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Entry version 157 (12 Aug 2020)
Sequence version 3 (27 Jul 2011)
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Protein

Protein argonaute-2

Gene

Ago2

Organism
Mus musculus (Mouse)
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. Regulates lymphoid and erythroid development and function, and this is independent of endonuclease activity.UniRule annotation3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi598Divalent metal cationUniRule annotation1
Metal bindingi670Divalent metal cationUniRule annotation1
Metal bindingi808Divalent metal cationUniRule annotation1

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

GO - Biological processi

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

Molecular functionDevelopmental protein, Endonuclease, Hydrolase, Nuclease, Repressor, Ribonucleoprotein, RNA-binding
Biological processDifferentiation, RNA-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-MMU-203927, MicroRNA (miRNA) biogenesis
R-MMU-426486, Small interfering RNA (siRNA) biogenesis
R-MMU-426496, Post-transcriptional silencing by small RNAs
R-MMU-5578749, Transcriptional regulation by small RNAs

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein argonaute-2UniRule annotation (EC:3.1.26.n2UniRule annotation)
Short name:
Argonaute2UniRule annotation
Short name:
mAgo2
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
Piwi/argonaute family protein meIF2C2
Protein slicerUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ago2
Synonyms:Eif2c2, Kiaa4215
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2446632, Ago2

<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 & Seán O’Donoghue; 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic death with a strong defect in neural tube closure and apparent cardiac failure.1 Publication

<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_00001940581 – 860Protein argonaute-2Add BLAST860

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'-nitrotyrosineCombined sources1
Modified residuei388PhosphoserineBy similarity1
Modified residuei7014-hydroxyprolineUniRule annotation1
Modified residuei829PhosphoserineBy similarity1

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

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

Keywords - PTMi

Hydroxylation, Nitration, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8CJG0

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8CJG0

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8CJG0

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

More...
PaxDbi
Q8CJG0

PeptideAtlas

More...
PeptideAtlasi
Q8CJG0

PRoteomics IDEntifications database

More...
PRIDEi
Q8CJG0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8CJG0

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

More...
PhosphoSitePlusi
Q8CJG0

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8CJG0

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

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

Ubiquitous expression in 9.5 day embryos with highest levels in forebrain, heart, limb buds, and branchial arches.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000036698, Expressed in mesenteric lymph node and 263 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8CJG0, MM

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

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

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 (PubMed:16357216).

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 (By similarity).

Interacts with TRIM71 (PubMed:19898466, PubMed:22508726, PubMed:22735451).

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).

Interacts with FMR1.

Interacts with ZFP36 (By similarity).

Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406).

Interacts with FAM172A (PubMed:29311329).

Found in a complex composed of AGO2, CHD7 and FAM172A (PubMed:29311329).

Interacts with SND1 and SYT11 (PubMed:24882364).

Interacts with CLNK (PubMed:26009488).

Interacts with GARRE1 (By similarity).

UniRule annotationBy similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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
232092, 51 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1073, RISC-loading complex, PRKRA variant
CPX-135, RISC-loading complex, TARBP2 variant

Database of interacting proteins

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DIPi
DIP-35014N

Protein interaction database and analysis system

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IntActi
Q8CJG0, 56 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000042207

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q8CJG0, 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

3D structure databases

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

More...
SMRi
Q8CJG0

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini236 – 349PAZUniRule annotationAdd BLAST114
Domaini518 – 819PiwiUniRule 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>Regioni312 – 317Interaction with guide RNABy similarity6
Regioni525 – 567Interaction with guide RNABy similarityAdd BLAST43
Regioni588 – 591Interaction with GW182 family membersSequence analysis4
Regioni651 – 661Interaction with GW182 family membersSequence analysisAdd BLAST11
Regioni710 – 711Interaction with guide RNABy similarity2
Regioni754 – 762Interaction with guide RNABy similarity9
Regioni791 – 813Interaction with guide RNABy similarityAdd 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).UniRule annotation

<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

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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
Q8CJG0

KEGG Orthology (KO)

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KOi
K11593

Identification of Orthologs from Complete Genome Data

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OMAi
RIKKSCD

Database of Orthologous Groups

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OrthoDBi
159407at2759

TreeFam database of animal gene trees

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TreeFami
TF101510

Family and domain databases

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

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SUPFAMi
SSF101690, SSF101690, 1 hit
SSF53098, SSF53098, 1 hit

