AGO2 argonaute RISC catalytic component 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: AGO2provided by HGNC
Official Full Name: argonaute RISC catalytic component 2provided by HGNC
Primary source: HGNC:HGNC:3263
See related: Ensembl:ENSG00000123908 MIM:606229; AllianceGenome:HGNC:3263
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: PPD; Q10; CASC7; EIF2C2; LESKRES; LINC00980
Summary: This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic, and contains a PAZ domain and a PIWI domain. It may interact with dicer1 and play a role in short-interfering-RNA-mediated gene silencing. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009]
Expression: Ubiquitous expression in skin (RPKM 3.3), ovary (RPKM 3.3) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 8q24.3

Exon count:: 23

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	8	NC_000008.11 (140520156..140642313, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	8	NC_060932.1 (141640512..141762332, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	8	NC_000008.10 (141530255..141645732, complement)

Chromosome 8 - NC_000008.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Tissue-specific circular RNA induction during human fetal development
Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
BioProject: PRJNA270632
Publication: PMID 26076956
Analysis date: Mon Apr 2 22:54:59 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Elucidating microRNA-34a organisation within human Argonaute-2 by dynamic nuclear polarisation-enhanced magic angle spinning NMR.
Title: Elucidating microRNA-34a organisation within human Argonaute-2 by dynamic nuclear polarisation-enhanced magic angle spinning NMR.
Loss of Lamin A leads to the nuclear translocation of AGO2 and compromised RNA interference.
Title: Loss of Lamin A leads to the nuclear translocation of AGO2 and compromised RNA interference.
Nuclear AGO2 promotes myocardial remodeling by activating ANKRD1 transcription in failing hearts.
Title: Nuclear AGO2 promotes myocardial remodeling by activating ANKRD1 transcription in failing hearts.
CRISPR-Cas9 Mediated AGO2 Knockout inhibits tumorigenesis in human colorectal cancer cells.
Title: CRISPR-Cas9 Mediated AGO2 Knockout inhibits tumorigenesis in human colorectal cancer cells.
Ago2/CAV1 interaction potentiates metastasis via controlling Ago2 localization and miRNA action.
Title: Ago2/CAV1 interaction potentiates metastasis via controlling Ago2 localization and miRNA action.
Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC.
Title: Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC.
Nuclear localization of Argonaute 2 is affected by cell density and may relieve repression by microRNAs.
Title: Nuclear localization of Argonaute 2 is affected by cell density and may relieve repression by microRNAs.
AGO2-RIP-Seq reveals miR-34/miR-449 cluster targetome in sinonasal cancers.
Title: AGO2-RIP-Seq reveals miR-34/miR-449 cluster targetome in sinonasal cancers.
Actin-dependent recruitment of AGO2 to the zonula adherens.
Title: Actin-dependent recruitment of AGO2 to the zonula adherens.
hsa_circ_0129047 Upregulates LYVE1 to Inhibit Hepatocellular Carcinoma Progression by Sponging miR-492.
Title: hsa_circ_0129047 Upregulates LYVE1 to Inhibit Hepatocellular Carcinoma Progression by Sponging miR-492.

Submit: New GeneRIF Correction See all GeneRIFs (251)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Lessel-Kreienkamp syndrome MedGen: C5436892 OMIM: 619149 GeneReviews: Not available	not available

EBI GWAS Catalog

Description
Genome-wide association analyses suggest NELL1 influences adverse metabolic response to HCTZ in African Americans. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Protein	Gene	Interaction	Pubs
Nef	nef	The interaction of HIV-1 Nef with AGO2 inhibits miRNA-induced silencing and the slicing activity of AGO2	PubMed
	nef	HIV-1 Nef interacts with AGO2 and two GW motifs at residues 12-13 and 140-141 in Nef are required for AGO2 binding	PubMed
	nef	HIV-1 Nef co-localizes with AGO2 in multivesicular bodies	PubMed
Pr55(Gag)	gag	Knockdown of AGO2 by shRNA leads to enhance enrichment of HIV-1 Gag in intracellular vacuoles, but decrease viral particle release in Gag expressing cells	PubMed
	gag	Mov10 overexpression results in translational repression of HIV-1 Gag and that AGO2 and/or RISC function is required to induce this translational repression	PubMed
	gag	The efficiency of incorporation of Mov10, A3G, and A3F into viral particles, which contains both HIV-1 Gag and genomic RNA, is much higher than that of the other P-body proteins AGO2, DCP1a, DCP2, and DDX6	PubMed
	gag	ABCE1, DDX6, and AGO2 proteins are associated with HIV-1 Gag in the intracellular high-molecular-weight assembly intermediates. DDX6 and AGO2 are enriched at early and late sites of Gag assembly at plasma membrane	PubMed
	gag	HIV-1 Gag interacts with and encapsidates AGO2 into virus particles in a miRNA- and P-body-independent manner. AGO2 is required for HIV-1 replication	PubMed

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH45183 (e-PCR)
- UniSTS:89345

