Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 214 (08 May 2019)
Sequence version 3 (18 Apr 2012)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Mus musculus (Mouse)
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. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 oxygenBy similarity1
Metal bindingi435Calcium 1; via amide nitrogenBy similarity1
Metal bindingi452Calcium 2By similarity1
Metal bindingi453Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi455Calcium 2By similarity1
Metal bindingi469Calcium 2By similarity1
Metal bindingi470Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi490Calcium 3By similarity1
Metal bindingi491Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi493Calcium 3By similarity1
Metal bindingi507Calcium 3By similarity1
Metal bindingi508Calcium 3; via carbonyl oxygenBy similarity1
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

GO - Biological processi

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1912420 Pre-NOTCH Processing in Golgi
R-MMU-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-350054 Notch-HLH transcription pathway
R-MMU-8941856 RUNX3 regulates NOTCH signaling

<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_and_taxonomy_section">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
Alternative name(s):
Motch A1 Publication
mT14
p300
Cleaved into the following 2 chains:
Notch 1 extracellular truncation1 Publication
Short name:
NEXT1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Synonyms:Motch1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97363 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_location_section">'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_location_section">'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 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi65S → A: No effect. 1 Publication1
Mutagenesisi146S → A: No effect. 1 Publication1
Mutagenesisi232T → V: No significant effect on its binding and activation by DLL1 or JAG1. No significant effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1. Significant decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1; when associated with V-1402. 1 Publication1
Mutagenesisi311T → V: Significant loss of binding and activation by DLL1 or JAG1. Decrease in RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG-mediated inhibition of its activation by JAG1. Significant loss of binding and activation by DLL1 or JAG1 and complete loss of RFNG- and LFNG-mediated enhancement of its activation by DLL1; when associated with V-466. Decreased localization to the plasma membrane; when associated with A-435. 2 Publications1
Mutagenesisi341S → A: No effect. 1 Publication1
Mutagenesisi349T → V: Reduced binding and activation by JAG1 but not DLL1. Decrease in MFNG-mediated enhancement of its activation by DLL1. 1 Publication1
Mutagenesisi378S → A: No effect. 1 Publication1
Mutagenesisi435S → A: No effect on localization to the plasma membrane. No effect on binding and activation by DLL1. Decreased localization to the plasma membrane; when associated with V-311. 1 Publication1
Mutagenesisi458S → A: No effect. 1 Publication1
Mutagenesisi466T → V: Reduced binding and activation by DLL1 but not JAG1. Decrease in RFNG- and LFNG-mediated enhancement of its activation by DLL1. Loss of RFNG-mediated enhancement of its activation by JAG1. Significant loss of binding and activation by DLL1 or JAG1 and complete loss of RFNG- and LFNG-mediated enhancement of its activation by DLL1; when associated with V-311. 1 Publication1
Mutagenesisi496S → A: No effect. 1 Publication1
Mutagenesisi534S → A: No effect. 1 Publication1
Mutagenesisi609S → A: No effect. 1 Publication1
Mutagenesisi647S → A: No effect. 1 Publication1
Mutagenesisi722S → A: No effect. 1 Publication1
Mutagenesisi759S → A: No effect. 1 Publication1
Mutagenesisi797S → A: No effect. 1 Publication1
Mutagenesisi951S → A: No effect. 1 Publication1
Mutagenesisi997T → V: Reduced binding and activation by DLL1 but not JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1. 1 Publication1
Mutagenesisi1027S → A: No effect. 1 Publication1
Mutagenesisi1035T → V: Reduced binding and activation by JAG1 but not DLL1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1. 1 Publication1
Mutagenesisi1065S → A: Reduced activity. 1 Publication1
Mutagenesisi1159T → V: No significant effect on its binding and activation by DLL1 or JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1. 1 Publication1
Mutagenesisi1189S → A: No effect. 1 Publication1
Mutagenesisi1273S → A: No effect. 1 Publication1
Mutagenesisi1362T → V: No significant effect on its binding and activation by DLL1 or JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1. 1 Publication1
Mutagenesisi1402T → V: No significant effect on its binding and activation by DLL1 or JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1. Significant decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1; when associated with V-232. 1 Publication1
Mutagenesisi1651 – 1654RQRR → AAAA: Processing by furin-like convertase abolished. 1 Publication4
Mutagenesisi1675C → S: Produces an activated, ligand-independent molecule; when associated with S-1682. 1 Publication1
Mutagenesisi1682C → S: Produces an activated, ligand-independent molecule; when associated with S-1675. 1 Publication1
Mutagenesisi1744V → L: NICD processing severely reduced. 1
Mutagenesisi1945N → A: Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and greatly reduced transactivation capacity. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with G-2012. Almost abolished transactivation capacity; when associated with A-2012. 2 Publications1
Mutagenesisi2012N → A: Slightly reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and almost abolished transactivation capacity; when associated with A-1945. 2 Publications1
Mutagenesisi2012N → G: Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with A-1945. 2 Publications1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000767719 – 2531Neurogenic locus notch homolog protein 1Add BLAST2513
