Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P46531 (NOTC1_HUMAN)

Entry version 234 (16 Oct 2019)
Sequence version 4 (23 Sep 2008)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Neurogenic locus notch homolog protein 1

Gene

NOTCH1

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 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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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 oxygen1
Metal bindingi1460Calcium 41
Metal bindingi1475Calcium 41
Metal bindingi1478Calcium 41

<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

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-210744 Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2644607 Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling
R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant
R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-350054 Notch-HLH transcription pathway
R-HSA-5083630 Defective LFNG causes SCDO3
R-HSA-8941856 RUNX3 regulates NOTCH signaling
R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription
R-HSA-9013695 NOTCH4 Intracellular Domain Regulates Transcription

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

More...SignaLinki		P46531

SIGNOR Signaling Network Open Resource

More...SIGNORi		P46531

Protein family/group databases

Transport Classification Database

More...TCDBi		9.B.87.1.12 the selenoprotein p receptor (selp-receptor) family

<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
Short name:
hN1
Alternative name(s):
Translocation-associated notch protein TAN-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_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:TAN1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 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_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
  • UP000005640 <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 9

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7881 NOTCH1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		190198 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P46531

<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 – 1735Extracellular2 PublicationsAdd BLAST1717
<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>Transmembranei1736 – 1756Helical2 PublicationsAdd BLAST21
Topological domaini1757 – 2555Cytoplasmic2 PublicationsAdd BLAST799

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

Aortic valve disease 1 (AOVD1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification, stenosis and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome.
Related information in OMIM
Adams-Oliver syndrome 5 (AOS5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins.
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_071960429C → R in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587777736EnsemblClinVar.1
Natural variantiVAR_0719611496C → Y in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587781259EnsemblClinVar.1
Natural variantiVAR_0719621989D → N in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587777734EnsemblClinVar.1

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>Mutagenesisi1728P → C: Formation of an artifactual disulfide bond with PSEN1. 1 Publication1
Mutagenesisi1755 – 1761Missing : Loss of proteolytic cleavage by gamma-secretase. 1 Publication7

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4851

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

More...GeneReviewsi		NOTCH1

MalaCards human disease database

More...MalaCardsi		NOTCH1
MIMi109730 phenotype
616028 phenotype

Open Targets

More...OpenTargetsi		ENSG00000148400

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

More...Orphaneti		974 Adams-Oliver syndrome
402075 Familial bicuspid aortic valve

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA31683

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P46531

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2146346

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NOTCH1

Domain mapping of disease mutations (DMDM)

More...DMDMi		206729936

<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_000000767419 – 2555Neurogenic locus notch homolog protein 1Add BLAST2537
ChainiPRO_00000076751721 – 2555Notch 1 extracellular truncationBy similarityAdd BLAST835
ChainiPRO_00000076761754 – 2555Notch 1 intracellular domainBy similarityAdd BLAST802

