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Q9UL18

- AGO1_HUMAN

UniProt

Q9UL18 - AGO1_HUMAN

Protein

Protein argonaute-1

Gene

AGO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs).3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. gene expression Source: Reactome
    5. innate immune response Source: Reactome
    6. negative regulation of translation involved in gene silencing by miRNA Source: UniProtKB
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. Notch signaling pathway Source: Reactome
    9. nuclear-transcribed mRNA catabolic process Source: UniProtKB
    10. phosphatidylinositol-mediated signaling Source: Reactome
    11. regulation of transcription, DNA-templated Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein

    Keywords - Biological processi

    RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118699. Post-transcriptional silencing by small RNAs.
    REACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172761. Ca2+ pathway.
    REACT_75829. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein argonaute-1
    Short name:
    Argonaute1
    Short name:
    hAgo1
    Alternative name(s):
    Argonaute RISC catalytic component 1
    Eukaryotic translation initiation factor 2C 1
    Short name:
    eIF-2C 1
    Short name:
    eIF2C 1
    Putative RNA-binding protein Q99
    Gene namesi
    Name:AGO1
    Synonyms:EIF2C1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3262. AGO1.

    Subcellular locationi

    CytoplasmP-body 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. micro-ribonucleoprotein complex Source: UniProtKB
    5. polysome Source: UniProtKB
    6. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi670 – 6701P → S: Confers modest RNA cleavage activity; when associated with Q-675 and H-805. 1 Publication
    Mutagenesisi674 – 6741L → F: Confers modest RNA cleavage activity; when associated with H-805. 1 Publication
    Mutagenesisi675 – 6751P → Q: Does not confer enzyme activity by itself. Confers low RNA cleavage activity; when associated with H-805. Confers modest RNA cleavage activity; when associated with S-670 and H-805. 1 Publication
    Mutagenesisi805 – 8051R → H: Does not confer enzyme activity by itself. Confers modest RNA cleavage activity; when associated with F-674. 2 Publications

    Organism-specific databases

    PharmGKBiPA27693.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 857857Protein argonaute-1PRO_0000194055Add
    BLAST

    Proteomic databases

    MaxQBiQ9UL18.
    PaxDbiQ9UL18.
    PRIDEiQ9UL18.

    PTM databases

    PhosphoSiteiQ9UL18.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UL18.
    BgeeiQ9UL18.
    CleanExiHS_EIF2C1.
    GenevestigatoriQ9UL18.

    Interactioni

    Subunit structurei

    Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47, DICER1, AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5, RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with LIMD1, WTIP and AJUBA. Interacts with APOBEC3F, APOBEC3G and APOBEC3H.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DICER1Q9UPY35EBI-527363,EBI-395506
    HSP90AB1P082383EBI-527363,EBI-352572
    IPO8O153972EBI-527363,EBI-358808
    TNRC6AQ8NDV74EBI-527363,EBI-2269715

    Protein-protein interaction databases

    BioGridi117726. 38 interactions.
    DIPiDIP-29193N.
    IntActiQ9UL18. 180 interactions.
    STRINGi9606.ENSP00000362300.

    Structurei

    Secondary structure

    1
    857
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 4614
    Beta strandi51 – 6212
    Helixi66 – 7914
    Helixi81 – 855
    Beta strandi94 – 1029
    Turni105 – 1084
    Beta strandi110 – 1156
    Beta strandi125 – 13713
    Helixi138 – 14710
    Helixi154 – 17118
    Beta strandi172 – 1754
    Beta strandi178 – 1803
    Beta strandi189 – 1913
    Beta strandi194 – 20613
    Beta strandi208 – 22316
    Helixi228 – 2369
    Turni241 – 2433
    Helixi250 – 26011
    Beta strandi264 – 2685
    Turni269 – 2724
    Beta strandi276 – 28611
    Turni287 – 2893
    Beta strandi291 – 2955
    Beta strandi301 – 3055
    Helixi306 – 3149
    Beta strandi323 – 3286
    Helixi331 – 3333
    Beta strandi335 – 3384
    Helixi339 – 3413
    Beta strandi342 – 3443
    Helixi356 – 36611
    Helixi370 – 38415
    Helixi386 – 3883
    Helixi390 – 3945
    Beta strandi404 – 4107
    Turni420 – 4234
    Beta strandi448 – 4536
    Turni457 – 4593
    Helixi462 – 47817
    Beta strandi488 – 4925
    Helixi496 – 4983
    Helixi499 – 50911
    Beta strandi515 – 5206
    Helixi526 – 53510
    Turni536 – 5383
    Beta strandi542 – 5465
    Helixi547 – 5515
    Helixi555 – 56814
    Helixi578 – 5803
    Helixi583 – 5864
    Beta strandi589 – 5979
    Beta strandi608 – 6158
    Beta strandi617 – 6204
    Beta strandi623 – 6319
    Helixi640 – 65516
    Beta strandi660 – 6667
    Helixi671 – 6733
    Helixi674 – 69219
    Beta strandi699 – 7068
    Beta strandi713 – 7175
    Helixi718 – 7203
    Turni723 – 7264
    Beta strandi732 – 7343
    Beta strandi736 – 7394
    Beta strandi741 – 7433
    Beta strandi745 – 7495
    Beta strandi755 – 7573
    Beta strandi761 – 7688
    Helixi774 – 78411
    Helixi799 – 81416
    Helixi837 – 8437
    Helixi848 – 8514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SI2X-ray2.60A225-369[»]
    1SI3X-ray2.60A225-369[»]
    4KREX-ray1.75A1-857[»]
    4KRFX-ray2.10A1-857[»]
    4KXTX-ray2.29A1-857[»]
    ProteinModelPortaliQ9UL18.
    SMRiQ9UL18. Positions 17-857.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UL18.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini226 – 346121PAZPROSITE-ProRule annotationAdd
    BLAST
    Domaini515 – 816302PiwiPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni309 – 3146Interaction with guide RNA
    Regioni522 – 56443Interaction with guide RNAAdd
    BLAST
    Regioni670 – 6756Impairs access of bound RNA to the active site
    Regioni708 – 7125Interaction with guide RNA
    Regioni751 – 7599Interaction with guide RNA
    Regioni788 – 81326Interaction with guide RNAAdd
    BLAST

