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Entry version 198 (29 Sep 2021)
Sequence version 3 (05 May 2009)
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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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal 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

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q9UKV8

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
R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux

SIGNOR Signaling Network Open Resource

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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

Human Gene Nomenclature Database

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HGNCi
HGNC:3263, AGO2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606229, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9UKV8

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000123908

<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

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

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OpenTargetsi
ENSG00000123908

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27694

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9UKV8, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
AGO2

Domain mapping of disease mutations (DMDM)

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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 or proteolytic cleavage.<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 residuei23'-nitrotyrosineUniRule 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
Ubiquitinated on surface-exposed lysines by a SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 during target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). Ubiquitination by the SCF-like E3 ubiquitin-protein ligase complex containing ZSWIM8 leads to its subsequent degradation, thereby exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237). ZSWIM8 recognizes and binds AGO2 when it is engaged with a TDMD target (PubMed:33184237).2 Publications

Keywords - PTMi

Hydroxylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9UKV8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9UKV8

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9UKV8

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

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PaxDbi
Q9UKV8

PeptideAtlas

More...
PeptideAtlasi
Q9UKV8

PRoteomics IDEntifications database

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PRIDEi
Q9UKV8

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
84894 [Q9UKV8-1]
84895 [Q9UKV8-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q9UKV8, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9UKV8

MetOSite database of methionine sulfoxide sites

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MetOSitei
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 forebrain and 233 other tissues

ExpressionAtlas, Differential and Baseline Expression

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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
ENSG00000123908, Low tissue specificity

<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).

Interacts with SYT11 (By similarity).

Interacts with CLNK (PubMed:26009488).

Interacts with GARRE1 (PubMed:29395067).

UniRule annotationBy similarity34 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
118041, 336 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9UKV8

Database of interacting proteins

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DIPi
DIP-29194N

Protein interaction database and analysis system

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IntActi
Q9UKV8, 211 interactors

Molecular INTeraction database

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MINTi
Q9UKV8

STRING: functional protein association networks

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STRINGi
9606.ENSP00000220592

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9UKV8, protein

<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

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

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SMRi
Q9UKV8

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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>Regioni1 – 27DisorderedSequence analysisAdd BLAST27
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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi8 – 24Pro residuesSequence analysisAdd BLAST17

<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

Ensembl GeneTree

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GeneTreei
ENSGT00940000155239

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_004544_4_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UKV8

Identification of Orthologs from Complete Genome Data

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OMAi
RIKKSCD

Database of Orthologous Groups

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OrthoDBi
159407at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UKV8

TreeFam database of animal gene trees

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TreeFami
TF101510

Family and domain databases

Database of protein disorder

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DisProti
DP00736

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.420.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_03031, AGO2, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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

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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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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.

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. Truncated N-terminus.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.<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

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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]

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]

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[»]
6MDZX-ray3.40A/B1-859[»]
6MFNX-ray2.50A1-859[»]
6MFRX-ray3.60A/B1-859[»]
6N4OX-ray2.90A1-859[»]
6NITX-ray3.80A/B1-859[»]
6RA4X-ray1.90A/B222-355[»]
7C6BX-ray1.70A/B/C440-578[»]
7D7UX-ray2.00A/B/C440-578[»]
SMRiQ9UKV8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi118041, 336 interactors
ComplexPortaliCPX-1072, RISC-loading complex, PRKRA variant
CPX-134, RISC-loading complex, TARBP2 variant
CORUMiQ9UKV8
DIPiDIP-29194N
IntActiQ9UKV8, 211 interactors
MINTiQ9UKV8
STRINGi9606.ENSP00000220592

PTM databases

GlyGeniQ9UKV8, 1 site, 1 O-linked glycan (1 site)
iPTMnetiQ9UKV8
MetOSiteiQ9UKV8
PhosphoSitePlusiQ9UKV8
SwissPalmiQ9UKV8

Genetic variation databases

BioMutaiAGO2
DMDMi229463006

Proteomic databases

EPDiQ9UKV8
jPOSTiQ9UKV8
MassIVEiQ9UKV8
PaxDbiQ9UKV8
PeptideAtlasiQ9UKV8
PRIDEiQ9UKV8
ProteomicsDBi84894 [Q9UKV8-1]
84895 [Q9UKV8-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
27626, 339 antibodies

The DNASU plasmid repository

More...
DNASUi
27161

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

GeneCards: human genes, protein and diseases

More...
GeneCardsi
AGO2
HGNCiHGNC:3263, AGO2
HPAiENSG00000123908, Low tissue specificity
MIMi606229, gene
neXtProtiNX_Q9UKV8
OpenTargetsiENSG00000123908
PharmGKBiPA27694
VEuPathDBiHostDB:ENSG00000123908

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1041, Eukaryota
GeneTreeiENSGT00940000155239
HOGENOMiCLU_004544_4_3_1
InParanoidiQ9UKV8
OMAiRIKKSCD
OrthoDBi159407at2759
PhylomeDBiQ9UKV8
TreeFamiTF101510

Enzyme and pathway databases

PathwayCommonsiQ9UKV8
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
R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
SIGNORiQ9UKV8

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
27161, 40 hits in 1025 CRISPR screens

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
PharosiQ9UKV8, Tbio

Protein Ontology

More...
PROi
PR:Q9UKV8
RNActiQ9UKV8, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000123908, Expressed in forebrain and 233 other tissues
ExpressionAtlasiQ9UKV8, baseline and differential
GenevisibleiQ9UKV8, HS

Family and domain databases

DisProtiDP00736
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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: September 29, 2021
This is version 198 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, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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