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UniProtKB - Q9UM47 (NOTC3_HUMAN)

Entry version 206 (26 Feb 2020)
Sequence version 2 (08 Feb 2011)
Previous versions | rss
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Protein

Neurogenic locus notch homolog protein 3

Gene

NOTCH3

Organism
Homo sapiens (Human)
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 Jagged1, Jagged2 and Delta1 to regulate cell-fate determination (PubMed:15350543). 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 (By similarity).By similarity1 Publication

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1912399 Pre-NOTCH Processing in the Endoplasmic Reticulum
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-1912420 Pre-NOTCH Processing in Golgi
R-HSA-350054 Notch-HLH transcription pathway
R-HSA-5083630 Defective LFNG causes SCDO3
R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription
R-HSA-9017802 Noncanonical activation of NOTCH3

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

More...SignaLinki		Q9UM47

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9UM47

<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 3
Short name:
Notch 3
Cleaved into the following 2 chains:
Notch 3 extracellular truncation
Notch 3 intracellular domain
<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:NOTCH3
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7883 NOTCH3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600276 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UM47

<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 domaini40 – 1643ExtracellularSequence analysisAdd BLAST1604
<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>Transmembranei1644 – 1664HelicalSequence analysisAdd BLAST21
Topological domaini1665 – 2321CytoplasmicSequence analysisAdd BLAST657