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 ↔ 37PROSITE-ProRule annotation
Disulfide bondi31 ↔ 46PROSITE-ProRule annotation
<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>Glycosylationi41N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi48 ↔ 57PROSITE-ProRule annotation
Disulfide bondi63 ↔ 74PROSITE-ProRule annotation
Glycosylationi65O-linked (Glc...) serineBy similarity1
Disulfide bondi68 ↔ 87PROSITE-ProRule annotation
Glycosylationi73O-linked (Fuc...) threonineBy similarity1
Disulfide bondi89 ↔ 98PROSITE-ProRule annotation
Disulfide bondi106 ↔ 117PROSITE-ProRule annotation
Disulfide bondi111 ↔ 127PROSITE-ProRule annotation
Glycosylationi116O-linked (Fuc...) threonineBy similarity1
Disulfide bondi129 ↔ 138PROSITE-ProRule annotation
Disulfide bondi144 ↔ 155PROSITE-ProRule annotation
Glycosylationi146O-linked (Glc...) serineBy similarity1
Disulfide bondi149 ↔ 164PROSITE-ProRule annotation
Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
Disulfide bondi182 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 204PROSITE-ProRule annotation
Glycosylationi194O-linked (Fuc...) threonineBy similarity1
Disulfide bondi206 ↔ 215PROSITE-ProRule annotation
Disulfide bondi222 ↔ 233PROSITE-ProRule annotation
Disulfide bondi227 ↔ 243PROSITE-ProRule annotation
Glycosylationi232O-linked (Fuc...) threonine; alternate1 Publication1
Glycosylationi232O-linked (GalNAc...) threonine; alternate1 Publication1
Disulfide bondi245 ↔ 254PROSITE-ProRule annotation
Disulfide bondi261 ↔ 272PROSITE-ProRule annotation
Disulfide bondi266 ↔ 281PROSITE-ProRule annotation
Disulfide bondi283 ↔ 292PROSITE-ProRule annotation
Disulfide bondi299 ↔ 312PROSITE-ProRule annotation
Disulfide bondi306 ↔ 321PROSITE-ProRule annotation
Glycosylationi311O-linked (Fuc...) threonineBy similarity1
Disulfide bondi323 ↔ 332PROSITE-ProRule annotation
Disulfide bondi339 ↔ 350PROSITE-ProRule annotation
Glycosylationi341O-linked (Glc...) serineBy similarity1
Disulfide bondi344 ↔ 359PROSITE-ProRule annotation
Glycosylationi349O-linked (Fuc...) threonineBy similarity1
Disulfide bondi361 ↔ 370PROSITE-ProRule annotation
Disulfide bondi376 ↔ 387PROSITE-ProRule annotation
Glycosylationi378O-linked (Glc...) serineBy similarity1
Disulfide bondi381 ↔ 398PROSITE-ProRule annotation
Disulfide bondi400 ↔ 409PROSITE-ProRule annotation
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Glycosylationi435O-linked (Glc...) serine1 Publication1
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458O-linked (Glc...) serineBy similarity1
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466O-linked (Fuc...) threonineBy similarity1
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496O-linked (Glc...) serineBy similarity1
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543PROSITE-ProRule annotation
Glycosylationi534O-linked (Glc...) serineBy similarity1
Disulfide bondi537 ↔ 552PROSITE-ProRule annotation
Disulfide bondi554 ↔ 563PROSITE-ProRule annotation
Disulfide bondi570 ↔ 580PROSITE-ProRule annotation
Disulfide bondi575 ↔ 589PROSITE-ProRule annotation
Disulfide bondi591 ↔ 600PROSITE-ProRule annotation
Disulfide bondi607 ↔ 618PROSITE-ProRule annotation
Glycosylationi609O-linked (Glc...) serineBy similarity1
Disulfide bondi612 ↔ 627PROSITE-ProRule annotation
Glycosylationi617O-linked (Fuc...) threonineBy similarity1
Disulfide bondi629 ↔ 638PROSITE-ProRule annotation
Disulfide bondi645 ↔ 655PROSITE-ProRule annotation
Glycosylationi647O-linked (Glc...) serineBy similarity1
Disulfide bondi650 ↔ 664PROSITE-ProRule annotation
Disulfide bondi666 ↔ 675PROSITE-ProRule annotation
Disulfide bondi682 ↔ 693PROSITE-ProRule annotation
Disulfide bondi687 ↔ 702PROSITE-ProRule annotation
Glycosylationi692O-linked (Fuc...) threonineBy similarity1
Disulfide bondi704 ↔ 713PROSITE-ProRule annotation
Disulfide bondi720 ↔ 730PROSITE-ProRule annotation
Glycosylationi722O-linked (Glc...) serineBy similarity1
Disulfide bondi725 ↔ 739PROSITE-ProRule annotation
Disulfide bondi741 ↔ 750PROSITE-ProRule annotation
Disulfide bondi757 ↔ 768PROSITE-ProRule annotation
Glycosylationi759O-linked (Glc...) serineBy similarity1
Disulfide bondi762 ↔ 777PROSITE-ProRule annotation
Glycosylationi767O-linked (Fuc...) threonineBy similarity1
Disulfide bondi779 ↔ 788PROSITE-ProRule annotation
Glycosylationi784O-linked (GlcNAc) serineBy similarity1
Disulfide bondi795 ↔ 806PROSITE-ProRule annotation