SHGC-146257 (e-PCR)
- UniSTS:175109

RH103829 (e-PCR)
- UniSTS:98154

SHGC-154248 (e-PCR)
- UniSTS:178036

D8S1635 (e-PCR)
- UniSTS:75396

D8S1717 (e-PCR)
- UniSTS:13452

Eif2c2 (e-PCR), detects polymorphism
- UniSTS:479157

WI-11623 (e-PCR)
- UniSTS:81391

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA 7-methylguanosine cap binding	IDA Inferred from Direct Assay more info	PubMed
enables RNA 7-methylguanosine cap binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	HDA more info	PubMed
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables RNA endonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables RNA endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables RNA endonuclease activity	IEA Inferred from Electronic Annotation more info
enables RNA endonuclease activity	TAS Traceable Author Statement more info
enables RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II complex binding	IDA Inferred from Direct Assay more info	PubMed
enables core promoter sequence-specific DNA binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables double-stranded RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables double-stranded RNA binding	IEA Inferred from Electronic Annotation more info
enables endonuclease activity	IEA Inferred from Electronic Annotation more info
enables endoribonuclease activity, cleaving miRNA-paired mRNA	IDA Inferred from Direct Assay more info	PubMed
enables endoribonuclease activity, cleaving miRNA-paired mRNA	IMP Inferred from Mutant Phenotype more info	PubMed
enables endoribonuclease activity, cleaving siRNA-paired mRNA	IDA Inferred from Direct Assay more info	PubMed
enables endoribonuclease activity, cleaving siRNA-paired mRNA	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables mRNA 3'-UTR AU-rich region binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA binding	IEA Inferred from Electronic Annotation more info
enables mRNA cap binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA cap binding	IEA Inferred from Electronic Annotation more info
enables mRNA cap binding	IPI Inferred from Physical Interaction more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables miRNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables miRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables miRNA binding	IEA Inferred from Electronic Annotation more info
enables miRNA binding	IPI Inferred from Physical Interaction more info	PubMed
enables miRNA binding	TAS Traceable Author Statement more info	PubMed
enables nuclease activity	IEA Inferred from Electronic Annotation more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
contributes_to siRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables siRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables siRNA binding	IEA Inferred from Electronic Annotation more info
enables single-stranded RNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables single-stranded RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables single-stranded RNA binding	IEA Inferred from Electronic Annotation more info
enables translation initiation factor activity	NAS Non-traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in P-body assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in RISC complex assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in RISC complex assembly	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within RNA stabilization	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within gene expression	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within miRNA metabolic process	IEA Inferred from Electronic Annotation more info
involved_in miRNA processing	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within miRNA processing	IEA Inferred from Electronic Annotation more info
involved_in miRNA-mediated gene silencing by inhibition of translation	IDA Inferred from Direct Assay more info	PubMed
involved_in miRNA-mediated gene silencing by inhibition of translation	IEA Inferred from Electronic Annotation more info
involved_in miRNA-mediated gene silencing by inhibition of translation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in miRNA-mediated gene silencing by mRNA destabilization	IDA Inferred from Direct Assay more info	PubMed
involved_in miRNA-mediated gene silencing by mRNA destabilization	IEA Inferred from Electronic Annotation more info
involved_in miRNA-mediated gene silencing by mRNA destabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of amyloid precursor protein biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of translational initiation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of translational initiation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of angiogenesis	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within positive regulation of gene expression	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of nuclear-transcribed mRNA poly(A) tail shortening	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of nuclear-transcribed mRNA poly(A) tail shortening	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of transcription by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of translation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of trophoblast cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within post-embryonic development	IEA Inferred from Electronic Annotation more info
involved_in pre-miRNA processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in pre-miRNA processing	IDA Inferred from Direct Assay more info	PubMed
involved_in pre-miRNA processing	IEA Inferred from Electronic Annotation more info
involved_in regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in regulation of synapse maturation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of synapse maturation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of translation	IEA Inferred from Electronic Annotation more info
involved_in regulatory ncRNA-mediated gene silencing	IEA Inferred from Electronic Annotation more info
involved_in regulatory ncRNA-mediated gene silencing	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulatory ncRNA-mediated post-transcriptional gene silencing	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulatory ncRNA-mediated post-transcriptional gene silencing	TAS Traceable Author Statement more info
involved_in siRNA processing	IDA Inferred from Direct Assay more info	PubMed
involved_in siRNA-mediated gene silencing by mRNA destabilization	IDA Inferred from Direct Assay more info	PubMed
involved_in siRNA-mediated gene silencing by mRNA destabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in translation	NAS Non-traceable Author Statement more info	PubMed
involved_in translational initiation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in P-body	IDA Inferred from Direct Assay more info	PubMed
located_in P-body	IEA Inferred from Electronic Annotation more info
part_of RISC complex	IBA Inferred from Biological aspect of Ancestor more info
part_of RISC complex	IDA Inferred from Direct Assay more info	PubMed
part_of RISC complex	IEA Inferred from Electronic Annotation more info
part_of RISC complex	IGI Inferred from Genetic Interaction more info	PubMed
part_of RISC complex	IPI Inferred from Physical Interaction more info	PubMed
part_of RISC-loading complex	IDA Inferred from Direct Assay more info	PubMed
part_of RISC-loading complex	IEA Inferred from Electronic Annotation more info
part_of RISC-loading complex	IPI Inferred from Physical Interaction more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasmic ribonucleoprotein granule	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic ribonucleoprotein granule	IDA Inferred from Direct Assay more info
located_in cytoplasmic ribonucleoprotein granule	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	TAS Traceable Author Statement more info
located_in dendrite	IEA Inferred from Electronic Annotation more info
located_in extracellular exosome	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	IMP Inferred from Mutant Phenotype more info	PubMed
located_in membrane	HDA more info	PubMed
located_in nucleoplasm	TAS Traceable Author Statement more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IC Inferred by Curator more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
is_active_in postsynapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in postsynapse	IMP Inferred from Mutant Phenotype more info	PubMed
part_of ribonucleoprotein complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: protein argonaute-2

