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Protein

Protein argonaute-4

Gene

AGO4

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) 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 RNA-directed transcription and replication of the human hapatitis delta virus (HDV).UniRule annotation3 Publications

GO - Molecular functioni

  • double-stranded RNA binding Source: BHF-UCL
  • miRNA binding Source: BHF-UCL
  • single-stranded RNA binding Source: BHF-UCL

GO - Biological processi

  • miRNA loading onto RISC involved in gene silencing by miRNA Source: BHF-UCL
  • miRNA mediated inhibition of translation Source: UniProtKB
  • mRNA catabolic process Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • 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
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

RNA-mediated gene silencing, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

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-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein argonaute-4UniRule annotation
Short name:
Argonaute4UniRule annotation
Short name:
hAgo4
Alternative name(s):
Argonaute RISC catalytic component 4
Eukaryotic translation initiation factor 2C 4UniRule annotation
Short name:
eIF-2C 4UniRule annotation
Short name:
eIF2C 4UniRule annotation
Gene namesi
Name:AGO4
Synonyms:EIF2C4, KIAA1567
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18424. AGO4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38330.

Polymorphism and mutation databases

BioMutaiAGO4.
DMDMi38372393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Protein argonaute-4PRO_0000194063Add
BLAST

Proteomic databases

EPDiQ9HCK5.
MaxQBiQ9HCK5.
PaxDbiQ9HCK5.
PRIDEiQ9HCK5.

PTM databases

iPTMnetiQ9HCK5.
PhosphoSiteiQ9HCK5.

Expressioni

Gene expression databases

BgeeiQ9HCK5.
CleanExiHS_EIF2C4.
GenevisibleiQ9HCK5. HS.

Organism-specific databases

HPAiCAB012179.

Interactioni

Subunit structurei

Interacts with EIF4B, IMP8, PRMT5, TNRC6A and TNRC6B.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IPO8O153973EBI-2269696,EBI-358808
TNRC6AQ8NDV74EBI-2269696,EBI-2269715

Protein-protein interaction databases

BioGridi128178. 68 interactions.
IntActiQ9HCK5. 74 interactions.
STRINGi9606.ENSP00000362306.

Structurei

3D structure databases

ProteinModelPortaliQ9HCK5.
SMRiQ9HCK5. Positions 12-861.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 338114PAZUniRule annotationAdd
BLAST
Domaini509 – 820312PiwiUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the argonaute family. Ago subfamily.UniRule annotation
Contains 1 PAZ domain.UniRule annotation
Contains 1 Piwi domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG1041. Eukaryota.
ENOG410XP07. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9HCK5.
KOiK11593.
OMAiMFKHLKL.
OrthoDBiEOG7HHWRC.
PhylomeDBiQ9HCK5.
TreeFamiTF101510.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_03033. AGO4.
InterProiIPR028604. AGO4.
IPR014811. 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.

Q9HCK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALGPGPPA SLFQPPRRPG LGTVGKPIRL LANHFQVQIP KIDVYHYDVD
60 70 80 90 100
IKPEKRPRRV NREVVDTMVR HFKMQIFGDR QPGYDGKRNM YTAHPLPIGR
110 120 130 140 150
DRVDMEVTLP GEGKDQTFKV SVQWVSVVSL QLLLEALAGH LNEVPDDSVQ
160 170 180 190 200
ALDVITRHLP SMRYTPVGRS FFSPPEGYYH PLGGGREVWF GFHQSVRPAM
210 220 230 240 250
WNMMLNIDVS ATAFYRAQPI IEFMCEVLDI QNINEQTKPL TDSQRVKFTK
260 270 280 290 300
EIRGLKVEVT HCGQMKRKYR VCNVTRRPAS HQTFPLQLEN GQAMECTVAQ
310 320 330 340 350
YFKQKYSLQL KYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ
360 370 380 390 400
TSTMIKATAR SAPDRQEEIS RLVKSNSMVG GPDPYLKEFG IVVHNEMTEL
410 420 430 440 450
TGRVLPAPML QYGGRNKTVA TPNQGVWDMR GKQFYAGIEI KVWAVACFAP
460 470 480 490 500
QKQCREDLLK SFTDQLRKIS KDAGMPIQGQ PCFCKYAQGA DSVEPMFKHL
510 520 530 540 550
KMTYVGLQLI VVILPGKTPV YAEVKRVGDT LLGMATQCVQ VKNVVKTSPQ
560 570 580 590 600
TLSNLCLKIN AKLGGINNVL VPHQRPSVFQ QPVIFLGADV THPPAGDGKK
610 620 630 640 650
PSIAAVVGSM DGHPSRYCAT VRVQTSRQEI SQELLYSQEV IQDLTNMVRE
660 670 680 690 700
LLIQFYKSTR FKPTRIIYYR GGVSEGQMKQ VAWPELIAIR KACISLEEDY
710 720 730 740 750
RPGITYIVVQ KRHHTRLFCA DKTERVGKSG NVPAGTTVDS TITHPSEFDF
760 770 780 790 800
YLCSHAGIQG TSRPSHYQVL WDDNCFTADE LQLLTYQLCH TYVRCTRSVS
810 820 830 840 850
IPAPAYYARL VAFRARYHLV DKDHDSAEGS HVSGQSNGRD PQALAKAVQI
860
HHDTQHTMYF A
Length:861
Mass (Da):97,097
Last modified:November 14, 2003 - v2
Checksum:iF236FF05047534C1
GO

