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UniProtKB - P07207 (NOTCH_DROME)

Entry version 250 (07 Apr 2021)
Sequence version 3 (02 Nov 2001)
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Protein

Neurogenic locus Notch protein

Gene

N

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Essential signaling protein which has a major role in many developmental processes (PubMed:3935325). Functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination (PubMed:10935637, PubMed:15620650, PubMed:12909620, PubMed:18243100). 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 (PubMed:7671825). Regulates oogenesis, the differentiation of the ectoderm and the development of the central and peripheral nervous system, eye, wing disk, muscles and segmental appendages such as antennae and legs, through lateral inhibition or induction (PubMed:11719214, PubMed:12369105, PubMed:3935325). Regulates neuroblast self-renewal, identity and proliferation through the regulation of bHLH-O proteins; in larval brains, involved in the maintenance of type II neuroblast self-renewal and identity by suppressing erm expression together with pnt; might also regulate dpn expression through the activation of the transcriptional regulator Su(H) (PubMed:27151950, PubMed:28899667, PubMed:20152183, PubMed:18342578, PubMed:23056424, PubMed:21262215).1 Publication13 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Developmental protein, Receptor
Biological processDifferentiation, Neurogenesis, Notch signaling pathway, Oogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-DME-1474228, Degradation of the extracellular matrix
R-DME-1971475, A tetrasaccharide linker sequence is required for GAG synthesis
R-DME-2022854, Keratan sulfate biosynthesis
R-DME-2022857, Keratan sulfate degradation
R-DME-2022870, Chondroitin sulfate biosynthesis
R-DME-2022923, Dermatan sulfate biosynthesis
R-DME-2024101, CS/DS degradation
R-DME-3000178, ECM proteoglycans
R-DME-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-DME-8957275, Post-translational protein phosphorylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P07207

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Neurogenic locus Notch protein
Cleaved into the following chain:
Processed neurogenic locus Notch protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:N
ORF Names:CG3936
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0004647, N

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini53 – 1745ExtracellularSequence analysisAdd BLAST1693
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1746 – 1766HelicalSequence analysisAdd BLAST21
Topological domaini1767 – 2703CytoplasmicSequence analysisAdd BLAST937

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown in the larval brain neuroblasts abolishes the expression of pnt, induces the ectopic expression of erm, results in the ectopic expression of Ase in type II neuroblasts (NBs) and their premature loss (PubMed:18342578, PubMed:23056424, PubMed:27151950). Simultaneous RNAi-mediated knockdown of pnt partially restores normal neuroblast numbers and inhibits ectopic erm expression (PubMed:27151950).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi739C → Y in mcd5; induces loss of microchaetae sensory precursors. 1
Mutagenesisi2060A → V in su42c; deltex-like mutation that induces outstreched wings and variability-fused ocelli. 1
Mutagenesisi2328Y → F: Abolishes interaction with Nedd4 and reduces ubiquitination. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 52Sequence analysisAdd BLAST52
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000767353 – 2703Neurogenic locus Notch proteinAdd BLAST2651
ChainiPRO_0000296234? – 2703Processed neurogenic locus Notch protein

