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Protein

Heparanase

Gene

HPSE

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

Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by EDTA, laminarin sulfate and, to a lower extent, by heparin and sulfamin and activated by calcium and magnesium.By similarity

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.53 sec(-1) for M09 S05a.1 Publication
  1. KM=7.7 µM for M09 S05a, an heparin sulfate analog with a nonasaccharide with N-sulfation and a single GlcNS(6S) toward the reducing end1 Publication

    pH dependencei

    Optimum pH is 4-6.4 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei97Heparan sulfate; via amide nitrogenCombined sources1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei225Proton donorCombined sources1 Publication1
    Binding sitei296Heparan sulfateCombined sources1 Publication1
    Binding sitei303Heparan sulfateCombined sources1 Publication1
    Active sitei343NucleophileCombined sources1 Publication1

    <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

    • beta-glucuronidase activity Source: ProtInc
    • heparanase activity Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • syndecan binding Source: UniProtKB

    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 functionHydrolase
    Biological processCell adhesion
    LigandCalcium, Magnesium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000173083-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.166 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-2024096 HS-GAG degradation
    R-HSA-6798695 Neutrophil degranulation

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q9Y251

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH79 Glycoside Hydrolase Family 79

    <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:
    Heparanase (EC:3.2.1.166)
    Alternative name(s):
    Endo-glucoronidase
    Heparanase-1
    Short name:
    Hpa1
    Cleaved into the following 2 chains:
    <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:HPSE
    Synonyms:HEP, HPA, HPA1, HPR1, HPSE1, HSE1
    <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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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 4

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000173083.14

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:5164 HPSE

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    604724 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9Y251

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Lysosome, Membrane, Nucleus, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi156Y → A or E: Alteration of the correct processing of heparanase which results in the cleavage at an upstream site in the linker peptide and no activation of proheparanase. 1 Publication1
    Mutagenesisi156Y → V: Normal processing. 1 Publication1
    Mutagenesisi158K → A: No association with GS-modified heparin; when associated with K-158. 1 Publication1
    Mutagenesisi161K → A: Two-fold increase in the level of secretion upon addition of GS-modified heparin. No association with GS-modified heparin; when associated with K-161. 1 Publication1
    Mutagenesisi162N → Q: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-178; Q-200; Q-217; Q-238 and Q-459. 1 Publication1
    Mutagenesisi178N → Q: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-162; Q-200; Q-217; Q-238 and Q-459. 1 Publication1
    Mutagenesisi200N → Q: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-217; Q-238 and Q-459. 1 Publication1
    Mutagenesisi217N → Q: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-200; Q-238 and Q-459. 1 Publication1
    Mutagenesisi225E → A: Loss of heparanase activity. No effect on HPSE-mediated cell adhesion. 2 Publications1
    Mutagenesisi238N → Q: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-459. 1 Publication1
    Mutagenesisi343E → A: Loss of heparanase activity. 1 Publication1
    Mutagenesisi367D → A: Strong decrease in heparanase activity. 1 Publication1
    Mutagenesisi378E → A: No reduction in heparanase activity. 1
    Mutagenesisi396E → A: No reduction in heparanase activity. 1
    Mutagenesisi414V → K: Abolishes processing, secretion and enzyme activity. 1 Publication1
    Mutagenesisi417K → E: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
    Mutagenesisi459N → Q: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-238. 1 Publication1
    Mutagenesisi525P → G: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
    Mutagenesisi527F → R: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
    Mutagenesisi528S → K: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
    Mutagenesisi529Y → A: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
    Mutagenesisi531F → R: Abolishes processing, secretion and enzyme activity. 1 Publication1
    Mutagenesisi533V → R: Abolishes processing, secretion and enzyme activity. 1 Publication1
    Mutagenesisi534I → D: Abolishes processing, secretion and enzyme activity. 1 Publication1
    Mutagenesisi535R → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi536N → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi537A → K: Abolishes processing, secretion and enzyme activity. 1 Publication1
    Mutagenesisi538K → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi539V → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi540A → K: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi541A → K: No effect on processing, secretion nor enzyme activity. 1 Publication1
    Mutagenesisi542C → A: Abolishes processing, secretion and enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    10855

