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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

  • core promoter binding Source: BHF-UCL
  • double-stranded RNA binding Source: BHF-UCL
  • miRNA binding Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II core binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • single-stranded RNA binding Source: BHF-UCL

GO - Biological processi

  • gene silencing by RNA Source: Reactome
  • miRNA loading onto RISC involved in gene silencing by miRNA Source: BHF-UCL
  • miRNA mediated inhibition of translation Source: UniProtKB
  • miRNA metabolic process Source: Ensembl
  • nuclear-transcribed mRNA catabolic process Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of NIK/NF-kappaB signaling Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • posttranscriptional gene silencing by RNA Source: Reactome
  • pre-miRNA processing Source: BHF-UCL
  • production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
  • RNA secondary structure unwinding Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
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

BioCyciZFISH:ENSG00000092847-MONOMER.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-4086398. Ca2+ pathway.
R-HSA-426486. Small interfering RNA (siRNA) biogenesis.
R-HSA-426496. Post-transcriptional silencing by small RNAs.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3262. AGO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • micro-ribonucleoprotein complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • polysome Source: UniProtKB
  • RISC complex Source: BHF-UCL
  • RISC-loading complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi670P → S: Confers modest RNA cleavage activity; when associated with Q-675 and H-805. 1 Publication1
Mutagenesisi674L → F: Confers modest RNA cleavage activity; when associated with H-805. 1 Publication1
Mutagenesisi675P → 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 Publication1
Mutagenesisi805R → H: Does not confer enzyme activity by itself. Confers modest RNA cleavage activity; when associated with F-674. 2 Publications1

Organism-specific databases

DisGeNETi26523.
OpenTargetsiENSG00000092847.
PharmGKBiPA27693.

Polymorphism and mutation databases

BioMutaiAGO1.
DMDMi88984241.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001940551 – 857Protein argonaute-1Add BLAST857

Proteomic databases

EPDiQ9UL18.
MaxQBiQ9UL18.
PaxDbiQ9UL18.
PeptideAtlasiQ9UL18.
PRIDEiQ9UL18.

PTM databases

iPTMnetiQ9UL18.
PhosphoSitePlusiQ9UL18.

Expressioni

Gene expression databases

BgeeiENSG00000092847.
CleanExiHS_EIF2C1.
ExpressionAtlasiQ9UL18. baseline and differential.
GenevisibleiQ9UL18. HS.

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

GO - Molecular functioni

  • RNA polymerase II core binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi117726. 44 interactors.
DIPiDIP-29193N.
IntActiQ9UL18. 180 interactors.
STRINGi9606.ENSP00000362300.

Structurei

Secondary structure

1857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 46Combined sources14
Beta strandi51 – 62Combined sources12
Helixi66 – 79Combined sources14
Helixi81 – 85Combined sources5
Beta strandi94 – 102Combined sources9
Turni105 – 108Combined sources4
Beta strandi110 – 115Combined sources6
Beta strandi125 – 137Combined sources13
Helixi138 – 147Combined sources10
Helixi154 – 171Combined sources18
Beta strandi172 – 175Combined sources4
Beta strandi178 – 180Combined sources3
Beta strandi189 – 191Combined sources3
Beta strandi194 – 206Combined sources13
Beta strandi208 – 223Combined sources16
Helixi228 – 236Combined sources9
Turni241 – 243Combined sources3
Helixi250 – 260Combined sources11
Beta strandi264 – 268Combined sources5
Turni269 – 272Combined sources4
Beta strandi276 – 286Combined sources11
Turni287 – 289Combined sources3
Beta strandi291 – 295Combined sources5
Beta strandi301 – 305Combined sources5
Helixi306 – 314Combined sources9
Beta strandi323 – 328Combined sources6
Helixi331 – 333Combined sources3
Beta strandi335 – 338Combined sources4
Helixi339 – 341Combined sources3
Beta strandi342 – 344Combined sources3
Helixi356 – 366Combined sources11
Helixi370 – 384Combined sources15
Helixi386 – 388Combined sources3
Helixi390 – 394Combined sources5
Beta strandi404 – 410Combined sources7
Turni420 – 423Combined sources4
Beta strandi448 – 453Combined sources6
Turni457 – 459Combined sources3
Helixi462 – 478Combined sources17
Beta strandi488 – 492Combined sources5
Helixi496 – 498Combined sources3
Helixi499 – 509Combined sources11
Beta strandi515 – 520Combined sources6
Helixi526 – 535Combined sources10
Turni536 – 538Combined sources3
Beta strandi542 – 546Combined sources5
Helixi547 – 551Combined sources5
Helixi555 – 568Combined sources14
Helixi578 – 580Combined sources3
Helixi583 – 586Combined sources4
Beta strandi589 – 597Combined sources9
Beta strandi608 – 615Combined sources8
Beta strandi617 – 620Combined sources4
Beta strandi623 – 631Combined sources9
Helixi640 – 655Combined sources16
Beta strandi660 – 666Combined sources7
Helixi671 – 673Combined sources3
Helixi674 – 692Combined sources19
Beta strandi699 – 706Combined sources8
Beta strandi713 – 717Combined sources5
Helixi718 – 720Combined sources3
Turni723 – 726Combined sources4
Beta strandi732 – 734Combined sources3
Beta strandi736 – 739Combined sources4
Beta strandi741 – 743Combined sources3
Beta strandi745 – 749Combined sources5
Beta strandi755 – 757Combined sources3
Beta strandi761 – 768Combined sources8
Helixi774 – 784Combined sources11
Helixi799 – 814Combined sources16
Helixi837 – 843Combined sources7
Helixi848 – 851Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UL18.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini226 – 346PAZPROSITE-ProRule annotationAdd BLAST121
Domaini515 – 816PiwiPROSITE-ProRule annotationAdd BLAST302

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni309 – 314Interaction with guide RNA6
Regioni522 – 564Interaction with guide RNAAdd BLAST43
Regioni670 – 675Impairs access of bound RNA to the active site6
Regioni708 – 712Interaction with guide RNA5
Regioni751 – 759Interaction with guide RNA9
Regioni788 – 813Interaction with guide RNAAdd BLAST26

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

eggNOGiKOG1041. Eukaryota.
ENOG410XP07. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9UL18.
KOiK11593.
OMAiEREYDIM.
OrthoDBiEOG091G020J.
PhylomeDBiQ9UL18.
TreeFamiTF101510.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR032472. ArgoL2.
IPR032473. Argonaute_Mid_dom.
IPR032474. Argonaute_N.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF08699. ArgoL1. 1 hit.
PF16488. ArgoL2. 1 hit.
PF16487. ArgoMid. 1 hit.
PF16486. ArgoN. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01163. DUF1785. 1 hit.
SM00949. 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 21, 2006 - v3
Checksum:i1DBB524AE7CBAF66
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti242D → N in AAH63275 (PubMed:15489334).Curated1

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_001304051.1. NM_001317122.1.
NP_001304052.1. NM_001317123.1.
NP_036331.1. NM_012199.4.
UniGeneiHs.22867.
Hs.656677.

Genome annotation databases

EnsembliENST00000373204; ENSP00000362300; ENSG00000092847.
GeneIDi26523.
KEGGihsa:26523.
UCSCiuc001bzl.4. human.

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_001304051.1. NM_001317122.1.
NP_001304052.1. NM_001317123.1.
NP_036331.1. NM_012199.4.
UniGeneiHs.22867.
Hs.656677.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117726. 44 interactors.
DIPiDIP-29193N.
IntActiQ9UL18. 180 interactors.
STRINGi9606.ENSP00000362300.

PTM databases

iPTMnetiQ9UL18.
PhosphoSitePlusiQ9UL18.

Polymorphism and mutation databases

BioMutaiAGO1.
DMDMi88984241.

Proteomic databases

EPDiQ9UL18.
MaxQBiQ9UL18.
PaxDbiQ9UL18.
PeptideAtlasiQ9UL18.
PRIDEiQ9UL18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373204; ENSP00000362300; ENSG00000092847.
GeneIDi26523.
KEGGihsa:26523.
UCSCiuc001bzl.4. human.

Organism-specific databases

CTDi26523.
DisGeNETi26523.
GeneCardsiAGO1.
HGNCiHGNC:3262. AGO1.
MIMi606228. gene.
neXtProtiNX_Q9UL18.
OpenTargetsiENSG00000092847.
PharmGKBiPA27693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1041. Eukaryota.
ENOG410XP07. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9UL18.
KOiK11593.
OMAiEREYDIM.
OrthoDBiEOG091G020J.
PhylomeDBiQ9UL18.
TreeFamiTF101510.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092847-MONOMER.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-4086398. Ca2+ pathway.
R-HSA-426486. Small interfering RNA (siRNA) biogenesis.
R-HSA-426496. Post-transcriptional silencing by small RNAs.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000092847.
CleanExiHS_EIF2C1.
ExpressionAtlasiQ9UL18. baseline and differential.
GenevisibleiQ9UL18. HS.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. ArgoL1.
IPR032472. ArgoL2.
IPR032473. Argonaute_Mid_dom.
IPR032474. Argonaute_N.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF08699. ArgoL1. 1 hit.
PF16488. ArgoL2. 1 hit.
PF16487. ArgoMid. 1 hit.
PF16486. ArgoN. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM01163. DUF1785. 1 hit.
SM00949. 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...

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: November 2, 2016
This is version 143 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

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 one 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.