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Protein argonaute-4 (Argonaute4) (hAgo4) (Argonaute RISC catalytic component 4) (Eukaryotic translation initiation factor 2C 4) (eIF-2C 4) (eIF2C 4)

 AGO4_HUMAN              Reviewed;         861 AA.
Q9HCK5; A7MD27;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
14-NOV-2003, sequence version 2.
22-NOV-2017, entry version 132.
RecName: Full=Protein argonaute-4 {ECO:0000255|HAMAP-Rule:MF_03033};
Short=Argonaute4 {ECO:0000255|HAMAP-Rule:MF_03033};
Short=hAgo4;
AltName: Full=Argonaute RISC catalytic component 4;
AltName: Full=Eukaryotic translation initiation factor 2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
Short=eIF-2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
Short=eIF2C 4 {ECO:0000255|HAMAP-Rule:MF_03033};
Name=AGO4; Synonyms=EIF2C4, KIAA1567;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"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.";
DNA Res. 7:273-281(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ASSOCIATION WITH MIRNA.
PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G.,
Tuschl T.;
"Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
siRNAs.";
Mol. Cell 15:185-197(2004).
[6]
FUNCTION.
PubMed=15337849; DOI=10.1261/rna.7131604;
Pillai R.S., Artus C.G., Filipowicz W.;
"Tethering of human Ago proteins to mRNA mimics the miRNA-mediated
repression of protein synthesis.";
RNA 10:1518-1525(2004).
[7]
INTERACTION WITH ZFP36.
PubMed=15766526; DOI=10.1016/j.cell.2004.12.038;
Jing Q., Huang S., Guth S., Zarubin T., Motoyama A., Chen J.,
Di Padova F., Lin S.C., Gram H., Han J.;
"Involvement of microRNA in AU-rich element-mediated mRNA
instability.";
Cell 120:623-634(2005).
[8]
SUBCELLULAR LOCATION.
PubMed=16081698; DOI=10.1126/science.1115079;
Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
Basyuk E., Bertrand E., Filipowicz W.;
"Inhibition of translational initiation by Let-7 MicroRNA in human
cells.";
Science 309:1573-1576(2005).
[9]
FUNCTION.
PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
Wu L., Fan J., Belasco J.G.;
"Importance of translation and nonnucleolytic ago proteins for on-
target RNA interference.";
Curr. Biol. 18:1327-1332(2008).
[10]
FUNCTION.
PubMed=18552826; DOI=10.1038/nsmb.1440;
Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A.;
"Capped small RNAs and MOV10 in human hepatitis delta virus
replication.";
Nat. Struct. Mol. Biol. 15:714-721(2008).
[11]
INTERACTION WITH EIF4B; IMP8; PRMT5; TNRC6A AND TNRC6B, AND
SUBCELLULAR LOCATION.
PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
Kremmer E., Benes V., Urlaub H., Meister G.;
"Importin 8 is a gene silencing factor that targets argonaute proteins
to distinct mRNAs.";
Cell 136:496-507(2009).
-!- 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.
Also required for RNA-directed transcription and replication of
the human hapatitis delta virus (HDV). {ECO:0000255|HAMAP-
Rule:MF_03033, ECO:0000269|PubMed:15337849,
ECO:0000269|PubMed:18552826, ECO:0000269|PubMed:18771919}.
-!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5, TNRC6A and TNRC6B
(PubMed:19167051). Interacts with ZFP36 (PubMed:15766526).
{ECO:0000255|HAMAP-Rule:MF_03033, ECO:0000269|PubMed:15766526,
ECO:0000269|PubMed:19167051}.
-!- INTERACTION:
O15397:IPO8; NbExp=3; IntAct=EBI-2269696, EBI-358808;
Q8NDV7:TNRC6A; NbExp=4; IntAct=EBI-2269696, EBI-2269715;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03033, ECO:0000269|PubMed:16081698,
ECO:0000269|PubMed:19167051}.
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03033}.
-!- SEQUENCE CAUTION:
Sequence=BAB13393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB046787; BAB13393.1; ALT_INIT; mRNA.
EMBL; AL359186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL354864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07400.1; -; Genomic_DNA.
EMBL; BC152450; AAI52451.1; -; mRNA.
CCDS; CCDS397.1; -.
RefSeq; NP_060099.2; NM_017629.3.
UniGene; Hs.744858; -.
ProteinModelPortal; Q9HCK5; -.
SMR; Q9HCK5; -.
BioGrid; 128178; 69.
CORUM; Q9HCK5; -.
IntAct; Q9HCK5; 75.
STRING; 9606.ENSP00000362306; -.
iPTMnet; Q9HCK5; -.
PhosphoSitePlus; Q9HCK5; -.
BioMuta; AGO4; -.
DMDM; 38372393; -.
EPD; Q9HCK5; -.
MaxQB; Q9HCK5; -.
PaxDb; Q9HCK5; -.
PeptideAtlas; Q9HCK5; -.
PRIDE; Q9HCK5; -.
DNASU; 192670; -.
Ensembl; ENST00000373210; ENSP00000362306; ENSG00000134698.
GeneID; 192670; -.
KEGG; hsa:192670; -.
UCSC; uc001bzj.3; human.
CTD; 192670; -.
DisGeNET; 192670; -.
EuPathDB; HostDB:ENSG00000134698.10; -.
GeneCards; AGO4; -.
HGNC; HGNC:18424; AGO4.
HPA; CAB012179; -.
HPA; HPA068896; -.
MIM; 607356; gene.
neXtProt; NX_Q9HCK5; -.
OpenTargets; ENSG00000134698; -.
PharmGKB; PA38330; -.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
InParanoid; Q9HCK5; -.
KO; K11593; -.
OMA; IQWVSVV; -.
OrthoDB; EOG091G020J; -.
PhylomeDB; Q9HCK5; -.
TreeFam; TF101510; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
GenomeRNAi; 192670; -.
PRO; PR:Q9HCK5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134698; -.
CleanEx; HS_EIF2C4; -.
Genevisible; Q9HCK5; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IEA:Ensembl.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
GO; GO:0007130; P:synaptonemal complex assembly; IEA:Ensembl.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03033; AGO4; 1.
InterPro; IPR028604; AGO4.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Reference proteome; Ribonucleoprotein;
RNA-binding; RNA-mediated gene silencing; Translation regulation.
CHAIN 1 861 Protein argonaute-4.
/FTId=PRO_0000194063.
DOMAIN 225 338 PAZ. {ECO:0000255|HAMAP-Rule:MF_03033}.
DOMAIN 509 820 Piwi. {ECO:0000255|HAMAP-Rule:MF_03033}.
SEQUENCE 861 AA; 97097 MW; F236FF05047534C1 CRC64;
MEALGPGPPA SLFQPPRRPG LGTVGKPIRL LANHFQVQIP KIDVYHYDVD IKPEKRPRRV
NREVVDTMVR HFKMQIFGDR QPGYDGKRNM YTAHPLPIGR DRVDMEVTLP GEGKDQTFKV
SVQWVSVVSL QLLLEALAGH LNEVPDDSVQ ALDVITRHLP SMRYTPVGRS FFSPPEGYYH
PLGGGREVWF GFHQSVRPAM WNMMLNIDVS ATAFYRAQPI IEFMCEVLDI QNINEQTKPL
TDSQRVKFTK EIRGLKVEVT HCGQMKRKYR VCNVTRRPAS HQTFPLQLEN GQAMECTVAQ
YFKQKYSLQL KYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ TSTMIKATAR
SAPDRQEEIS RLVKSNSMVG GPDPYLKEFG IVVHNEMTEL TGRVLPAPML QYGGRNKTVA
TPNQGVWDMR GKQFYAGIEI KVWAVACFAP QKQCREDLLK SFTDQLRKIS KDAGMPIQGQ
PCFCKYAQGA DSVEPMFKHL KMTYVGLQLI VVILPGKTPV YAEVKRVGDT LLGMATQCVQ
VKNVVKTSPQ TLSNLCLKIN AKLGGINNVL VPHQRPSVFQ QPVIFLGADV THPPAGDGKK
PSIAAVVGSM DGHPSRYCAT VRVQTSRQEI SQELLYSQEV IQDLTNMVRE LLIQFYKSTR
FKPTRIIYYR GGVSEGQMKQ VAWPELIAIR KACISLEEDY RPGITYIVVQ KRHHTRLFCA
DKTERVGKSG NVPAGTTVDS TITHPSEFDF YLCSHAGIQG TSRPSHYQVL WDDNCFTADE
LQLLTYQLCH TYVRCTRSVS IPAPAYYARL VAFRARYHLV DKDHDSAEGS HVSGQSNGRD
PQALAKAVQI HHDTQHTMYF A


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