    Sequence similaritiesi

    Belongs to the argonaute family. Ago subfamily.Curated
    Contains 1 PAZ domain.PROSITE-ProRule annotation
    Contains 1 Piwi domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG279895.
    HOGENOMiHOG000116043.
    InParanoidiQ9UL18.
    KOiK11593.
    OMAiEVTHRAN.
    PhylomeDBiQ9UL18.
    TreeFamiTF101510.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF08699. DUF1785. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view]
    SMARTiSM00949. PAZ. 1 hit.
    SM00950. Piwi. 1 hit.
    [Graphical view]
    SUPFAMiSSF101690. SSF101690. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEiPS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UL18-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI    50
    DVYHYEVDIK PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT 100
    VTALPIGNER VDFEVTIPGE GKDRIFKVSI KWLAIVSWRM LHEALVSGQI 150
    PVPLESVQAL DVAMRHLASM RYTPVGRSFF SPPEGYYHPL GGGREVWFGF 200
    HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN IDEQPKPLTD 250
    SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ 300
    TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC 350
    IKKLTDNQTS TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK 400
    DDMTEVTGRV LPAPILQYGG RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA 450
    IACFAPQKQC REEVLKNFTD QLRKISKDAG MPIQGQPCFC KYAQGADSVE 500
    PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM ATQCVQVKNV 550
    VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP 600
    AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ 650
    FYKSTRFKPT RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI 700
    TYIVVQKRHH TRLFCADKNE RIGKSGNIPA GTTVDTNITH PFEFDFYLCS 750
    HAGIQGTSRP SHYYVLWDDN RFTADELQIL TYQLCHTYVR CTRSVSIPAP 800
    AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL AKAVQVHQDT 850
    LRTMYFA 857
    Length:857
    Mass (Da):97,214
    Last modified:February 21, 2006 - v3
    Checksum:i1DBB524AE7CBAF66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421D → N in AAH63275. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093097 mRNA. Translation: AAF00068.1.
    AL139286 Genomic DNA. Translation: CAI22804.1.
    BC063275 mRNA. Translation: AAH63275.1.
    CCDSiCCDS398.1.
    RefSeqiNP_036331.1. NM_012199.2.
    UniGeneiHs.22867.
    Hs.656677.

    Genome annotation databases

    EnsembliENST00000373204; ENSP00000362300; ENSG00000092847.
    GeneIDi26523.
    KEGGihsa:26523.
    UCSCiuc001bzk.3. human.

    Polymorphism databases

    DMDMi88984241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093097 mRNA. Translation: AAF00068.1 .
    AL139286 Genomic DNA. Translation: CAI22804.1 .
    BC063275 mRNA. Translation: AAH63275.1 .
    CCDSi CCDS398.1.
    RefSeqi NP_036331.1. NM_012199.2.
    UniGenei Hs.22867.
    Hs.656677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SI2 X-ray 2.60 A 225-369 [» ]
    1SI3 X-ray 2.60 A 225-369 [» ]
    4KRE X-ray 1.75 A 1-857 [» ]
    4KRF X-ray 2.10 A 1-857 [» ]
    4KXT X-ray 2.29 A 1-857 [» ]
    ProteinModelPortali Q9UL18.
    SMRi Q9UL18. Positions 17-857.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117726. 38 interactions.
    DIPi DIP-29193N.
    IntActi Q9UL18. 180 interactions.
    STRINGi 9606.ENSP00000362300.

    PTM databases

    PhosphoSitei Q9UL18.

    Polymorphism databases

    DMDMi 88984241.

    Proteomic databases

    MaxQBi Q9UL18.
    PaxDbi Q9UL18.
    PRIDEi Q9UL18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373204 ; ENSP00000362300 ; ENSG00000092847 .
    GeneIDi 26523.
    KEGGi hsa:26523.
    UCSCi uc001bzk.3. human.

    Organism-specific databases

    CTDi 26523.
    GeneCardsi GC01P036336.
    HGNCi HGNC:3262. AGO1.
    MIMi 606228. gene.
    neXtProti NX_Q9UL18.
    PharmGKBi PA27693.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279895.
    HOGENOMi HOG000116043.
    InParanoidi Q9UL18.
    KOi K11593.
    OMAi EVTHRAN.
    PhylomeDBi Q9UL18.
    TreeFami TF101510.

    Enzyme and pathway databases

    Reactomei REACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118699. Post-transcriptional silencing by small RNAs.
    REACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172761. Ca2+ pathway.
    REACT_75829. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi EIF2C1. human.
    EvolutionaryTracei Q9UL18.
    GeneWikii EIF2C1.
    GenomeRNAii 26523.
    NextBioi 48846.
    PROi Q9UL18.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UL18.
    Bgeei Q9UL18.
    CleanExi HS_EIF2C1.
    Genevestigatori Q9UL18.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR014811. DUF1785.
    IPR003100. PAZ_dom.
    IPR003165. Piwi.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF08699. DUF1785. 1 hit.
    PF02170. PAZ. 1 hit.
    PF02171. Piwi. 1 hit.
    [Graphical view ]
    SMARTi SM00949. PAZ. 1 hit.
    SM00950. Piwi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101690. SSF101690. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEi PS50821. PAZ. 1 hit.
    PS50822. PIWI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence, genomic organization, localization to chromosomal bands 1p34-p35, and expression."
      Koesters R., Adams V., Betts D., Moos R., Schmid M., Siermann A., Hassam S., Weitz S., Lichter P., Heitz P.U., von Knebel Doeberitz M., Briner J.
      Genomics 61:210-218(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    4. "Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs."
      Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G., Tuschl T.
      Mol. Cell 15:185-197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH MIRNA.
    5. Cited for: FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, SUBCELLULAR LOCATION.
    6. Cited for: FUNCTION.
    7. "Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54."
      Chu C.-Y., Rana T.M.
      PLoS Biol. 4:E210-E210(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX6 AND AGO2.
    8. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH POLYSOMES AND MNRP, INTERACTION WITH DDB1; DDX5; DHX30; DHX36; DDX47; ELAVL1; HNRNPF; IGF2BP1; ILF3; MATR3; PABPC1; RBM4; SART3; UPF1 AND YBX1.
    9. "Importance of translation and nonnucleolytic ago proteins for on-target RNA interference."
      Wu L., Fan J., Belasco J.G.
      Curr. Biol. 18:1327-1332(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs."
      Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P., Kremmer E., Benes V., Urlaub H., Meister G.
      Cell 136:496-507(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IMP8.
    11. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies."
      Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.
      J. Virol. 86:11712-11724(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOBEC3F; APOBEC3G AND APOBEC3H.
    14. "Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain."
      Ma J.-B., Ye K., Patel D.J.
      Nature 429:318-322(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 225-369, RNA-BINDING.
    15. "Eukaryote-specific insertion elements control human ARGONAUTE slicer activity."
      Nakanishi K., Ascano M., Gogakos T., Ishibe-Murakami S., Serganov A.A., Briskin D., Morozov P., Tuschl T., Patel D.J.
      Cell Rep. 3:1893-1900(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH RNA, RNA-BINDING, MUTAGENESIS OF PRO-670; PRO-675 AND ARG-805, LACK OF CATALYTIC ACTIVITY.
    16. "The making of a slicer: activation of human Argonaute-1."
      Faehnle C.R., Elkayam E., Haase A.D., Hannon G.J., Joshua-Tor L.
      Cell Rep. 3:1901-1909(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH RNA, LACK OF CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-674 AND ARG-805.

    Entry informationi

    Entry nameiAGO1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UL18
    Secondary accession number(s): Q5TA57, Q6P4S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Miscellaneous

    Lacks RNA cleavage activity due to the absence of the conserved His at position 805, but also because it binds the RNA in a subtly different manner that precludes efficient cleavage.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    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

    External Data

    Dasty 3