Sequence cautioni

The sequence BAB13393.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046787 mRNA. Translation: BAB13393.1. Different initiation.
AL359186, AL354864 Genomic DNA. Translation: CAH71584.1.
AL354864, AL359186 Genomic DNA. Translation: CAH73806.1.
CH471059 Genomic DNA. Translation: EAX07400.1.
BC152450 mRNA. Translation: AAI52451.1.
CCDSiCCDS397.1.
RefSeqiNP_060099.2. NM_017629.3.
UniGeneiHs.744858.

Genome annotation databases

EnsembliENST00000373210; ENSP00000362306; ENSG00000134698.
GeneIDi192670.
KEGGihsa:192670.
UCSCiuc001bzj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046787 mRNA. Translation: BAB13393.1. Different initiation.
AL359186, AL354864 Genomic DNA. Translation: CAH71584.1.
AL354864, AL359186 Genomic DNA. Translation: CAH73806.1.
CH471059 Genomic DNA. Translation: EAX07400.1.
BC152450 mRNA. Translation: AAI52451.1.
CCDSiCCDS397.1.
RefSeqiNP_060099.2. NM_017629.3.
UniGeneiHs.744858.

3D structure databases

ProteinModelPortaliQ9HCK5.
SMRiQ9HCK5. Positions 12-861.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128178. 68 interactions.
IntActiQ9HCK5. 74 interactions.
STRINGi9606.ENSP00000362306.

PTM databases

iPTMnetiQ9HCK5.
PhosphoSiteiQ9HCK5.

Polymorphism and mutation databases

BioMutaiAGO4.
DMDMi38372393.

Proteomic databases

EPDiQ9HCK5.
MaxQBiQ9HCK5.
PaxDbiQ9HCK5.
PRIDEiQ9HCK5.

Protocols and materials databases

DNASUi192670.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373210; ENSP00000362306; ENSG00000134698.
GeneIDi192670.
KEGGihsa:192670.
UCSCiuc001bzj.3. human.

Organism-specific databases

CTDi192670.
GeneCardsiAGO4.
HGNCiHGNC:18424. AGO4.
HPAiCAB012179.
MIMi607356. gene.
neXtProtiNX_Q9HCK5.
PharmGKBiPA38330.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1041. Eukaryota.
ENOG410XP07. LUCA.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9HCK5.
KOiK11593.
OMAiMFKHLKL.
OrthoDBiEOG7HHWRC.
PhylomeDBiQ9HCK5.
TreeFamiTF101510.

Enzyme and pathway databases

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-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

GenomeRNAii192670.
PROiQ9HCK5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCK5.
CleanExiHS_EIF2C4.
GenevisibleiQ9HCK5. HS.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_03033. AGO4.
InterProiIPR028604. AGO4.
IPR014811. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "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.
  6. "Tethering of human Ago proteins to mRNA mimics the miRNA-mediated repression of protein synthesis."
    Pillai R.S., Artus C.G., Filipowicz W.
    RNA 10:1518-1525(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Inhibition of translational initiation by Let-7 MicroRNA in human cells."
    Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N., Basyuk E., Bertrand E., Filipowicz W.
    Science 309:1573-1576(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "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.
  9. "Capped small RNAs and MOV10 in human hepatitis delta virus replication."
    Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A.
    Nat. Struct. Mol. Biol. 15:714-721(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 EIF4B; IMP8; PRMT5; TNRC6A AND TNRC6B, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAGO4_HUMAN
AccessioniPrimary (citable) accession number: Q9HCK5
Secondary accession number(s): A7MD27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: June 8, 2016
This is version 121 of the entry and version 2 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

Keywords - Technical termi

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. 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.