ChainiPRO_00000076781711 – 2531Notch 1 extracellular truncation2 PublicationsAdd BLAST821
ChainiPRO_00000076791744 – 2531Notch 1 intracellular domain3 PublicationsAdd 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
Disulfide bondi63 ↔ 74By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi65O-linked (Glc...) serine1 Publication1
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73O-linked (Fuc...) threonine2 Publications1
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116O-linked (Fuc...) threonine2 Publications1
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146O-linked (Glc...) serine1 Publication1
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194O-linked (Fuc...) threonine2 Publications1
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232O-linked (Fuc...) threonine; alternate1 Publication1
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...) threonine1 Publication1
Disulfide bondi323 ↔ 332By similarity
Disulfide bondi339 ↔ 350By similarity
Glycosylationi341O-linked (Glc...) serine1 Publication1
Disulfide bondi344 ↔ 359By similarity
Glycosylationi349O-linked (Fuc...) threonine1 Publication1
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378O-linked (Glc...) serine1 Publication1
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Glycosylationi435O-linked (Glc...) serine1 Publication1
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458O-linked (Glc...) serine2 Publications1
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466O-linked (Fuc...) threonine2 Publications1
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496O-linked (Glc...) serine1 Publication1
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534O-linked (Glc...) serine1 Publication1
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...) serine1 Publication1
Disulfide bondi612 ↔ 627By similarity
Glycosylationi617O-linked (Fuc...) threonine1 Publication1
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647O-linked (Glc...) serine1 Publication1
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Glycosylationi692O-linked (Fuc...) threonine1 Publication1
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722O-linked (Glc...) serine1 Publication1
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759O-linked (Glc...) serine2 Publications1
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767O-linked (Fuc...) threonine2 Publications1
Disulfide bondi779 ↔ 788By similarity
Glycosylationi784O-linked (GlcNAc) serine1 Publication1
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797O-linked (Glc...) serine2 Publications1
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805O-linked (Fuc...) threonine2 Publications1
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) threonine1 Publication1
Disulfide bondi911 ↔ 922By similarity
Disulfide bondi916 ↔ 931By similarity
Glycosylationi921O-linked (Fuc) serine1 Publication1
Disulfide bondi933 ↔ 942By similarity
Disulfide bondi949 ↔ 960By similarity
Glycosylationi951O-linked (Glc...) serine1 Publication1
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Glycosylationi997O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027O-linked (Glc...) serine1 Publication1
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035O-linked (Fuc...) threonine2 Publications1
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065O-linked (Glc...) serine1 Publication1
Disulfide bondi1068 ↔ 1083By similarity
Disulfide bondi1085 ↔ 1094By similarity
Disulfide bondi1101 ↔ 1122By similarity
Disulfide bondi1116 ↔ 1131By similarity
Disulfide bondi1133 ↔ 1142By similarity
Disulfide bondi1149 ↔ 1160By similarity
Disulfide bondi1154 ↔ 1169By similarity
Glycosylationi1159O-linked (Fuc...) threonine1 Publication1
Disulfide bondi1171 ↔ 1180By similarity
Glycosylationi1179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189O-linked (Glc...) serine1 Publication1
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197O-linked (Fuc...) threonine2 Publications1
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...) serine1 Publication1
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...) threonine2 Publications1
Disulfide bondi1374 ↔ 1383By similarity
Glycosylationi1379O-linked (GlcNAc...) threonine1 Publication1
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402O-linked (Fuc...) threonine; alternate1 Publication1
Glycosylationi1402O-linked (GalNAc...) threonine; alternate1 Publication1
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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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)1 Publication
<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 residuei1851PhosphothreonineCombined sources1
Modified residuei1945(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications1
Modified residuei2012(3S)-3-hydroxyasparagine; by HIF1AN; partial2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 (PubMed:10882062, PubMed:10882063). 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) (PubMed:10882062, PubMed:10882063). 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 (PubMed:10882062, PubMed:11518718, PubMed:11459941).4 Publications
Phosphorylated.
O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). O-glycosylated on the EGF-like domains (PubMed:21757702). O-glucosylated at Ser-435 by KDELC1 and KDELC2 (PubMed:30127001). 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 (By similarity). O-glycosylation at Ser-1027 is only partial (PubMed:21757702). 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 (PubMed:28089369).By similarity3 Publications
Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1 (PubMed:18628966, PubMed:23886940). 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 (PubMed:15240571).3 Publications
Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD.2 Publications

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 protease1 Publication2
Sitei1710 – 1711Cleavage; by ADAM172 Publications2

