment Source: BHF-UCL
  95. pericardium morphogenesis Source: BHF-UCL
  96. positive regulation of apoptotic process Source: MGI
  97. positive regulation of astrocyte differentiation Source: UniProtKB
  98. positive regulation of BMP signaling pathway Source: UniProtKB
  99. positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
  100. positive regulation of cell migration Source: BHF-UCL
  101. positive regulation of cell proliferation Source: MGI
  102. positive regulation of ephrin receptor signaling pathway Source: BHF-UCL
  103. positive regulation of epithelial cell proliferation Source: MGI
  104. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  105. positive regulation of JAK-STAT cascade Source: UniProtKB
  106. positive regulation of keratinocyte differentiation Source: MGI
  107. positive regulation of transcription, DNA-templated Source: UniProtKB
  108. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  109. positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  110. positive regulation of transcription of Notch receptor target Source: MGI
  111. prostate gland epithelium morphogenesis Source: MGI
  112. pulmonary valve morphogenesis Source: Ensembl
  113. regulation of cell adhesion involved in heart morphogenesis Source: BHF-UCL
  114. regulation of cell migration Source: BHF-UCL
  115. regulation of epithelial cell proliferation Source: MGI
  116. regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
  117. regulation of extracellular matrix assembly Source: BHF-UCL
  118. regulation of gene expression Source: MGI
  119. regulation of neurogenesis Source: MGI
  120. regulation of somitogenesis Source: MGI
  121. regulation of transcription from RNA polymerase II promoter Source: MGI
  122. regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
  123. response to muramyl dipeptide Source: BHF-UCL
  124. secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: MGI
  125. skeletal muscle cell differentiation Source: MGI
  126. somatic stem cell division Source: MGI
  127. sprouting angiogenesis Source: MGI
  128. tube formation Source: UniProtKB
  129. vasculogenesis involved in coronary vascular morphogenesis Source: BHF-UCL
  130. venous endothelial cell differentiation Source: BHF-UCL
  131. ventricular septum morphogenesis Source: Ensembl
  132. 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

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_196517. Pre-NOTCH Processing in Golgi.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196604. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_196638. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_222486. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_223683. Notch-HLH transcription pathway.
REACT_268602. Pre-NOTCH Transcription and Translation.

Protein family/group databases

MEROPSiI63.001.

