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UniProtKB - Q07008 (NOTC1_RAT)

Entry version 209 (02 Dec 2020)
Sequence version 3 (16 Oct 2013)
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Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Rattus norvegicus (Rat)
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

Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination (By similarity). Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus (By similarity). Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (By similarity). Involved in the maturation of both CD4+ and CD8+ cells in the thymus (By similarity). Important for follicular differentiation and possibly cell fate selection within the follicle (By similarity). During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia (PubMed:11182080). Represses neuronal and myogenic differentiation (By similarity). May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation (By similarity). May be involved in mesoderm development, somite formation and neurogenesis (By similarity). May enhance HIF1A function by sequestering HIF1AN away from HIF1A (By similarity). Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury (By similarity). Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi432Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi435Calcium 1; via amide nitrogenCombined sources1 Publication1
Metal bindingi452Calcium 2Combined sources1 Publication1
Metal bindingi453Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi455Calcium 2Combined sources1 Publication1
Metal bindingi469Calcium 2Combined sources1 Publication1
Metal bindingi470Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi490Calcium 3Combined sources1 Publication1
Metal bindingi491Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi493Calcium 3Combined sources1 Publication1
Metal bindingi507Calcium 3Combined sources1 Publication1
Metal bindingi508Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1457Calcium 4; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi1460Calcium 4PROSITE-ProRule annotation1
Metal bindingi1475Calcium 4PROSITE-ProRule annotation1
Metal bindingi1478Calcium 4PROSITE-ProRule annotation1

<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 processAngiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation
LigandCalcium, Metal-binding

<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 homolog protein 1
Short name:
Notch 1
Cleaved into the following 2 chains:
Notch 1 extracellular truncation
Short name:
NEXT
Notch 1 intracellular domain
Short name:
NICD
<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:Notch1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 3
  • UP000234681 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...RGDi		3187, Notch1

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 domaini19 – 1725ExtracellularCuratedAdd BLAST1707
<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>Transmembranei1726 – 1746HelicalBy similarityAdd BLAST21
Topological domaini1747 – 2531CytoplasmicCuratedAdd BLAST785

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

<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 – 18Sequence analysisAdd BLAST18
<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_000000768019 – 2531Neurogenic locus notch homolog protein 1Add BLAST2513
ChainiPRO_00000076811711 – 2531Notch 1 extracellular truncationBy similarityAdd BLAST821
ChainiPRO_00000076821744 – 2531Notch 1 intracellular domainBy similarityAdd BLAST788

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 bondi24 ↔ 37By similarity
Disulfide bondi31 ↔ 46By similarity
<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>Glycosylationi41N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi48 ↔ 57By similarity
Disulfide bondi63 ↔ 74By similarity
Glycosylationi65O-linked (Glc...) serineBy similarity1
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73O-linked (Fuc...) threonineBy similarity1
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116O-linked (Fuc...) threonineBy similarity1
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146O-linked (Glc...) serineBy similarity1
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194O-linked (Fuc...) threonineBy similarity1
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi232O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi245 ↔ 254By similarity
Disulfide bondi261 ↔ 272By similarity
Disulfide bondi266 ↔ 281By similarity
Disulfide bondi283 ↔ 292By similarity
Disulfide bondi299 ↔ 312By similarity
Disulfide bondi306 ↔ 321By similarity
Glycosylationi311O-linked (Fuc...) threonineBy similarity1
Disulfide bondi323 ↔ 332By similarity
Disulfide bondi339 ↔ 350By similarity
Glycosylationi341O-linked (Glc...) serineBy similarity1
Disulfide bondi344 ↔ 359By similarity
Glycosylationi349O-linked (Fuc...) threonineBy similarity1
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378O-linked (Glc...) serineBy similarity1
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429Combined sources1 Publication
Disulfide bondi423 ↔ 438Combined sources1 Publication
Glycosylationi435O-linked (Glc...) serineCombined sources1 Publication1
Disulfide bondi440 ↔ 449Combined sources1 Publication
Disulfide bondi456 ↔ 467Combined sources1 Publication
Glycosylationi458O-linked (Glc...) serine1 Publication1
Disulfide bondi461 ↔ 476Combined sources1 Publication
Glycosylationi466O-linked (Fuc...) threonineCombined sources1 Publication1
Disulfide bondi478 ↔ 487Combined sources1 Publication
Disulfide bondi494 ↔ 505Combined sources1 Publication
Glycosylationi496O-linked (Glc...) serine1 Publication1
Disulfide bondi499 ↔ 514Combined sources1 Publication
Disulfide bondi516 ↔ 525Combined sources1 Publication
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534O-linked (Glc...) serineBy similarity1
Disulfide bondi537 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi570 ↔ 580By similarity
Disulfide bondi575 ↔ 589By similarity
Disulfide bondi591 ↔ 600By similarity
Disulfide bondi607 ↔ 618By similarity
Glycosylationi609O-linked (Glc...) serineBy similarity1
Disulfide bondi612 ↔ 627By similarity
Glycosylationi617O-linked (Fuc...) threonineBy similarity1
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647O-linked (Glc...) serineBy similarity1
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Glycosylationi692O-linked (Fuc...) threonineBy similarity1
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722O-linked (Glc...) serineBy similarity1
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759O-linked (Glc...) serineBy similarity1
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767O-linked (Fuc...) threonineBy similarity1
Disulfide bondi779 ↔ 788By similarity
Glycosylationi784O-linked (GlcNAc) serineBy similarity1
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797O-linked (Glc...) serineBy similarity1
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805O-linked (Fuc...) threonineBy similarity1
Disulfide bondi817 ↔ 826By similarity
Disulfide bondi833 ↔ 844By similarity
Disulfide bondi838 ↔ 855By similarity
Disulfide bondi857 ↔ 866By similarity
Disulfide bondi873 ↔ 884By similarity
Disulfide bondi878 ↔ 893By similarity
Glycosylationi888N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi895 ↔ 904By similarity
Glycosylationi900O-linked (GlcNAc) threonineBy similarity1
Disulfide bondi911 ↔ 922By similarity
Disulfide bondi916 ↔ 931By similarity
Glycosylationi921O-linked (Fuc) serineBy similarity1
Disulfide bondi933 ↔ 942By similarity
Disulfide bondi949 ↔ 960By similarity
Glycosylationi951O-linked (Glc...) serineBy similarity1
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Glycosylationi997O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027O-linked (Glc...) serineBy similarity1
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065O-linked (Glc...) serineBy similarity1
Disulfide bondi1068 ↔ 1083By similarity
Disulfide bondi1085 ↔ 1094By similarity
Disulfide bondi1101 ↔ 1122Curated
Disulfide bondi1116 ↔ 1131By similarity
Disulfide bondi1133 ↔ 1142By similarity
Disulfide bondi1149 ↔ 1160By similarity
Disulfide bondi1154 ↔ 1169By similarity
Glycosylationi1159O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1171 ↔ 1180By similarity
Glycosylationi1179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189O-linked (Glc...) serineBy similarity1
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1209 ↔ 1218By similarity
Disulfide bondi1225 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1253By similarity
Glycosylationi1241N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1255 ↔ 1264By similarity
Disulfide bondi1271 ↔ 1284By similarity
Glycosylationi1273O-linked (Glc...) serineBy similarity1
Disulfide bondi1276 ↔ 1293By similarity
Disulfide bondi1295 ↔ 1304By similarity
Disulfide bondi1311 ↔ 1322By similarity
Disulfide bondi1316 ↔ 1334By similarity
Disulfide bondi1336 ↔ 1345By similarity
Disulfide bondi1352 ↔ 1363By similarity
Disulfide bondi1357 ↔ 1372By similarity
Glycosylationi1362O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1374 ↔ 1383By similarity
Glycosylationi1379O-linked (GlcNAc...) threonineBy similarity1
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi1402O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 1472By similarity
Disulfide bondi1454 ↔ 1467By similarity
Disulfide bondi1463 ↔ 1479By similarity
Glycosylationi1489N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1490 ↔ 1514By similarity
Disulfide bondi1496 ↔ 1509By similarity
Disulfide bondi1505 ↔ 1521By similarity
Disulfide bondi1536 ↔ 1549By similarity
Disulfide bondi1545 ↔ 1561By similarity
Glycosylationi1587N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1715O-linked (GalNAc...) threonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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 residuei1851PhosphothreonineBy similarity1
Modified residuei1945(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei2012(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1