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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cerebral arteriopathy, autosomal dominant, with subcortical infarcts and leukoencephalopathy, 1 (CADASIL1)22 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA cerebrovascular disease characterized by multiple subcortical infarcts, pseudobulbar palsy, dementia, and the presence of granular deposits in small cerebral arteries producing ischemic stroke.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04423043C → G in CADASIL1. 2 Publications1
Natural variantiVAR_04423149C → F in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs193921045EnsemblClinVar.1
Natural variantiVAR_01287149C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_04423254R → C in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1555730189EnsemblClinVar.1
Natural variantiVAR_04423360S → C in CADASIL1. 2 Publications1
Natural variantiVAR_04423465C → S in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555730176EnsemblClinVar.1
Natural variantiVAR_04423567C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_01287271W → C in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs28937321EnsemblClinVar.1
Natural variantiVAR_04423676C → R in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555729610EnsemblClinVar.1
Natural variantiVAR_04423776C → W in CADASIL1. 2 Publications1
Natural variantiVAR_04423877 – 82Missing in CADASIL1. 1 Publication6
Natural variantiVAR_04423980 – 84Missing in CADASIL1. 3 Publications5
Natural variantiVAR_04424087C → R in CADASIL1. 2 Publications1
Natural variantiVAR_04424187C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_01287390R → C in CADASIL1. 8 PublicationsCorresponds to variant dbSNP:rs1555729604EnsemblClinVar.1
Natural variantiVAR_04424293C → F in CADASIL1. 3 Publications1
Natural variantiVAR_04424393C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044244106C → W in CADASIL1. 1 Publication1
Natural variantiVAR_044245108C → W in CADASIL1. 1 Publication1
Natural variantiVAR_044246108C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_012874110R → C in CADASIL1. 7 PublicationsCorresponds to variant dbSNP:rs775836288EnsemblClinVar.1
Natural variantiVAR_012875114 – 120Missing in CADASIL1. 2 Publications7
Natural variantiVAR_044247117C → F in CADASIL1. 4 PublicationsCorresponds to variant dbSNP:rs773539041EnsemblClinVar.1
Natural variantiVAR_044248118S → C in CADASIL1. 1 Publication1
Natural variantiVAR_044249123C → F in CADASIL1. 3 Publications1
Natural variantiVAR_044250123C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044251128C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_012876133R → C in CADASIL1; no effect on ligand-binding; no effect on cell membrane localization; reduced proteolytic processing. 11 PublicationsCorresponds to variant dbSNP:rs137852642EnsemblClinVar.1
Natural variantiVAR_044252134C → W in CADASIL1. 4 Publications1
Natural variantiVAR_012877141R → C in CADASIL1. 9 Publications1
Natural variantiVAR_044253142F → C in CADASIL1. 1 Publication1
Natural variantiVAR_044254144C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044255144C → S in CADASIL1. 3 Publications1
Natural variantiVAR_044256144C → Y in CADASIL1. 3 Publications1
Natural variantiVAR_044257145S → C in CADASIL1. 1 Publication1
Natural variantiVAR_012878146C → R in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555729510EnsemblClinVar.1
Natural variantiVAR_044258149G → C in CADASIL1. 2 Publications1
Natural variantiVAR_044259150Y → C in CADASIL1. 3 Publications1
Natural variantiVAR_044260153 – 155Missing in CADASIL1. 2 Publications3
Natural variantiVAR_012879153R → C in CADASIL1. 8 PublicationsCorresponds to variant dbSNP:rs797045014EnsemblClinVar.1
Natural variantiVAR_044261155C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044262162C → S in CADASIL1. 1 Publication1
Natural variantiVAR_012880169R → C in CADASIL1. 8 PublicationsCorresponds to variant dbSNP:rs28933696EnsemblClinVar.1
Natural variantiVAR_012882171G → C in CADASIL1. 1 Publication1
Natural variantiVAR_044263174C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044264174C → R in CADASIL1. 3 Publications1
Natural variantiVAR_044265174C → Y in CADASIL1. 5 PublicationsCorresponds to variant dbSNP:rs1555729486EnsemblClinVar.1
Natural variantiVAR_044266180S → C in CADASIL1. 1 Publication1
Natural variantiVAR_012883182R → C in CADASIL1. 9 PublicationsCorresponds to variant dbSNP:rs28933697EnsemblClinVar.1
Natural variantiVAR_044267183C → F in CADASIL1. 2 Publications1
Natural variantiVAR_044268183C → R in CADASIL1; no effect on ligand-binding; no effect on cell membrane localization; reduced proteolytic processing. 5 Publications1
Natural variantiVAR_044269183C → S in CADASIL1. 3 Publications1
Natural variantiVAR_044270185C → G in CADASIL1. 1 Publication1
Natural variantiVAR_012884185C → R in CADASIL1. 5 Publications1
Natural variantiVAR_044271189Y → C in CADASIL1. 1 Publication1
Natural variantiVAR_044272194C → F in CADASIL1. 3 Publications1
Natural variantiVAR_044273194C → R in CADASIL1. 1 Publication1
Natural variantiVAR_044274194C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044275194C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044276201C → Y in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1555729468EnsemblClinVar.1
Natural variantiVAR_044277206C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044278207R → C in CADASIL1. 6 PublicationsCorresponds to variant dbSNP:rs775267348EnsemblClinVar.1
