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P07207

- NOTCH_DROME

UniProt

P07207 - NOTCH_DROME

Protein

Neurogenic locus Notch protein

Gene

N

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 3 (02 Nov 2001)
      Previous versions | rss
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    Functioni

    Signaling protein, which regulates, with both positive and negative signals, the differentiation of at least central and peripheral nervous system and eye, wing disk, oogenesis, segmental appendages such as antennae and legs, and muscles, through lateral inhibition or induction. Functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination. Upon ligand activation, and releasing from the cell membrane, the Notch intracellular domain (NICD) forms a transcriptional activator complex with Su(H) (Suppressor of hairless) and activates genes of the E(spl) complex. Essential for proper differentiation of ectoderm. Fringe (fng) acts in the Golgi to determine the type of O-linked fucose on the EGF modules in N, altering the ability of N to bind with Delta (Dl). O-fut1 also has a role in modulating the interaction. Rumi acts in the endoplasmic reticulum to glucosylate the EGF modules in N, this is required for correct folding and cleavage of N.2 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. chromatin binding Source: FlyBase
    3. protein binding Source: UniProtKB
    4. receptor activity Source: FlyBase
    5. transmembrane signaling receptor activity Source: FlyBase

    GO - Biological processi

    1. actin filament organization Source: FlyBase
    2. anterior/posterior pattern specification Source: FlyBase
    3. asymmetric cell division Source: FlyBase
    4. axon guidance Source: FlyBase
    5. border follicle cell migration Source: FlyBase
    6. cell adhesion Source: FlyBase
    7. cell fate specification Source: FlyBase
    8. chaeta development Source: FlyBase
    9. chaeta morphogenesis Source: FlyBase
    10. compound eye cone cell fate commitment Source: FlyBase
    11. compound eye development Source: FlyBase
    12. compound eye morphogenesis Source: FlyBase
    13. compound eye retinal cell programmed cell death Source: FlyBase
    14. crystal cell differentiation Source: FlyBase
    15. determination of adult lifespan Source: FlyBase
    16. dorsal/ventral lineage restriction, imaginal disc Source: FlyBase
    17. dorsal/ventral pattern formation, imaginal disc Source: FlyBase
    18. dorsal appendage formation Source: FlyBase
    19. dorsal closure Source: FlyBase
    20. ectoderm development Source: FlyBase
    21. embryonic crystal cell differentiation Source: FlyBase
    22. embryonic hemopoiesis Source: FlyBase
    23. epithelial cell proliferation involved in Malpighian tubule morphogenesis Source: FlyBase
    24. epithelial cell type specification, open tracheal system Source: FlyBase
    25. establishment of ommatidial planar polarity Source: FlyBase
    26. eye-antennal disc development Source: FlyBase
    27. foregut morphogenesis Source: FlyBase
    28. formation of a compartment boundary Source: FlyBase
    29. germarium-derived egg chamber formation Source: FlyBase
    30. germarium-derived female germ-line cyst encapsulation Source: FlyBase
    31. germ-line stem cell maintenance Source: FlyBase
    32. glial cell differentiation Source: FlyBase
    33. glial cell fate determination Source: FlyBase
    34. glial cell migration Source: FlyBase
    35. hemocyte proliferation Source: FlyBase
    36. heterophilic cell-cell adhesion Source: FlyBase
    37. I-kappaB phosphorylation Source: FlyBase
    38. imaginal disc-derived leg joint morphogenesis Source: FlyBase
    39. imaginal disc-derived leg segmentation Source: FlyBase
    40. imaginal disc-derived male genitalia morphogenesis Source: FlyBase
    41. imaginal disc-derived wing margin morphogenesis Source: FlyBase
    42. imaginal disc-derived wing morphogenesis Source: FlyBase
    43. imaginal disc-derived wing vein specification Source: FlyBase
    44. imaginal disc growth Source: FlyBase
    45. imaginal disc pattern formation Source: FlyBase
    46. intestinal stem cell homeostasis Source: FlyBase
    47. lamellocyte differentiation Source: FlyBase
    48. larval lymph gland hemopoiesis Source: FlyBase
    49. lateral inhibition Source: FlyBase
    50. leg disc morphogenesis Source: FlyBase
    51. long-term memory Source: FlyBase
    52. lymph gland crystal cell differentiation Source: FlyBase
    53. lymph gland development Source: FlyBase
    54. Malpighian tubule tip cell differentiation Source: FlyBase
    55. mesoderm development Source: FlyBase
    56. morphogenesis of follicular epithelium Source: FlyBase
    57. motor neuron axon guidance Source: FlyBase
    58. muscle cell fate determination Source: FlyBase
    59. negative regulation of compound eye photoreceptor development Source: FlyBase
    60. negative regulation of fusion cell fate specification Source: FlyBase
    61. negative regulation of gene expression Source: FlyBase
    62. negative regulation of JNK cascade Source: FlyBase
    63. negative regulation of neurogenesis Source: FlyBase
    64. negative regulation of terminal cell fate specification, open tracheal system Source: FlyBase
    65. negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
    66. neuroblast fate determination Source: FlyBase
    67. neurological system process Source: FlyBase
    68. neuron development Source: FlyBase
    69. Notch signaling pathway Source: UniProtKB-KW
    70. oocyte anterior/posterior axis specification Source: FlyBase
    71. oocyte localization involved in germarium-derived egg chamber formation Source: FlyBase
    72. oogenesis Source: FlyBase
    73. open tracheal system development Source: FlyBase
    74. ovarian follicle cell development Source: FlyBase
    75. ovarian follicle cell migration Source: FlyBase
    76. ovarian follicle cell stalk formation Source: FlyBase
    77. peripheral nervous system development Source: FlyBase
    78. positive regulation of cell proliferation Source: FlyBase
    79. positive regulation of G1/S transition of mitotic cell cycle Source: FlyBase
    80. positive regulation of Notch signaling pathway Source: FlyBase
    81. positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
    82. R1/R6 cell differentiation Source: FlyBase
    83. R3/R4 cell fate commitment Source: FlyBase
    84. R7 cell differentiation Source: FlyBase
    85. R8 cell development Source: FlyBase
    86. R8 cell differentiation Source: FlyBase
    87. R8 cell fate commitment Source: FlyBase
    88. regulation of cardioblast cell fate specification Source: FlyBase
    89. regulation of cell differentiation Source: FlyBase
    90. regulation of crystal cell differentiation Source: FlyBase
    91. regulation of filopodium assembly Source: FlyBase
    92. regulation of growth Source: FlyBase
    93. regulation of mitotic cell cycle Source: FlyBase
    94. regulation of neurogenesis Source: FlyBase
    95. regulation of R8 cell spacing in compound eye Source: FlyBase
    96. response to symbiont Source: FlyBase
    97. retinal cell programmed cell death Source: FlyBase
    98. second mitotic wave involved in compound eye morphogenesis Source: FlyBase
    99. sensory organ development Source: FlyBase
    100. skeletal muscle tissue development Source: FlyBase
    101. stem cell differentiation Source: FlyBase
    102. transcription, DNA-templated Source: UniProtKB-KW
    103. ventral cord development Source: FlyBase
    104. wing disc dorsal/ventral pattern formation Source: FlyBase
    105. wing disc pattern formation Source: FlyBase
    106. wing disc proximal/distal pattern formation Source: FlyBase

    Keywords - Molecular functioni

    Activator, Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation, Neurogenesis, Notch signaling pathway, Oogenesis, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    REACT_180769. Pre-NOTCH Processing in Golgi.
    REACT_180784. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_184296. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_184298. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_184380. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_184382. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_184383. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_212548. Signaling by NOTCH4.
    REACT_218930. Signaling by NOTCH3.
    REACT_221100. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
    SignaLinkiP07207.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurogenic locus Notch protein
    Cleaved into the following chain:
    Gene namesi
    Name:N
    ORF Names:CG3936
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0004647. N.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome 1 Publication
    Note: Transported to early endosomes by O-fut1.
    Chain Processed neurogenic locus Notch protein : Nucleus
    Note: Upon activation and S3 cleavage, it is released from the cell membrane and enters into the nucleus in conjunction with Su(H).

    GO - Cellular componenti

    1. adherens junction Source: FlyBase
    2. cell surface Source: FlyBase
    3. cytoplasm Source: FlyBase
    4. cytosol Source: Reactome
    5. endocytic vesicle Source: FlyBase
    6. endoplasmic reticulum lumen Source: Reactome
    7. endosome Source: FlyBase
    8. Golgi lumen Source: Reactome
    9. integral component of membrane Source: FlyBase
    10. intracellular Source: FlyBase
    11. nucleoplasm Source: Reactome
    12. nucleus Source: FlyBase
    13. plasma membrane Source: FlyBase
    14. protein complex Source: FlyBase
    15. subapical complex Source: FlyBase

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi739 – 7391C → Y in mcd5; induces loss of microchaetae sensory precursors.
    Mutagenesisi2060 – 20601A → V in su42c; deltex-like mutation that induces outstreched wings and variability-fused ocelli.
    Mutagenesisi2328 – 23281Y → F: Abolishes interaction with Nedd4 and reduces ubiquitination. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 2703Processed neurogenic locus Notch proteinPRO_0000296234
    Signal peptidei1 – 5252Sequence AnalysisAdd
    BLAST
    Chaini53 – 27032651Neurogenic locus Notch proteinPRO_0000007673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 73By similarity
    Disulfide bondi67 ↔ 83By similarity
    Disulfide bondi85 ↔ 94By similarity
    Disulfide bondi100 ↔ 111By similarity
    Disulfide bondi105 ↔ 124By similarity
    Disulfide bondi126 ↔ 135By similarity
    Disulfide bondi143 ↔ 154By similarity
    Disulfide bondi148 ↔ 164By similarity
    Disulfide bondi166 ↔ 175By similarity
    Disulfide bondi181 ↔ 192By similarity
    Disulfide bondi186 ↔ 203By similarity
    Disulfide bondi205 ↔ 214By similarity
    Disulfide bondi221 ↔ 232By similarity
    Disulfide bondi226 ↔ 241By similarity
    Disulfide bondi243 ↔ 252By similarity
    Disulfide bondi259 ↔ 270By similarity
    Disulfide bondi264 ↔ 279By similarity
    Disulfide bondi281 ↔ 290By similarity
    Disulfide bondi297 ↔ 308By similarity
    Disulfide bondi302 ↔ 317By similarity
    Disulfide bondi319 ↔ 328By similarity
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi335 ↔ 349By similarity
    Disulfide bondi343 ↔ 358By similarity
    Disulfide bondi360 ↔ 369By similarity
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 387By similarity
    Disulfide bondi381 ↔ 396By similarity
    Disulfide bondi398 ↔ 407By similarity
    Disulfide bondi413 ↔ 424By similarity
    Disulfide bondi418 ↔ 435By similarity
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi437 ↔ 446By similarity
    Disulfide bondi453 ↔ 465By similarity
    Disulfide bondi459 ↔ 474By similarity
    Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi476 ↔ 485By similarity