Glycosylationi797O-linked (Glc...) serineBy similarity1
Disulfide bondi800 ↔ 815PROSITE-ProRule annotation
Glycosylationi805O-linked (Fuc...) threonineBy similarity1
Disulfide bondi817 ↔ 826PROSITE-ProRule annotation
Disulfide bondi833 ↔ 844PROSITE-ProRule annotation
Disulfide bondi838 ↔ 855PROSITE-ProRule annotation
Disulfide bondi857 ↔ 866PROSITE-ProRule annotation
Disulfide bondi873 ↔ 884PROSITE-ProRule annotation
Disulfide bondi878 ↔ 893PROSITE-ProRule annotation
Disulfide bondi895 ↔ 904PROSITE-ProRule annotation
Disulfide bondi911 ↔ 922PROSITE-ProRule annotation
Disulfide bondi916 ↔ 931PROSITE-ProRule annotation
Glycosylationi921O-linked (Fuc) serineBy similarity1
Disulfide bondi933 ↔ 942PROSITE-ProRule annotation
Disulfide bondi949 ↔ 960PROSITE-ProRule annotation
Glycosylationi951O-linked (Glc...) serineBy similarity1
Disulfide bondi954 ↔ 969PROSITE-ProRule annotation
Glycosylationi959N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi971 ↔ 980PROSITE-ProRule annotation
Disulfide bondi987 ↔ 998PROSITE-ProRule annotation
Disulfide bondi992 ↔ 1007PROSITE-ProRule annotation
Glycosylationi997O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1009 ↔ 1018PROSITE-ProRule annotation
Disulfide bondi1025 ↔ 1036PROSITE-ProRule annotation
Glycosylationi1027O-linked (Glc...) serineBy similarity1
Disulfide bondi1030 ↔ 1045PROSITE-ProRule annotation
Glycosylationi1035O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1047 ↔ 1056PROSITE-ProRule annotation
Disulfide bondi1063 ↔ 1074PROSITE-ProRule annotation
Glycosylationi1065O-linked (Glc...) serineBy similarity1
Disulfide bondi1068 ↔ 1083PROSITE-ProRule annotation
Disulfide bondi1085 ↔ 1094PROSITE-ProRule annotation
Disulfide bondi1101 ↔ 1122By similarity
Disulfide bondi1116 ↔ 1131PROSITE-ProRule annotation
Disulfide bondi1133 ↔ 1142PROSITE-ProRule annotation
Disulfide bondi1149 ↔ 1160PROSITE-ProRule annotation
Disulfide bondi1154 ↔ 1169PROSITE-ProRule annotation
Glycosylationi1159O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1171 ↔ 1180PROSITE-ProRule annotation
Glycosylationi1179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1187 ↔ 1198PROSITE-ProRule annotation
Glycosylationi1189O-linked (Glc...) serineBy similarity1
Disulfide bondi1192 ↔ 1207PROSITE-ProRule annotation
Glycosylationi1197O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1209 ↔ 1218PROSITE-ProRule annotation
Disulfide bondi1238 ↔ 1253PROSITE-ProRule annotation
Glycosylationi1241N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1255 ↔ 1264PROSITE-ProRule annotation
Disulfide bondi1271 ↔ 1284PROSITE-ProRule annotation
Glycosylationi1273O-linked (Glc...) serineBy similarity1
Disulfide bondi1276 ↔ 1293PROSITE-ProRule annotation
Disulfide bondi1295 ↔ 1304PROSITE-ProRule annotation
Disulfide bondi1311 ↔ 1322PROSITE-ProRule annotation
Disulfide bondi1316 ↔ 1334PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1345PROSITE-ProRule annotation
Disulfide bondi1352 ↔ 1363PROSITE-ProRule annotation
Disulfide bondi1357 ↔ 1372PROSITE-ProRule annotation
Glycosylationi1362O-linked (Fuc...) threonineBy similarity1
Disulfide bondi1374 ↔ 1383PROSITE-ProRule annotation
Glycosylationi1379O-linked (GlcNAc...) threonineBy similarity1
Disulfide bondi1391 ↔ 1403PROSITE-ProRule annotation
Disulfide bondi1397 ↔ 1414PROSITE-ProRule annotation
Glycosylationi1402O-linked (Fuc...) threonine; alternate1 Publication1
Glycosylationi1402O-linked (GalNAc...) threonine; alternate1 Publication1
Disulfide bondi1416 ↔ 1425PROSITE-ProRule annotation
Disulfide bondi1449 ↔ 14721 Publication
Disulfide bondi1454 ↔ 14671 Publication
Disulfide bondi1463 ↔ 14791 Publication
Glycosylationi1489N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1490 ↔ 1514PROSITE-ProRule annotation
Disulfide bondi1496 ↔ 1509PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1521PROSITE-ProRule annotation
Disulfide bondi1536 ↔ 1549PROSITE-ProRule annotation
Disulfide bondi1545 ↔ 1561PROSITE-ProRule annotation
Glycosylationi1587N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1725O-linked (GalNAc...) threonine1 Publication1
<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-linki1759Glycyl 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 residuei1861PhosphothreonineBy similarity1
Modified residuei1955(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei2022(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1

<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 (By similarity). 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:24226769). 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:30598546).By similarity2 Publications
Phosphorylated.By similarity
O-glycosylated on the EGF-like domains (PubMed:24226769). 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-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) (PubMed:24226769). 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 similarity2 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-1759 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:24226769).3 Publications
Hydroxylated at Asn-1955 by HIF1AN. Hydroxylated at Asn-2022 by HIF1AN (By similarity). 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>Sitei1664 – 1665Cleavage; by furin-like proteaseBy similarity2
Sitei1710 – 1711Cleavage; by ADAM17By similarity2

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P46531

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P46531

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P46531

MaxQB - The MaxQuant DataBase

More...MaxQBi		P46531

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

More...PaxDbi		P46531

PeptideAtlas

More...PeptideAtlasi		P46531

PRoteomics IDEntifications database

More...PRIDEi		P46531

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55742

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P46531

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

More...PhosphoSitePlusi		P46531

<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

In fetal tissues most abundant in spleen, brain stem and lung. Also present in most adult tissues where it is found mainly in lymphoid tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000148400 Expressed in 219 organ(s), highest expression level in visceral pleura

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P46531 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB008112
CAB022466
HPA067168

<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 (PubMed:11101851, PubMed:12370315). The NOTCH1 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 (PubMed:10713164). 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 (PubMed:17573339).

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 (By similarity).

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).

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 (PubMed:30598546).

By similarity8 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110913, 232 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P46531

Database of interacting proteins

More...DIPi		DIP-29919N

Protein interaction database and analysis system

More...IntActi		P46531, 155 interactors

Molecular INTeraction database

More...MINTi		P46531

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000277541

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P46531

<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

12555
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		P46531

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P46531

<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 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 20PROSITE-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 27PROSITE-ProRule annotationAdd BLAST37
Domaini1059 – 1095EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1097 – 1143EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1145 – 1181EGF-like 30PROSITE-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 1PROSITE-ProRule annotationAdd BLAST41
Repeati1490 – 1531LNR 2PROSITE-ProRule annotationAdd BLAST42
Repeati1532 – 1571LNR 3PROSITE-ProRule annotationAdd BLAST40
Repeati1927 – 1956ANK 1Sequence analysisAdd BLAST30
Repeati1960 – 1990ANK 2Sequence analysisAdd BLAST31
Repeati1994 – 2023ANK 3Sequence analysisAdd BLAST30
Repeati2027 – 2056ANK 4Sequence analysisAdd BLAST30
Repeati2060 – 2089ANK 5Sequence analysisAdd BLAST30
Repeati2095 – 2122ANK 6Add BLAST28