Natural variantiVAR_012885212C → S in CADASIL1. 3 PublicationsCorresponds to variant dbSNP:rs1555729455EnsemblClinVar.1
Natural variantiVAR_044279213R → K in CADASIL1. 1 Publication1
Natural variantiVAR_012886222C → G in CADASIL1. 3 Publications1
Natural variantiVAR_044280222C → Y in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1555729452EnsemblClinVar.1
Natural variantiVAR_012887224C → Y in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555729451EnsemblClinVar.1
Natural variantiVAR_044281233C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044282233C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044283239 – 253Missing in CADASIL1. 2 PublicationsAdd BLAST15
Natural variantiVAR_044284240C → S in CADASIL1. 2 Publications1
Natural variantiVAR_044285245C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044286251C → R in CADASIL1. 2 Publications1
Natural variantiVAR_012888258Y → C in CADASIL1. 2 Publications1
Natural variantiVAR_044287260C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044288319A → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_044289332R → C in CADASIL1. 4 PublicationsCorresponds to variant dbSNP:rs137852641EnsemblClinVar.1
Natural variantiVAR_044290335S → C in CADASIL1. 2 Publications1
Natural variantiVAR_044291337Y → C in CADASIL1. 2 Publications1
Natural variantiVAR_044292379C → S in CADASIL1. 2 Publications1
Natural variantiVAR_044293395C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044294420G → C in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1323608032EnsemblClinVar.1
Natural variantiVAR_044295421R → C in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555729068EnsemblClinVar.1
Natural variantiVAR_044296428C → S in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs267606915EnsemblClinVar.1
Natural variantiVAR_044297428C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044298440C → G in CADASIL1. 2 Publications1
Natural variantiVAR_044299440C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044300446C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044301449R → C in CADASIL1. 1 Publication1
Natural variantiVAR_044302455C → R in CADASIL1; impaired ligand-binding; strongly reduced signaling activity; no effect on cell membrane localization; reduced proteolytic processing. 2 PublicationsCorresponds to variant dbSNP:rs28933698EnsemblClinVar.1
Natural variantiVAR_044303484C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044304484C → Y in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1313319587EnsemblClinVar.1
Natural variantiVAR_044305495C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044306511C → R in CADASIL1. 2 Publications1
Natural variantiVAR_012890542C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044307544R → C in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs201118034EnsemblClinVar.1
Natural variantiVAR_044308549C → Y in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555728814EnsemblClinVar.1
Natural variantiVAR_012891558R → C in CADASIL1. 5 PublicationsCorresponds to variant dbSNP:rs75068032EnsemblClinVar.1
Natural variantiVAR_012892578R → C in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs769773673Ensembl.1
Natural variantiVAR_044309607R → C in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs777751303EnsemblClinVar.1
Natural variantiVAR_072080710Y → C in CADASIL1; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 PublicationCorresponds to variant dbSNP:rs1328784046Ensembl.1
Natural variantiVAR_012893728R → C in CADASIL1. 3 PublicationsCorresponds to variant dbSNP:rs1057519101EnsemblClinVar.1
Natural variantiVAR_044310775C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044311953G → C in CADASIL1. 2 Publications1
Natural variantiVAR_044312984F → C in CADASIL1. 1 Publication1
Natural variantiVAR_012894985R → C in CADASIL1. 5 Publications1
Natural variantiVAR_0128951006R → C in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1555727942EnsemblClinVar.1
Natural variantiVAR_0443131015C → R in CADASIL1. 1 Publication1
Natural variantiVAR_0443151021Y → C in CADASIL1. 1 PublicationCorresponds to variant dbSNP:rs1167405466EnsemblClinVar.1
Natural variantiVAR_0128961031R → C in CADASIL1. 2 Publications1
Natural variantiVAR_0443161063D → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_0128991231R → C in CADASIL1. 3 PublicationsCorresponds to variant dbSNP:rs201680145EnsemblClinVar.1
Natural variantiVAR_0129001261C → R in CADASIL1. 2 Publications1
Natural variantiVAR_0443171261C → Y in CADASIL1. 2 PublicationsCorresponds to variant dbSNP:rs1209610920Ensembl.1
Myofibromatosis, infantile 2 (IMF2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0699271519L → P in IMF2. 1 PublicationCorresponds to variant dbSNP:rs367543285EnsemblClinVar.1
Lateral meningocele syndrome (LMNS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA very rare skeletal disorder with facial anomalies, hypotonia and neurologic dysfunction due to meningocele, a protrusion of the meninges, unaccompanied by neural tissue, through a bony defect in the skull or vertebral column. LMNS facial features include hypertelorism and telecanthus, high arched eyebrows, ptosis, mid-facial hypoplasia, micrognathia, high and narrow palate, low-set ears and a hypotonic appearance. Additional variable features are connective tissue abnormalities, aortic dilation, a high-pitched nasal voice, wormian bones and osteolysis.
Related information in OMIM