    Disulfide bondi492 ↔ 503By similarity
    Disulfide bondi497 ↔ 512By similarity
    Disulfide bondi514 ↔ 523By similarity
    Disulfide bondi530 ↔ 541By similarity
    Disulfide bondi535 ↔ 550By similarity
    Disulfide bondi552 ↔ 561By similarity
    Disulfide bondi568 ↔ 579By similarity
    Disulfide bondi573 ↔ 588By similarity
    Disulfide bondi590 ↔ 599By similarity
    Disulfide bondi606 ↔ 616By similarity
    Disulfide bondi611 ↔ 625By similarity
    Disulfide bondi627 ↔ 636By similarity
    Disulfide bondi643 ↔ 654By similarity
    Disulfide bondi648 ↔ 663By similarity
    Disulfide bondi665 ↔ 674By similarity
    Disulfide bondi681 ↔ 692By similarity
    Disulfide bondi686 ↔ 701By similarity
    Disulfide bondi703 ↔ 712By similarity
    Disulfide bondi719 ↔ 730By similarity
    Disulfide bondi724 ↔ 739By similarity
    Disulfide bondi741 ↔ 750By similarity
    Disulfide bondi757 ↔ 768By similarity
    Disulfide bondi762 ↔ 777By similarity
    Disulfide bondi779 ↔ 788By similarity
    Disulfide bondi795 ↔ 806By similarity
    Disulfide bondi800 ↔ 815By similarity
    Disulfide bondi817 ↔ 826By similarity
    Disulfide bondi833 ↔ 844By similarity
    Disulfide bondi838 ↔ 853By similarity
    Disulfide bondi855 ↔ 864By similarity
    Disulfide bondi871 ↔ 882By similarity
    Disulfide bondi876 ↔ 893By similarity
    Disulfide bondi895 ↔ 904By similarity
    Disulfide bondi911 ↔ 923By similarity
    Disulfide bondi917 ↔ 932By similarity
    Disulfide bondi934 ↔ 943By similarity
    Disulfide bondi950 ↔ 961By similarity
    Disulfide bondi955 ↔ 970By similarity
    Disulfide bondi972 ↔ 981By similarity
    Disulfide bondi988 ↔ 999By similarity
    Disulfide bondi993 ↔ 1008By similarity
    Disulfide bondi1010 ↔ 1019By similarity
    Disulfide bondi1026 ↔ 1037By similarity
    Disulfide bondi1031 ↔ 1046By similarity
    Glycosylationi1045 – 10451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1048 ↔ 1057By similarity
    Disulfide bondi1064 ↔ 1075By similarity
    Disulfide bondi1069 ↔ 1084By similarity
    Disulfide bondi1086 ↔ 1095By similarity
    Disulfide bondi1102 ↔ 1113By similarity
    Disulfide bondi1107 ↔ 1122By similarity
    Disulfide bondi1124 ↔ 1133By similarity
    Disulfide bondi1140 ↔ 1160By similarity
    Disulfide bondi1155 ↔ 1169By similarity
    Glycosylationi1157 – 11571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1171 ↔ 1180By similarity
    Disulfide bondi1187 ↔ 1198By similarity
    Disulfide bondi1192 ↔ 1207By similarity
    Disulfide bondi1209 ↔ 1218By similarity
    Disulfide bondi1225 ↔ 1236By similarity
    Disulfide bondi1230 ↔ 1245By similarity
    Glycosylationi1242 – 12421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1247 ↔ 1256By similarity
    Disulfide bondi1263 ↔ 1274By similarity
    Disulfide bondi1268 ↔ 1283By similarity
    Glycosylationi1271 – 12711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1285 ↔ 1294By similarity
    Disulfide bondi1301 ↔ 1314By similarity
    Disulfide bondi1306 ↔ 1323By similarity
    Disulfide bondi1325 ↔ 1334By similarity
    Disulfide bondi1341 ↔ 1352By similarity
    Disulfide bondi1346 ↔ 1361By similarity
    Disulfide bondi1363 ↔ 1372By similarity
    Disulfide bondi1379 ↔ 1389By similarity
    Disulfide bondi1384 ↔ 1400By similarity
    Disulfide bondi1402 ↔ 1411By similarity
    Disulfide bondi1419 ↔ 1430By similarity
    Disulfide bondi1424 ↔ 1439By similarity
    Disulfide bondi1441 ↔ 1450By similarity
    Disulfide bondi1482 ↔ 1505By similarity
    Disulfide bondi1487 ↔ 1500By similarity
    Disulfide bondi1496 ↔ 1512By similarity
    Glycosylationi1521 – 15211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1522 ↔ 1545By similarity
    Disulfide bondi1527 ↔ 1540By similarity
    Disulfide bondi1536 ↔ 1552By similarity
    Disulfide bondi1559 ↔ 1585By similarity
    Disulfide bondi1567 ↔ 1580By similarity
    Disulfide bondi1576 ↔ 1592By similarity
    Glycosylationi1594 – 15941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1627 – 16271N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2447 – 24471Phosphoserine1 Publication

