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Browse our AGO2 Proteins (EIF2C2)

Full name:
Eukaryotic Translation Initiation Factor 2C, 2 Proteins (EIF2C2)
On www.antibodies-online.com are 17 Eukaryotic Translation Initiation Factor 2C, 2 (EIF2C2) Proteins from 6 different suppliers available. Additionally we are shipping AGO2 Antibodies (70) and AGO2 Kits (6) and many more products for this protein. A total of 96 AGO2 products are currently listed.
Synonyms:
1110029L17Rik, 2310051F07Rik, AG02, ago, ago-2, AGO 2, ago2, AI225898, AL022874, Argonaute2, argonaute 2, AW546247, CG7439, CG13452, dAgo2, Dm Ago2, Dmel\\CG7439, eif2c1, eIF2C2, ENSMUSG00000072493, Gerp95, Gm10365, mKIAA4215, Q10, T19E23.7, T19E23_7
list all proteins Gene Name GeneID UniProt
EIF2C2 27161 Q9UKV8
Rat EIF2C2 EIF2C2 59117 Q9QZ81
EIF2C2 239528 Q8CJG0

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AGO2 Proteins (EIF2C2) by Origin

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Top referenced AGO2 Proteins

  1. Human AGO2 Protein expressed in Baculovirus infected Insect Cells - ABIN2003923 : Rand, Petersen, Du, Wang: Argonaute2 cleaves the anti-guide strand of siRNA during RISC activation. in Cell 2005 (PubMed)
    Show all 6 references for ABIN2003923

  2. Mouse (Murine) AGO2 Protein expressed in Baculovirus infected Insect Cells - ABIN2008152 : Qi, Ongusaha, Myllyharju, Cheng, Pakkanen, Shi, Lee, Peng, Shi: Prolyl 4-hydroxylation regulates Argonaute 2 stability. in Nature 2008 (PubMed)
    Show all 5 references for ABIN2008152

  3. Human AGO2 Protein expressed in Wheat germ - ABIN1352524 : Rawlings, Krishnan, Walter: Viral RNAi suppressor reversibly binds siRNA to outcompete Dicer and RISC via multiple turnover. in Journal of molecular biology 2011 (PubMed)

More Proteins for AGO2 Interaction Partners

Arabidopsis thaliana Eukaryotic Translation Initiation Factor 2C, 2 (EIF2C2) interaction partners

  1. AGO1, AGO2 and AGO10 promoted anti-TuMV defense in a modular way in various organs, with AGO2 providing a prominent antiviral role in leaves. AGO5, AGO7 and AGO10 had minor effects in leaves.

  2. Base pairing at the 15th nucleotide of a miRNA duplex is important for miRNA sorting in both Arabidopsis AGO1 (show EIF2C1 Proteins) and AGO2. AGO2 favours miRNA duplexes with no middle mismatches.

  3. Complementation analyses in ago mutant plants revealed that the catalytic residues of AGO1, AGO2, and AGO7 are required to restore the defects of Arabidopsis ago1-25, ago2-1, and zip-1 (AGO7-defective) mutants, respectively.

  4. AGO2 and HEN1 (show HENMT1 Proteins) participate in the DCL2-mediated antiviral defense to ensure the survival of Turnip crinkle virus-infected plants at high temperature.

  5. This study reveals that miR408, which has a 5'A, regulates its target Plantacyanin through either AGO1 (show EIF2C1 Proteins) or AGO2.

  6. AGO1 (show EIF2C1 Proteins) and AGO2 are involved in defense against mutant of Cucumber mosaic virus, which act downstream the biogenesis of viral secondary siRNAs in a nonredundant and cooperative manner.

  7. Results show that AGO2-bound small RNA miR393b( *) targets a Golgi-localized SNARE (show NAPA Proteins) gene, MEMB12.

  8. second layer is activated when the first layer is suppressed because AGO2 is repressed by AGO1 (show EIF2C1 Proteins) via miR403

Human Eukaryotic Translation Initiation Factor 2C, 2 (EIF2C2) interaction partners

  1. deciphering Ago2:RNA interactions using crosslinking immunoprecipitation coupled with high-throughput sequencing (HITS-CLIP) to generate the first transcriptome-wide map of miR (show MLXIP Proteins) targeting events in human myocardium, detecting 4000 cardiac Ago2 binding sites across 2200 target transcripts

  2. AGO2 immunoprecipitation revealed LATS1 as a novel proapoptotic target of miR (show MLXIP Proteins)-21 in T cells.

  3. The miRNA biogenesis factors, DDX17 (show DDX17 Proteins) and KHSRP (show KHSRP Proteins), regulate the protein level of Ago2 in human cells.

  4. 1174 regions within the 45S rRNA transcript that have the ability to form a perfect duplex with position 2-6 (seed sequence) of each microRNA expressed in HEK293T cells. Of these potential AGO2 binding sites, 479 occurred within experimentally verified AGO2-rRNA cross-linking sites. The ability of AGO2 to cross-link to rRNA was almost completely lost in a DICER (show DICER1 Proteins) knock-out cell line.

  5. this study analysed binding of miR-122/ Argonaute 2 complexes to two conserved binding sites in the 5' UTR of hepatitis C virus RNA.

  6. overactivity of KRAS due to mutation inhibits localization of Ago2 to multivesicular endosomes (MVEs) and decreases Ago2 secretion in exosomes.

  7. TP53 (show TP53 Proteins) regulates miRNA association with AGO2 to remodel the miRNA-mRNA interaction network

  8. These results support the notion that the cereblon (show CRBN Proteins) binding partner AGO2 plays an important role in regulating MM cell growth and survival and AGO2 could be considered as a novel drug target for overcoming IMiD resistance in MM cells.

  9. KRAS engages AGO2 to enhance cellular neoplastic transformation.

  10. Authors found that target binding of core-RISC starts at the seed region of the guide RNA. After target binding, four distinct reactions followed: target cleavage, transient binding, stable binding, and Argonaute 2 unloading.

Mouse (Murine) Eukaryotic Translation Initiation Factor 2C, 2 (EIF2C2) interaction partners

  1. We propose that RISC-mediated inhibition of specific sets of chromatin regulators is a primary mechanism for preserving embryonic stem cell pluripotency while inhibiting the onset of embryonic developmental programs

  2. Increased AGO2 was detected in autophagy-deficient ATG5 (show ATG5 Proteins)-/- and ATG16 (show ATG16L1 Proteins)-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.

  3. DIS3L2 (show DIS3L2 Proteins) interacts with Ago2 and governs target RNA-directed miRNA degradation.

  4. Results from the liver show that, siRNA targets 3'UTR and the coding sequence (CDs (show ABHD5 Proteins)) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR-targeted siRNA-mediated knockdown are active with the help of Ago1 (show EIF2C1 Proteins) and Ago3 (show EIF2C3 Proteins).

  5. Roquin (show RC3H1 Proteins) also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR (show MLXIP Proteins)-146a, a microRNA that targets Icos (show ICOS Proteins) mRNA.

  6. Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs.

  7. Mouse AGO2 binds tighter to miRNA targets than its RNAi cleavage product, even though the cleaved product contains more base pairs. By re-writing the rules for nucleic acid hybridization, Argonautes allow oligonucleotides to serve as specificity determinants with thermodynamic and kinetic properties more typical of RNA-binding proteins than of RNA or DNA.

  8. Mouse Ago2 can be expressed as a fusion protein with the maltose binding protein in a soluble and enzymatically active form, without requiring coexpression with chaperones and cleave the complementary RNA in absence of other cellular factors.

  9. This study identifies the targeting of Ago2 by miR (show MLXIP Proteins)-184 as an essential component of the compensatory response to regulate proliferation according to insulin (show INS Proteins) sensitivity.

  10. study identifies Fkbp4 and Fkbp5 as novel components of the Ago2 RISC loading complex

Fruit Fly (Drosophila melanogaster) Eukaryotic Translation Initiation Factor 2C, 2 (EIF2C2) interaction partners

  1. Mutation of T1149 or R1158 in the conserved PIWI (show PIWIL1 Proteins) domain causes AGO2 protein instability, but only T1149 affects RNAi activity. Mass spec analysis shows that several proteasome components co-purify with both wildtype and mutant AGO2, and knockdown of two proteasome pathway components results in AGO2 protein accumulation.