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
Regioni1728 – 1760Interaction with PSEN11 PublicationAdd BLAST33
Regioni1947 – 1955HIF1AN-bindingBy similarity9
Regioni2014 – 2022HIF1AN-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 biasi1575 – 1578Poly-Val4
Compositional biasi1661 – 1664Poly-Arg4
Compositional biasi1728 – 1731Poly-Pro4
Compositional biasi1740 – 1743Poly-Ala4
Compositional biasi1901 – 1904Poly-Glu4
Compositional biasi2259 – 2262Poly-Gly4
Compositional biasi2403 – 2406Poly-Gln4
Compositional biasi2410 – 2417Poly-Pro8
Compositional biasi2521 – 2524Poly-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.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		ENSGT00940000157157

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000234369

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P46531

KEGG Orthology (KO)

More...KOi		K02599

Identification of Orthologs from Complete Genome Data

More...OMAi		NEGSCLD

Database of Orthologous Groups

More...OrthoDBi		1171129at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P46531

TreeFam database of animal gene trees

More...TreeFami		TF351641

Family and domain databases

Database of protein disorder

More...DisProti		DP01104

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, 25 hits
PF07645 EGF_CA, 4 hits
PF12661 hEGF, 2 hits
PF06816 NOD, 1 hit
PF07684 NODP, 1 hit
PF00066 Notch, 3 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002279 Notch, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01452 LNOTCHREPEAT
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, 20 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>. 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_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.

P46531-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPLLAPLLC LALLPALAAR GPRCSQPGET CLNGGKCEAA NGTEACVCGG 
        60         70         80         90        100
AFVGPRCQDP NPCLSTPCKN AGTCHVVDRR GVADYACSCA LGFSGPLCLT 
       110        120        130        140        150
PLDNACLTNP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA 
       160        170        180        190        200
NGGQCLPFEA SYICHCPPSF HGPTCRQDVN ECGQKPGLCR HGGTCHNEVG 
       210        220        230        240        250
SYRCVCRATH TGPNCERPYV PCSPSPCQNG GTCRPTGDVT HECACLPGFT 
       260        270        280        290        300
GQNCEENIDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 
       310        320        330        340        350
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFHGATC 
       360        370        380        390        400
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC 
       410        420        430        440        450
PSGYTGPACS QDVDECSLGA NPCEHAGKCI NTLGSFECQC LQGYTGPRCE 
       460        470        480        490        500
IDVNECVSNP CQNDATCLDQ IGEFQCICMP GYEGVHCEVN TDECASSPCL 
       510        520        530        540        550
HNGRCLDKIN EFQCECPTGF TGHLCQYDVD ECASTPCKNG AKCLDGPNTY 
       560        570        580        590        600
TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CRPGYTGHHC 
       610        620        630        640        650
ETNINECSSQ PCRHGGTCQD RDNAYLCFCL KGTTGPNCEI NLDDCASSPC 
       660        670        680        690        700
DSGTCLDKID GYECACEPGY TGSMCNINID ECAGNPCHNG GTCEDGINGF 
       710        720        730        740        750
TCRCPEGYHD PTCLSEVNEC NSNPCVHGAC RDSLNGYKCD CDPGWSGTNC 
       760        770        780        790        800
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC 
       810        820        830        840        850
LNQGTCIDDV AGYKCNCLLP YTGATCEVVL APCAPSPCRN GGECRQSEDY 
       860        870        880        890        900
ESFSCVCPTG WQGQTCEVDI NECVLSPCRH GASCQNTHGG YRCHCQAGYS 
       910        920        930        940        950
GRNCETDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFRGT FCEEDINECA 
       960        970        980        990       1000
SDPCRNGANC TDCVDSYTCT CPAGFSGIHC ENNTPDCTES SCFNGGTCVD 
      1010       1020       1030       1040       1050
GINSFTCLCP PGFTGSYCQH DVNECDSQPC LHGGTCQDGC GSYRCTCPQG 
      1060       1070       1080       1090       1100
YTGPNCQNLV HWCDSSPCKN GGKCWQTHTQ YRCECPSGWT GLYCDVPSVS 
      1110       1120       1130       1140       1150
CEVAAQRQGV DVARLCQHGG LCVDAGNTHH CRCQAGYTGS YCEDLVDECS 
      1160       1170       1180       1190       1200
PSPCQNGATC TDYLGGYSCK CVAGYHGVNC SEEIDECLSH PCQNGGTCLD 
      1210       1220       1230       1240       1250
LPNTYKCSCP RGTQGVHCEI NVDDCNPPVD PVSRSPKCFN NGTCVDQVGG 
      1260       1270       1280       1290       1300
YSCTCPPGFV GERCEGDVNE CLSNPCDARG TQNCVQRVND FHCECRAGHT 
      1310       1320       1330       1340       1350
GRRCESVING CKGKPCKNGG TCAVASNTAR GFICKCPAGF EGATCENDAR 
      1360       1370       1380       1390       1400
TCGSLRCLNG GTCISGPRSP TCLCLGPFTG PECQFPASSP CLGGNPCYNQ 
      1410       1420       1430       1440       1450
GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFGGGAGRDI PPPLIEEACE 
      1460       1470       1480       1490       1500
LPECQEDAGN KVCSLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 
      1510       1520       1530       1540       1550
SDGHCDSQCN SAGCLFDGFD CQRAEGQCNP LYDQYCKDHF SDGHCDQGCN 
      1560       1570       1580       1590       1600
SAECEWDGLD CAEHVPERLA AGTLVVVVLM PPEQLRNSSF HFLRELSRVL 
      1610       1620       1630       1640       1650
HTNVVFKRDA HGQQMIFPYY GREEELRKHP IKRAAEGWAA PDALLGQVKA 
      1660       1670       1680       1690       1700
SLLPGGSEGG RRRRELDPMD VRGSIVYLEI DNRQCVQASS QCFQSATDVA 
      1710       1720       1730       1740       1750
AFLGALASLG SLNIPYKIEA VQSETVEPPP PAQLHFMYVA AAAFVLLFFV 
      1760       1770       1780       1790       1800
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA 
      1810       1820       1830       1840       1850
SDGALMDDNQ NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA 
      1860       1870       1880       1890       1900
ADLRMSAMAP TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS 
      1910       1920       1930       1940       1950
EEEEDAPAVI SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA 
      1960       1970       1980       1990       2000
SADANIQDNM GRTPLHAAVS ADAQGVFQIL IRNRATDLDA RMHDGTTPLI 
      2010       2020       2030       2040       2050
LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN 
      2060       2070       2080       2090       2100
GANKDMQNNR EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI 
      2110       2120       2130       2140       2150
AQERMHHDIV RLLDEYNLVR SPQLHGAPLG GTPTLSPPLC SPNGYLGSLK 
      2160       2170       2180       2190       2200
PGVQGKKVRK PSSKGLACGS KEAKDLKARR KKSQDGKGCL LDSSGMLSPV 
      2210       2220       2230       2240       2250
DSLESPHGYL SDVASPPLLP SPFQQSPSVP LNHLPGMPDT HLGIGHLNVA 
      2260       2270       2280       2290       2300
AKPEMAALGG GGRLAFETGP PRLSHLPVAS GTSTVLGSSS GGALNFTVGG 
      2310       2320       2330       2340       2350
STSLNGQCEW LSRLQSGMVP NQYNPLRGSV APGPLSTQAP SLQHGMVGPL 
      2360       2370       2380       2390       2400
HSSLAASALS QMMSYQGLPS TRLATQPHLV QTQQVQPQNL QMQQQNLQPA 
      2410       2420       2430       2440       2450
NIQQQQSLQP PPPPPQPHLG VSSAASGHLG RSFLSGEPSQ ADVQPLGPSS 
      2460       2470       2480       2490       2500
LAVHTILPQE SPALPTSLPS SLVPPVTAAQ FLTPPSQHSY SSPVDNTPSH 
      2510       2520       2530       2540       2550
QLQVPEHPFL TPSPESPDQW SSSSPHSNVS DWSEGVSSPP TSMQSQIARI 

PEAFK
Length:2,555
Mass (Da):272,505
Last modified:September 23, 2008 - v4
<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:iE173C872D195F028
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 conflicti187G → R in AAG33848 (Ref. 1) Curated1
Sequence conflicti187G → R in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti282R → P in AAG33848 (Ref. 1) Curated1
Sequence conflicti282R → P in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti477I → M in AAG33848 (Ref. 1) Curated1
Sequence conflicti477I → M in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti614 – 615HG → LR in AAG33848 (Ref. 1) Curated2
Sequence conflicti614 – 615HG → LR in AAA60614 (PubMed:1831692).Curated2
Sequence conflicti621R → P in AAG33848 (Ref. 1) Curated1
Sequence conflicti621R → P in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti677I → S in AAG33848 (Ref. 1) Curated1
Sequence conflicti677I → S in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti775Y → I in AAG33848 (Ref. 1) Curated1
Sequence conflicti775Y → I in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti803Q → K in AAG33848 (Ref. 1) Curated1
Sequence conflicti803Q → K in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti860 – 862GWQ → AGAK in AAG33848 (Ref. 1) Curated3
Sequence conflicti860 – 862GWQ → AGAK in AAA60614 (PubMed:1831692).Curated3
Sequence conflicti1021D → V in AAG33848 (Ref. 1) Curated1
Sequence conflicti1021D → V in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1028Q → R in AAG33848 (Ref. 1) Curated1
Sequence conflicti1028Q → R in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1032H → L in AAG33848 (Ref. 1) Curated1
Sequence conflicti1032H → L in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1040 – 1043CGSY → RGLH in AAG33848 (Ref. 1) Curated4
Sequence conflicti1040 – 1043CGSY → RGLH in AAA60614 (PubMed:1831692).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034898300Q → R. Corresponds to variant dbSNP:rs11574885Ensembl.1
Natural variantiVAR_071960429C → R in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587777736EnsemblClinVar.1
Natural variantiVAR_048990879R → W. Corresponds to variant dbSNP:rs11574895Ensembl.1
Natural variantiVAR_0719611496C → Y in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587781259EnsemblClinVar.1
Natural variantiVAR_0466181671V → I. Corresponds to variant dbSNP:rs2229968EnsemblClinVar.1
Natural variantiVAR_0719621989D → N in AOS5. 1 PublicationCorresponds to variant dbSNP:rs587777734EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF308602 mRNA Translation: AAG33848.1
AL592301 Genomic DNA No translation available.
AL354671 Genomic DNA No translation available.
M73980 mRNA Translation: AAA60614.1
AB209873 mRNA Translation: BAD93110.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS43905.1

Protein sequence database of the Protein Information Resource

More...PIRi		A40043

NCBI Reference Sequences

More...RefSeqi		NP_060087.3, NM_017617.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000651671; ENSP00000498587; ENSG00000148400

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4851

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4851

UCSC genome browser

More...UCSCi		uc004chz.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308602 mRNA Translation: AAG33848.1
AL592301 Genomic DNA No translation available.
AL354671 Genomic DNA No translation available.
M73980 mRNA Translation: AAA60614.1
AB209873 mRNA Translation: BAD93110.1
CCDSiCCDS43905.1
PIRiA40043
RefSeqiNP_060087.3, NM_017617.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PB5NMR-A1446-1480[»]
1TOZNMR-A411-526[»]
1YYHX-ray1.90A/B1872-2114[»]
2F8XX-ray3.25K1872-2126[»]
2F8YX-ray1.55A/B1905-2126[»]
2HE0X-ray1.90A/B1872-2114[»]
2VJ3X-ray2.60A411-526[»]
3ETOX-ray2.00A/B1446-1733[»]
3I08X-ray3.20A/C1446-1664[»]
B/D1665-1733[»]
3L95X-ray2.19X/Y1448-1728[»]
3NBNX-ray3.45B/E1872-2126[»]
3V79X-ray3.85K1872-2126[»]
R1759-1777[»]
4CUDX-ray1.85A411-526[»]
4CUEX-ray3.00A411-526[»]
4CUFX-ray2.29A411-526[»]
4D0EX-ray1.61A411-526[»]
4D0FX-ray2.80A411-526[»]
5FM9X-ray2.92A140-294[»]
5FMAX-ray2.46A/B142-294[»]
5KZONMR-A1721-1771[»]
5L0RX-ray1.50B452-491[»]
5UB5X-ray2.09B452-491[»]
6IDFelectron microscopy2.70E1721-1821[»]
6PY8X-ray3.75F/K1759-2127[»]
SMRiP46531
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110913, 232 interactors
CORUMiP46531
DIPiDIP-29919N
IntActiP46531, 155 interactors
MINTiP46531
STRINGi9606.ENSP00000277541

Chemistry databases

BindingDBiP46531
ChEMBLiCHEMBL2146346

Protein family/group databases

TCDBi9.B.87.1.12 the selenoprotein p receptor (selp-receptor) family

PTM databases

iPTMnetiP46531
PhosphoSitePlusiP46531

Polymorphism and mutation databases

BioMutaiNOTCH1
DMDMi206729936

Proteomic databases

EPDiP46531
jPOSTiP46531
MassIVEiP46531
MaxQBiP46531
PaxDbiP46531
PeptideAtlasiP46531
PRIDEiP46531
ProteomicsDBi55742

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P46531

Genome annotation databases

EnsembliENST00000651671; ENSP00000498587; ENSG00000148400
GeneIDi4851
KEGGihsa:4851
UCSCiuc004chz.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4851
DisGeNETi4851

GeneCards: human genes, protein and diseases

More...GeneCardsi		NOTCH1
GeneReviewsiNOTCH1
HGNCiHGNC:7881 NOTCH1
HPAiCAB008112
CAB022466
HPA067168
MalaCardsiNOTCH1
MIMi109730 phenotype
190198 gene
616028 phenotype
neXtProtiNX_P46531
OpenTargetsiENSG00000148400
Orphaneti974 Adams-Oliver syndrome
402075 Familial bicuspid aortic valve
PharmGKBiPA31683

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IR7G Eukaryota
COG0666 LUCA
GeneTreeiENSGT00940000157157
HOGENOMiHOG000234369
InParanoidiP46531
KOiK02599
OMAiNEGSCLD
OrthoDBi1171129at2759
PhylomeDBiP46531
TreeFamiTF351641

Enzyme and pathway databases

ReactomeiR-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-210744 Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2644607 Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling
R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant
R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-350054 Notch-HLH transcription pathway
R-HSA-5083630 Defective LFNG causes SCDO3
R-HSA-8941856 RUNX3 regulates NOTCH signaling
R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription
R-HSA-9013695 NOTCH4 Intracellular Domain Regulates Transcription
SignaLinkiP46531
SIGNORiP46531

Miscellaneous databases

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

More...ChiTaRSi		NOTCH1 human
EvolutionaryTraceiP46531

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Notch-1

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

More...GenomeRNAii		4851
PharosiP46531

Protein Ontology

More...PROi		PR:P46531

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000148400 Expressed in 219 organ(s), highest expression level in visceral pleura
GenevisibleiP46531 HS

Family and domain databases

DisProtiDP01104
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, 25 hits
PF07645 EGF_CA, 4 hits
PF12661 hEGF, 2 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, 33 hits
SM00004 NL, 3 hits
SM01338 NOD, 1 hit
SM01339 NODP, 1 hit
SUPFAMiSSF48403 SSF48403, 1 hit
SSF57184 SSF57184, 6 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, 20 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_HUMAN
<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: P46531
Secondary accession number(s): Q59ED8, Q5SXM3
<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_and_isoforms">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: September 23, 2008
Last modified: October 16, 2019
This is version 234 of the entry and version 4 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again