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Q01705

- NOTC1_MOUSE

UniProt

Q01705 - NOTC1_MOUSE

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
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 3 (18 Apr 2012)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    8. receptor activity Source: InterPro
    9. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    10. sequence-specific DNA binding Source: MGI
    11. 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

    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_196520. Pre-NOTCH Transcription and Translation.
    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.

    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.

    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

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651S → A: No effect. 2 Publications
    Mutagenesisi146 – 1461S → A: No effect. 2 Publications
    Mutagenesisi341 – 3411S → A: No effect. 2 Publications
    Mutagenesisi378 – 3781S → A: No effect. 2 Publications
    Mutagenesisi458 – 4581S → A: No effect. 2 Publications
    Mutagenesisi496 – 4961S → A: No effect. 2 Publications
    Mutagenesisi534 – 5341S → A: No effect. 2 Publications
    Mutagenesisi609 – 6091S → A: No effect. 2 Publications
    Mutagenesisi647 – 6471S → A: No effect. 2 Publications
    Mutagenesisi722 – 7221S → A: No effect. 2 Publications
    Mutagenesisi759 – 7591S → A: No effect. 2 Publications
    Mutagenesisi797 – 7971S → A: No effect. 2 Publications
    Mutagenesisi951 – 9511S → A: No effect. 2 Publications
    Mutagenesisi1027 – 10271S → A: No effect. 2 Publications
    Mutagenesisi1065 – 10651S → A: Reduced activity. 2 Publications
    Mutagenesisi1189 – 11891S → A: No effect. 2 Publications
    Mutagenesisi1273 – 12731S → A: No effect. 2 Publications
    Mutagenesisi1651 – 16544RQRR → AAAA: Processing by furin-like convertase abolished. 1 Publication
    Mutagenesisi1744 – 17441V → L: NICD processing severely reduced. 1 Publication
    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. 3 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. 3 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. 3 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)2 Publications
    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

    ArrayExpressiQ01705.
    BgeeiQ01705.
    CleanExiMM_NOTCH1.
    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 – 4583
    Beta strandi462 – 4643
    Beta strandi466 – 4694
    Beta strandi471 – 4777
    Turni484 – 4874
    Helixi1921 – 19277
    Helixi1931 – 19399
    Helixi1954 – 19618
    Helixi1964 – 19729
    Helixi1975 – 19773
    Helixi1988 – 19958
    Helixi2000 – 20067
    Helixi2021 – 20277
    Helixi2031 – 20399
    Helixi2054 – 20618
    Helixi2064 – 20729
    Helixi2087 – 20937
    Helixi2097 – 21037

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1726 – 174621HelicalSequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00730000110611.
    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

    MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG     50
    AFVGQRCQDS NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT 100
    PLDNACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA 150
    NGGQCLPFES SYICRCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG 200
    SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA 250
    GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 300
    LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC 350
    HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC 400
    PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE 450
    IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL 500
    HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG AKCLDGPNTY 550
    TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC 600
    ETNINECHSQ PCRHGGTCQD RDNSYLCLCL KGTTGPNCEI NLDDCASNPC 650
    DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF 700
    TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC 750
    DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC 800
    LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY 850
    ESFSCVCPTG WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 900
    GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA 950
    SNPCQNGANC TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD 1000
    GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG 1050
    YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ YHCECRSGWT GVNCDVLSVS 1100
    CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS YCEDEVDECS 1150
    PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 1200
    LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG 1250
    YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT 1300
    GRRCESVING CRGKPCKNGG VCAVASNTAR GFICRCPAGF EGATCENDAR 1350
    TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ 1400
    GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE 1450
    LPECQVDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 1500
    SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN 1550
    SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL 1600
    HTNVVFKRDA QGQQMIFPYY GHEEELRKHP IKRSTVGWAT SSLLPGTSGG 1650
    RQRRELDPMD IRGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG 1700
    SLNIPYKIEA VKSEPVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR 1750
    RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 1800
    NEWGDEDLET KKFRFEEPVV LPDLSDQTDH RQWTQQHLDA ADLRMSAMAP 1850
    TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI 1900
    SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM 1950
    GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM 2000
    LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK 2050
    EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 2100
    RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK 2150
    PSTKGLACGS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL 2200
    SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG 2250
    GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW 2300
    LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHSMMGPL HSSLSTNTLS 2350
    PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ LQPQNLQPPS QPHLSVSSAA 2400
    NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP 2450
    MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS 2500
    PHSNISDWSE GISSPPTTMP SQITHIPEAF K 2531
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00730000110611.
    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_196520. Pre-NOTCH Transcription and Translation.
    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.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q01705.
    Bgeei Q01705.
    CleanExi MM_NOTCH1.
    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

    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: October 1, 2014
    This is version 168 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