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi62 ↔ 73PROSITE-ProRule annotation
Disulfide bondi67 ↔ 83PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi72O-linked (Fuc...) threonine1 Publication1
Disulfide bondi85 ↔ 94PROSITE-ProRule annotation
Disulfide bondi100 ↔ 111PROSITE-ProRule annotation
Disulfide bondi105 ↔ 124PROSITE-ProRule annotation
Glycosylationi110O-linked (Fuc...) threonine1 Publication1
Disulfide bondi126 ↔ 135PROSITE-ProRule annotation
Disulfide bondi143 ↔ 154PROSITE-ProRule annotation
Disulfide bondi148 ↔ 164PROSITE-ProRule annotation
Glycosylationi153O-linked (Fuc...) threonine1 Publication1
Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
Disulfide bondi181 ↔ 192PROSITE-ProRule annotation
Glycosylationi183O-linked (Glc...) serine1 Publication1
Disulfide bondi186 ↔ 203PROSITE-ProRule annotation
Glycosylationi191O-linked (Fuc...) threonine1 Publication1
Disulfide bondi205 ↔ 214PROSITE-ProRule annotation
Glycosylationi210O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi221 ↔ 232PROSITE-ProRule annotation
Glycosylationi223O-linked (Glc...) serine1 Publication1
Disulfide bondi226 ↔ 241PROSITE-ProRule annotation
Glycosylationi231O-linked (Fuc...) threonine1 Publication1
Disulfide bondi243 ↔ 252PROSITE-ProRule annotation
Disulfide bondi259 ↔ 270PROSITE-ProRule annotation
Disulfide bondi264 ↔ 279PROSITE-ProRule annotation
Disulfide bondi281 ↔ 290PROSITE-ProRule annotation
Disulfide bondi297 ↔ 308PROSITE-ProRule annotation
Disulfide bondi302 ↔ 317PROSITE-ProRule annotation
Glycosylationi307O-linked (Fuc...) threonine1 Publication1
Disulfide bondi319 ↔ 328PROSITE-ProRule annotation
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi335 ↔ 349PROSITE-ProRule annotation
Disulfide bondi343 ↔ 358PROSITE-ProRule annotation
Glycosylationi348O-linked (Fuc...) threonine1 Publication1
Disulfide bondi360 ↔ 369PROSITE-ProRule annotation
Glycosylationi371N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi376 ↔ 387PROSITE-ProRule annotation
Disulfide bondi381 ↔ 396PROSITE-ProRule annotation
Glycosylationi386O-linked (Fuc...) threonine1 Publication1
Disulfide bondi398 ↔ 407PROSITE-ProRule annotation
Disulfide bondi413 ↔ 424PROSITE-ProRule annotation
Disulfide bondi418 ↔ 435PROSITE-ProRule annotation
Glycosylationi427O-linked (Glc...) serine1 Publication1
Glycosylationi430N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi437 ↔ 446PROSITE-ProRule annotation
Disulfide bondi453 ↔ 465PROSITE-ProRule annotation
Disulfide bondi459 ↔ 474PROSITE-ProRule annotation
Glycosylationi475N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi476 ↔ 485PROSITE-ProRule annotation
Glycosylationi481O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi492 ↔ 503PROSITE-ProRule annotation
Glycosylationi494O-linked (Glc...) serine1 Publication1
Disulfide bondi497 ↔ 512PROSITE-ProRule annotation
Glycosylationi502O-linked (Fuc...) serine1 Publication1
Disulfide bondi514 ↔ 523PROSITE-ProRule annotation
Glycosylationi519O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi530 ↔ 541PROSITE-ProRule annotation
Glycosylationi532O-linked (Glc...) serine1 Publication1
Disulfide bondi535 ↔ 550PROSITE-ProRule annotation
Disulfide bondi552 ↔ 561PROSITE-ProRule annotation
Disulfide bondi568 ↔ 579PROSITE-ProRule annotation
Glycosylationi570O-linked (Glc...) serine1 Publication1
Disulfide bondi573 ↔ 588PROSITE-ProRule annotation
Disulfide bondi590 ↔ 599PROSITE-ProRule annotation
Glycosylationi595O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi606 ↔ 616PROSITE-ProRule annotation
Glycosylationi608O-linked (Glc...) serine1 Publication1
Disulfide bondi611 ↔ 625PROSITE-ProRule annotation
Disulfide bondi627 ↔ 636PROSITE-ProRule annotation
Disulfide bondi643 ↔ 654PROSITE-ProRule annotation
Glycosylationi645O-linked (Glc...) serine1 Publication1
Disulfide bondi648 ↔ 663PROSITE-ProRule annotation
Disulfide bondi665 ↔ 674PROSITE-ProRule annotation
Disulfide bondi681 ↔ 692PROSITE-ProRule annotation
Glycosylationi683O-linked (Glc...) serine1 Publication1
Disulfide bondi686 ↔ 701PROSITE-ProRule annotation
Glycosylationi691O-linked (Fuc...) threonine1 Publication1
Disulfide bondi703 ↔ 712PROSITE-ProRule annotation
Disulfide bondi719 ↔ 730PROSITE-ProRule annotation
Glycosylationi721O-linked (Glc...) serine1 Publication1
Disulfide bondi724 ↔ 739PROSITE-ProRule annotation
Disulfide bondi741 ↔ 750PROSITE-ProRule annotation
Disulfide bondi757 ↔ 768PROSITE-ProRule annotation
Glycosylationi759O-linked (Glc...) serine1 Publication1
Disulfide bondi762 ↔ 777PROSITE-ProRule annotation
Disulfide bondi779 ↔ 788PROSITE-ProRule annotation
Disulfide bondi795 ↔ 806PROSITE-ProRule annotation
Glycosylationi797O-linked (Glc...) serine1 Publication1
Disulfide bondi800 ↔ 815PROSITE-ProRule annotation
Glycosylationi805O-linked (Fuc...) threonine1 Publication1
Disulfide bondi817 ↔ 826PROSITE-ProRule annotation
Glycosylationi822O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi833 ↔ 844PROSITE-ProRule annotation
Disulfide bondi838 ↔ 853PROSITE-ProRule annotation
Glycosylationi843O-linked (Fuc...) threonine1 Publication1
Disulfide bondi855 ↔ 864PROSITE-ProRule annotation
Disulfide bondi871 ↔ 882PROSITE-ProRule annotation
Disulfide bondi876 ↔ 893PROSITE-ProRule annotation
Disulfide bondi895 ↔ 904PROSITE-ProRule annotation
Disulfide bondi911 ↔ 923PROSITE-ProRule annotation
Disulfide bondi917 ↔ 932PROSITE-ProRule annotation
Glycosylationi922O-linked (Fuc...) serine1 Publication1
Disulfide bondi934 ↔ 943PROSITE-ProRule annotation
Disulfide bondi950 ↔ 961PROSITE-ProRule annotation
Glycosylationi952O-linked (Glc...) serine1 Publication1
Disulfide bondi955 ↔ 970PROSITE-ProRule annotation
Glycosylationi960O-linked (Fuc...) threonine1 Publication1
Disulfide bondi972 ↔ 981PROSITE-ProRule annotation
Disulfide bondi988 ↔ 999PROSITE-ProRule annotation
Glycosylationi990O-linked (Glc...) serine1 Publication1
Disulfide bondi993 ↔ 1008PROSITE-ProRule annotation
Glycosylationi998O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1010 ↔ 1019PROSITE-ProRule annotation
Disulfide bondi1026 ↔ 1037PROSITE-ProRule annotation
Disulfide bondi1031 ↔ 1046PROSITE-ProRule annotation
Glycosylationi1036O-linked (Fuc...) serine1 Publication1
Glycosylationi1045N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1048 ↔ 1057PROSITE-ProRule annotation
Disulfide bondi1064 ↔ 1075PROSITE-ProRule annotation
Glycosylationi1066O-linked (Glc...) serine1 Publication1
Disulfide bondi1069 ↔ 1084PROSITE-ProRule annotation
Glycosylationi1074O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1086 ↔ 1095PROSITE-ProRule annotation