Names: PAZ Piwi domain protein; argonaute 2, RISC catalytic component; cancer susceptibility candidate 7 (non-protein coding); eukaryotic translation initiation factor 2C, 2; long intergenic non-protein coding RNA 980; protein slicer

NP_001158095.1

EC 3.1.26.n2

NP_036286.2

EC 3.1.26.n2

XP_011515267.1

EC 3.1.26.n2

XP_011515270.3

EC 3.1.26.n2

XP_047277651.1

EC 3.1.26.n2

XP_047277652.1

EC 3.1.26.n2

XP_047277653.1

EC 3.1.26.n2

XP_054216272.1

EC 3.1.26.n2

XP_054216273.1

EC 3.1.26.n2

XP_054216274.1

EC 3.1.26.n2

XP_054216275.1

EC 3.1.26.n2

XP_054216276.1

EC 3.1.26.n2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001164623.3 → NP_001158095.1 protein argonaute-2 isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks an alternate in-frame exon in the 3' coding region, compared to variant 1. The resulting isoform (2) is shorter than isoform 1.

Source sequence(s)

AC067931, AC107375

Consensus CDS

CCDS55279.1

UniProtKB/TrEMBL

A4FVC0

Related

ENSP00000430176.1, ENST00000519980.5

Conserved Domains (4) summary

cd02846
Location:227 → 347

PAZ_argonaute_like; PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. ...

cd04657
Location:392 → 783

Piwi_ago-like; Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of the RNA-induced silencing complex (RISC) and related complexes. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of ...

pfam08699
Location:176 → 226

ArgoL1; Argonaute linker 1 domain

pfam16486
Location:92 → 166

ArgoN; N-terminal domain of argonaute
NM_012154.5 → NP_036286.2 protein argonaute-2 isoform 1

See identical proteins and their annotated locations for NP_036286.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

Source sequence(s)

AC067931, AC107375

Consensus CDS

CCDS6380.1

UniProtKB/Swiss-Prot

Q8TCZ5, Q8WV58, Q96ID1, Q9UKV8

UniProtKB/TrEMBL

A4FVC0

Related

ENSP00000220592.5, ENST00000220592.10

Conserved Domains (4) summary

cd02846
Location:227 → 347

PAZ_argonaute_like; PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. ...

cd04657
Location:392 → 817

Piwi_ago-like; PIWI domain, Argonaute-like subfamily. Argonaute is the central component of the RNA-induced silencing complex (RISC) and related complexes. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the ...

pfam08699
Location:176 → 226

ArgoL1; Argonaute linker 1 domain

pfam16486
Location:92 → 166

ArgoN; N-terminal domain of argonaute

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000008.11 Reference GRCh38.p14 Primary Assembly

Range

140520156..140642313 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011516968.3 → XP_011515270.3 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0
XM_047421697.1 → XP_047277653.1 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0
XM_047421695.1 → XP_047277651.1 protein argonaute-2 isoform X2

UniProtKB/TrEMBL

A4FVC0
XM_011516965.3 → XP_011515267.1 protein argonaute-2 isoform X1

UniProtKB/TrEMBL

A4FVC0

Conserved Domains (5) summary

PLN03202
Location:39 → 872

PLN03202; protein argonaute; Provisional

cd02846
Location:241 → 361

PAZ_argonaute_like; PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. ...

cd04657
Location:406 → 831

Piwi_ago-like; Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of the RNA-induced silencing complex (RISC) and related complexes. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of ...

pfam08699
Location:191 → 240

ArgoL1; Argonaute linker 1 domain

pfam16486
Location:42 → 180

ArgoN; N-terminal domain of argonaute
XM_047421696.1 → XP_047277652.1 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0

Alternate T2T-CHM13v2.0

Genomic

NC_060932.1 Alternate T2T-CHM13v2.0

Range

141640512..141762332 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054360301.1 → XP_054216276.1 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0
XM_054360300.1 → XP_054216275.1 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0
XM_054360298.1 → XP_054216273.1 protein argonaute-2 isoform X2

UniProtKB/TrEMBL

A4FVC0
XM_054360297.1 → XP_054216272.1 protein argonaute-2 isoform X1

UniProtKB/TrEMBL

A4FVC0
XM_054360299.1 → XP_054216274.1 protein argonaute-2 isoform X3

UniProtKB/TrEMBL

A4FVC0