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Protein

Protein argonaute-1

Gene

AGO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. double-stranded RNA binding Source: BHF-UCL
  2. miRNA binding Source: BHF-UCL
  3. poly(A) RNA binding Source: UniProtKB
  4. pre-miRNA binding Source: BHF-UCL
  5. RNA binding Source: UniProtKB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  7. single-stranded RNA binding Source: BHF-UCL

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. miRNA loading onto RISC involved in gene silencing by miRNA Source: BHF-UCL
  7. miRNA metabolic process Source: Ensembl
  8. negative regulation of translation involved in gene silencing by miRNA Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. Notch signaling pathway Source: Reactome
  11. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  12. phosphatidylinositol-mediated signaling Source: Reactome
  13. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  14. posttranscriptional gene silencing Source: Reactome
  15. pre-miRNA processing Source: BHF-UCL
  16. production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
  17. RNA secondary structure unwinding Source: BHF-UCL
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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_263982. Ca2+ pathway.
REACT_268530. Transcriptional regulation by small RNAs.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3262. AGO1.

Subcellular locationi

CytoplasmP-body 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. micro-ribonucleoprotein complex Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. polysome Source: UniProtKB
  7. ribonucleoprotein complex Source: UniProtKB
  8. RISC complex Source: BHF-UCL
  9. RISC-loading complex Source: BHF-UCL
Complete GO annotation...

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

BgeeiQ9UL18.
CleanExiHS_EIF2C1.
ExpressionAtlasiQ9UL18. baseline and differential.
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. 39 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 – 4614Combined sources
Beta strandi51 – 6212Combined sources
Helixi66 – 7914Combined sources
Helixi81 – 855Combined sources
Beta strandi94 – 1029Combined sources
Turni105 – 1084Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi125 – 13713Combined sources
Helixi138 – 14710Combined sources
Helixi154 – 17118Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 20613Combined sources
Beta strandi208 – 22316Combined sources
Helixi228 – 2369Combined sources
Turni241 – 2433Combined sources
Helixi250 – 26011Combined sources
Beta strandi264 – 2685Combined sources
Turni269 – 2724Combined sources
Beta strandi276 – 28611Combined sources
Turni287 – 2893Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi301 – 3055Combined sources
Helixi306 – 3149Combined sources
Beta strandi323 – 3286Combined sources
Helixi331 – 3333Combined sources
Beta strandi335 – 3384Combined sources
Helixi339 – 3413Combined sources
Beta strandi342 – 3443Combined sources
Helixi356 – 36611Combined sources
Helixi370 – 38415Combined sources
Helixi386 – 3883Combined sources
Helixi390 – 3945Combined sources
Beta strandi404 – 4107Combined sources
Turni420 – 4234Combined sources
Beta strandi448 – 4536Combined sources
Turni457 – 4593Combined sources
Helixi462 – 47817Combined sources
Beta strandi488 – 4925Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 50911Combined sources
Beta strandi515 – 5206Combined sources
Helixi526 – 53510Combined sources
Turni536 – 5383Combined sources
Beta strandi542 – 5465Combined sources
Helixi547 – 5515Combined sources
Helixi555 – 56814Combined sources
Helixi578 – 5803Combined sources
Helixi583 – 5864Combined sources
Beta strandi589 – 5979Combined sources
Beta strandi608 – 6158Combined sources
Beta strandi617 – 6204Combined sources
Beta strandi623 – 6319Combined sources
Helixi640 – 65516Combined sources
Beta strandi660 – 6667Combined sources
Helixi671 – 6733Combined sources
Helixi674 – 69219Combined sources
Beta strandi699 – 7068Combined sources
Beta strandi713 – 7175Combined sources
Helixi718 – 7203Combined sources
Turni723 – 7264Combined sources
Beta strandi732 – 7343Combined sources
Beta strandi736 – 7394Combined sources
Beta strandi741 – 7433Combined sources
Beta strandi745 – 7495Combined sources
Beta strandi755 – 7573Combined sources
Beta strandi761 – 7688Combined sources
Helixi774 – 78411Combined sources
Helixi799 – 81416Combined sources
Helixi837 – 8437Combined sources
Helixi848 – 8514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9UL18.
KOiK11593.
OMAiLELDWYL.
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

        10         20         30         40         50
MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI
60 70 80 90 100
DVYHYEVDIK PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT
110 120 130 140 150
VTALPIGNER VDFEVTIPGE GKDRIFKVSI KWLAIVSWRM LHEALVSGQI
160 170 180 190 200
PVPLESVQAL DVAMRHLASM RYTPVGRSFF SPPEGYYHPL GGGREVWFGF
210 220 230 240 250
HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN IDEQPKPLTD
260 270 280 290 300
SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ
310 320 330 340 350
TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC
360 370 380 390 400
IKKLTDNQTS TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK
410 420 430 440 450
DDMTEVTGRV LPAPILQYGG RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA
460 470 480 490 500
IACFAPQKQC REEVLKNFTD QLRKISKDAG MPIQGQPCFC KYAQGADSVE
510 520 530 540 550
PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM ATQCVQVKNV
560 570 580 590 600
VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP
610 620 630 640 650
AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ
660 670 680 690 700
FYKSTRFKPT RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI
710 720 730 740 750
TYIVVQKRHH TRLFCADKNE RIGKSGNIPA GTTVDTNITH PFEFDFYLCS
760 770 780 790 800
HAGIQGTSRP SHYYVLWDDN RFTADELQIL TYQLCHTYVR CTRSVSIPAP
810 820 830 840 850
AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL AKAVQVHQDT

LRTMYFA
Length:857
Mass (Da):97,214
Last modified:February 20, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi117726. 39 interactions.
DIPiDIP-29193N.
IntActiQ9UL18. 180 interactions.
STRINGi9606.ENSP00000362300.

PTM databases

PhosphoSiteiQ9UL18.

Polymorphism databases

DMDMi88984241.

Proteomic databases

MaxQBiQ9UL18.
PaxDbiQ9UL18.
PRIDEiQ9UL18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26523.
GeneCardsiGC01P036336.
HGNCiHGNC:3262. AGO1.
MIMi606228. gene.
neXtProtiNX_Q9UL18.
PharmGKBiPA27693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279895.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9UL18.
KOiK11593.
OMAiLELDWYL.
PhylomeDBiQ9UL18.
TreeFamiTF101510.

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_263982. Ca2+ pathway.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_75829. PIP3 activates AKT signaling.

Miscellaneous databases

EvolutionaryTraceiQ9UL18.
GeneWikiiEIF2C1.
GenomeRNAii26523.
NextBioi48846.
PROiQ9UL18.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UL18.
CleanExiHS_EIF2C1.
ExpressionAtlasiQ9UL18. baseline and differential.
GenevestigatoriQ9UL18.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [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(2005) [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(2003) [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(2003) [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(2005) [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(2006) [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(2007) [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(2008) [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(2011) [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(2003) [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(2012) [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(2012) [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: November 30, 2000
Last sequence update: February 20, 2006
Last modified: March 31, 2015
This is version 127 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.