<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

Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by ADAM17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by one of the catalytic subunits of gamma-secretase (PSEN1 or PSEN2) to release a Notch-derived peptide containing the intracellular domain (NICD) from the membrane.By similarity
Phosphorylated.By similarity
O-glycosylated on the EGF-like domains. O-glucosylated at Ser-435 by KDELC1 and KDELC2 (By similarity). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4 (PubMed:25700513). O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (By similarity).By similarity1 Publication
Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1. Monoubiquitination at Lys-1749 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch.By similarity
Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1654 – 1655Cleavage; by furin-like proteaseBy similarity2
Sitei1710 – 1711Cleavage; by ADAM17By similarity2

Keywords - PTMi

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

Proteomic databases

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

More...PaxDbi		Q07008

PRoteomics IDEntifications database

More...PRIDEi		Q07008

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q07008, 48 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q07008

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q07008

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the brain, kidney and spleen. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. Found in both subventricular and ventricular germinal zones.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the embryo, highest levels occur between days 12 and 14 and decrease rapidly to much lower levels in the adult.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000019322, Expressed in lung and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q07008, RN

<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

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds.

Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH.

Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization.

Forms a trimeric complex with FBXW7 and SGK1.

Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation.

Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion.

Interacts (via NICD) with MDM2A.

Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity (By similarity).

Interacts with THBS4 (By similarity).

Interacts (via the EGF-like repeat region) with CCN3 (via CTCK domain) (By similarity).

Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (PubMed:25700513).

Interacts with ZMIZ1 (By similarity).

Interacts (via NICD domain) with MEGF10 (via the cytoplasmic domain).

Interacts with DLL1 and JAG1 (By similarity).

Interacts (via NICD domain) with PRAG1 (By similarity).

Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (By similarity).

Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity).

By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei469Interaction with DLL4Combined sources1 Publication1

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q07008, 3 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000026212

<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

12531
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		Q07008

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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>Domaini20 – 58EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini59 – 99EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini102 – 139EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini140 – 176EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini178 – 216EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini218 – 255EGF-like 6PROSITE-ProRule annotationAdd BLAST38
Domaini257 – 293EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini295 – 333EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini335 – 371EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini372 – 410EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini412 – 450EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini452 – 488EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini490 – 526EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini528 – 564EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini566 – 601EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini603 – 639EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini641 – 676EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini678 – 714EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini716 – 751EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini753 – 789EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini791 – 827EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini829 – 867EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini869 – 905EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini907 – 943EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini945 – 981EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini983 – 1019EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1021 – 1057EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1059 – 1095EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1097 – 1143EGF-like 29CuratedAdd BLAST47
Domaini1145 – 1181EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1183 – 1219EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1221 – 1265EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1267 – 1305EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1307 – 1346EGF-like 34PROSITE-ProRule annotationAdd BLAST40
Domaini1348 – 1384EGF-like 35PROSITE-ProRule annotationAdd BLAST37
Domaini1387 – 1426EGF-like 36PROSITE-ProRule annotationAdd BLAST40
<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>Repeati1449 – 1489LNR 1Add BLAST41
Repeati1490 – 1531LNR 2Add BLAST42
Repeati1532 – 1571LNR 3Add BLAST40
Repeati1917 – 1946ANK 1Add BLAST30
Repeati1950 – 1980ANK 2Add BLAST31
Repeati1984 – 2013ANK 3Add BLAST30
Repeati2017 – 2046ANK 4Add BLAST30
Repeati2050 – 2079ANK 5Add BLAST30

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>Regioni420 – 421Interaction with DLL4Combined sources1 Publication2
Regioni448 – 452Interaction with DLL4Combined sources1 Publication5
Regioni1718 – 1750Interaction with PSEN1By similarityAdd BLAST33
Regioni1937 – 1945HIF1AN-bindingBy similarity9
Regioni2004 – 2012HIF1AN-bindingBy similarity9

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 biasi1730 – 1733Poly-Ala4
Compositional biasi1891 – 1894Poly-Glu4
Compositional biasi2258 – 2261Poly-Pro4
Compositional biasi2497 – 2500Poly-Ser4

<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

Interaction with PSEN1 causes partial unwinding of the transmembrane helix, facilitating access to the scissile peptide bond.By similarity

<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		ENSGT00940000157157

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000576_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q07008

Identification of Orthologs from Complete Genome Data

More...OMAi		NEGSCLD

Database of Orthologous Groups

More...OrthoDBi		7525at2759

TreeFam database of animal gene trees

More...TreeFami		TF351641

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.20, 1 hit

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
IPR022362, Notch_1
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12796, Ank_2, 2 hits
PF11936, DUF3454, 1 hit
PF00008, EGF, 20 hits
PF07645, EGF_CA, 5 hits
PF12661, hEGF, 4 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
PR01984, NOTCH1

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00248, ANK, 6 hits
SM01334, DUF3454, 1 hit
SM00181, EGF, 36 hits
SM00179, EGF_CA, 32 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, 4 hits
PS00010, ASX_HYDROXYL, 22 hits
PS00022, EGF_1, 35 hits
PS01186, EGF_2, 27 hits
PS50026, EGF_3, 36 hits
PS01187, EGF_CA, 21 hits
PS50258, LNR, 3 hits

<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>Sequencei

<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.

Q07008-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG 
        60         70         80         90        100
AFVGQRCQDP SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT 
       110        120        130        140        150
PLANACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA 
       160        170        180        190        200
NGGQCLPFES SYICGCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG 
       210        220        230        240        250
SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA 
       260        270        280        290        300
GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 
       310        320        330        340        350
LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC 
       360        370        380        390        400
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC 
       410        420        430        440        450
PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE 
       460        470        480        490        500
IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL 
       510        520        530        540        550
HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG AKCLDGPNTY 
       560        570        580        590        600
TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC 
       610        620        630        640        650
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC 
       660        670        680        690        700
DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF 
       710        720        730        740        750
TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC 
       760        770        780        790        800
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC 
       810        820        830        840        850
LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY 
       860        870        880        890        900
ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 
       910        920        930        940        950
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA 
       960        970        980        990       1000
SNPCQNGANC TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD 
      1010       1020       1030       1040       1050
GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG 
      1060       1070       1080       1090       1100
YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ YHCECRSGWT GFNCDVLSVS 
      1110       1120       1130       1140       1150
CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS YCEDEVDECS 
      1160       1170       1180       1190       1200
PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 
      1210       1220       1230       1240       1250
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG 
      1260       1270       1280       1290       1300
YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT 
      1310       1320       1330       1340       1350
GRRCESVING CRGKPCRNGG VCAVASNTAR GFICRCPAGF EGATCENDAR 
      1360       1370       1380       1390       1400
TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ 
      1410       1420       1430       1440       1450
GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE 
      1460       1470       1480       1490       1500
LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 
      1510       1520       1530       1540       1550
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN 
      1560       1570       1580       1590       1600
SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL 
      1610       1620       1630       1640       1650
HTNVVFKRDA QGQQMIFPYY GREEELRKHP IKRSAVGWAT TSLLPGTNGG 
      1660       1670       1680       1690       1700
RQRRELDPMD IHGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG 
      1710       1720       1730       1740       1750
SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR 
      1760       1770       1780       1790       1800
RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 
      1810       1820       1830       1840       1850
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP 
      1860       1870       1880       1890       1900
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI 
      1910       1920       1930       1940       1950
SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM 
      1960       1970       1980       1990       2000
GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM 
      2010       2020       2030       2040       2050
LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK 
      2060       2070       2080       2090       2100
EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 
      2110       2120       2130       2140       2150
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK 
      2160       2170       2180       2190       2200
PSTKGLACSS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL 
      2210       2220       2230       2240       2250
SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG 
      2260       2270       2280       2290       2300
GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW 
      2310       2320       2330       2340       2350
LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI HSSLSTNTLS 
      2360       2370       2380       2390       2400
PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA 
      2410       2420       2430       2440       2450
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP 
      2460       2470       2480       2490       2500
MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS 
      2510       2520       2530 
PHSNISDWSE GISSPPTSMP SQITHIPEAF K
Length:2,531
Mass (Da):270,822
Last modified:October 16, 2013 - 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:i3E61AE863AA237F2
GO

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 conflicti309G → A in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti334E → D in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti402S → R in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti577Y → I in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti951S → T in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti1339G → R in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti1435G → A in CAA40667 (PubMed:1764995).Curated1
Sequence conflicti1595 – 1596EL → DV in CAA40667 (PubMed:1764995).Curated2
Sequence conflicti2501P → R in CAA40667 (PubMed:1764995).Curated1

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
X57405 mRNA Translation: CAA40667.1
AABR06021907 Genomic DNA No translation available.
AABR06021908 Genomic DNA No translation available.
CH474001 Genomic DNA Translation: EDL93491.1

Protein sequence database of the Protein Information Resource

More...PIRi		S18188

NCBI Reference Sequences

More...RefSeqi		NP_001099191.1, NM_001105721.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25496

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25496

UCSC genome browser

More...UCSCi		RGD:3187, rat

<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
X57405 mRNA Translation: CAA40667.1
AABR06021907 Genomic DNA No translation available.
AABR06021908 Genomic DNA No translation available.
CH474001 Genomic DNA Translation: EDL93491.1
PIRiS18188
RefSeqiNP_001099191.1, NM_001105721.1

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
4XL1X-ray2.30A/D412-526[»]
4XLWX-ray3.39A/C/E/G412-526[»]
5UK5X-ray2.51A295-488[»]
SMRiQ07008
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ07008, 3 interactors
STRINGi10116.ENSRNOP00000026212

PTM databases

GlyGeniQ07008, 48 sites
iPTMnetiQ07008
PhosphoSitePlusiQ07008

Proteomic databases

PaxDbiQ07008
PRIDEiQ07008

Genome annotation databases

EnsembliENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322
GeneIDi25496
KEGGirno:25496
UCSCiRGD:3187, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4851
RGDi3187, Notch1

Phylogenomic databases

eggNOGiKOG1217, Eukaryota
GeneTreeiENSGT00940000157157
HOGENOMiCLU_000576_0_0_1
InParanoidiQ07008
OMAiNEGSCLD
OrthoDBi7525at2759
TreeFamiTF351641

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q07008

Gene expression databases

BgeeiENSRNOG00000019322, Expressed in lung and 21 other tissues
GenevisibleiQ07008, RN

Family and domain databases

Gene3Di1.25.40.20, 1 hit
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
IPR022362, Notch_1
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom
PfamiView protein in Pfam
PF12796, Ank_2, 2 hits
PF11936, DUF3454, 1 hit
PF00008, EGF, 20 hits
PF07645, EGF_CA, 5 hits
PF12661, hEGF, 4 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits
PIRSFiPIRSF002279, Notch, 1 hit
PRINTSiPR01452, LNOTCHREPEAT
PR01984, NOTCH1
SMARTiView protein in SMART
SM00248, ANK, 6 hits
SM01334, DUF3454, 1 hit
SM00181, EGF, 36 hits
SM00179, EGF_CA, 32 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, 4 hits
PS00010, ASX_HYDROXYL, 22 hits
PS00022, EGF_1, 35 hits
PS01186, EGF_2, 27 hits
PS50026, EGF_3, 36 hits
PS01187, EGF_CA, 21 hits
PS50258, LNR, 3 hits

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 nameiNOTC1_RAT
<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: Q07008
Secondary accession number(s): F1M9E7
<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, 1995
Last sequence update: October 16, 2013
Last modified: December 2, 2020
This is version 209 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 programChordata Protein Annotation Program

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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