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
Q01705

PeptideAtlas

More...
PeptideAtlasi
Q01705

PRoteomics IDEntifications database

More...
PRIDEi
Q01705

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01705

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

More...
PhosphoSitePlusi
Q01705

<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

Highly expressed in the brain, lung and thymus. Expressed at lower levels in the spleen, bone-marrow, spinal cord, eyes, mammary gland, liver, intestine, skeletal muscle, kidney and heart. In the hair follicle, highly expressed exclusively in the epithelial compartment.1 Publication

<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

First detected in the mesoderm at 7.5 dpc By 8.5 dpc highly expressed in presomitic mesoderm, mesenchyme and endothelial cells, while much lower levels are seen in the neuroepithelium. Between 9.5-10.5 dpc expressed at high levels in the neuroepithelium. At 13.5 dpc expressed in the surface ectoderm, eye and developing whisker follicles. Hair follicle matrix cells expression starts as different cell types become distinguishable in the developing follicle. Expression persists throughout the growth phase of the follicle and maintains the same expression profile in the second hair cycle. The cells in the follicle that undergo a phase of high level expression are in transition from mitotic precursors to several discrete, differentiating cell types. Specifically expressed in cerebellar Bergmann glial cells during postnatal development.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026923 Expressed in 376 organ(s), highest expression level in hair follicle

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q01705 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01705 MM

<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_section">'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_section">'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. Interacts with THBS4. Interacts (via the EGF-like repeat region) with CCN3 (via CTCK domain) (PubMed:12050162). Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By similarity). Interacts with ZMIZ1. Interacts (via NICD domain) with MEGF10 (via the cytoplasmic domain) (PubMed:28498977). Interacts with DLL1 and JAG1 (PubMed:28089369). Interacts (via NICD domain) with PRAG1 (PubMed:25038227). Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (PubMed:25038227). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity).By similarity12 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei469Interaction with DLL4By similarity1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
201808, 20 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q01705

Database of interacting proteins

More...
DIPi
DIP-214N

Protein interaction database and analysis system

More...
IntActi
Q01705, 11 interactors

Molecular INTeraction database

More...
MINTi
Q01705

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000028288

<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

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
1YMPX-ray2.20A/B1971-2105[»]
2QC9X-ray2.35A/B1899-2106[»]
2RQZNMR-A452-489[»]
2RR0NMR-A452-489[»]
2RR2NMR-A452-489[»]
3P3NX-ray2.40B1930-1949[»]
3P3PX-ray2.60B1999-2016[»]
5KY0X-ray1.53B452-491[»]
5KY4X-ray1.47B983-1022[»]
5KY8X-ray1.65B452-491[»]
5KY9X-ray1.83B452-491[»]

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

More...
SMRi
Q01705

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q01705

<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_and_domains_section">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 10; calcium-bindingPROSITE-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 29PROSITE-ProRule annotationAdd 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 DLL4By similarity2
Regioni448 – 452Interaction with DLL4By similarity5
Regioni1718 – 1750Interaction with PSEN1By similarityAdd BLAST33
Regioni1937 – 1945HIF1AN-binding9
Regioni2004 – 2012HIF1AN-binding9

<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
ENOG410IR7G Eukaryota
COG0666 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157157

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234369

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01705

KEGG Orthology (KO)

More...
KOi
K02599

Identification of Orthologs from Complete Genome Data

More...
OMAi
GRDCESK

Database of Orthologous Groups

More...
OrthoDBi
7525at2759

TreeFam database of animal gene trees

More...
TreeFami
TF351641

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00204 ANK, 2 hits

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, 21 hits
PF07645 EGF_CA, 5 hits
PF12661 hEGF, 3 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, 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, 6 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q01705-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG
60 70 80 90 100
AFVGQRCQDS NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT
110 120 130 140 150
PLDNACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA
160 170 180 190 200
NGGQCLPFES SYICRCPPGF 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 TCHNTHGGYN 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
HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG AKCLDGPNTY
560 570 580 590 600
TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC
610 620 630 640 650
ETNINECHSQ PCRHGGTCQD RDNSYLCLCL 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 WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
910 920 930 940 950
GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA
960 970 980 990 1000
SNPCQNGANC TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD
1010 1020 1030 1040 1050
GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG
1060 1070 1080 1090 1100
YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ YHCECRSGWT GVNCDVLSVS
1110 1120 1130 1140 1150
CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS YCEDEVDECS
1160 1170 1180 1190 1200
PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
1210 1220 1230 1240 1250
LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG
1260 1270 1280 1290 1300
YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT
1310 1320 1330 1340 1350
GRRCESVING CRGKPCKNGG VCAVASNTAR GFICRCPAGF EGATCENDAR
1360 1370 1380 1390 1400
TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ
1410 1420 1430 1440 1450
GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE
1460 1470 14