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Protein

Neprilysin

Gene

MME

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

Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573).6 Publications

Miscellaneous

Important cell surface marker in the diagnostic of human acute lymphocytic leukemia.

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

<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 in a dose dependent manner by opiorphin.1 Publication

<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

  1. KM=55.1 µM for angiotensin-11 Publication
  2. KM=179 µM for angiotensin-21 Publication
  3. KM=111.4 µM for angiotensin 1-91 Publication

    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 sitei103Substrate carboxylBy similarity1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi584Zinc; catalytic1
    <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 sitei5851
    Metal bindingi588Zinc; catalytic1
    Metal bindingi647Zinc; catalytic1
    Active sitei651Proton donorPROSITE-ProRule annotation1 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

    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, Metalloprotease, Protease
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.24.11 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
    R-HSA-6798695 Neutrophil degranulation

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P08473

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M13.001

    <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:
    Neprilysin (EC:3.4.24.113 Publications)
    Alternative name(s):
    Atriopeptidase
    Common acute lymphocytic leukemia antigen
    Short name:
    CALLA
    Enkephalinase
    Neutral endopeptidase 24.11
    Short name:
    NEP
    Short name:
    Neutral endopeptidase
    Skin fibroblast elastase
    Short name:
    SFE
    CD_antigen: CD10
    <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:MME
    Synonyms:EPN
    <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 3

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000196549.10

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:7154 MME

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    120520 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P08473

    <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

    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 domaini2 – 28CytoplasmicSequence analysisAdd BLAST27
    <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>Transmembranei29 – 51Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
    Topological domaini52 – 750ExtracellularSequence analysisAdd BLAST699

    Keywords - Cellular componenti

    Cell membrane, Membrane

    <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

    Charcot-Marie-Tooth disease 2T (CMT2T)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
    See also OMIM:617017
    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_07768412D → A in CMT2T; unknown pathological significance. 1 Publication1
    Natural variantiVAR_077686347Y → C in CMT2T; results in reduction of neprilysin activity. 1 PublicationCorresponds to variant dbSNP:rs138218277Ensembl.1
    Natural variantiVAR_077687348A → P in CMT2T; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs199567914Ensembl.1
    Natural variantiVAR_077688411Missing in CMT2T; unknown pathological significance. 1 Publication1
    Natural variantiVAR_077689422A → D in CMT2T; late-onset form; results in reduction of neprilysin activity. 1 PublicationCorresponds to variant dbSNP:rs777476150EnsemblClinVar.1
    Natural variantiVAR_077691621C → R in CMT2T; decrease of protein expression. 1 PublicationCorresponds to variant dbSNP:rs879253752EnsemblClinVar.1
    Spinocerebellar ataxia 43 (SCA43)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA43 is a slowly progressive, autosomal dominant form.
    See also OMIM:617018
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_077685143C → Y in SCA43. 1 PublicationCorresponds to variant dbSNP:rs879255651EnsemblClinVar.1

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy, Spinocerebellar ataxia

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    4311

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

    More...
    GeneReviewsi
    MME

    MalaCards human disease database

    More...
    MalaCardsi
    MME
    MIMi617017 phenotype
    617018 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000196549

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

    More...
    Orphaneti
    495274 Charcot-Marie-Tooth disease type 2T
    497757 MME-related autosomal dominant Charcot Marie Tooth disease type 2
    497764 Spinocerebellar ataxia type 43

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA30864

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1944

    Drug and drug target database

    More...
    DrugBanki
    DB00616 Candoxatril
    DB11623 Candoxatrilat
    DB06655 Liraglutide
    DB02558 N-(3-Phenyl-2-Sulfanylpropanoyl)Phenylalanylalanine
    DB00886 Omapatrilat
    DB02557 Phosphoramidon
    DB09292 Sacubitril
    DB05796 SLV 306
    DB08626 Thiorphan

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1611

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    MME

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    128062

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
    <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_00000782132 – 750NeprilysinAdd BLAST749

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
    <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 residuei4PhosphoserineCombined sources1
    Modified residuei6PhosphoserineCombined sources1
    <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 bondi57 ↔ 62
    Disulfide bondi80 ↔ 735
    Disulfide bondi88 ↔ 695
    Disulfide bondi143 ↔ 411
    <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>Glycosylationi145N-linked (GlcNAc...) asparagine4 Publications1
    Disulfide bondi234 ↔ 242
    Glycosylationi285N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi325N-linked (GlcNAc...) asparagine3 Publications1
    Disulfide bondi621 ↔ 747
    Glycosylationi628N-linked (GlcNAc...) asparagine4 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

    Myristoylation is a determinant of membrane targeting.1 Publication
    Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P08473

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P08473

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P08473

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

    More...
    PaxDbi
    P08473

    PeptideAtlas

    More...
    PeptideAtlasi
    P08473

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P08473

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    52110

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P08473

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    1541

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P08473

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

    More...
    PhosphoSitePlusi
    P08473

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000196549 Expressed in 156 organ(s), highest expression level in metanephric glomerulus

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_MME

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P08473 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P08473 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB000013
    HPA052583
    HPA056072

    <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%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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    110455, 102 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P08473, 80 interactors

    Molecular INTeraction database

    More...
    MINTi
    P08473

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000353679

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P08473

    <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

    1750
    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
    1DL9model-A508-750[»]
    1DMTX-ray2.10A55-750[»]
    1QVDmodel-A55-750[»]
    1R1HX-ray1.95A55-750[»]
    1R1IX-ray2.60A55-750[»]
    1R1JX-ray2.35A55-750[»]
    1Y8JX-ray2.25A55-750[»]
    2QPJX-ray2.05A55-750[»]
    2YB9X-ray2.40A55-750[»]
    4CTHX-ray2.15A52-750[»]
    5JMYX-ray2.00A/B53-750[»]
    6GIDX-ray1.90A55-750[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P08473

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

    More...
    SMRi
    P08473

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P08473

    <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

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi16 – 23Stop-transfer sequenceSequence analysis8

    <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 peptidase M13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3624 Eukaryota
    COG3590 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156745

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000245574

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG005554

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P08473

    KEGG Orthology (KO)

    More...
    KOi
    K01389

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    APRNHDA

    Database of Orthologous Groups

    More...
    OrthoDBi
    1450599at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P08473

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF315192

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd08662 M13, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.390.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR024079 MetalloPept_cat_dom_sf
    IPR029727 MME/CD10/NEP
    IPR000718 Peptidase_M13
    IPR018497 Peptidase_M13_C
    IPR008753 Peptidase_M13_N

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11733 PTHR11733, 1 hit
    PTHR11733:SF114 PTHR11733:SF114, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01431 Peptidase_M13, 1 hit
    PF05649 Peptidase_M13_N, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00786 NEPRILYSIN

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00142 ZINC_PROTEASE, 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>Sequence (1+)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 has 1 described isoform and 7 potential isoforms that are computationally mapped.Show allAlign All

    P08473-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA
    60 70 80 90 100
    TYDDGICKSS DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET
    110 120 130 140 150
    SSRYGNFDIL RDELEVVLKD VLQEPKTEDI VAVQKAKALY RSCINESAID
    160 170 180 190 200
    SRGGEPLLKL LPDIYGWPVA TENWEQKYGA SWTAEKAIAQ LNSKYGKKVL
    210 220 230 240 250
    INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE ACTAYVDFMI
    260 270 280 290 300
    SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
    310 320 330 340 350
    NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE
    360 370 380 390 400
    YLTKLKPILT KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG
    410 420 430 440 450
    TTSETATWRR CANYVNGNME NAVGRLYVEA AFAGESKHVV EDLIAQIREV
    460 470 480 490 500
    FIQTLDDLTW MDAETKKRAE EKALAIKERI GYPDDIVSND NKLNNEYLEL
    510 520 530 540 550
    NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA VVNAFYSSGR
    560 570 580 590 600
    NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
    610 620 630 640 650
    GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA
    660 670 680 690 700
    DNGGLGQAYR AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP
    710 720 730 740 750
    EYAVNSIKTD VHSPGNFRII GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW
    Length:750
    Mass (Da):85,514
    Last modified:January 23, 2007 - 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:iBCF3827C39898630
    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 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9JR96C9JR96_HUMAN
    Neprilysin
    MME
    233Annotation 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>
    C9J9X7C9J9X7_HUMAN
    Neprilysin
    MME
    161Annotation 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>
    C9IYX7C9IYX7_HUMAN
    Neprilysin
    MME
    119Annotation 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>
    C9JDZ3C9JDZ3_HUMAN
    Neprilysin
    MME
    93Annotation 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>
    Q3KQS6Q3KQS6_HUMAN
    MME protein
    MME
    80Annotation 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>
    A0A087WWM7A0A087WWM7_HUMAN
    Neprilysin
    MME
    79Annotation 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>
    C9J7X4C9J7X4_HUMAN
    Neprilysin
    MME
    15Annotation 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAA30157 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    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 conflicti26P → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti44T → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti81T → R in AAA51915 (PubMed:14702039).Curated1
    Sequence conflicti304T → R in AAA51915 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07768412D → A in CMT2T; unknown pathological significance. 1 Publication1
    Natural variantiVAR_077685143C → Y in SCA43. 1 PublicationCorresponds to variant dbSNP:rs879255651EnsemblClinVar.1
    Natural variantiVAR_077686347Y → C in CMT2T; results in reduction of neprilysin activity. 1 PublicationCorresponds to variant dbSNP:rs138218277Ensembl.1
    Natural variantiVAR_077687348A → P in CMT2T; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs199567914Ensembl.1
    Natural variantiVAR_077688411Missing in CMT2T; unknown pathological significance. 1 Publication1
    Natural variantiVAR_077689422A → D in CMT2T; late-onset form; results in reduction of neprilysin activity. 1 PublicationCorresponds to variant dbSNP:rs777476150EnsemblClinVar.1
    Natural variantiVAR_077690497Y → H1 PublicationCorresponds to variant dbSNP:rs200308207Ensembl.1
    Natural variantiVAR_077691621C → R in CMT2T; decrease of protein expression. 1 PublicationCorresponds to variant dbSNP:rs879253752EnsemblClinVar.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
    Y00811 mRNA Translation: CAA68752.1
    J03779 mRNA Translation: AAA51915.1
    M26628
    , M26607, M26608, M26609, M26610, M26611, M26612, M26613, M26614, M26615, M26616, M26617, M26618, M26619, M26620, M26621, M26622, M26623, M26624, M26625, M26626, M26627 Genomic DNA Translation: AAA52294.1
    AK291761 mRNA Translation: BAF84450.1
    EU326307 Genomic DNA Translation: ACA05913.1
    CH471052 Genomic DNA Translation: EAW78754.1
    CH471052 Genomic DNA Translation: EAW78755.1
    CH471052 Genomic DNA Translation: EAW78756.1
    CH471052 Genomic DNA Translation: EAW78757.1
    CH471052 Genomic DNA Translation: EAW78758.1
    BC101632 mRNA Translation: AAI01633.1
    BC101658 mRNA Translation: AAI01659.1
    X07166 mRNA Translation: CAA30157.1 Different initiation.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS3172.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A41387 HYHUN

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000893.2, NM_000902.3
    NP_009218.2, NM_007287.2
    NP_009219.2, NM_007288.2
    NP_009220.2, NM_007289.2
    XP_006713709.1, XM_006713646.3
    XP_006713710.1, XM_006713647.3
    XP_011511157.1, XM_011512855.2
    XP_011511158.1, XM_011512856.2
    XP_011511159.1, XM_011512857.2

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.307734

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000360490; ENSP00000353679; ENSG00000196549
    ENST00000460393; ENSP00000418525; ENSG00000196549
    ENST00000462745; ENSP00000419653; ENSG00000196549
    ENST00000492661; ENSP00000420389; ENSG00000196549
    ENST00000493237; ENSP00000417079; ENSG00000196549
    ENST00000615825; ENSP00000478173; ENSG00000196549

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4311

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:4311

    UCSC genome browser

    More...
    UCSCi
    uc003fab.2 human

    <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
    Y00811 mRNA Translation: CAA68752.1
    J03779 mRNA Translation: AAA51915.1
    M26628
    , M26607, M26608, M26609, M26610, M26611, M26612, M26613, M26614, M26615, M26616, M26617, M26618, M26619, M26620, M26621, M26622, M26623, M26624, M26625, M26626, M26627 Genomic DNA Translation: AAA52294.1
    AK291761 mRNA Translation: BAF84450.1
    EU326307 Genomic DNA Translation: ACA05913.1
    CH471052 Genomic DNA Translation: EAW78754.1
    CH471052 Genomic DNA Translation: EAW78755.1
    CH471052 Genomic DNA Translation: EAW78756.1
    CH471052 Genomic DNA Translation: EAW78757.1
    CH471052 Genomic DNA Translation: EAW78758.1
    BC101632 mRNA Translation: AAI01633.1
    BC101658 mRNA Translation: AAI01659.1
    X07166 mRNA Translation: CAA30157.1 Different initiation.
    CCDSiCCDS3172.1
    PIRiA41387 HYHUN
    RefSeqiNP_000893.2, NM_000902.3
    NP_009218.2, NM_007287.2
    NP_009219.2, NM_007288.2
    NP_009220.2, NM_007289.2
    XP_006713709.1, XM_006713646.3
    XP_006713710.1, XM_006713647.3
    XP_011511157.1, XM_011512855.2
    XP_011511158.1, XM_011512856.2
    XP_011511159.1, XM_011512857.2
    UniGeneiHs.307734

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1DL9model-A508-750[»]
    1DMTX-ray2.10A55-750[»]
    1QVDmodel-A55-750[»]
    1R1HX-ray1.95A55-750[»]
    1R1IX-ray2.60A55-750[»]
    1R1JX-ray2.35A55-750[»]
    1Y8JX-ray2.25A55-750[»]
    2QPJX-ray2.05A55-750[»]
    2YB9X-ray2.40A55-750[»]
    4CTHX-ray2.15A52-750[»]
    5JMYX-ray2.00A/B53-750[»]
    6GIDX-ray1.90A55-750[»]
    ProteinModelPortaliP08473
    SMRiP08473
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110455, 102 interactors
    IntActiP08473, 80 interactors
    MINTiP08473
    STRINGi9606.ENSP00000353679

    Chemistry databases

    BindingDBiP08473
    ChEMBLiCHEMBL1944
    DrugBankiDB00616 Candoxatril
    DB11623 Candoxatrilat
    DB06655 Liraglutide
    DB02558 N-(3-Phenyl-2-Sulfanylpropanoyl)Phenylalanylalanine
    DB00886 Omapatrilat
    DB02557 Phosphoramidon
    DB09292 Sacubitril
    DB05796 SLV 306
    DB08626 Thiorphan
    GuidetoPHARMACOLOGYi1611

    Protein family/group databases

    MEROPSiM13.001

    PTM databases

    CarbonylDBiP08473
    GlyConnecti1541
    iPTMnetiP08473
    PhosphoSitePlusiP08473

    Polymorphism and mutation databases

    BioMutaiMME
    DMDMi128062

    Proteomic databases

    EPDiP08473
    jPOSTiP08473
    MaxQBiP08473
    PaxDbiP08473
    PeptideAtlasiP08473
    PRIDEiP08473
    ProteomicsDBi52110

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000360490; ENSP00000353679; ENSG00000196549
    ENST00000460393; ENSP00000418525; ENSG00000196549
    ENST00000462745; ENSP00000419653; ENSG00000196549
    ENST00000492661; ENSP00000420389; ENSG00000196549
    ENST00000493237; ENSP00000417079; ENSG00000196549
    ENST00000615825; ENSP00000478173; ENSG00000196549
    GeneIDi4311
    KEGGihsa:4311
    UCSCiuc003fab.2 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    4311
    DisGeNETi4311
    EuPathDBiHostDB:ENSG00000196549.10

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    MME
    GeneReviewsiMME
    HGNCiHGNC:7154 MME
    HPAiCAB000013
    HPA052583
    HPA056072
    MalaCardsiMME
    MIMi120520 gene
    617017 phenotype
    617018 phenotype
    neXtProtiNX_P08473
    OpenTargetsiENSG00000196549
    Orphaneti495274 Charcot-Marie-Tooth disease type 2T
    497757 MME-related autosomal dominant Charcot Marie Tooth disease type 2
    497764 Spinocerebellar ataxia type 43
    PharmGKBiPA30864

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG3624 Eukaryota
    COG3590 LUCA
    GeneTreeiENSGT00940000156745
    HOGENOMiHOG000245574
    HOVERGENiHBG005554
    InParanoidiP08473
    KOiK01389
    OMAiAPRNHDA
    OrthoDBi1450599at2759
    PhylomeDBiP08473
    TreeFamiTF315192

    Enzyme and pathway databases

    BRENDAi3.4.24.11 2681
    ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
    R-HSA-6798695 Neutrophil degranulation
    SIGNORiP08473

    Miscellaneous databases

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

    More...
    ChiTaRSi
    MME human
    EvolutionaryTraceiP08473

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Neprilysin

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

    More...
    GenomeRNAii
    4311

    Protein Ontology

    More...
    PROi
    PR:P08473

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000196549 Expressed in 156 organ(s), highest expression level in metanephric glomerulus
    CleanExiHS_MME
    ExpressionAtlasiP08473 baseline and differential
    GenevisibleiP08473 HS

    Family and domain databases

    CDDicd08662 M13, 1 hit
    Gene3Di3.40.390.10, 1 hit
    InterProiView protein in InterPro
    IPR024079 MetalloPept_cat_dom_sf
    IPR029727 MME/CD10/NEP
    IPR000718 Peptidase_M13
    IPR018497 Peptidase_M13_C
    IPR008753 Peptidase_M13_N
    PANTHERiPTHR11733 PTHR11733, 1 hit
    PTHR11733:SF114 PTHR11733:SF114, 1 hit
    PfamiView protein in Pfam
    PF01431 Peptidase_M13, 1 hit
    PF05649 Peptidase_M13_N, 1 hit
    PRINTSiPR00786 NEPRILYSIN
    PROSITEiView protein in PROSITE
    PS00142 ZINC_PROTEASE, 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 nameiNEP_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: P08473
    Secondary accession number(s): A8K6U6, D3DNJ9, Q3MIX4
    <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: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 220 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, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
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