  2. We speculate that the repeated evolution of testis specificity in obscura group Ago2 genes, combined with their dynamic turnover and strong signatures of adaptive evolution, may be associated with highly derived roles in the suppression of transposable elements or meiotic drive

  3. We find there are large differences in evolutionary rates and gene turnover between pathways, and that paralogs of Ago2, Ago3, and Piwi/Aub show contrasting rates of evolution after duplication.

  4. Study shows that the Cricket Paralysis virus suppressor of RNA silencing, CrPV-1A but not B2 strongly interfere with the Ago-2-dependent miRNA silencing in Drosophila.

  5. siRNA biogenesis does not stabilize AGO2 in Drosophila.

  6. The results of this study found that mutations in Drosophila Argonaute 2 (Ago2) resulted in exacerbated transposon expression in the brain, progressive and age-dependent memory impairment, and shortened lifespan

  7. analysis of regulation of Argonaute (show EIF2C1 Proteins) slicer activity by guide RNA 3' end interactions with the N-terminal lobe

  8. two new nuclear roles for Ago-2: one in pre-mRNA splicing and one in transcriptional repression.

  9. Highlighting its role in antiviral defense, fly Ago2 dissociates so slowly from extensively complementary target RNAs that essentially every fully paired target is cleaved. Conversely, mouse AGO2, which mainly mediates miRNA-directed repression, dissociates rapidly and with similar rates for fully paired and seed-matched targets.

  10. Nora virus VP1 and the viral suppressor of RNAi of Cricket paralysis virus (1A) antagonized Argonaute-2 (AGO2) Slicer activity of RNA induced silencing complexes pre-loaded with a methylated single-stranded guide strand.

AGO2 (EIF2C2) Protein Profile

Protein 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.

Alternative names and synonyms associated with AGO2 (EIF2C2)

  • eukaryotic translation initiation factor 2C, 2 (EIF2C2)
  • Argonaute family protein (AGO2)
  • argonaute RISC catalytic component 2 (AGO2)
  • argonaute RISC catalytic component 2 (Ago2)
  • argonaute RISC catalytic component 2 (ago2)
  • argonaute RISC catalytic subunit 2 (Ago2)
  • Argonaute 2 (AGO2)
  • 1110029L17Rik protein
  • 2310051F07Rik protein
  • AG02 protein
  • ago protein
  • ago-2 protein
  • AGO 2 protein
  • ago2 protein
  • AI225898 protein
  • AL022874 protein
  • Argonaute2 protein
  • argonaute 2 protein
  • AW546247 protein
  • CG7439 protein
  • CG13452 protein
  • dAgo2 protein
  • Dm Ago2 protein
  • Dmel\\CG7439 protein
  • eif2c1 protein
  • eIF2C2 protein
  • ENSMUSG00000072493 protein
  • Gerp95 protein
  • Gm10365 protein
  • mKIAA4215 protein
  • Q10 protein
  • T19E23.7 protein
  • T19E23_7 protein

Protein level used designations for EIF2C2

eukaryotic translation initiation factor 2C, 2 , protein argonaute-2-like , PAZ Piwi domain protein , PPD , argonaute 2 , argonaute2 , eIF-2C 2 , eIF2C 2 , hAgo2 , protein argonaute-2 , protein slicer , GERp95 , golgi ER protein 95 kDa , Protein slicer , eukaryotic translation initiation factor 2C, 1 , Piwi/Argonaute family protein meIF2C2 , argonaute RISC catalytic component 2 , mAgo2 , eukaryotic translation initiation factor 2C 2 , Eukaryotic translation initiation factor 2C 2 , translation initiation factor eIF2C , AGO2-PB , AGO2-PC , AGO2-PE , ARGONAUTE2 , CG7439-PB , CG7439-PC , CG7439-PE , argonaute , argonaute-2

GENE ID SPECIES
475107 Canis lupus familiaris
737376 Pan troglodytes
100082977 Ornithorhynchus anatinus
100464244 Ailuropoda melanoleuca
840016 Arabidopsis thaliana
27161 Homo sapiens
59117 Rattus norvegicus
446823 Xenopus laevis
239528 Mus musculus
404130 Bos taurus
100009457 Oryctolagus cuniculus
39683 Drosophila melanogaster
448205 Xenopus (Silurana) tropicalis
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