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Q9H9G7 (AGO3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein argonaute-3

Short name=Argonaute3
Short name=hAgo3
Alternative name(s):
Argonaute RISC catalytic component 3
Eukaryotic translation initiation factor 2C 3
Short name=eIF-2C 3
Short name=eIF2C 3
Gene names
Name:AGO3
Synonyms:EIF2C3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length860 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Proposed to be involved in stabilization of small RNA derivates (riRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent riRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. Ref.6 Ref.9

Subunit structure

Interacts with EIF4B, IMP8, PRMT5 and TNRC6B. Interacts with APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4. Ref.7 Ref.8 Ref.9

Subcellular location

CytoplasmP-body Ref.5.

Sequence similarities

Belongs to the argonaute family. Ago subfamily.

Contains 1 PAZ domain.

Contains 1 Piwi domain.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
Translation regulation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mRNA catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of translation involved in gene silencing by miRNA

Inferred from direct assay Ref.6. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

regulation of stem cell proliferation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentRISC complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cytoplasmic mRNA processing body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

micro-ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionmiRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H9G7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H9G7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-234: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 860860Protein argonaute-3 HAMAP-Rule MF_03032
PRO_0000194061

Regions

Domain236 – 349114PAZ
Domain518 – 819302Piwi

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10

Natural variations

Alternative sequence1 – 234234Missing in isoform 2.
VSP_041084

Experimental info

Sequence conflict251T → A in BAB14262. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 6FF1277995E5322E

FASTA86097,360
        10         20         30         40         50         60 
MEIGSAGPAG AQPLLMVPRR PGYGTMGKPI KLLANCFQVE IPKIDVYLYE VDIKPDKCPR 

        70         80         90        100        110        120 
RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDVT LPGEGGKDRP 

       130        140        150        160        170        180 
FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE LDKPISTNPV HAVDVVLRHL PSMKYTPVGR 

       190        200        210        220        230        240 
SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD 

       250        260        270        280        290        300 
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE 

       310        320        330        340        350        360 
NGQTVERTVA QYFREKYTLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN 

       370        380        390        400        410        420 
QTSTMIKATA RSAPDRQEEI SRLVRSANYE TDPFVQEFQF KVRDEMAHVT GRVLPAPMLQ 

       430        440        450        460        470        480 
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEILKG FTDQLRKISK 

       490        500        510        520        530        540 
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRVGDTL 

       550        560        570        580        590        600 
LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT 

       610        620        630        640        650        660 
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF 

       670        680        690        700        710        720 
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD 

       730        740        750        760        770        780 
RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL 

       790        800        810        820        830        840 
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP 

       850        860 
QALAKAVQIH QDTLRTMYFA 

« Hide

Isoform 2 [UniParc].

Checksum: 5475FD0337AAD9CE
Show »

FASTA62671,211

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Leukocyte.
[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]"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.
[6]"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.
[7]"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 AND TNRC6B.
[8]"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.
[9]"DICER- and AGO3-dependent generation of retinoic acid-induced DR2 Alu RNAs regulates human stem cell proliferation."
Hu Q., Tanasa B., Trabucchi M., Li W., Zhang J., Ohgi K.A., Rose D.W., Glass C.K., Rosenfeld M.G.
Nat. Struct. Mol. Biol. 19:1168-1175(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EDC4.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022827 mRNA. Translation: BAB14262.1.
AL139286, AL138787 Genomic DNA. Translation: CAI22802.1.
AL138787, AL139286 Genomic DNA. Translation: CAI22268.1.
AL138787 Genomic DNA. Translation: CAI22269.1.
BC025769 mRNA. No translation available.
RefSeqNP_079128.2. NM_024852.3.
NP_803171.1. NM_177422.2.
XP_005270632.1. XM_005270575.1.
UniGeneHs.657659.

3D structure databases

ProteinModelPortalQ9H9G7.
SMRQ9H9G7. Positions 12-860.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128177. 51 interactions.
DIPDIP-54486N.
IntActQ9H9G7. 49 interactions.
STRING9606.ENSP00000362287.

PTM databases

PhosphoSiteQ9H9G7.

Polymorphism databases

DMDM76803660.

Proteomic databases

PaxDbQ9H9G7.
PRIDEQ9H9G7.

Protocols and materials databases

DNASU192669.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246314; ENSP00000246314; ENSG00000126070. [Q9H9G7-2]
ENST00000373191; ENSP00000362287; ENSG00000126070. [Q9H9G7-1]
GeneID192669.
KEGGhsa:192669.
UCSCuc001bzp.3. human. [Q9H9G7-1]

Organism-specific databases

CTD192669.
GeneCardsGC01P036399.
HGNCHGNC:18421. AGO3.
HPAHPA048342.
MIM607355. gene.
neXtProtNX_Q9H9G7.
PharmGKBPA38329.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279895.
HOGENOMHOG000116043.
InParanoidQ9H9G7.
KOK11593.
OMAGRSMPEP.
OrthoDBEOG7HHWRC.
PhylomeDBQ9H9G7.
TreeFamTF101510.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9H9G7.
BgeeQ9H9G7.
CleanExHS_EIF2C3.
GenevestigatorQ9H9G7.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
HAMAPMF_03032. AGO3.
InterProIPR028603. AGO3.
IPR014811. DUF1785.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF08699. DUF1785. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTSM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF2C3. human.
GenomeRNAi192669.
NextBio89367.
PROQ9H9G7.
SOURCESearch...

Entry information

Entry nameAGO3_HUMAN
AccessionPrimary (citable) accession number: Q9H9G7
Secondary accession number(s): B1ALI0, Q5TA55, Q9H1U6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM