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Protein

Protein argonaute-2

Gene

AGO2

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

Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions.UniRule annotationBy similarity23 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 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

Mg2+1 Publication, Mn2+1 Publication

<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.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=1.1 nM for a synthetic 21-nucleotide single-stranded RNA2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi597Divalent metal cationCurated1
    Metal bindingi669Divalent metal cationCurated1
    Metal bindingi807Divalent metal cationCurated1

    <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 functionEndonuclease, Hydrolase, Nuclease, Repressor, Ribonucleoprotein, RNA-binding
    Biological processRNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1912408 Pre-NOTCH Transcription and Translation
    R-HSA-203927 MicroRNA (miRNA) biogenesis
    R-HSA-4086398 Ca2+ pathway
    R-HSA-426486 Small interfering RNA (siRNA) biogenesis
    R-HSA-426496 Post-transcriptional silencing by small RNAs
    R-HSA-5578749 Transcriptional regulation by small RNAs
    R-HSA-5628897 TP53 Regulates Metabolic Genes
    R-HSA-5687128 MAPK6/MAPK4 signaling
    R-HSA-8934593 Regulation of RUNX1 Expression and Activity
    R-HSA-8943723 Regulation of PTEN mRNA translation
    R-HSA-8948700 Competing endogenous RNAs (ceRNAs) regulate PTEN translation
    R-HSA-8986944 Transcriptional Regulation by MECP2
    R-HSA-9018519 Estrogen-dependent gene expression
    R-HSA-9022692 Regulation of MECP2 expression and activity

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q9UKV8

    <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:
    Protein argonaute-2UniRule annotation (EC:3.1.26.n2UniRule annotation)
    Short name:
    Argonaute2UniRule annotation
    Short name:
    hAgo2
    Alternative name(s):
    Argonaute RISC catalytic component 2
    Eukaryotic translation initiation factor 2C 2UniRule annotation
    Short name:
    eIF-2C 2UniRule annotation
    Short name:
    eIF2C 2UniRule annotation
    PAZ Piwi domain protein
    Short name:
    PPD
    Protein slicerUniRule annotation
    <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:AGO2
    Synonyms:EIF2C2
    <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 8

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000123908.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:3263 AGO2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    606229 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9UKV8

    <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

    Cytoplasm, Nucleus

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

    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>Mutagenesisi140L → W: No effect. 1 Publication1
    Mutagenesisi470F → V: No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation. Abolishes interaction with TNRC6C; when associated with V-505. 2 Publications1
    Mutagenesisi470F → W: No effect on binding to the 7-methylguanosine cap of mRNA or inhibition of translation. 2 Publications1
    Mutagenesisi505F → V: No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation and abolishes interaction with TNRC6C; when associated with V-470. 2 Publications1
    Mutagenesisi505F → W: No effect on binding to the 7-methylguanosine cap of mRNA or inhibition of translation. 2 Publications1
    Mutagenesisi533K → A: Impairs RNA cleavage. 1 Publication1
    Mutagenesisi545Q → A: Impairs RNA cleavage. 1 Publication1
    Mutagenesisi570K → A: Impairs RNA cleavage. 1 Publication1
    Mutagenesisi597D → A: Abrogates RNA cleavage but does not affect binding to siRNA or translational repression. 3 Publications1
    Mutagenesisi633Q → A: No effect. 1 Publication1
    Mutagenesisi633Q → R: Abrogates RNA cleavage. Binds siRNA. 1 Publication1
    Mutagenesisi634H → P or A: Abrogates RNA cleavage. Binds siRNA. 1 Publication1
    Mutagenesisi669D → A: Abrogates RNA cleavage but does not affect binding to siRNA. 3 Publications1
    Mutagenesisi673E → A: Impairs RNA cleavage. 2 Publications1
    Mutagenesisi673E → G: No effect on RNA cleavage. 2 Publications1
    Mutagenesisi676F → A, I, M, R or Y: Impairs RNA cleavage. 1 Publication1
    Mutagenesisi676F → V: Abrogates RNA cleavage. 1 Publication1
    Mutagenesisi682H → Y: No effect. 1 Publication1
    Mutagenesisi683E → G: No effect on RNA cleavage. 1 Publication1
    Mutagenesisi700P → A: Reduced protein stability. 1 Publication1
    Mutagenesisi704F → Y: No effect. 1 Publication1
    Mutagenesisi744T → Y: No effect. 1 Publication1
    Mutagenesisi807H → A or R: Abrogates RNA cleavage. 2 Publications1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    27161

    Open Targets

    More...
    OpenTargetsi
    ENSG00000123908

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA27694

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    AGO2

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    229463006

    <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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001940571 – 859Protein argonaute-2Add BLAST859

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 residuei2Nitrated tyrosineUniRule annotationBy similarity1
    Modified residuei387PhosphoserineCombined sources1
    Modified residuei7004-hydroxyprolineUniRule annotation1 Publication1
    Modified residuei828PhosphoserineCombined sources1

    <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

    Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity.UniRule annotation1 Publication

    Keywords - PTMi

    Hydroxylation, Nitration, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9UKV8

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

    More...
    PaxDbi
    Q9UKV8

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9UKV8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9UKV8

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    84894
    84895 [Q9UKV8-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9UKV8

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

    More...
    PhosphoSitePlusi
    Q9UKV8

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q9UKV8

    <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
    ENSG00000123908 Expressed in 220 organ(s), highest expression level in forebrain

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_EIF2C2

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9UKV8 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9UKV8 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB019309
    HPA058075

    <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

    Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Note however that the term RISC has also been used to describe the trimeric RLC/miRLC. The formation of RISC complexes containing siRNAs rather than miRNAs appears to occur independently of DICER1. Interacts with AGO1. Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with the P-body components DCP1A and XRN1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the interaction is modulated under stress-induced conditions, occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation-independent manner. Interacts with LIMD1, WTIP and AJUBA. Interacts with TRIM71; the interaction increases in presence of RNA (PubMed:23125361). Interacts with APOBEC3G in an RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large RNA-induced silencing complex (RISC) (PubMed:17507929, PubMed:24726324). Interacts with FMR1 (PubMed:14703574). Interacts with ZFP36 (PubMed:15766526). Found in a complex, composed of AGO2, CHD7 and FAM172A (By similarity). Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406). Interacts with SND1 (PubMed:14508492, PubMed:28546213).UniRule annotationBy similarity32 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    118041, 103 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1072 RISC-loading complex, PRKRA variant
    CPX-134 RISC-loading complex, TARBP2 variant

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q9UKV8

    Database of interacting proteins

    More...
    DIPi
    DIP-29194N

    Protein interaction database and analysis system

    More...
    IntActi
    Q9UKV8, 197 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q9UKV8

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000220592

    <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

    1859
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Database of protein disorder

    More...
    DisProti
    DP00736

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9UKV8

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

    More...
    SMRi
    Q9UKV8

    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
    Q9UKV8

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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini235 – 348PAZUniRule annotationAdd BLAST114
    Domaini517 – 818PiwiUniRule annotationAdd BLAST302

    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>Regioni311 – 316Interaction with guide RNA6
    Regioni524 – 566Interaction with guide RNAAdd BLAST43
    Regioni587 – 590Interaction with GW182 family membersSequence analysis4
    Regioni650 – 660Interaction with GW182 family membersSequence analysisAdd BLAST11
    Regioni709 – 710Interaction with guide RNA2
    Regioni753 – 761Interaction with guide RNA9
    Regioni790 – 812Interaction with guide RNAAdd BLAST23

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

    The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH).

    <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 argonaute family. Ago subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1041 Eukaryota
    ENOG410XP07 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155239

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000116043

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9UKV8

    KEGG Orthology (KO)

    More...
    KOi
    K11593

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SPDGYYH

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G020J

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9UKV8

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF101510

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.420.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_03031 AGO2, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR028602 AGO2
    IPR014811 ArgoL1
    IPR032472 ArgoL2
    IPR032473 Argonaute_Mid_dom
    IPR032474 Argonaute_N
    IPR003100 PAZ_dom
    IPR036085 PAZ_dom_sf
    IPR003165 Piwi
    IPR012337 RNaseH-like_sf
    IPR036397 RNaseH_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08699 ArgoL1, 1 hit
    PF16488 ArgoL2, 1 hit
    PF16487 ArgoMid, 1 hit
    PF16486 ArgoN, 1 hit
    PF02170 PAZ, 1 hit
    PF02171 Piwi, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01163 DUF1785, 1 hit
    SM00949 PAZ, 1 hit
    SM00950 Piwi, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF101690 SSF101690, 1 hit
    SSF53098 SSF53098, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50821 PAZ, 1 hit
    PS50822 PIWI, 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 (2+)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.

    This entry describes 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9UKV8-1) [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
    MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP
    60 70 80 90 100
    KIDIYHYELD IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL
    110 120 130 140 150
    YTAMPLPIGR DKVELEVTLP GEGKDRIFKV SIKWVSCVSL QALHDALSGR
    160 170 180 190 200
    LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS FFTASEGCSN PLGGGREVWF
    210 220 230 240 250
    GFHQSVRPSL WKMMLNIDVS ATAFYKAQPV IEFVCEVLDF KSIEEQQKPL
    260 270 280 290 300
    TDSQRVKFTK EIKGLKVEIT HCGQMKRKYR VCNVTRRPAS HQTFPLQQES
    310 320 330 340 350
    GQTVECTVAQ YFKDRHKLVL RYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ
    360 370 380 390 400
    RCIKKLTDNQ TSTMIRATAR SAPDRQEEIS KLMRSASFNT DPYVREFGIM
    410 420 430 440 450
    VKDEMTDVTG RVLQPPSILY GGRNKAIATP VQGVWDMRNK QFHTGIEIKV
    460 470 480 490 500
    WAIACFAPQR QCTEVHLKSF TEQLRKISRD AGMPIQGQPC FCKYAQGADS
    510 520 530 540 550
    VEPMFRHLKN TYAGLQLVVV ILPGKTPVYA EVKRVGDTVL GMATQCVQMK
    560 570 580 590 600
    NVQRTTPQTL SNLCLKINVK LGGVNNILLP QGRPPVFQQP VIFLGADVTH
    610 620 630 640 650
    PPAGDGKKPS IAAVVGSMDA HPNRYCATVR VQQHRQEIIQ DLAAMVRELL
    660 670 680 690 700
    IQFYKSTRFK PTRIIFYRDG VSEGQFQQVL HHELLAIREA CIKLEKDYQP
    710 720 730 740 750
    GITFIVVQKR HHTRLFCTDK NERVGKSGNI PAGTTVDTKI THPTEFDFYL
    760 770 780 790 800
    CSHAGIQGTS RPSHYHVLWD DNRFSSDELQ ILTYQLCHTY VRCTRSVSIP
    810 820 830 840 850
    APAYYAHLVA FRARYHLVDK EHDSAEGSHT SGQSNGRDHQ ALAKAVQVHQ

    DTLRTMYFA
    Length:859
    Mass (Da):97,208
    Last modified:May 5, 2009 - v3
    <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:i5C8552C43FC81345
    GO
    Isoform 2 (identifier: Q9UKV8-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         724-757: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:825
    Mass (Da):93,620
    Checksum:i464C15B9413608D4
    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
    E5RJY2E5RJY2_HUMAN
    Protein argonaute-2
    AGO2
    36Annotation 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>
    E5RGG9E5RGG9_HUMAN
    Protein argonaute-2
    AGO2
    73Annotation 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 AAH07633 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAL76093 differs from that shown. cDNA contains a duplication of an internal sequence at the 5' end.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 conflicti564C → W in AAF13034 (PubMed:10534406).Curated1
    Sequence conflicti589Q → E in AAF13034 (PubMed:10534406).Curated1
    Sequence conflicti617S → R in AAF13034 (PubMed:10534406).Curated1
    Sequence conflicti637E → K in AAL76093 (PubMed:11914277).Curated1

    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_037001724 – 757Missing in isoform 2. 1 PublicationAdd BLAST34

    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
    AC067931 Genomic DNA No translation available.
    AC107375 Genomic DNA No translation available.
    BC007633 mRNA Translation: AAH07633.1 Different initiation.
    BC018727 mRNA Translation: AAH18727.2
    BC125214 mRNA No translation available.
    AY077717 mRNA Translation: AAL76093.1 Sequence problems.
    BT007229 mRNA Translation: AAP35893.1
    AF121255 mRNA Translation: AAF13034.2

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS55279.1 [Q9UKV8-2]
    CCDS6380.1 [Q9UKV8-1]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001158095.1, NM_001164623.2 [Q9UKV8-2]
    NP_036286.2, NM_012154.4 [Q9UKV8-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.660189
    Hs.743313

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000220592; ENSP00000220592; ENSG00000123908 [Q9UKV8-1]
    ENST00000519980; ENSP00000430176; ENSG00000123908 [Q9UKV8-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    27161

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:27161

    UCSC genome browser

    More...
    UCSCi
    uc003yvm.5 human [Q9UKV8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    AC067931 Genomic DNA No translation available.
    AC107375 Genomic DNA No translation available.
    BC007633 mRNA Translation: AAH07633.1 Different initiation.
    BC018727 mRNA Translation: AAH18727.2
    BC125214 mRNA No translation available.
    AY077717 mRNA Translation: AAL76093.1 Sequence problems.
    BT007229 mRNA Translation: AAP35893.1
    AF121255 mRNA Translation: AAF13034.2
    CCDSiCCDS55279.1 [Q9UKV8-2]
    CCDS6380.1 [Q9UKV8-1]
    RefSeqiNP_001158095.1, NM_001164623.2 [Q9UKV8-2]
    NP_036286.2, NM_012154.4 [Q9UKV8-1]
    UniGeneiHs.660189
    Hs.743313

    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
    3LUCX-ray1.69A/B/C439-575[»]
    3LUDX-ray2.10A/B/C439-575[»]
    3LUGX-ray1.85A/B/C439-575[»]
    3LUHX-ray2.00A/B/C439-575[»]
    3LUJX-ray1.80A/B/C439-575[»]
    3LUKX-ray1.70A/B/C439-575[»]
    3QX8X-ray2.30A/B/C439-575[»]
    3QX9X-ray2.00A/B/C439-575[»]
    4F3TX-ray2.25A1-859[»]
    4OLAX-ray2.30A1-859[»]
    4OLBX-ray2.90A1-859[»]
    4W5NX-ray2.90A1-859[»]
    4W5OX-ray1.80A1-859[»]
    4W5QX-ray3.10A1-859[»]
    4W5RX-ray2.50A1-859[»]
    4W5TX-ray2.50A1-859[»]
    4Z4CX-ray2.30A1-859[»]
    4Z4DX-ray1.60A1-859[»]
    4Z4EX-ray1.80A1-859[»]
    4Z4FX-ray2.80A1-859[»]
    4Z4GX-ray2.70A1-859[»]
    4Z4HX-ray2.50A1-859[»]
    4Z4IX-ray2.80A1-859[»]
    5JS1X-ray2.50A1-859[»]
    5JS2X-ray2.95A1-859[»]
    5KI6X-ray2.15A1-859[»]
    5T7BX-ray2.53A1-859[»]
    5WEAX-ray3.12A1-859[»]
    6CBDX-ray2.20A1-859[»]
    DisProtiDP00736
    ProteinModelPortaliQ9UKV8
    SMRiQ9UKV8
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi118041, 103 interactors
    ComplexPortaliCPX-1072 RISC-loading complex, PRKRA variant
    CPX-134 RISC-loading complex, TARBP2 variant
    CORUMiQ9UKV8
    DIPiDIP-29194N
    IntActiQ9UKV8, 197 interactors
    MINTiQ9UKV8
    STRINGi9606.ENSP00000220592

    PTM databases

    iPTMnetiQ9UKV8
    PhosphoSitePlusiQ9UKV8
    SwissPalmiQ9UKV8

    Polymorphism and mutation databases

    BioMutaiAGO2
    DMDMi229463006

    Proteomic databases

    EPDiQ9UKV8
    PaxDbiQ9UKV8
    PeptideAtlasiQ9UKV8
    PRIDEiQ9UKV8
    ProteomicsDBi84894
    84895 [Q9UKV8-2]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    27161
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000220592; ENSP00000220592; ENSG00000123908 [Q9UKV8-1]
    ENST00000519980; ENSP00000430176; ENSG00000123908 [Q9UKV8-2]
    GeneIDi27161
    KEGGihsa:27161
    UCSCiuc003yvm.5 human [Q9UKV8-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    27161
    DisGeNETi27161
    EuPathDBiHostDB:ENSG00000123908.11

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    AGO2
    HGNCiHGNC:3263 AGO2
    HPAiCAB019309
    HPA058075
    MIMi606229 gene
    neXtProtiNX_Q9UKV8
    OpenTargetsiENSG00000123908
    PharmGKBiPA27694

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1041 Eukaryota
    ENOG410XP07 LUCA
    GeneTreeiENSGT00940000155239
    HOGENOMiHOG000116043
    InParanoidiQ9UKV8
    KOiK11593
    OMAiSPDGYYH
    OrthoDBiEOG091G020J
    PhylomeDBiQ9UKV8
    TreeFamiTF101510

    Enzyme and pathway databases

    ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
    R-HSA-203927 MicroRNA (miRNA) biogenesis
    R-HSA-4086398 Ca2+ pathway
    R-HSA-426486 Small interfering RNA (siRNA) biogenesis
    R-HSA-426496 Post-transcriptional silencing by small RNAs
    R-HSA-5578749 Transcriptional regulation by small RNAs
    R-HSA-5628897 TP53 Regulates Metabolic Genes
    R-HSA-5687128 MAPK6/MAPK4 signaling
    R-HSA-8934593 Regulation of RUNX1 Expression and Activity
    R-HSA-8943723 Regulation of PTEN mRNA translation
    R-HSA-8948700 Competing endogenous RNAs (ceRNAs) regulate PTEN translation
    R-HSA-8986944 Transcriptional Regulation by MECP2
    R-HSA-9018519 Estrogen-dependent gene expression
    R-HSA-9022692 Regulation of MECP2 expression and activity
    SIGNORiQ9UKV8

    Miscellaneous databases

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

    More...
    ChiTaRSi
    AGO2 human
    EvolutionaryTraceiQ9UKV8

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    EIF2C2

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

    More...
    GenomeRNAii
    27161

    Protein Ontology

    More...
    PROi
    PR:Q9UKV8

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000123908 Expressed in 220 organ(s), highest expression level in forebrain
    CleanExiHS_EIF2C2
    ExpressionAtlasiQ9UKV8 baseline and differential
    GenevisibleiQ9UKV8 HS

    Family and domain databases

    Gene3Di3.30.420.10, 1 hit
    HAMAPiMF_03031 AGO2, 1 hit
    InterProiView protein in InterPro
    IPR028602 AGO2
    IPR014811 ArgoL1
    IPR032472 ArgoL2
    IPR032473 Argonaute_Mid_dom
    IPR032474 Argonaute_N
    IPR003100 PAZ_dom
    IPR036085 PAZ_dom_sf
    IPR003165 Piwi
    IPR012337 RNaseH-like_sf
    IPR036397 RNaseH_sf
    PfamiView protein in Pfam
    PF08699 ArgoL1, 1 hit
    PF16488 ArgoL2, 1 hit
    PF16487 ArgoMid, 1 hit
    PF16486 ArgoN, 1 hit
    PF02170 PAZ, 1 hit
    PF02171 Piwi, 1 hit
    SMARTiView protein in SMART
    SM01163 DUF1785, 1 hit
    SM00949 PAZ, 1 hit
    SM00950 Piwi, 1 hit
    SUPFAMiSSF101690 SSF101690, 1 hit
    SSF53098 SSF53098, 1 hit
    PROSITEiView protein in PROSITE
    PS50821 PAZ, 1 hit
    PS50822 PIWI, 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 nameiAGO2_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: Q9UKV8
    Secondary accession number(s): Q8TCZ5, Q8WV58, Q96ID1
    <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: December 1, 2000
    Last sequence update: May 5, 2009
    Last modified: December 5, 2018
    This is version 178 of the entry and version 3 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 chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Translation initiation factors
      List of translation initiation factor entries
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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