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Entry version 53 (02 Jun 2021)
Sequence version 2 (16 Oct 2013)
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Protein

Neurogenic locus notch homolog protein 1

Gene

NOTCH1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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 (By similarity).

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) (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi448Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi451Calcium 1; via amide nitrogenBy similarity1
Metal bindingi468Calcium 2By similarity1
Metal bindingi469Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi471Calcium 2By similarity1
Metal bindingi485Calcium 2By similarity1
Metal bindingi486Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi506Calcium 3By similarity1
Metal bindingi507Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi509Calcium 3By similarity1
Metal bindingi523Calcium 3By similarity1
Metal bindingi524Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1473Calcium 4; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi1476Calcium 4PROSITE-ProRule annotation1
Metal bindingi1491Calcium 4PROSITE-ProRule annotation1
Metal bindingi1494Calcium 4PROSITE-ProRule annotation1

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

GO - Biological processi

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

Molecular functionActivator, Developmental protein, Receptor
Biological processAngiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation
LigandCalcium, Metal-binding

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 1
Short name:
Notch 1
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NOTCH1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<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 identifieri10029 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus
<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
  • UP000001075 <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: Unassembled WGS sequence

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini37 – 1741ExtracellularCuratedAdd BLAST1705
<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>Transmembranei1742 – 1762HelicalBy similarityAdd BLAST21
Topological domaini1763 – 2527CytoplasmicCuratedAdd BLAST765

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 36Sequence analysisAdd BLAST36
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000042401337 – 2527Neurogenic locus notch homolog protein 1Add BLAST2491
ChainiPRO_00004240141727 – 2527Notch 1 extracellular truncationBy similarityAdd BLAST801
ChainiPRO_00004240151760 – 2527Notch 1 intracellular domainBy similarityAdd BLAST768