    Post-translational modificationi

    Upon binding its ligands such as Delta or Serrate, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain. S2 cleavage is probably mediated by Kuz. It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane. S3 cleavage requires Psn.
    O-glycosylated. O-fucosylated by O-fut1 in the EGF repeat doamin which inhibits both Serrate/Ser- and Delta/Dl-binding.1 Publication
    Ubiquitinated by Nedd4; which promotes ligand-independent endocytosis and proteasomal degradation. May also be ubiquitinated by Su(dx).1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP07207.
    PRIDEiP07207.

    Expressioni

    Gene expression databases

    BgeeiP07207.

    Interactioni

    Subunit structurei

    Homomer. Interacts with Su(H) when activated. Interacts with Dx via its ANK repeats. Interacts with Dl via the EGF repeats and the Dl EGF repeats. Interacts with Nedd4 and Su(dx). Interacts with O-fut1; the interaction glycosylates N and transports N to early endosomes.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cnoQ242793EBI-103438,EBI-868783
    DlP100412EBI-103438,EBI-115346
    Su(H)P281594EBI-103438,EBI-92180

    Protein-protein interaction databases

    BioGridi57823. 138 interactions.
    DIPiDIP-5N.
    IntActiP07207. 8 interactions.
    MINTiMINT-133064.

    Structurei

    Secondary structure

    1
    2703
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1930 – 195021
    Helixi1954 – 19607
    Helixi1964 – 19729
    Helixi1987 – 19937
    Helixi1997 – 20048
    Helixi2021 – 20277
    Helixi2033 – 20397
    Helixi2054 – 20607
    Helixi2064 – 20729
    Helixi2087 – 20937
    Helixi2097 – 21059
    Helixi2120 – 21267
    Helixi2130 – 21367

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OT8X-ray2.00A/B/C1902-2139[»]
    2JMFNMR-B2318-2333[»]
    ProteinModelPortaliP07207.
    SMRiP07207. Positions 46-1452, 1482-1726, 1862-2198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07207.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini53 – 17451693ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1767 – 2703937CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1746 – 176621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 9538EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini96 – 13641EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini139 – 17638EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini177 – 21539EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 25337EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini255 – 29137EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini293 – 32937EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini331 – 37040EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini372 – 40837EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini409 – 44739EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini449 – 48638EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 52437EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini526 – 56237EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 60037EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini602 – 63736EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini639 – 67537EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini677 – 71337EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini715 – 75137EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini753 – 78937EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 82737EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini829 – 86537EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini867 – 90539EGF-like 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 94438EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini946 – 98237EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini984 – 102037EGF-like 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini1022 – 105837EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1060 – 109637EGF-like 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini1098 – 113437EGF-like 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini1136 – 118146EGF-like 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini1183 – 121937EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1221 – 125737EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1259 – 129537EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1297 – 133539EGF-like 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini1337 – 137337EGF-like 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini1375 – 141238EGF-like 35PROSITE-ProRule annotationAdd
    BLAST
    Domaini1415 – 145137EGF-like 36PROSITE-ProRule annotationAdd
    BLAST
    Repeati1482 – 152140LNR 1Add
    BLAST
    Repeati1522 – 155736LNR 2Add
    BLAST
    Repeati1559 – 159941LNR 3Add
    BLAST
    Repeati1901 – 194545ANK 1Add
    BLAST
    Repeati1950 – 197930ANK 2Add
    BLAST
    Repeati1983 – 201331ANK 3Add
    BLAST
    Repeati2017 – 204630ANK 4Add
    BLAST
    Repeati2050 – 207930ANK 5Add
    BLAST
    Repeati2083 – 211230ANK 6Add
    BLAST
    Repeati2116 – 213924ANK 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2325 – 23284Interaction with Nedd4

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2486 – 249813Poly-GlyAdd
    BLAST
    Compositional biasi2538 – 256831Poly-Gln (OPA repeat)Add
    BLAST
    Compositional biasi2664 – 26674Poly-Ser

    Domaini

    Crystal structure of the ANK repeat domain shows that there are 7 repeats and the stabilizing C-terminal repeat enhances the protein stability by extending the ankyrin domain.1 Publication

    Sequence similaritiesi

    Belongs to the NOTCH family.Curated
    Contains 7 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.
    InParanoidiP07207.
    KOiK02599.
    OMAiGHYICSC.
    OrthoDBiEOG7992RD.
    PhylomeDBiP07207.

    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.
    IPR000800. Notch_dom.
    IPR010660. Notch_NOD_dom.
    IPR011656. Notch_NODP_dom.
    [Graphical view]
    PfamiPF00023. Ank. 5 hits.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 24 hits.
    PF07645. EGF_CA. 4 hits.
    PF06816. NOD. 1 hit.
    PF07684. NODP. 1 hit.
    PF00066. Notch. 3 hits.
    [Graphical view]
    PIRSFiPIRSF002279. Notch. 1 hit.
    PRINTSiPR01452. LNOTCHREPEAT.
    SMARTiSM00248. ANK. 7 hits.
    SM00181. EGF. 12 hits.
    SM00179. EGF_CA. 24 hits.
    SM00004. NL. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF57184. SSF57184. 5 hits.
    SSF90193. SSF90193. 3 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS00010. ASX_HYDROXYL. 22 hits.
    PS00022. EGF_1. 34 hits.
    PS01186. EGF_2. 28 hits.
    PS50026. EGF_3. 36 hits.
    PS01187. EGF_CA. 21 hits.
    PS50258. LNR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07207-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV     50
    RGTDTALVAA SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC 100
    NSMRCQNGGT CQVTFRNGRP GISCKCPLGF DESLCEIAVP NACDHVTCLN 150
    GGTCQLKTLE EYTCACANGY TGERCETKNL CASSPCRNGA TCTALAGSSS 200
    FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ CMCPTGYTGK 250
    DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH 300
    LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT 350
    NTHGSYSCIC VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK 400
    GKTGLLCHLD DACTSNPCHA DAICDTSPIN GSYACSCATG YKGVDCSEDI 450
    DECDQGSPCE HNGICVNTPG SYRCNCSQGF TGPRCETNIN ECESHPCQNE 500
    GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT CHDKINGFKC 550
    SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE 600
    ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF 650
    DGHCQDRVGS YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK 700
    CQCVPGFTGQ HCEKNVDECI SSPCANNGVC IDQVNGYKCE CPRGFYDAHC 750
    LSDVDECASN PCVNEGRCED GINEFICHCP PGYTGKRCEL DIDECSSNPC 800
    QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN GGTCIDKVNG 850
    YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT 900
    GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC 950
    ASFPCQNGGT CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS 1000
    QYVNSYTCTC PLGFSGINCQ TNDEDCTESS CLNGGSCIDG INGYNCSCLA 1050
    GYSGANCQYK LNKCDSNPCL NGATCHEQNN EYTCHCPSGF TGKQCSEYVD 1100
    WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC QDAADRKGLS 1150
    LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD 1200
    LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG 1250
    TMGIICEINK DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE 1300
    CLSNPCSNAG TLDCVQLVNN YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG 1350
    NCNIRQSGHH CICNNGFYGK NCELSGQDCD SNPCRVGNCV VADEGFGYRC 1400
    ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL CPSKWKGKRC 1450
    DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC 1500
    NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH 1550
    DCERKLKSCD SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV 1600
    LAEGAMSVVM LMNVEAFREI QAQFLRNMSH MLRTTVRLKK DALGHDIIIN 1650
    WKDNVRVPEI EDTDFARKNK ILYTQQVHQT GIQIYLEIDN RKCTECFTHA 1700
    VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP ANVKYVITGI 1750
    ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM 1800
    RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY 1850
    ASDHTMVSEY EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP 1900
    CGLTPLMIAA VRGGGLDTGE DIENNEDSTA QVISDLLAQG AELNATMDKT 1950
    GETSLHLAAR FARADAAKRL LDAGADANCQ DNTGRTPLHA AVAADAMGVF 2000
    QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA DADINAADNS 2050
    GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC 2100
    KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT 2150
    PQAMIGSPPP GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA 2200
    AKKAKLIEGS PDNGLDATGS LRRKASSKKT SAASKKAANL NGLNPGQLTG 2250
    GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH ELEGSPVGVG MGGNLPSPYD 2300
    TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS LQGNGLDMIK 2350
    LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG 2400
    AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT 2450
    SPTHIQAMRH ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ 2500
    NSPVSLGIIS PTGSDMGIML APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ 2550
    HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD LNGFCGSPDS FHSGQMNPPS 2600
    IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH TPQHLVQTLD 2650
    SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA 2700
    IYI 2703
    Length:2,703
    Mass (Da):288,853
    Last modified:November 2, 2001 - v3
    Checksum:i0EAE23F426FECD7B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91R → G in CAB37610. (PubMed:10731137)Curated
    Sequence conflicti84 – 841A → G in CAB37610. (PubMed:10731137)Curated
    Sequence conflicti103 – 1031M → I in AAB59220. (PubMed:3935325)Curated
    Sequence conflicti119 – 1191R → H in AAA28725. (PubMed:3097517)Curated
    Sequence conflicti231 – 2311T → I in AAB59220. (PubMed:3935325)Curated
    Sequence conflicti240 – 2401Q → R in CAB37610. (PubMed:10731137)Curated
    Sequence conflicti267 – 2671G → A in AAB59220. (PubMed:3935325)Curated
    Sequence conflicti1561 – 15611S → T in AAB59220. (PubMed:3935325)Curated
    Sequence conflicti1561 – 15611S → T in AAA28725. (PubMed:3097517)Curated
    Sequence conflicti2257 – 22571G → S in AAA28725. (PubMed:3097517)Curated
    Sequence conflicti2577 – 25771A → E in AAA74496. (PubMed:2981631)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti578 – 5781I → T.
    Natural varianti2044 – 20441I → R.
    Natural varianti2265 – 22651A → V.
    Natural varianti2407 – 24071H → R.
    Natural varianti2445 – 24451R → L.
    Natural varianti2568 – 25681Q → QQQQQ.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16152
    , M16153, M16149, M16150, M16151 Genomic DNA. Translation: AAB59220.1.
    K03508, M13689, K03507 Genomic DNA. Translation: AAA28725.1.
    AE014298 Genomic DNA. Translation: AAF45848.2.
    AL035436, AL035395 Genomic DNA. Translation: CAB37610.1.
    M16025 Genomic DNA. Translation: AAA28726.1.
    M12175 Genomic DNA. Translation: AAA74496.1.
    PIRiA24420.
    RefSeqiNP_001245510.1. NM_001258581.1.
    NP_476859.2. NM_057511.3.
    UniGeneiDm.4702.

    Genome annotation databases

    EnsemblMetazoaiFBtr0070507; FBpp0070483; FBgn0004647.
    FBtr0304659; FBpp0293201; FBgn0004647.
    GeneIDi31293.
    KEGGidme:Dmel_CG3936.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16152
    , M16153 , M16149 , M16150 , M16151 Genomic DNA. Translation: AAB59220.1 .
    K03508 , M13689 , K03507 Genomic DNA. Translation: AAA28725.1 .
    AE014298 Genomic DNA. Translation: AAF45848.2 .
    AL035436 , AL035395 Genomic DNA. Translation: CAB37610.1 .
    M16025 Genomic DNA. Translation: AAA28726.1 .
    M12175 Genomic DNA. Translation: AAA74496.1 .
    PIRi A24420.
    RefSeqi NP_001245510.1. NM_001258581.1.
    NP_476859.2. NM_057511.3.
    UniGenei Dm.4702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OT8 X-ray 2.00 A/B/C 1902-2139 [» ]
    2JMF NMR - B 2318-2333 [» ]
    ProteinModelPortali P07207.
    SMRi P07207. Positions 46-1452, 1482-1726, 1862-2198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 57823. 138 interactions.
    DIPi DIP-5N.
    IntActi P07207. 8 interactions.
    MINTi MINT-133064.

    Proteomic databases

    PaxDbi P07207.
    PRIDEi P07207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070507 ; FBpp0070483 ; FBgn0004647 .
    FBtr0304659 ; FBpp0293201 ; FBgn0004647 .
    GeneIDi 31293.
    KEGGi dme:Dmel_CG3936.

    Organism-specific databases

    CTDi 109544.
    FlyBasei FBgn0004647. N.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00730000110611.
    InParanoidi P07207.
    KOi K02599.
    OMAi GHYICSC.
    OrthoDBi EOG7992RD.
    PhylomeDBi P07207.

    Enzyme and pathway databases

    Reactomei REACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    REACT_180769. Pre-NOTCH Processing in Golgi.
    REACT_180784. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_184296. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
    REACT_184298. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_184380. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
    REACT_184382. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_184383. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_212548. Signaling by NOTCH4.
    REACT_218930. Signaling by NOTCH3.
    REACT_221100. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
    SignaLinki P07207.

    Miscellaneous databases

    EvolutionaryTracei P07207.
    GenomeRNAii 31293.
    NextBioi 772898.
    PROi P07207.

    Gene expression databases

    Bgeei P07207.

    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.
    IPR000800. Notch_dom.
    IPR010660. Notch_NOD_dom.
    IPR011656. Notch_NODP_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 5 hits.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 24 hits.
    PF07645. EGF_CA. 4 hits.
    PF06816. NOD. 1 hit.
    PF07684. NODP. 1 hit.
    PF00066. Notch. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002279. Notch. 1 hit.
    PRINTSi PR01452. LNOTCHREPEAT.
    SMARTi SM00248. ANK. 7 hits.
    SM00181. EGF. 12 hits.
    SM00179. EGF_CA. 24 hits.
    SM00004. NL. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF57184. SSF57184. 5 hits.
    SSF90193. SSF90193. 3 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS00010. ASX_HYDROXYL. 22 hits.
    PS00022. EGF_1. 34 hits.
    PS01186. EGF_2. 28 hits.
    PS50026. EGF_3. 36 hits.
    PS01187. EGF_CA. 21 hits.
    PS50258. LNR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats."
      Wharton K.A., Johansen K.M., Xu T., Artavanis-Tsakonas S.
      Cell 43:567-581(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Oregon-R.
      Tissue: Embryo.
    2. "Sequence of the notch locus of Drosophila melanogaster: relationship of the encoded protein to mammalian clotting and growth factors."
      Kidd S., Kelley M.R., Young M.W.
      Mol. Cell. Biol. 6:3094-3108(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S and Oregon-R.
      Tissue: Embryo.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Oregon-R.
    6. "Restriction of P-element insertions at the Notch locus of Drosophila melanogaster."
      Kelley M.R., Kidd S., Berg R.L., Young M.W.
      Mol. Cell. Biol. 7:1545-1548(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
    7. "opa: a novel family of transcribed repeats shared by the Notch locus and other developmentally regulated loci in D. melanogaster."
      Wharton K.A., Yedvobnick B., Finnerty V.G., Artavanis-Tsakonas S.
      Cell 40:55-62(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2611.
      Strain: Oregon-R.
      Tissue: Embryo.
    8. "Hypervariability of simple sequences as a general source for polymorphic DNA markers."
      Tautz D.
      Nucleic Acids Res. 17:6463-6471(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2604.
    9. "Cytosolic interaction between deltex and Notch ankyrin repeats implicates deltex in the Notch signaling pathway."
      Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.
      Development 120:473-481(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DX, MUTANT SU42C.
    10. "Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats."
      Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M., Artavanis-Tsakonas S.
      Development 121:2633-2644(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DX.
    11. "Presenilin is required for activity and nuclear access of Notch in Drosophila."
      Struhl G., Greenwald I.
      Nature 398:522-525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: S3 CLEAVAGE BY PSN.
    12. "Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants."
      Ye Y., Lukinova N., Fortini M.E.
      Nature 398:525-529(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: S3 CLEAVAGE BY PSN.
    13. "Glycosyltransferase activity of Fringe modulates Notch-Delta interactions."
      Bruckner K., Perez L., Clausen H., Cohen S.
      Nature 406:411-415(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DL.
    14. "Novel Notch alleles reveal a Deltex-dependent pathway repressing neural fate."
      Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C., Heitzler P.
      Curr. Biol. 11:1729-1738(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANT MCD5.
    15. "Kuzbanian-mediated cleavage of Drosophila Notch."
      Lieber T., Kidd S., Young M.W.
      Genes Dev. 16:209-221(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: S2 CLEAVAGE BY KUZ.
    16. "General outlines of the molecular genetics of the Notch signalling pathway in Drosophila melanogaster: a review."
      Portin P.
      Hereditas 136:89-96(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe."
      Okajima T., Xu A., Irvine K.D.
      J. Biol. Chem. 278:42340-42345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, LIGAND-BINDING.
    18. "Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation."
      Sakata T., Sakaguchi H., Tsuda L., Higashitani A., Aigaki T., Matsuno K., Hayashi S.
      Curr. Biol. 14:2228-2236(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4, UBIQUITINATION, MUTAGENESIS OF TYR-2328.
    19. "Regulation of notch endosomal sorting and signaling by Drosophila Nedd4 family proteins."
      Wilkin M.B., Carbery A.-M., Fostier M., Aslam H., Mazaleyrat S.L., Higgs J., Myat A., Evans D.A.P., Cornell M., Baron M.
      Curr. Biol. 14:2237-2244(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SU(DX).
    20. "The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila."
      Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S., Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.
      Development 134:1347-1356(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH O-FUT1.
    21. "Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling."
      Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A., Pan H., Haltiwanger R.S., Bellen H.J.
      Cell 132:247-258(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2447, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.
    23. "Structure and stability of the ankyrin domain of the Drosophila Notch receptor."
      Zweifel M.E., Leahy D.J., Hughson F.M., Barrick D.
      Protein Sci. 12:2622-2632(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1901-2139, DOMAIN ANK REPEATS, SUBUNIT.

    Entry informationi

    Entry nameiNOTCH_DROME
    AccessioniPrimary (citable) accession number: P07207
    Secondary accession number(s): O97458, P04154, Q9W4T8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: November 2, 2001
    Last modified: October 1, 2014
    This is version 188 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    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