    Open Targets

    More...
    OpenTargetsi
    ENSG00000173083

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA29435

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3921

    Drug and drug target database

    More...
    DrugBanki
    DB06779 Dalteparin
    DB01109 Heparin

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2996

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    HPSE

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    296434532

    <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 – 351 PublicationAdd BLAST35
    <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_000004226036 – 109Heparanase 8 kDa subunitAdd BLAST74
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000042261110 – 157Linker peptide3 PublicationsAdd BLAST48
    ChainiPRO_0000042262158 – 543Heparanase 50 kDa subunitAdd BLAST386

    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 bondi127 ↔ 179Combined sources1 Publication
    <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>Glycosylationi162N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Glycosylationi178N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi200N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Glycosylationi217N-linked (GlcNAc...) asparagineCombined sources4 Publications1
    Glycosylationi238N-linked (GlcNAc...) asparagineCombined sources3 Publications1
    Disulfide bondi437 ↔ 542Combined sources2 Publications
    Glycosylationi459N-linked (GlcNAc...) asparagineCombined sources2 Publications1

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

    Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme.6 Publications
    N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9Y251

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9Y251

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

    More...
    PaxDbi
    Q9Y251

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9Y251

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9Y251

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    85653

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    Q9Y251-1 [Q9Y251-1]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9Y251

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

    More...
    PhosphoSitePlusi
    Q9Y251

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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

    Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase.5 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000173083 Expressed in 131 organ(s), highest expression level in blood

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_HPSE

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9Y251 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9Y251 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB009813
    HPA055344

    <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; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity. Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1. Interacts with HPSE2.5 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    116066, 14 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-362 Heparanase complex

    Protein interaction database and analysis system

    More...
    IntActi
    Q9Y251, 7 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000308107

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9Y251

    <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

    1543
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5E8MX-ray1.75A158-543[»]
    B36-109[»]
    5E97X-ray1.63A158-543[»]
    B36-109[»]
    5E98X-ray1.63A158-543[»]
    B36-109[»]
    5E9BX-ray1.88A158-543[»]
    B36-109[»]
    5E9CX-ray1.73A158-543[»]
    B36-109[»]
    5L9YX-ray1.88A158-543[»]
    B36-109[»]
    5L9ZX-ray1.57A158-543[»]
    B36-109[»]
    5LA4X-ray1.90A36-543[»]
    5LA7X-ray1.94A36-543[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9Y251

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

    More...
    SMRi
    Q9Y251

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    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>Regioni62 – 64Heparan sulfate-bindingCombined sources1 Publication3
    Regioni158 – 162Heparan sulfate-binding1 Publication5
    Regioni270 – 280Heparan sulfate-bindingCombined sources2 PublicationsAdd BLAST11
    Regioni288 – 417Required for heterodimerization with the heparanase 8 kDa subunit1 PublicationAdd BLAST130
    Regioni348 – 350Heparan sulfate-bindingCombined sources1 Publication3
    Regioni389 – 391Heparan sulfate-bindingCombined sources1 Publication3
    Regioni527 – 543Required for transferring proheparanase to the Golgi apparatus, secretion and subsequent enzyme activity and for enhancement of PKB/AKT1 phosphorylationAdd BLAST17

    <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 glycosyl hydrolase 79 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IHNV Eukaryota
    ENOG410YDJW LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000004874

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000007256

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG081606

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9Y251

    KEGG Orthology (KO)

    More...
    KOi
    K07964

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    MSWELGN

    Database of Orthologous Groups

    More...
    OrthoDBi
    1132327at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9Y251

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF328999

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005199 Glyco_hydro_79
    IPR017853 Glycoside_hydrolase_SF

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR14363 PTHR14363, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03662 Glyco_hydro_79n, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

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

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

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

    This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9Y251-1) [UniParc]FASTAAdd to basket

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

    « Hide
            10         20         30         40         50
    MLLRSKPALP PPLMLLLLGP LGPLSPGALP RPAQAQDVVD LDFFTQEPLH
    60 70 80 90 100
    LVSPSFLSVT IDANLATDPR FLILLGSPKL RTLARGLSPA YLRFGGTKTD
    110 120 130 140 150
    FLIFDPKKES TFEERSYWQS QVNQDICKYG SIPPDVEEKL RLEWPYQEQL
    160 170 180 190 200
    LLREHYQKKF KNSTYSRSSV DVLYTFANCS GLDLIFGLNA LLRTADLQWN
    210 220 230 240 250
    SSNAQLLLDY CSSKGYNISW ELGNEPNSFL KKADIFINGS QLGEDFIQLH
    260 270 280 290 300
    KLLRKSTFKN AKLYGPDVGQ PRRKTAKMLK SFLKAGGEVI DSVTWHHYYL
    310 320 330 340 350
    NGRTATKEDF LNPDVLDIFI SSVQKVFQVV ESTRPGKKVW LGETSSAYGG
    360 370 380 390 400
    GAPLLSDTFA AGFMWLDKLG LSARMGIEVV MRQVFFGAGN YHLVDENFDP
    410 420 430 440 450
    LPDYWLSLLF KKLVGTKVLM ASVQGSKRRK LRVYLHCTNT DNPRYKEGDL
    460 470 480 490 500
    TLYAINLHNV TKYLRLPYPF SNKQVDKYLL RPLGPHGLLS KSVQLNGLTL
    510 520 530 540
    KMVDDQTLPP LMEKPLRPGS SLGLPAFSYS FFVIRNAKVA ACI
    Length:543
    Mass (Da):61,149
    Last modified:May 18, 2010 - 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:iA990F5AFD639CA1A
    GO
    Isoform 2 (identifier: Q9Y251-2) [UniParc]FASTAAdd to basket
    Also known as: 55 kDa, splice 5

    The sequence of this isoform differs from the canonical sequence as follows:
         167-225: RSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNE → K

    Note: Escapes proteolytic cleavage, devoid of HS degradation activity.
    Show »
    Length:485
    Mass (Da):54,734
    Checksum:iDCF33CD4B2BC3A43
    GO
    Isoform 3 (identifier: Q9Y251-3) [UniParc]FASTAAdd to basket
    Also known as: ex9-10del

    The sequence of this isoform differs from the canonical sequence as follows:
         329-402: Missing.

    Show »
    Length:469
    Mass (Da):53,161
    Checksum:iF0E4853CC0CF0D88
    GO
    Isoform 4 (identifier: Q9Y251-4) [UniParc]FASTAAdd to basket
    Also known as: ex10del

    The sequence of this isoform differs from the canonical sequence as follows:
         365-380: WLDKLGLSARMGIEVV → IIGYLFCSRNWWAPRC
         381-543: Missing.

    Show »
    Length:380
    Mass (Da):42,791
    Checksum:i913407210F45CF1E
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    D6RHG4D6RHG4_HUMAN
    Heparanase
    HPSE
    226Annotation score:

    Annotation score:1 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>
    D6RAQ1D6RAQ1_HUMAN
    Heparanase
    HPSE
    168Annotation score:

    Annotation score:1 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 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 conflicti13L → LL in AAD54516 (PubMed:10764835).Curated1
    Sequence conflicti36Q → QQ in AAD54516 (PubMed:10764835).Curated1
    Sequence conflicti291D → G in BAD96706 (Ref. 11) Curated1