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 bondi40 ↔ 53By similarity
Disulfide bondi47 ↔ 62By 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>Glycosylationi57N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi64 ↔ 73By similarity
Disulfide bondi79 ↔ 90By similarity
Glycosylationi81O-linked (Glc...) serineBy similarity1
Disulfide bondi84 ↔ 103By similarity
Glycosylationi89O-linked (Fuc...) threonineBy similarity1
Disulfide bondi105 ↔ 114By similarity
Disulfide bondi122 ↔ 133By similarity
Disulfide bondi127 ↔ 143By similarity
Glycosylationi132O-linked (Fuc...) threonineBy similarity1
Disulfide bondi145 ↔ 154By similarity
Disulfide bondi160 ↔ 171By similarity
Glycosylationi162O-linked (Glc...) serineBy similarity1
Disulfide bondi165 ↔ 180By similarity
Disulfide bondi182 ↔ 191By similarity
Disulfide bondi198 ↔ 211By similarity
Disulfide bondi205 ↔ 220By similarity
Glycosylationi210O-linked (Fuc...) threonineBy similarity1
Disulfide bondi222 ↔ 231By similarity
Disulfide bondi238 ↔ 249By similarity
Disulfide bondi243 ↔ 259By similarity
Glycosylationi248O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi248O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi261 ↔ 270By similarity
Disulfide bondi277 ↔ 288By similarity
Disulfide bondi282 ↔ 297By similarity
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi315 ↔ 328By similarity
Disulfide bondi322 ↔ 337By similarity
Glycosylationi327O-linked (Fuc...) threonineBy similarity1
Disulfide bondi339 ↔ 348By similarity
Disulfide bondi355 ↔ 366By similarity
Glycosylationi357O-linked (Glc...) serineBy similarity1
Disulfide bondi360 ↔ 375By similarity
Glycosylationi365O-linked (Fuc...) threonineBy similarity1
Disulfide bondi377 ↔ 386By similarity
Disulfide bondi392 ↔ 403By similarity
Glycosylationi394O-linked (Glc...) serineBy similarity1
Disulfide bondi397 ↔ 414By similarity
Disulfide bondi416 ↔ 425By similarity
Disulfide bondi432 ↔ 445By similarity
Disulfide bondi439 ↔ 454By similarity
Glycosylationi451O-linked (Glc...) serineBy similarity1
Disulfide bondi456 ↔ 465By similarity
Disulfide bondi472 ↔ 483By similarity
Glycosylationi474O-linked (Glc...) serineBy similarity1
Disulfide bondi477 ↔ 492By similarity
Glycosylationi482O-linked (Fuc...) threonineBy similarity1
Disulfide bondi494 ↔ 503By similarity
Disulfide bondi510 ↔ 521By similarity
Glycosylationi512O-linked (Glc...) serineBy similarity1
Disulfide bondi515 ↔ 530By similarity
Disulfide bondi532 ↔ 541By similarity
Disulfide bondi548 ↔ 559By similarity
Glycosylationi550O-linked (Glc...) serineBy similarity1
Disulfide bondi553 ↔ 568By similarity
Disulfide bondi570 ↔ 579By similarity
Disulfide bondi586 ↔ 596By similarity
Disulfide bondi591 ↔ 605By similarity
Disulfide bondi607 ↔ 616By similarity
Disulfide bondi623 ↔ 634By similarity
Glycosylationi625O-linked (Glc...) serineBy similarity1
Disulfide bondi628 ↔ 643By similarity
Glycosylationi633O-linked (Fuc...) threonineBy similarity1
Disulfide bondi645 ↔ 654By similarity
Disulfide bondi661 ↔ 671By similarity
Glycosylationi663O-linked (Glc...) serineBy similarity1
Disulfide bondi666 ↔ 680By similarity
Disulfide bondi682 ↔ 691By similarity
Disulfide bondi698 ↔ 709By similarity
Disulfide bondi703 ↔ 718By similarity
Glycosylationi708O-linked (Fuc...) threonineBy similarity1
Disulfide bondi720 ↔ 729By similarity
Disulfide bondi736 ↔ 746By similarity
Glycosylationi738O-linked (Glc...) serineBy similarity1
Disulfide bondi741 ↔ 755By similarity
Disulfide bondi757 ↔ 766By similarity
Disulfide bondi773 ↔ 784By similarity
Glycosylationi775O-linked (Glc...) serineBy similarity1
Disulfide bondi778 ↔ 793By similarity
Glycosylationi783O-linked (Fuc...) threonineBy similarity1
Disulfide bondi795 ↔ 804By similarity
Glycosylationi800O-linked (GlcNAc) serineBy similarity1
Disulfide bondi811 ↔ 822By similarity
Glycosylationi813O-linked (Glc...) serineBy similarity1
Disulfide bondi816 ↔ 831By similarity
Glycosylationi821O-linked (Fuc...) threonineBy similarity1
Disulfide bondi833 ↔ 842By similarity
Disulfide bondi849 ↔ 860By similarity
Glycosylationi904N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi916O-linked (GlcNAc) threonineBy similarity1
Glycosylationi937O-linked (Fuc) serineBy similarity1
Glycosylationi967O-linked (Glc...) serineBy similarity1
Glycosylationi975N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1013O-linked (Fuc...) threonineBy similarity1
Glycosylationi1043O-linked (Glc...) serineBy similarity1
Glycosylationi1051O-linked (Fuc...) threonineBy similarity1
Glycosylationi1081O-linked (Glc...) serineBy similarity1
Disulfide bondi1117 ↔ 1138Curated
Glycosylationi1175O-linked (Fuc...) threonineBy similarity1
Glycosylationi1195N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1205O-linked (Glc...) serineBy similarity1
Glycosylationi1213O-linked (Fuc...) threonineBy similarity1
Glycosylationi1257N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1289O-linked (Glc...) serineBy similarity1
Glycosylationi1378O-linked (Fuc...) threonineBy similarity1
Glycosylationi1395O-linked (GlcNAc...) threonineBy similarity1
Glycosylationi1418O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi1418O-linked (GalNAc...) threonine; alternateBy similarity1
Glycosylationi1505N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1603N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1731O-linked (GalNAc...) threonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1765Glycyl 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 residuei1867PhosphothreonineBy similarity1
Modified residuei1961(3S)-3-hydroxyasparagine; by HIF1AN; partialBy similarity1
Modified residuei2028(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by ADAM17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by one of the catalytic subunits of gamma-secretase (PSEN1 or PSEN2) to release a Notch-derived peptide containing the intracellular domain (NICD) from the membrane.By similarity
Phosphorylated.By similarity
O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). O-glycosylated on the EGF-like domains (PubMed:10734111). O-glucosylated at Ser-451 by KDELC1 and KDELC2 (By similarity). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4. MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (By similarity).By similarity1 Publication
Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1. Monoubiquitination at Lys-1765 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch.By similarity
Hydroxylated at Asn-1961 by HIF1AN. Hydroxylated at Asn-2028 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>Sitei1670 – 1671Cleavage; by furin-like proteaseBy similarity2
Sitei1726 – 1727Cleavage; by ADAM17By similarity2

Keywords - PTMi

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

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

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

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

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

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

Forms a trimeric complex with FBXW7 and SGK1.

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

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

Interacts (via NICD) with MDM2A.

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

Interacts with THBS4 (By similarity).