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
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:97363. Notch1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 17251707ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1726 – 174621HelicalSequence AnalysisAdd
BLAST
Topological domaini1747 – 2531785CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell periphery Source: MGI
  2. cell surface Source: MGI
  3. cytoplasm Source: MGI
  4. cytoskeleton Source: UniProtKB
  5. cytosol Source: Reactome
  6. endoplasmic reticulum membrane Source: Reactome
  7. extracellular region Source: Reactome
  8. Golgi membrane Source: Reactome
  9. integral component of plasma membrane Source: UniProtKB
  10. lamellipodium Source: UniProtKB
  11. MAML1-RBP-Jkappa- ICN1 complex Source: Ensembl
  12. nucleoplasm Source: Reactome
  13. nucleus Source: UniProtKB
  14. plasma membrane Source: MGI
  15. receptor complex Source: MGI
  16. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651S → A: No effect. 1 Publication
Mutagenesisi146 – 1461S → A: No effect. 1 Publication
Mutagenesisi341 – 3411S → A: No effect. 1 Publication
Mutagenesisi378 – 3781S → A: No effect. 1 Publication
Mutagenesisi458 – 4581S → A: No effect. 1 Publication
Mutagenesisi496 – 4961S → A: No effect. 1 Publication
Mutagenesisi534 – 5341S → A: No effect. 1 Publication
Mutagenesisi609 – 6091S → A: No effect. 1 Publication
Mutagenesisi647 – 6471S → A: No effect. 1 Publication
Mutagenesisi722 – 7221S → A: No effect. 1 Publication
Mutagenesisi759 – 7591S → A: No effect. 1 Publication
Mutagenesisi797 – 7971S → A: No effect. 1 Publication
Mutagenesisi951 – 9511S → A: No effect. 1 Publication
Mutagenesisi1027 – 10271S → A: No effect. 1 Publication
Mutagenesisi1065 – 10651S → A: Reduced activity. 1 Publication
Mutagenesisi1189 – 11891S → A: No effect. 1 Publication
Mutagenesisi1273 – 12731S → A: No effect. 1 Publication
Mutagenesisi1651 – 16544RQRR → AAAA: Processing by furin-like convertase abolished. 1 Publication
Mutagenesisi1744 – 17441V → L: NICD processing severely reduced.
Mutagenesisi1945 – 19451N → 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 Publications
Mutagenesisi2012 – 20121N → 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 Publications
Mutagenesisi2012 – 20121N → 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 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 25312513Neurogenic locus notch homolog protein 1PRO_0000007677Add
BLAST
Chaini1711 – 2531821Notch 1 extracellular truncationPRO_0000007678Add
BLAST
Chaini1744 – 2531788Notch 1 intracellular domainPRO_0000007679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 37By similarity
Disulfide bondi31 ↔ 46By similarity
Disulfide bondi63 ↔ 74By similarity
Glycosylationi65 – 651O-linked (Glc...)1 Publication
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73 – 731O-linked (Fuc...)1 Publication
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116 – 1161O-linked (Fuc...)1 Publication
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146 – 1461O-linked (Glc...)1 Publication
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194 – 1941O-linked (Fuc...)1 Publication
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232 – 2321O-linked (Fuc...); alternateBy similarity
Glycosylationi232 – 2321O-linked (GalNAc...); alternateBy similarity
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
Glycosylationi341 – 3411O-linked (Glc...)1 Publication
Disulfide bondi344 ↔ 359By similarity
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378 – 3781O-linked (Glc...)1 Publication
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458 – 4581O-linked (Glc...)1 Publication
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466 – 4661O-linked (Fuc...)1 Publication
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496 – 4961O-linked (Glc...)1 Publication
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534 – 5341O-linked (Glc...)1 Publication
Disulfide bondi537 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi570 ↔ 580By similarity
Disulfide bondi575 ↔ 589By similarity
Disulfide bondi591 ↔ 600By similarity
Disulfide bondi607 ↔ 618By similarity
Glycosylationi609 – 6091O-linked (Glc...)1 Publication
Disulfide bondi612 ↔ 627By similarity
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647 – 6471O-linked (Glc...)1 Publication
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722 – 7221O-linked (Glc...)1 Publication
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759 – 7591O-linked (Glc...)1 Publication
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767 – 7671O-linked (Fuc...)1 Publication
Disulfide bondi779 ↔ 788By similarity
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797 – 7971O-linked (Glc...)1 Publication
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805 – 8051O-linked (Fuc...)1 Publication
Disulfide bondi817 ↔ 826By similarity
Disulfide bondi833 ↔ 844By similarity
Disulfide bondi838 ↔ 855By similarity
Disulfide bondi857 ↔ 866By similarity
Disulfide bondi873 ↔ 884By similarity
Disulfide bondi878 ↔ 893By similarity
Glycosylationi888 – 8881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi895 ↔ 904By similarity
Disulfide bondi911 ↔ 922By similarity
Disulfide bondi916 ↔ 931By similarity
Disulfide bondi933 ↔ 942By similarity
Disulfide bondi949 ↔ 960By similarity
Glycosylationi951 – 9511O-linked (Glc...)1 Publication
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027 – 10271O-linked (Glc...)1 Publication
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035 – 10351O-linked (Fuc...)1 Publication
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065 – 10651O-linked (Glc...)1 Publication
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
Glycosylationi1179 – 11791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189 – 11891O-linked (Glc...)1 Publication
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197 – 11971O-linked (Fuc...)1 Publication
Disulfide bondi1209 ↔ 1218By similarity
Disulfide bondi1225 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1253By similarity
Glycosylationi1241 – 12411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1255 ↔ 1264By similarity
Disulfide bondi1271 ↔ 1284By similarity
Glycosylationi1273 – 12731O-linked (Glc...)1 Publication
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
Glycosylationi1362 – 13621O-linked (Fuc...)1 Publication
Disulfide bondi1374 ↔ 1383By similarity
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402 – 14021O-linked (Fuc...); alternateBy similarity
Glycosylationi1402 – 14021O-linked (GalNAc...); alternateBy similarity
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 1472By similarity
Disulfide bondi1454 ↔ 1467By similarity
Disulfide bondi1463 ↔ 1479By similarity
Glycosylationi1489 – 14891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1490 ↔ 1514By similarity
Disulfide bondi1496 ↔ 1509By similarity
Disulfide bondi1505 ↔ 1521By similarity
Disulfide bondi1536 ↔ 1549By similarity
Disulfide bondi1545 ↔ 1561By similarity
Glycosylationi1587 – 15871N-linked (GlcNAc...)Sequence Analysis
Cross-linki1749 – 1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1945 – 19451(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications
Modified residuei2012 – 20121(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications

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. Contains both O-linked fucose and O-linked glucose. O-glycosylation at Ser-1027 is only partial.1 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

Keywords - PTMi

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

Proteomic databases

PaxDbiQ01705.
PRIDEiQ01705.

PTM databases

PhosphoSiteiQ01705.

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

BgeeiQ01705.
CleanExiMM_NOTCH1.
ExpressionAtlasiQ01705. baseline and differential.
GenevestigatoriQ01705.

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 THBS4.8 Publications

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-214N.
IntActiQ01705. 5 interactions.
MINTiMINT-142586.

Structurei

Secondary structure

1
2531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni456 – 4583Combined sources
Beta strandi462 – 4643Combined sources
Beta strandi466 – 4694Combined sources
Beta strandi471 – 4777Combined sources
Turni484 – 4874Combined sources
Helixi1921 – 19277Combined sources
Helixi1931 – 19399Combined sources
Helixi1954 – 19618Combined sources
Helixi1964 – 19729Combined sources
Helixi1975 – 19773Combined sources
Helixi1988 – 19958Combined sources
Helixi2000 – 20067Combined sources
Helixi2021 – 20277Combined sources
Helixi2031 – 20399Combined sources
Helixi2054 – 20618Combined sources
Helixi2064 – 20729Combined sources
Helixi2087 – 20937Combined sources
Helixi2097 – 21037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 411-526, 1446-1718, 1873-2112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01705.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5839EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini59 – 9941EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini102 – 13938EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 17637EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini178 – 21639EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini218 – 25538EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 29337EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini295 – 33339EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini335 – 37137EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini372 – 41039EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini412 – 45039EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini452 – 48837EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini490 – 52637EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini528 – 56437EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini566 – 60136EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini603 – 63937EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini641 – 67636EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini678 – 71437EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini716 – 75136EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini753 – 78937EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini791 – 82737EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini829 – 86739EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini869 – 90537EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini907 – 94337EGF-like 24PROSITE-ProRule annotationAdd
BLAST
Domaini945 – 98137EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini983 – 101937EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1021 – 105737EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 109537EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1097 – 114347EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Domaini1145 – 118137EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1183 – 121937EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1221 – 126545EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1267 – 130539EGF-like 33PROSITE-ProRule annotationAdd
BLAST
Domaini1307 – 134640EGF-like 34PROSITE-ProRule annotationAdd
BLAST
Domaini1348 – 138437EGF-like 35PROSITE-ProRule annotationAdd
BLAST
Domaini1387 – 142640EGF-like 36PROSITE-ProRule annotationAdd
BLAST
Repeati1449 – 148941LNR 1Add
BLAST
Repeati1490 – 153142LNR 2Add
BLAST
Repeati1532 – 157140LNR 3Add
BLAST
Repeati1917 – 194630ANK 1Add
BLAST
Repeati1950 – 198031ANK 2Add
BLAST
Repeati1984 – 201330ANK 3Add
BLAST
Repeati2017 – 204630ANK 4Add
BLAST
Repeati2050 – 207930ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1937 – 19459HIF1AN-binding
Regioni2004 – 20129HIF1AN-binding

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

eggNOGiCOG0666.
GeneTreeiENSGT00760000118786.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ01705.
KOiK02599.
OMAiGASCQNT.
OrthoDBiEOG7992RD.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
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]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171L → R in CAA77941. (PubMed:8449489)Curated
Sequence conflicti41 – 411N → S in CAA77941. (PubMed:8449489)Curated
Sequence conflicti41 – 411N → S in AAM28905. (PubMed:12123574)Curated
Sequence conflicti48 – 481C → A in CAA77941. (PubMed:8449489)Curated
Sequence conflicti51 – 511A → S in CAA77941. (PubMed:8449489)Curated
Sequence conflicti60 – 601S → P in CAA77941. (PubMed:8449489)Curated
Sequence conflicti67 – 671P → R in CAA77941. (PubMed:8449489)Curated
Sequence conflicti75 – 751H → Y in CAA77941. (PubMed:8449489)Curated
Sequence conflicti82 – 821T → I in CAA77941. (PubMed:8449489)Curated
Sequence conflicti104 – 1052NA → KP in CAA77941. (PubMed:8449489)Curated
Sequence conflicti130 – 1301P → S in CAA77941. (PubMed:8449489)Curated
Sequence conflicti194 – 1941T → H in CAA77941. (PubMed:8449489)Curated
Sequence conflicti207 – 2071R → C in CAA77941. (PubMed:8449489)Curated
Sequence conflicti231 – 2311G → A in CAA77941. (PubMed:8449489)Curated
Sequence conflicti287 – 2871W → V in CAA77941. (PubMed:8449489)Curated
Sequence conflicti309 – 3091G → A in CAA77941. (PubMed:8449489)Curated
Sequence conflicti373 – 3742ND → KH in CAA77941. (PubMed:8449489)Curated
Sequence conflicti396 – 3961A → R in CAA77941. (PubMed:8449489)Curated
Sequence conflicti417 – 4171A → D in CAA77941. (PubMed:8449489)Curated
Sequence conflicti422 – 4221P → R in CAA77941. (PubMed:8449489)Curated
Sequence conflicti448 – 4481R → G in CAA77941. (PubMed:8449489)Curated
Sequence conflicti510 – 5101N → H in CAA77941. (PubMed:8449489)Curated
Sequence conflicti835 – 8351T → I in AAK14898. (PubMed:1426644)Curated
Sequence conflicti933 – 9342CL → SV in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1050 – 10501G → R in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1104 – 11063Missing in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1155 – 11551Q → L in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1209 – 12091C → W in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1438 – 14381R → P in CAA77941. (PubMed:8449489)Curated
Sequence conflicti1545 – 15451C → S in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1556 – 15561W → R in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1572 – 15721G → R in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1576 – 15761L → V in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1609 – 16091D → H in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1661 – 16611I → T in BAE32653. (PubMed:16141072)Curated
Sequence conflicti1864 – 18641V → D in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1890 – 18901S → R in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1896 – 18983APA → RPG in AAK14898. (PubMed:1426644)Curated
Sequence conflicti1933 – 19342AA → RR in CAA77941. (PubMed:8449489)Curated
Sequence conflicti1938 – 19381Missing in CAA77941. (PubMed:8449489)Curated
Sequence conflicti1997 – 19971V → L in AAM28905. (PubMed:12123574)Curated
Sequence conflicti2046 – 20472MQ → IE in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2054 – 20541P → S in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2058 – 20625AAREG → SIRRE in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2075 – 20751A → G in CAA57909. (PubMed:9384671)Curated
Sequence conflicti2086 – 20861L → M in BAE34095. (PubMed:16141072)Curated
Sequence conflicti2136 – 21361L → P in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2172 – 21721K → S in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2179 – 21791C → W in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2185 – 21851S → SS in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2206 – 22061P → H in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2258 – 22581P → H in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2273 – 22731S → C in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2347 – 23471N → S in BAE34095. (PubMed:16141072)Curated
Sequence conflicti2380 – 23801Q → P in CAA77941. (PubMed:8449489)Curated
Sequence conflicti2483 – 24842HP → PT in CAA77941. (PubMed:8449489)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747MPRLL…TEACV → MQTPLLSLAGATTELCFLPA SVLASSLPGPSL in isoform 4. CuratedVSP_043065Add
BLAST
Alternative sequencei1 – 2121MPRLL…LAARG → MKNSNTLTNKWRMEQC in isoform 3. CuratedVSP_043064Add
BLAST
Alternative sequencei857 – 91458Missing in isoform 2. 1 PublicationVSP_001402Add
BLAST
Alternative sequencei1329 – 135527Missing in isoform 2. 1 PublicationVSP_001403Add
BLAST
Alternative sequencei1636 – 1854219Missing in isoform 2. 1 PublicationVSP_001404Add
BLAST

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.

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 .
CCDSi CCDS15806.1. [Q01705-1 ]
PIRi A46438.
B49175.
RefSeqi NP_032740.3. NM_008714.3. [Q01705-1 ]
UniGenei Mm.290610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YMP X-ray 2.20 A/B 1971-2105 [» ]
2QC9 X-ray 2.35 A/B 1899-2106 [» ]
2RQZ NMR - A 452-489 [» ]
2RR0 NMR - A 452-489 [» ]
2RR2 NMR - A 452-489 [» ]
3P3N X-ray 2.40 B 1930-1949 [» ]
3P3P X-ray 2.60 B 1999-2016 [» ]
ProteinModelPortali Q01705.
SMRi Q01705. Positions 411-526, 1446-1718, 1873-2112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-214N.
IntActi Q01705. 5 interactions.
MINTi MINT-142586.

Protein family/group databases

MEROPSi I63.001.

PTM databases

PhosphoSitei Q01705.

Proteomic databases

PaxDbi Q01705.
PRIDEi Q01705.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028288 ; ENSMUSP00000028288 ; ENSMUSG00000026923 . [Q01705-1 ]
GeneIDi 18128.
KEGGi mmu:18128.
UCSCi uc008ivl.2. mouse.

Organism-specific databases

CTDi 4851.
MGIi MGI:97363. Notch1.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118786.
HOGENOMi HOG000234369.
HOVERGENi HBG052650.
InParanoidi Q01705.
KOi K02599.
OMAi GASCQNT.
OrthoDBi EOG7992RD.
TreeFami TF351641.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_196517. Pre-NOTCH Processing in Golgi.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196604. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_196638. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_222486. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_223683. Notch-HLH transcription pathway.
REACT_268602. Pre-NOTCH Transcription and Translation.

Miscellaneous databases

EvolutionaryTracei Q01705.
NextBioi 293356.
PROi Q01705.
SOURCEi Search...

Gene expression databases

Bgeei Q01705.
CleanExi MM_NOTCH1.
ExpressionAtlasi Q01705. baseline and differential.
Genevestigatori Q01705.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view ]
Pfami PF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
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 ]
PIRSFi PIRSF002279. Notch. 1 hit.
PRINTSi PR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTi SM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 3 hits.
PROSITEi PS50297. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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, IDENTIFICATION BY 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. "O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1."
    Rana N.A., Nita-Lazar A., Takeuchi H., Kakuda S., Luther K.B., Haltiwanger R.S.
    J. Biol. Chem. 286:31623-31637(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-65; THR-73; THR-116; SER-146; THR-194; SER-341; SER-378; SER-458; THR-466; SER-496; SER-534; SER-609; SER-647; SER-722; SER-759; THR-767; SER-797; THR-805; SER-951; SER-1027; THR-1035; SER-1065; SER-1189; THR-1197; SER-1273 AND THR-1362, MUTAGENESIS OF SER-65; SER-146; SER-341; SER-378; SER-458; SER-496; SER-534; SER-609; SER-647; SER-722; SER-759; SER-797; SER-951; SER-1027; SER-1065; SER-1189 AND SER-1273.
  26. "BCL6 controls neurogenesis through Sirt1-dependent epigenetic repression of selective Notch targets."
    Tiberi L., van den Ameele J., Dimidschstein J., Piccirilli J., Gall D., Herpoel A., Bilheu A., Bonnefont J., Iacovino M., Kyba M., Bouschet T., Vanderhaeghen P.
    Nat. Neurosci. 15:1627-1635(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NEUROGENESIS REPRESSOR, INTERACTION WITH BCL6.
  27. "Protective astrogenesis from the SVZ niche after injury is controlled by Notch modulator Thbs4."
    Benner E.J., Luciano D., Jo R., Abdi K., Paez-Gonzalez P., Sheng H., Warner D.S., Liu C., Eroglu C., Kuo C.T.
    Nature 497:369-373(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THBS4.
  28. "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.
  29. 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, IDENTIFICATION BY MASS SPECTROMETRY.

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 26, 2014
This is version 170 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

External Data

Dasty 3