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4854

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		NOTCH3

MalaCards human disease database

More...MalaCardsi		NOTCH3
MIMi125310 phenotype
130720 phenotype
615293 phenotype

Open Targets

More...OpenTargetsi		ENSG00000074181

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		136 CADASIL
2591 Infantile myofibromatosis
2789 Lateral meningocele syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA31685

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UM47 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3407319

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2860

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NOTCH3

Domain mapping of disease mutations (DMDM)

More...DMDMi		322510053

<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 – 39Sequence analysisAdd BLAST39
<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_000000769240 – 2321Neurogenic locus notch homolog protein 3Add BLAST2282
ChainiPRO_00000076931629 – 2321Notch 3 extracellular truncationBy similarityAdd BLAST693
ChainiPRO_00000076941662 – 2321Notch 3 intracellular domainBy similarityAdd BLAST660

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 bondi43 ↔ 55By similarity
Disulfide bondi49 ↔ 65By similarity
Disulfide bondi67 ↔ 76By similarity
Disulfide bondi82 ↔ 93By similarity
Disulfide bondi87 ↔ 106By similarity
Disulfide bondi108 ↔ 117By similarity
Disulfide bondi123 ↔ 134By similarity
Disulfide bondi128 ↔ 144By similarity
Disulfide bondi146 ↔ 155By similarity
Disulfide bondi162 ↔ 174By similarity
Disulfide bondi168 ↔ 183By similarity
Disulfide bondi185 ↔ 194By similarity
Disulfide bondi201 ↔ 212By similarity
Disulfide bondi206 ↔ 222By similarity
Disulfide bondi224 ↔ 233By similarity
Disulfide bondi240 ↔ 251By similarity
Disulfide bondi245 ↔ 260By similarity
Disulfide bondi262 ↔ 271By similarity
Disulfide bondi278 ↔ 291By similarity
Disulfide bondi285 ↔ 300By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi318 ↔ 329By similarity
Disulfide bondi323 ↔ 338By similarity
Disulfide bondi340 ↔ 349By similarity
Disulfide bondi355 ↔ 366By similarity
Disulfide bondi360 ↔ 377By similarity
Disulfide bondi379 ↔ 388By similarity
Disulfide bondi395 ↔ 408By similarity
Disulfide bondi402 ↔ 417By similarity
Disulfide bondi419 ↔ 428By similarity
Disulfide bondi435 ↔ 446By similarity
Disulfide bondi440 ↔ 455By similarity
Disulfide bondi457 ↔ 466By similarity
Disulfide bondi473 ↔ 484By similarity
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi495 ↔ 504By similarity
Disulfide bondi511 ↔ 522By similarity
Disulfide bondi516 ↔ 531By similarity
Disulfide bondi533 ↔ 542By similarity
Disulfide bondi549 ↔ 559By similarity
Disulfide bondi554 ↔ 568By similarity
Disulfide bondi570 ↔ 579By similarity
Disulfide bondi586 ↔ 597By similarity
Disulfide bondi591 ↔ 606By similarity
Disulfide bondi608 ↔ 617By similarity
Disulfide bondi624 ↔ 634By similarity
Disulfide bondi629 ↔ 643By similarity
Disulfide bondi645 ↔ 654By similarity
Disulfide bondi661 ↔ 672By similarity
Disulfide bondi666 ↔ 681By similarity
Disulfide bondi683 ↔ 692By similarity
Disulfide bondi699 ↔ 709By similarity
Disulfide bondi704 ↔ 718By similarity
Disulfide bondi720 ↔ 729By similarity
Disulfide bondi738 ↔ 749By similarity
Disulfide bondi743 ↔ 758By similarity
Disulfide bondi760 ↔ 769By similarity
Disulfide bondi775 ↔ 786By similarity
Disulfide bondi780 ↔ 796By similarity
Disulfide bondi798 ↔ 807By similarity
Disulfide bondi814 ↔ 826By similarity
Disulfide bondi820 ↔ 835By similarity
Disulfide bondi837 ↔ 846By similarity
Disulfide bondi853 ↔ 864By similarity
Disulfide bondi858 ↔ 873By similarity
Disulfide bondi875 ↔ 884By similarity
Disulfide bondi891 ↔ 901By similarity
Disulfide bondi896 ↔ 910By similarity
Disulfide bondi912 ↔ 921By similarity
Disulfide bondi928 ↔ 939By similarity
Disulfide bondi933 ↔ 948By similarity
Disulfide bondi950 ↔ 959By similarity
Disulfide bondi966 ↔ 977By similarity
Disulfide bondi971 ↔ 986By similarity
Disulfide bondi988 ↔ 997By similarity
Disulfide bondi1004 ↔ 1015By similarity
Disulfide bondi1009 ↔ 1022By similarity
Disulfide bondi1024 ↔ 1033By similarity
Disulfide bondi1040 ↔ 1061By similarity
Disulfide bondi1055 ↔ 1070By similarity
Disulfide bondi1072 ↔ 1081By similarity
Disulfide bondi1088 ↔ 1099By similarity
Disulfide bondi1093 ↔ 1108By similarity
Disulfide bondi1110 ↔ 1119By similarity
Disulfide bondi1126 ↔ 1137By similarity
Disulfide bondi1131 ↔ 1146By similarity
Disulfide bondi1148 ↔ 1157By similarity
Disulfide bondi1164 ↔ 1182By similarity
Disulfide bondi1176 ↔ 1191By 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>Glycosylationi1179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1193 ↔ 1202By similarity
Disulfide bondi1209 ↔ 1222By similarity
Disulfide bondi1214 ↔ 1232By similarity
Disulfide bondi1234 ↔ 1243By similarity
Disulfide bondi1250 ↔ 1261By similarity
Disulfide bondi1255 ↔ 1275By similarity
Disulfide bondi1277 ↔ 1286By similarity
Disulfide bondi1293 ↔ 1304By similarity
Disulfide bondi1298 ↔ 1313By similarity
Disulfide bondi1315 ↔ 1324By similarity
Glycosylationi1336N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1339 ↔ 1350By similarity
Disulfide bondi1344 ↔ 1361By similarity
Disulfide bondi1363 ↔ 1372By similarity
Disulfide bondi1387 ↔ 1410By similarity
Disulfide bondi1392 ↔ 1405By similarity
Disulfide bondi1401 ↔ 1417By similarity
Disulfide bondi1428 ↔ 1451By similarity
Disulfide bondi1433 ↔ 1446By similarity
Glycosylationi1438N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1442 ↔ 1458By similarity
Disulfide bondi1467 ↔ 1493By similarity
Disulfide bondi1475 ↔ 1488By similarity
Disulfide bondi1484 ↔ 1500By 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 residuei2174Omega-N-methylarginineCombined sources1

<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 TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane.1 Publication
Phosphorylated.By similarity
Hydroxylated by HIF1AN.1 Publication

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>Sitei1571 – 1572Cleavage; by furin-like proteaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UM47

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UM47

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UM47

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9UM47

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

More...PaxDbi		Q9UM47

PeptideAtlas

More...PeptideAtlasi		Q9UM47

PRoteomics IDEntifications database

More...PRIDEi		Q9UM47

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		85176

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UM47

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

More...PhosphoSitePlusi		Q9UM47

<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

Ubiquitously expressed in fetal and adult tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000074181 Expressed in vagina and 218 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UM47 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UM47 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB005393
HPA044392

<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 a N-terminal fragment N(EC) which are probably linked by disulfide bonds (By similarity).

Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3.

Interacts with PSMA1.

Interacts with HIF1AN.

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110916, 71 interactors

Database of interacting proteins

More...DIPi		DIP-39827N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q9UM47

Protein interaction database and analysis system

More...IntActi		Q9UM47, 37 interactors

Molecular INTeraction database

More...MINTi		Q9UM47

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000263388

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9UM47

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9UM47 protein

<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

12321
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		Q9UM47

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>Domaini40 – 77EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini78 – 118EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini119 – 156EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini158 – 195EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini197 – 234EGF-like 5PROSITE-ProRule annotationAdd BLAST38
Domaini236 – 272EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini274 – 312EGF-like 7PROSITE-ProRule annotationAdd BLAST39
Domaini314 – 350EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini351 – 389EGF-like 9PROSITE-ProRule annotationAdd BLAST39
Domaini391 – 429EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini431 – 467EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini469 – 505EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini507 – 543EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini545 – 580EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini582 – 618EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini620 – 655EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini657 – 693EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini695 – 730EGF-like 18PROSITE-ProRule annotationAdd BLAST36
Domaini734 – 770EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini771 – 808EGF-like 20PROSITE-ProRule annotationAdd BLAST38
Domaini810 – 847EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini849 – 885EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini887 – 922EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini924 – 960EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini962 – 998EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1000 – 1034EGF-like 26PROSITE-ProRule annotationAdd BLAST35
Domaini1047 – 1082EGF-like 27PROSITE-ProRule annotationAdd BLAST36
Domaini1084 – 1120EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1122 – 1158EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1160 – 1203EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini1205 – 1244EGF-like 31PROSITE-ProRule annotationAdd BLAST40
Domaini1246 – 1287EGF-like 32PROSITE-ProRule annotationAdd BLAST42
Domaini1289 – 1325EGF-like 33PROSITE-ProRule annotationAdd BLAST37
Domaini1335 – 1373EGF-like 34PROSITE-ProRule annotationAdd BLAST39
<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>Repeati1387 – 1427LNR 1Add BLAST41
Repeati1428 – 1458LNR 2Add BLAST31
Repeati1467 – 1505LNR 3Add BLAST39
Repeati1838 – 1867ANK 1Add BLAST30
Repeati1871 – 1901ANK 2Add BLAST31
Repeati1905 – 1934ANK 3Add BLAST30
Repeati1938 – 1967ANK 4Add BLAST30
Repeati1971 – 2000ANK 5Add BLAST30

<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

The EGF-like domains 10 and 11 are required for binding the ligands JAG1 and DLL1.1 Publication

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

Belongs to the NOTCH family.Curated

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IR7G Eukaryota
COG0666 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160234

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms