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P07207

- NOTCH_DROME

UniProt

P07207 - NOTCH_DROME

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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

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. receptor activity Source: FlyBase
  4. 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 via plasma membrane cell adhesion molecules 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
Complete GO annotation...

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_218930. Signaling by NOTCH3.
REACT_221100. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_239279. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_271460. Signaling by NOTCH4.
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).

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini53 – 17451693ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1746 – 176621HelicalSequence AnalysisAdd
BLAST
Topological domaini1767 – 2703937CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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.
ExpressionAtlasiP07207. differential.

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 – 195021Combined sources
Helixi1954 – 19607Combined sources
Helixi1964 – 19729Combined sources
Helixi1987 – 19937Combined sources
Helixi1997 – 20048Combined sources
Helixi2021 – 20277Combined sources
Helixi2033 – 20397Combined sources
Helixi2054 – 20607Combined sources
Helixi2064 – 20729Combined sources
Helixi2087 – 20937Combined sources
Helixi2097 – 21059Combined sources
Helixi2120 – 21267Combined sources
Helixi2130 – 21367Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT8X-ray2.00A/B/C1902-2139[»]
2JMFNMR-B2318-2333[»]
ProteinModelPortaliP07207.
SMRiP07207. Positions 105-1450, 1482-1726, 1871-2198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07207.

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.
GeneTreeiENSGT00760000118786.
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

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        10         20         30         40         50
MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV
60 70 80 90 100
RGTDTALVAA SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC
110 120 130 140 150
NSMRCQNGGT CQVTFRNGRP GISCKCPLGF DESLCEIAVP NACDHVTCLN
160 170 180 190 200
GGTCQLKTLE EYTCACANGY TGERCETKNL CASSPCRNGA TCTALAGSSS
210 220 230 240 250
FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ CMCPTGYTGK
260 270 280 290 300
DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH
310 320 330 340 350
LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT
360 370 380 390 400
NTHGSYSCIC VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK
410 420 430 440 450
GKTGLLCHLD DACTSNPCHA DAICDTSPIN GSYACSCATG YKGVDCSEDI
460 470 480 490 500
DECDQGSPCE HNGICVNTPG SYRCNCSQGF TGPRCETNIN ECESHPCQNE
510 520 530 540 550
GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT CHDKINGFKC
560 570 580 590 600
SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE
610 620 630 640 650
ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF
660 670 680 690 700
DGHCQDRVGS YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK
710 720 730 740 750
CQCVPGFTGQ HCEKNVDECI SSPCANNGVC IDQVNGYKCE CPRGFYDAHC
760 770 780 790 800
LSDVDECASN PCVNEGRCED GINEFICHCP PGYTGKRCEL DIDECSSNPC
810 820 830 840 850
QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN GGTCIDKVNG
860 870 880 890 900
YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT
910 920 930 940 950
GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC
960 970 980 990 1000
ASFPCQNGGT CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS
1010 1020 1030 1040 1050
QYVNSYTCTC PLGFSGINCQ TNDEDCTESS CLNGGSCIDG INGYNCSCLA
1060 1070 1080 1090 1100
GYSGANCQYK LNKCDSNPCL NGATCHEQNN EYTCHCPSGF TGKQCSEYVD
1110 1120 1130 1140 1150
WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC QDAADRKGLS
1160 1170 1180 1190 1200
LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD
1210 1220 1230 1240 1250
LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG
1260 1270 1280 1290 1300
TMGIICEINK DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE
1310 1320 1330 1340 1350
CLSNPCSNAG TLDCVQLVNN YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG
1360 1370 1380 1390 1400
NCNIRQSGHH CICNNGFYGK NCELSGQDCD SNPCRVGNCV VADEGFGYRC
1410 1420 1430 1440 1450
ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL CPSKWKGKRC
1460 1470 1480 1490 1500
DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC
1510 1520 1530 1540 1550
NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH
1560 1570 1580 1590 1600
DCERKLKSCD SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV
1610 1620 1630 1640 1650
LAEGAMSVVM LMNVEAFREI QAQFLRNMSH MLRTTVRLKK DALGHDIIIN
1660 1670 1680 1690 1700
WKDNVRVPEI EDTDFARKNK ILYTQQVHQT GIQIYLEIDN RKCTECFTHA
1710 1720 1730 1740 1750
VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP ANVKYVITGI
1760 1770 1780 1790 1800
ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM
1810 1820 1830 1840 1850
RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY
1860 1870 1880 1890 1900
ASDHTMVSEY EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP
1910 1920 1930 1940 1950
CGLTPLMIAA VRGGGLDTGE DIENNEDSTA QVISDLLAQG AELNATMDKT
1960 1970 1980 1990 2000
GETSLHLAAR FARADAAKRL LDAGADANCQ DNTGRTPLHA AVAADAMGVF
2010 2020 2030 2040 2050
QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA DADINAADNS
2060 2070 2080 2090 2100
GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC
2110 2120 2130 2140 2150
KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT
2160 2170 2180 2190 2200
PQAMIGSPPP GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA
2210 2220 2230 2240 2250
AKKAKLIEGS PDNGLDATGS LRRKASSKKT SAASKKAANL NGLNPGQLTG
2260 2270 2280 2290 2300
GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH ELEGSPVGVG MGGNLPSPYD
2310 2320 2330 2340 2350
TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS LQGNGLDMIK
2360 2370 2380 2390 2400
LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG
2410 2420 2430 2440 2450
AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT
2460 2470 2480 2490 2500
SPTHIQAMRH ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ
2510 2520 2530 2540 2550
NSPVSLGIIS PTGSDMGIML APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ
2560 2570 2580 2590 2600
HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD LNGFCGSPDS FHSGQMNPPS
2610 2620 2630 2640 2650
IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH TPQHLVQTLD
2660 2670 2680 2690 2700
SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA

IYI
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:
EMBLi
GenBanki
DDBJi
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_001258581.2.
NP_476859.2. NM_057511.4.

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:
EMBLi
GenBanki
DDBJi
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_001258581.2.
NP_476859.2. NM_057511.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 105-1450, 1482-1726, 1871-2198.
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 ENSGT00760000118786.
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_218930. Signaling by NOTCH3.
REACT_221100. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_239279. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_271460. Signaling by NOTCH4.
SignaLinki P07207.

Miscellaneous databases

ChiTaRSi N. fly.
EvolutionaryTracei P07207.
GenomeRNAii 31293.
NextBioi 772898.
PROi P07207.

Gene expression databases

Bgeei P07207.
ExpressionAtlasi P07207. differential.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 190 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