PROSITE; a protein domain and family database

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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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Q8CJG0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI
60 70 80 90 100
PKIDIYHYEL DIKPEKCPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN
110 120 130 140 150
LYTAMPLPIG RDKVELEVTL PGEGKDRIFK VSIKWVSCVS LQALHDALSG
160 170 180 190 200
RLPSVPFETI QALDVVMRHL PSMRYTPVGR SFFTASEGCS NPLGGGREVW
210 220 230 240 250
FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD FKSIEEQQKP
260 270 280 290 300
LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE
310 320 330 340 350
SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG
360 370 380 390 400
QRCIKKLTDN QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI
410 420 430 440 450
MVKDEMTDVT GRVLQPPSIL YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK
460 470 480 490 500
VWAIACFAPQ RQCTEVHLKS FTEQLRKISR DAGMPIQGQP CFCKYAQGAD
510 520 530 540 550
SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV LGMATQCVQM
560 570 580 590 600
KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT
610 620 630 640 650
HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL
660 670 680 690 700
LIQFYKSTRF KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKDYQ
710 720 730 740 750
PGITFIVVQK RHHTRLFCTD KNERVGKSGN IPAGTTVDTK ITHPTEFDFY
760 770 780 790 800
LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL QILTYQLCHT YVRCTRSVSI
810 820 830 840 850
PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH QALAKAVQVH
860
QDTLRTMYFA
Length:860
Mass (Da):97,304
Last modified:July 27, 2011 - 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:iA4E13C633846062C
GO

<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 AAH96465 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.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 conflicti65E → G in AAH96465 (PubMed:15489334).Curated1
Sequence conflicti67C → R in BAC15767 (PubMed:12526743).Curated1
Sequence conflicti129F → L in BAC15767 (PubMed:12526743).Curated1
Sequence conflicti360N → D in BAC15767 (PubMed:12526743).Curated1
Sequence conflicti563N → D in AAH96465 (PubMed:15489334).Curated1
Sequence conflicti711R → P in AAH96465 (PubMed:15489334).Curated1
Sequence conflicti761S → G in BAC15767 (PubMed:12526743).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB081472 mRNA Translation: BAC15767.1
BC096465 mRNA Translation: AAH96465.1 Different initiation.
BC128379 mRNA Translation: AAI28380.1
BC129922 mRNA Translation: AAI29923.1
AK220193 mRNA Translation: BAD90378.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS37098.1

NCBI Reference Sequences

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RefSeqi
NP_694818.3, NM_153178.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698

Database of genes from NCBI RefSeq genomes

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GeneIDi
239528

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:239528

UCSC genome browser

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UCSCi
uc007wbu.2, mouse

<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
AB081472 mRNA Translation: BAC15767.1
BC096465 mRNA Translation: AAH96465.1 Different initiation.
BC128379 mRNA Translation: AAI28380.1
BC129922 mRNA Translation: AAI29923.1
AK220193 mRNA Translation: BAD90378.1
CCDSiCCDS37098.1
RefSeqiNP_694818.3, NM_153178.4

3D structure databases

SMRiQ8CJG0
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi232092, 51 interactors
ComplexPortaliCPX-1073, RISC-loading complex, PRKRA variant
CPX-135, RISC-loading complex, TARBP2 variant
DIPiDIP-35014N
IntActiQ8CJG0, 56 interactors
STRINGi10090.ENSMUSP00000042207

PTM databases

iPTMnetiQ8CJG0
PhosphoSitePlusiQ8CJG0
SwissPalmiQ8CJG0

Proteomic databases

EPDiQ8CJG0
jPOSTiQ8CJG0
MaxQBiQ8CJG0
PaxDbiQ8CJG0
PeptideAtlasiQ8CJG0
PRIDEiQ8CJG0

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
27626, 299 antibodies

Genome annotation databases

EnsembliENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698
GeneIDi239528
KEGGimmu:239528
UCSCiuc007wbu.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
27161
MGIiMGI:2446632, Ago2

Rodent Unidentified Gene-Encoded large proteins database

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Rougei
Search...

Phylogenomic databases

eggNOGiKOG1041, Eukaryota
GeneTreeiENSGT00940000155239
HOGENOMiCLU_004544_4_3_1
InParanoidiQ8CJG0
KOiK11593
OMAiRIKKSCD
OrthoDBi159407at2759
TreeFamiTF101510

Enzyme and pathway databases

ReactomeiR-MMU-203927, MicroRNA (miRNA) biogenesis
R-MMU-426486, Small interfering RNA (siRNA) biogenesis
R-MMU-426496, Post-transcriptional silencing by small RNAs
R-MMU-5578749, Transcriptional regulation by small RNAs

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
239528, 5 hits in 18 CRISPR screens

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

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ChiTaRSi
Ago2, mouse

Protein Ontology

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PROi
PR:Q8CJG0
RNActiQ8CJG0, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000036698, Expressed in mesenteric lymph node and 263 other tissues
GenevisibleiQ8CJG0, MM

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_MOUSE
<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: Q8CJG0
Secondary accession number(s): A1A563, Q4VAB3, Q571J6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: July 27, 2011
Last modified: August 12, 2020
This is version 157 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

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

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
  3. Translation initiation factors
    List of translation initiation factor entries
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