Disulfide bondi1102 ↔ 1113PROSITE-ProRule annotation
Disulfide bondi1107 ↔ 1122PROSITE-ProRule annotation
Glycosylationi1112O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1124 ↔ 1133PROSITE-ProRule annotation
Disulfide bondi1155 ↔ 1160PROSITE-ProRule annotation
Glycosylationi1157N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1171 ↔ 1180PROSITE-ProRule annotation
Disulfide bondi1187 ↔ 1198PROSITE-ProRule annotation
Glycosylationi1189O-linked (Glc...) serine1 Publication1
Disulfide bondi1192 ↔ 1207PROSITE-ProRule annotation
Glycosylationi1197O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1209 ↔ 1218PROSITE-ProRule annotation
Disulfide bondi1225 ↔ 1236PROSITE-ProRule annotation
Disulfide bondi1230 ↔ 1245PROSITE-ProRule annotation
Glycosylationi1235O-linked (Fuc...) threonine1 Publication1
Glycosylationi1242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1247 ↔ 1256PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1274PROSITE-ProRule annotation
Disulfide bondi1268 ↔ 1283PROSITE-ProRule annotation
Glycosylationi1271N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1273O-linked (Fuc...) serine1 Publication1
Disulfide bondi1285 ↔ 1294PROSITE-ProRule annotation
Disulfide bondi1301 ↔ 1314PROSITE-ProRule annotation
Glycosylationi1303O-linked (Glc...) serine1 Publication1
Disulfide bondi1306 ↔ 1323PROSITE-ProRule annotation
Disulfide bondi1325 ↔ 1334PROSITE-ProRule annotation
Disulfide bondi1341 ↔ 1352PROSITE-ProRule annotation
Disulfide bondi1346 ↔ 1361PROSITE-ProRule annotation
Disulfide bondi1363 ↔ 1372PROSITE-ProRule annotation
Disulfide bondi1379 ↔ 1389PROSITE-ProRule annotation
Glycosylationi1381O-linked (Glc...) serine1 Publication1
Disulfide bondi1384 ↔ 1400PROSITE-ProRule annotation
Disulfide bondi1402 ↔ 1411PROSITE-ProRule annotation
Disulfide bondi1419 ↔ 1430PROSITE-ProRule annotation
Disulfide bondi1424 ↔ 1439PROSITE-ProRule annotation
Disulfide bondi1441 ↔ 1450PROSITE-ProRule annotation
Disulfide bondi1482 ↔ 1505PROSITE-ProRule annotation
Disulfide bondi1487 ↔ 1500PROSITE-ProRule annotation
Disulfide bondi1496 ↔ 1512PROSITE-ProRule annotation
Glycosylationi1521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1522 ↔ 1545PROSITE-ProRule annotation
Disulfide bondi1527 ↔ 1540PROSITE-ProRule annotation
Disulfide bondi1536 ↔ 1552PROSITE-ProRule annotation
Disulfide bondi1559 ↔ 1585PROSITE-ProRule annotation
Disulfide bondi1567 ↔ 1580PROSITE-ProRule annotation
Disulfide bondi1576 ↔ 1592PROSITE-ProRule annotation
Glycosylationi1594N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1627N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2447Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 (PubMed:27268051). Three forms of O-glycosylation (O-fucosylation, O-glucosylation and O-GlcNAcylation) are detected (PubMed:27268051). O-fucosylated by O-fut1 and fng in the EGF repeat domain inhibits both Serrate/Ser- and Delta/Dl-binding (PubMed:12909620, PubMed:10935637). O-glucosylation by rumi in the endoplasmic reticulum is necessary for correct folding and signaling (PubMed:18243100).4 Publications
Ubiquitinated by Nedd4; which promotes ligand-independent endocytosis and proteasomal degradation. May also be ubiquitinated by Su(dx) and Cbl.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07207