    Natural variant

    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_023600260N → S in some hepatocellular carcinoma. 1 Publication1
    Natural variantiVAR_068907307K → R10 PublicationsCorresponds to variant dbSNP:rs11099592Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044537167 – 225RSSVD…ELGNE → K in isoform 2. 1 PublicationAdd BLAST59
    Alternative sequenceiVSP_044664329 – 402Missing in isoform 3. 1 PublicationAdd BLAST74
    Alternative sequenceiVSP_053730365 – 380WLDKL…GIEVV → IIGYLFCSRNWWAPRC in isoform 4. 1 PublicationAdd BLAST16
    Alternative sequenceiVSP_053731381 – 543Missing in isoform 4. 1 PublicationAdd BLAST163

    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
    AF152376 mRNA Translation: AAD45669.1
    AF155510 mRNA Translation: AAD54941.1
    AF144325 mRNA Translation: AAD41342.1
    AF165154 mRNA Translation: AAD45379.1
    AF084467 mRNA Translation: AAD54516.1
    AM419200 mRNA Translation: CAL91960.1
    AY948074 mRNA Translation: AAX47106.1
    GQ337901 mRNA Translation: ACT98237.1
    GQ337902 mRNA Translation: ACT98238.1
    AK222986 mRNA Translation: BAD96706.1
    AC114781 Genomic DNA No translation available.
    BC051321 mRNA Translation: AAH51321.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS3602.1 [Q9Y251-1]
    CCDS54774.1 [Q9Y251-3]
    CCDS56337.1 [Q9Y251-2]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001092010.1, NM_001098540.2 [Q9Y251-1]
    NP_001159970.1, NM_001166498.2 [Q9Y251-3]
    NP_001186759.1, NM_001199830.1 [Q9Y251-2]
    NP_006656.2, NM_006665.5 [Q9Y251-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.44227

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000311412; ENSP00000308107; ENSG00000173083 [Q9Y251-1]
    ENST00000405413; ENSP00000384262; ENSG00000173083 [Q9Y251-1]
    ENST00000509906; ENSP00000421038; ENSG00000173083 [Q9Y251-4]
    ENST00000512196; ENSP00000423265; ENSG00000173083 [Q9Y251-3]
    ENST00000513463; ENSP00000421365; ENSG00000173083 [Q9Y251-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    10855

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:10855

    UCSC genome browser

    More...
    UCSCi
    uc003hoi.4 human [Q9Y251-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF152376 mRNA Translation: AAD45669.1
    AF155510 mRNA Translation: AAD54941.1
    AF144325 mRNA Translation: AAD41342.1
    AF165154 mRNA Translation: AAD45379.1
    AF084467 mRNA Translation: AAD54516.1
    AM419200 mRNA Translation: CAL91960.1
    AY948074 mRNA Translation: AAX47106.1
    GQ337901 mRNA Translation: ACT98237.1
    GQ337902 mRNA Translation: ACT98238.1
    AK222986 mRNA Translation: BAD96706.1
    AC114781 Genomic DNA No translation available.
    BC051321 mRNA Translation: AAH51321.1
    CCDSiCCDS3602.1 [Q9Y251-1]
    CCDS54774.1 [Q9Y251-3]
    CCDS56337.1 [Q9Y251-2]
    RefSeqiNP_001092010.1, NM_001098540.2 [Q9Y251-1]
    NP_001159970.1, NM_001166498.2 [Q9Y251-3]
    NP_001186759.1, NM_001199830.1 [Q9Y251-2]
    NP_006656.2, NM_006665.5 [Q9Y251-1]
    UniGeneiHs.44227

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5E8MX-ray1.75A158-543[»]
    B36-109[»]
    5E97X-ray1.63A158-543[»]
    B36-109[»]
    5E98X-ray1.63A158-543[»]
    B36-109[»]
    5E9BX-ray1.88A158-543[»]
    B36-109[»]
    5E9CX-ray1.73A158-543[»]
    B36-109[»]
    5L9YX-ray1.88A158-543[»]
    B36-109[»]
    5L9ZX-ray1.57A158-543[»]
    B36-109[»]
    5LA4X-ray1.90A36-543[»]
    5LA7X-ray1.94A36-543[»]
    ProteinModelPortaliQ9Y251
    SMRiQ9Y251
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116066, 14 interactors
    ComplexPortaliCPX-362 Heparanase complex
    IntActiQ9Y251, 7 interactors
    STRINGi9606.ENSP00000308107

    Chemistry databases

    BindingDBiQ9Y251
    ChEMBLiCHEMBL3921
    DrugBankiDB06779 Dalteparin
    DB01109 Heparin
    GuidetoPHARMACOLOGYi2996

    Protein family/group databases

    CAZyiGH79 Glycoside Hydrolase Family 79

    PTM databases

    iPTMnetiQ9Y251
    PhosphoSitePlusiQ9Y251

    Polymorphism and mutation databases

    BioMutaiHPSE
    DMDMi296434532

    Proteomic databases

    EPDiQ9Y251
    jPOSTiQ9Y251
    PaxDbiQ9Y251
    PeptideAtlasiQ9Y251
    PRIDEiQ9Y251
    ProteomicsDBi85653
    TopDownProteomicsiQ9Y251-1 [Q9Y251-1]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    10855
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000311412; ENSP00000308107; ENSG00000173083 [Q9Y251-1]
    ENST00000405413; ENSP00000384262; ENSG00000173083 [Q9Y251-1]
    ENST00000509906; ENSP00000421038; ENSG00000173083 [Q9Y251-4]
    ENST00000512196; ENSP00000423265; ENSG00000173083 [Q9Y251-3]
    ENST00000513463; ENSP00000421365; ENSG00000173083 [Q9Y251-2]
    GeneIDi10855
    KEGGihsa:10855
    UCSCiuc003hoi.4 human [Q9Y251-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10855
    DisGeNETi10855
    EuPathDBiHostDB:ENSG00000173083.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    HPSE
    HGNCiHGNC:5164 HPSE
    HPAiCAB009813
    HPA055344
    MIMi604724 gene
    neXtProtiNX_Q9Y251
    OpenTargetsiENSG00000173083
    PharmGKBiPA29435

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG410IHNV Eukaryota
    ENOG410YDJW LUCA
    GeneTreeiENSGT00390000004874
    HOGENOMiHOG000007256
    HOVERGENiHBG081606
    InParanoidiQ9Y251
    KOiK07964
    OMAiMSWELGN
    OrthoDBi1132327at2759
    PhylomeDBiQ9Y251
    TreeFamiTF328999

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000173083-MONOMER
    BRENDAi3.2.1.166 2681
    ReactomeiR-HSA-2024096 HS-GAG degradation
    R-HSA-6798695 Neutrophil degranulation
    SIGNORiQ9Y251

    Miscellaneous databases

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

    More...
    ChiTaRSi
    HPSE human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Heparanase

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

    More...
    GenomeRNAii
    10855

    Protein Ontology

    More...
    PROi
    PR:Q9Y251

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000173083 Expressed in 131 organ(s), highest expression level in blood
    CleanExiHS_HPSE
    ExpressionAtlasiQ9Y251 baseline and differential
    GenevisibleiQ9Y251 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR005199 Glyco_hydro_79
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR14363 PTHR14363, 1 hit
    PfamiView protein in Pfam
    PF03662 Glyco_hydro_79n, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiHPSE_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: Q9Y251
    Secondary accession number(s): A9JIG7
    , C7F7I3, C7F7I4, E9PCA9, E9PGR1, Q53GE5, Q9UL39
    <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: October 11, 2005
    Last sequence update: May 18, 2010
    Last modified: January 16, 2019
    This is version 163 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
    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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    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
    7. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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