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

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

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 (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei485Interaction with DLL4By similarity1

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10029.XP_007637278.1

<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>Domaini75 – 115EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini118 – 155EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini156 – 192EGF-like 3PROSITE-ProRule annotationAdd BLAST37
Domaini194 – 232EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini234 – 271EGF-like 5PROSITE-ProRule annotationAdd BLAST38
Domaini273 – 309EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini311 – 349EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini351 – 387EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini388 – 426EGF-like 9PROSITE-ProRule annotationAdd BLAST39
Domaini428 – 466EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini468 – 504EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini506 – 542EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini544 – 580EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini582 – 617EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini619 – 655EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini657 – 692EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini694 – 730EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini732 – 767EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini769 – 805EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini807 – 843EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini845 – 883EGF-like 21PROSITE-ProRule annotationAdd BLAST39
Domaini885 – 921EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini923 – 959EGF-like 23PROSITE-ProRule annotationAdd BLAST37
Domaini961 – 997EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini999 – 1035EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1037 – 1073EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1075 – 1111EGF-like 27PROSITE-ProRule annotationAdd BLAST37
Domaini1113 – 1159EGF-like 28CuratedAdd BLAST47
Domaini1161 – 1197EGF-like 29PROSITE-ProRule annotationAdd BLAST37
Domaini1199 – 1235EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1237 – 1281EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1283 – 1321EGF-like 32PROSITE-ProRule annotationAdd BLAST39
Domaini1323 – 1362EGF-like 33PROSITE-ProRule annotationAdd BLAST40
Domaini1364 – 1400EGF-like 34PROSITE-ProRule annotationAdd BLAST37
Domaini1403 – 1442EGF-like 35PROSITE-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>Repeati1465 – 1505LNR 1Add BLAST41
Repeati1506 – 1547LNR 2Add BLAST42
Repeati1548 – 1587LNR 3Add BLAST40
Repeati1933 – 1962ANK 1Add BLAST30
Repeati1966 – 1996ANK 2Add BLAST31
Repeati2000 – 2029ANK 3Add BLAST30
Repeati2033 – 2062ANK 4Add BLAST30
Repeati2066 – 2095ANK 5Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni436 – 437Interaction with DLL4By similarity2
Regioni464 – 468Interaction with DLL4By similarity5
Regioni1734 – 1766Interaction with PSEN1By similarityAdd BLAST33
Regioni1786 – 1818DisorderedSequence analysisAdd BLAST33
Regioni1953 – 1961HIF1AN-bindingBy similarity9
Regioni2020 – 2028HIF1AN-bindingBy similarity9
Regioni2157 – 2243DisorderedSequence analysisAdd BLAST87
Regioni2360 – 2527DisorderedSequence analysisAdd BLAST168

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2176 – 2193Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi2360 – 2398Polar residuesSequence analysisAdd BLAST39
Compositional biasi2425 – 2478Polar residuesSequence analysisAdd BLAST54
Compositional biasi2486 – 2520Polar residuesSequence analysisAdd BLAST35

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

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

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

Belongs to the NOTCH family.Curated

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1217, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
G3I6Z6

Database of Orthologous Groups

More...
OrthoDBi
7525at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR024600, DUF3454_notch
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR008297, Notch
IPR035993, Notch-like_dom_sf
IPR022362, Notch_1
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796, Ank_2, 2 hits
PF11936, DUF3454, 1 hit
PF00008, EGF, 20 hits
PF07645, EGF_CA, 5 hits
PF12661, hEGF, 3 hits
PF06816, NOD, 1 hit
PF07684, NODP, 1 hit
PF00066, Notch, 3 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002279, Notch, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01452, LNOTCHREPEAT
PR01984, NOTCH1

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 6 hits
SM01334, DUF3454, 1 hit
SM00181, EGF, 36 hits
SM00179, EGF_CA, 33 hits
SM00004, NL, 3 hits
SM01338, NOD, 1 hit
SM01339, NODP, 1 hit

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS00010, ASX_HYDROXYL, 22 hits
PS00022, EGF_1, 35 hits
PS01186, EGF_2, 28 hits
PS50026, EGF_3, 36 hits
PS01187, EGF_CA, 21 hits
PS50258, LNR, 3 hits

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

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

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

G3I6Z6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRSDSRAGA LLEGGCEQNI DPRRAAHCHH PRLATSSLRC SQPSGTCLNG
60 70 80 90 100
GRCEVANGTE ACVCSGPFVG QRCQDPNPCL STPCKNAGTC HVVEHGGTVN
110 120 130 140 150
YACSCPLGFS GPLCLTPLDN ACLANPCRNG GTCDLLTLTE YKCRCPPGWS
160 170 180 190 200
GKSCQQADPC ASNPCANGGQ CLPFESSYIC GCPPGFHGPT CRQDVNECSQ
210 220 230 240 250
NPGLCRHGGT CHNEIGSYRC VCRATHTGPH CELPYVPCSP SPCQNGGTCR
260 270 280 290 300
PTGDTTHECA CLPGFAGQNC EENVDDCPGN NCKNGGACVD GVNTYNCRCP
310 320 330 340 350
PEWTGQYCTE DVDECQLMPN ACQNGGTCHN THGGYNCVCV NGWTGEDCSE
360 370 380 390 400
NIDDCASAAC FQGATCHDRV ASFYCECPHG RTGLLCHLND ACISNPCNEG
410 420 430 440 450
SNCDTNPVNG KAICTCPSGY TGPACSQDVD ECALGANPCE HAGKCLNTLG
460 470 480 490 500
SFECQCLQGY TGPRCEIDVN ECISNPCQND ATCLDQIGEF QCICMPGYEG
510 520 530 540 550
VYCEINTDEC ASSPCLHNGH CMDKINEFLC QCPKGFSGHL CQYDVDECAS
560 570 580 590 600
TPCKNGAKCL DGPNTYTCVC TEGYTGTHCE VDIDECDPDP CHYGFCKDGV
610 620 630 640 650
ATFTCLCQPG YTGHHCETNI NECHSQPCRH GGTCQDRDNS YLCLCLKGTT
660 670 680 690 700
GPNCEINLDD CASNPCDSGT CLDKIDGYEC ACEPGYTGSM CNVNIDECAG
710 720 730 740 750
SPCHNGGTCE DGIAGFTCRC PEGYHDPTCL SEVNECNSNP CIHGACRDGL
760 770 780 790 800
NGYKCDCAPG WSGTNCDINN NECESNPCVN GGTCKDMTSG YVCTCREGFS
810 820 830 840 850
GPNCQTNINE CASNPCLNQG TCIDDVAGYK CNCPLPYTGA TCEVVLAPCA
860 870 880 890 900
TSPCKNSGVC KESEDYESFS CVCPTGWQGQ TCEIDINECV KSPCRHGASC
910 920 930 940 950
QNTNGSYRCL CQAGYTGRNC ESDIDDCRPN PCHNGGSCTD GINMAFCDCL
960 970 980 990 1000
PGFQGAFCEE DINECASNPC RNGANCTDCV DSYTCTCPAG FNGIHCENNT
1010 1020 1030 1040 1050
PDCTESSCFN GGTCVDGINS FTCLCPPGFT GSYCQYDVNE CDSRPCLHGG
1060 1070 1080 1090 1100
TCQDSYGTYK CTCPQGYTGL NCQNLVHWCD SAPCKNGGKC WQTNTQYHCE
1110 1120 1130 1140 1150
CRSGWTGFNC DVLSVSCEVA AQKRGIDVTL LCQHGGLCVD EEDKHYCHCQ
1160 1170 1180 1190 1200
AGYTGSYCED EVDECSPNPC QNGATCTDYL GGFSCKCVAG YHGSNCSEEI
1210 1220 1230 1240 1250
NECLSQPCQN GGTCIDLTNT YKCSCPRGTQ GVHCEINVDD CHPHLDPASR
1260 1270 1280 1290 1300
SPKCFNNGTC VDQVGGYSCT CPPGFVGERC EGDINECLSN PCDPRGTQDC
1310 1320 1330 1340 1350
VQRVNDFHCE CRAGHTGRRC ESVINGCRGK PCKNGGVCAV ASNTARGFIC
1360 1370 1380 1390 1400
RCPAGFEGAT CENDARTCGS LRCLNGGTCI SGPRSPTCLC LGSFTGPECQ
1410 1420 1430 1440 1450
FPASSPCVGS NPCYNQGTCE PTSESPFYRC LCPAKFNGLL CHILDYSFTG
1460 1470 1480 1490 1500
GAGRDIPPPQ IEEACELPEC QEDAGNKVCN LQCNNHACGW DGGDCSLNFN
1510 1520 1530 1540 1550
DPWKNCTQSL QCWKYFSDGH CDSQCNSASC LFDGFDCQRT EGQCNPLYDQ
1560 1570 1580 1590 1600
YCKDHFSDGH CDQGCNSAEC DWDGLDCADH VPERLAAGTL VLVVLLPPEQ
1610 1620 1630 1640 1650
LRNNSFHFLR ELSHVLHTNV VFKRDAEGQQ MIFPYYGHEE ELRKHPIKRS
1660 1670 1680 1690 1700
AVGWTTSSLL PSTNGGRQRR ELDPMDIRGS IVYLEIDNRQ CVQSSSQCFQ
1710 1720 1730 1740 1750
SATDVAAFLG ALASLGNLNI PYKIEAVKSE TVEPPLPSQL HLMYLAAAAF
1760 1770 1780 1790 1800
VLLFFVGCGV LLSRKRRRQH GQLWFPEGFK VSEASKKKRR EPLGEDSVGL
1810 1820 1830 1840 1850
KPLKNASDGA LMDDNQNEWG DEDLETKKFR FEEPVVVPDL DDQTDHRQWT
1860 1870 1880 1890 1900
QQHLDAADLR MSAMAPTPPQ GEVDADCMDV NVRGPDGFTP LMIASCSGGG
1910 1920 1930 1940 1950
LETGNSEEEE DAPAVISDFI YQGASLHNQT DRTGETALHL AARYSRSDAA
1960 1970 1980 1990 2000
KRLLEASADA NIQDNMGRTP LHAAVSADAQ GVFQILLRNR ATDLDARMHD
2010 2020 2030 2040 2050
GTTPLILAAR LAVEGMLEDL INSHADVNAV DDLGKSALHW AAAVNNVDAA
2060 2070 2080 2090 2100
VVLLKNGANK DMQNNKEETP LFLAAREGSY ETAKVLLDHF ANRDITDHMD
2110 2120 2130 2140 2150
RLPRDIAQER MHHDIVRLLD EYNLVRSPQL HGTALGGTPT LSPTLCSPNG
2160 2170 2180 2190 2200
YLGNLKSATQ GKKARKPSTK GLACGSKEAK DLKARRKKSQ DGKGCLLDSS
2210 2220 2230 2240 2250
SMLSPVDSLE SPHGYLSDVA SPPLLPSPFQ QSPSMPLSHL PGMPDTHLGI
2260 2270 2280 2290 2300
SHLNVAAKPE MAALAGSSRL AFEPPPPRLP HLPVASSAST VLSTNGSXGE
2310 2320 2330 2340 2350
EEWLAPSQYN PLRPGVASGT LSTQAAGLQH GMMGPLHSSL STNTLSPMIY
2360 2370 2380 2390 2400
QGLPNTRLAT QPHLVQTQQV QPQNLQIQPQ NLQPPSQPHL SVSSAANGHL
2410 2420 2430 2440 2450
GRSFLGGEHS QADVQPLGPS SLPVHTILPQ ESQALPTSLP SSMVPPMTTT
2460 2470 2480 2490 2500
QFLTPPSQHS YSSSPVDNTP SHQLQVPEHP FLTPSPESPD QWSSSSPHSN
2510 2520
ISDWSEGISS PPTSMPSQIT HIPEAFK
Length:2,527
Mass (Da):270,858
Last modified:October 16, 2013 - v2
<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:i5E20EC5287850426
GO

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
JH001398 Genomic DNA Translation: EGW12778.1

NCBI Reference Sequences

More...
RefSeqi
XP_003510910.1, XM_003510862.3

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH001398 Genomic DNA Translation: EGW12778.1
RefSeqiXP_003510910.1, XM_003510862.3

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

Protein-protein interaction databases

STRINGi10029.XP_007637278.1

Phylogenomic databases

eggNOGiKOG1217, Eukaryota
InParanoidiG3I6Z6
OrthoDBi7525at2759

Family and domain databases

Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR024600, DUF3454_notch
IPR001881, EGF-like_Ca-bd_dom
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR008297, Notch
IPR035993, Notch-like_dom_sf
IPR022362, Notch_1
IPR000800, Notch_dom
IPR010660, Notch_NOD_dom
IPR011656, Notch_NODP_dom
PfamiView protein in Pfam
PF12796, Ank_2, 2 hits
PF11936, DUF3454, 1 hit
PF00008, EGF, 20 hits
PF07645, EGF_CA, 5 hits
PF12661, hEGF, 3 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, 5 hits
SSF90193, SSF90193, 3 hits
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS00010, ASX_HYDROXYL, 22 hits
PS00022, EGF_1, 35 hits
PS01186, EGF_2, 28 hits
PS50026, EGF_3, 36 hits
PS01187, EGF_CA, 21 hits
PS50258, LNR, 3 hits

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_CRIGR
<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: G3I6Z6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 16, 2013
Last modified: June 2, 2021
This is version 53 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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