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07207

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0004647, Expressed in embryo and 39 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P07207, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07207, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Interacts with Akap200; the interaction stabilizes N/Notch protein levels by preventing Cbl-mediated ubiquitination and subsequent lysosomal degradation of N/Notch (PubMed:29309414).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		57823, 309 interactors

Database of interacting proteins

More...DIPi		DIP-5N

Protein interaction database and analysis system

More...IntActi		P07207, 229 interactors

Molecular INTeraction database

More...MINTi		P07207

STRING: functional protein association networks

More...STRINGi		7227.FBpp0070483

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12703
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07207

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P07207

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini58 – 95EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini96 – 136EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini139 – 176EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini177 – 215EGF-like 4PROSITE-ProRule annotationAdd BLAST39
Domaini217 – 253EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini255 – 291EGF-like 6PROSITE-ProRule annotationAdd BLAST37
Domaini293 – 329EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini331 – 370EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini372 – 408EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini409 – 447EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini449 – 486EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini488 – 524EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini526 – 562EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini564 – 600EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini602 – 637EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini639 – 675EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini677 – 713EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini715 – 751EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini753 – 789EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini791 – 827EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini829 – 865EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini867 – 905EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini907 – 944EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini946 – 982EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini984 – 1020EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1022 – 1058EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1060 – 1096EGF-like 27PROSITE-ProRule annotationAdd BLAST37
Domaini1098 – 1134EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1136 – 1181EGF-like 29PROSITE-ProRule annotationAdd BLAST46
Domaini1183 – 1219EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1221 – 1257EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1259 – 1295EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1297 – 1335EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1337 – 1373EGF-like 34PROSITE-ProRule annotationAdd BLAST37
Domaini1375 – 1412EGF-like 35PROSITE-ProRule annotationAdd BLAST38
Domaini1415 – 1451EGF-like 36PROSITE-ProRule annotationAdd BLAST37
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1482 – 1521LNR 1PROSITE-ProRule annotationAdd BLAST40
Repeati1522 – 1557LNR 2PROSITE-ProRule annotationAdd BLAST36
Repeati1559 – 1599LNR 3PROSITE-ProRule annotationAdd BLAST41
Repeati1901 – 1945ANK 1Sequence analysisAdd BLAST45
Repeati1950 – 1979ANK 2Sequence analysisAdd BLAST30
Repeati1983 – 2013ANK 3Sequence analysisAdd BLAST31
Repeati2017 – 2046ANK 4Sequence analysisAdd BLAST30
Repeati2050 – 2079ANK 5Sequence analysisAdd BLAST30
Repeati2083 – 2112ANK 6Sequence analysisAdd BLAST30
Repeati2116 – 2139ANK 7Sequence analysisAdd BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2325 – 2328Interaction with Nedd44

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2264 – 2277Ala-richPROSITE-ProRule annotationAdd BLAST14
Compositional biasi2369 – 2498Gly-richPROSITE-ProRule annotationAdd BLAST130
Compositional biasi2533 – 2568Gln-richPROSITE-ProRule annotationAdd BLAST36
Compositional biasi2587 – 2675Ser-richPROSITE-ProRule annotationAdd BLAST89

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NOTCH family.Curated

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1217, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00980000198606

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000576_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07207

Identification of Orthologs from Complete Genome Data

More...OMAi		NEGSCLD

Database of Orthologous Groups

More...OrthoDBi		7525at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07207

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.20, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50157

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR024600, DUF3454_notch
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR008297, Notch
IPR035993, Notch-like_dom_sf
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 1 hit
PF11936, DUF3454, 1 hit
PF00008, EGF, 24 hits
PF07645, EGF_CA, 3 hits
PF12661, hEGF, 2 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002279, Notch, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01452, LNOTCHREPEAT

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00248, ANK, 7 hits
SM01334, DUF3454, 1 hit
SM00181, EGF, 36 hits
SM00179, EGF_CA, 33 hits
SM00004, NL, 3 hits
SM01338, NOD, 1 hit
SM01339, NODP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48403, SSF48403, 1 hit
SSF57184, SSF57184, 5 hits
SSF90193, SSF90193, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P07207-1 [UniParc]FASTAAdd to basket
« Hide
        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0EAE23F426FECD7B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M9NE67M9NE67_DROME
Notch, isoform B
N 1.1, 16-178, 16-55, anon-EST:Liang-1.12, Ax
2,703Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti9R → G in CAB37610 (PubMed:10731137).Curated1
Sequence conflicti84A → G in CAB37610 (PubMed:10731137).Curated1
Sequence conflicti103M → I in AAB59220 (PubMed:3935325).Curated1
Sequence conflicti119R → H in AAA28725 (PubMed:3097517).Curated1
Sequence conflicti231T → I in AAB59220 (PubMed:3935325).Curated1
Sequence conflicti240Q → R in CAB37610 (PubMed:10731137).Curated1
Sequence conflicti267G → A in AAB59220 (PubMed:3935325).Curated1
Sequence conflicti1561S → T in AAB59220 (PubMed:3935325).Curated1
Sequence conflicti1561S → T in AAA28725 (PubMed:3097517).Curated1
Sequence conflicti2257G → S in AAA28725 (PubMed:3097517).Curated1
Sequence conflicti2577A → E in AAA74496 (PubMed:2981631).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti578I → T. 1
Natural varianti2044I → R. 1
Natural varianti2265A → V. 1
Natural varianti2407H → R. 1
Natural varianti2445R → L. 1
Natural varianti2568Q → QQQQQ. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M16152 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

Protein sequence database of the Protein Information Resource

More...PIRi		A24420

NCBI Reference Sequences

More...RefSeqi		NP_001245510.1, NM_001258581.2
NP_476859.2, NM_057511.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0070507; FBpp0070483; FBgn0004647
FBtr0304659; FBpp0293201; FBgn0004647

Database of genes from NCBI RefSeq genomes

More...GeneIDi		31293

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG3936

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16152 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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OT8X-ray2.00A/B/C1902-2139[»]
2JMFNMR-B2318-2333[»]
SMRiP07207
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi57823, 309 interactors
DIPiDIP-5N
IntActiP07207, 229 interactors
MINTiP07207
STRINGi7227.FBpp0070483

PTM databases

iPTMnetiP07207

Proteomic databases

PaxDbiP07207

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		109544
FlyBaseiFBgn0004647, N

Phylogenomic databases

eggNOGiKOG1217, Eukaryota
GeneTreeiENSGT00980000198606
HOGENOMiCLU_000576_0_1_1
InParanoidiP07207
OMAiNEGSCLD
OrthoDBi7525at2759
PhylomeDBiP07207

Enzyme and pathway databases

ReactomeiR-DME-1474228, Degradation of the extracellular matrix
R-DME-1971475, A tetrasaccharide linker sequence is required for GAG synthesis
R-DME-2022854, Keratan sulfate biosynthesis
R-DME-2022857, Keratan sulfate degradation
R-DME-2022870, Chondroitin sulfate biosynthesis
R-DME-2022923, Dermatan sulfate biosynthesis
R-DME-2024101, CS/DS degradation
R-DME-3000178, ECM proteoglycans
R-DME-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-DME-8957275, Post-translational protein phosphorylation
SignaLinkiP07207

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		31293, 0 hits in 3 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		N, fly
EvolutionaryTraceiP07207

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		31293

Protein Ontology

More...PROi		PR:P07207

Gene expression databases

BgeeiFBgn0004647, Expressed in embryo and 39 other tissues
ExpressionAtlasiP07207, baseline and differential
GenevisibleiP07207, DM

Family and domain databases

Gene3Di1.25.40.20, 1 hit
IDEALiIID50157
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR024600, DUF3454_notch
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR008297, Notch
IPR035993, Notch-like_dom_sf
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom
PfamiView protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 1 hit
PF11936, DUF3454, 1 hit
PF00008, EGF, 24 hits
PF07645, EGF_CA, 3 hits
PF12661, hEGF, 2 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits
PIRSFiPIRSF002279, Notch, 1 hit
PRINTSiPR01452, LNOTCHREPEAT
SMARTiView protein in SMART
SM00248, ANK, 7 hits
SM01334, DUF3454, 1 hit
SM00181, EGF, 36 hits
SM00179, EGF_CA, 33 hits
SM00004, NL, 3 hits
SM01338, NOD, 1 hit
SM01339, NODP, 1 hit
SUPFAMiSSF48403, SSF48403, 1 hit
SSF57184, SSF57184, 5 hits
SSF90193, SSF90193, 3 hits
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNOTCH_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07207
Secondary accession number(s): O97458, P04154, Q9W4T8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 2, 2001
Last modified: April 7, 2021
This is version 250 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
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