Q9UL18 (AGO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein argonaute-1
Short name=Argonaute1
Short name=hAgo1

Alternative name(s):
Eukaryotic translation initiation factor 2C 1
Short name=eIF-2C 1
Short name=eIF2C 1
Putative RNA-binding protein Q99

Gene names

Name:	EIF2C1
Synonyms:	AGO1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.5 Ref.6 Ref.9
Subunit structure	Interacts with DDB1, DDX5, DDX6, DHX30, DHX36, DDX47, DICER1, EIF2C2/AGO2, ELAVL1, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5, RBM4, SART3, TNRC6B, UPF1 and YBX1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Ref.5 Ref.7 Ref.8 Ref.10
Subcellular location	Cytoplasm › P-body Ref.5.
Sequence similarities	Belongs to the argonaute family. Ago subfamily. Contains 1 PAZ domain. Contains 1 Piwi domain.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing Transcription Transcription regulation Translation regulation
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Repressor Ribonucleoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of translation involved in gene silencing by miRNA Inferred from direct assay Ref.9. Source: UniProtKB nuclear-transcribed mRNA catabolic process Inferred from direct assay Ref.9. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome micro-ribonucleoprotein complex Inferred from direct assay Ref.8. Source: UniProtKB polysome Inferred from direct assay Ref.8. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DICER1	Q9UPY3	2	EBI-527363,EBI-395506
IPO8	O15397	2	EBI-527363,EBI-358808

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Protein argonaute-1

PRO_0000194055

Regions

Domain

226 – 346

121

PAZ

Domain

515 – 816

302

Piwi

Experimental info

Sequence conflict

242

1

D → N in AAH63275. Ref.3

Secondary structure

1

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857

Helix Strand Turn

Details...

Helix

228 – 236

9

Turn

241 – 243

3

Helix

250 – 260

11

Beta strand

264 – 267

4

Turn

269 – 272

4

Beta strand

276 – 286

11

Turn

287 – 289

3

Beta strand

291 – 293

3

Beta strand

303 – 305

3

Helix

306 – 312

7

Beta strand

323 – 329

7

Helix

331 – 333

3

Beta strand

335 – 338

4

Helix

339 – 341

3

Beta strand

342 – 344

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UL18 [UniParc]. Last modified February 21, 2006. Version 3. Checksum: 1DBB524AE7CBAF66	FASTA	857	97,214
	10 20 30 40 50 60 MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI DVYHYEVDIK 70 80 90 100 110 120 PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT VTALPIGNER VDFEVTIPGE 130 140 150 160 170 180 GKDRIFKVSI KWLAIVSWRM LHEALVSGQI PVPLESVQAL DVAMRHLASM RYTPVGRSFF 190 200 210 220 230 240 SPPEGYYHPL GGGREVWFGF HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN 250 260 270 280 290 300 IDEQPKPLTD SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ 310 320 330 340 350 360 TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC IKKLTDNQTS 370 380 390 400 410 420 TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK DDMTEVTGRV LPAPILQYGG 430 440 450 460 470 480 RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA IACFAPQKQC REEVLKNFTD QLRKISKDAG 490 500 510 520 530 540 MPIQGQPCFC KYAQGADSVE PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM 550 560 570 580 590 600 ATQCVQVKNV VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP 610 620 630 640 650 660 AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ FYKSTRFKPT 670 680 690 700 710 720 RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI TYIVVQKRHH TRLFCADKNE 730 740 750 760 770 780 RIGKSGNIPA GTTVDTNITH PFEFDFYLCS HAGIQGTSRP SHYYVLWDDN RFTADELQIL 790 800 810 820 830 840 TYQLCHTYVR CTRSVSIPAP AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL 850 AKAVQVHQDT LRTMYFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1999) [PubMed: 10534406] [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(2006) [PubMed: 16710414] [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: 15489334] [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(2004) [PubMed: 15260970] [Abstract] Cited for: ASSOCIATION WITH MIRNA.
[5]	"Identification of novel argonaute-associated proteins." Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R., Tuschl T. Curr. Biol. 15:2149-2155(2005) [PubMed: 16289642] [Abstract] Cited for: FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, SUBCELLULAR LOCATION.
[6]	"Involvement of AGO1 and AGO2 in mammalian transcriptional silencing." Janowski B.A., Huffman K.E., Schwartz J.C., Ram R., Nordsell R., Shames D.S., Minna J.D., Corey D.R. Nat. Struct. Mol. Biol. 13:787-792(2006) [PubMed: 16936728] [Abstract] 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(2006) [PubMed: 16756390] [Abstract] Cited for: INTERACTION WITH DDX6 AND EIF2C2.
[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(2007) [PubMed: 17932509] [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(2008) [PubMed: 18771919] [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: 19167051] [Abstract] Cited for: INTERACTION WITH IMP8.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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(2004) [PubMed: 15152257] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 225-369, RNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF093097 mRNA. Translation: AAF00068.1.
AL139286 Genomic DNA. Translation: CAI22804.1.
BC063275 mRNA. Translation: AAH63275.1.

IPI

IPI00007736.

RefSeq

NP_036331.1. NM_012199.2.

UniGene

Hs.22867.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SI2	X-ray	2.60	A	225-369	[»]
1SI3	X-ray	2.60	A	225-369	[»]

ProteinModelPortal

Q9UL18.

SMR

Q9UL18. Positions 220-387, 438-856.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29193N.

IntAct

Q9UL18. 10 interactions.

STRING

Q9UL18.

PTM databases

PhosphoSite

Q9UL18.

Polymorphism databases

DMDM

88984241.

Proteomic databases

PRIDE

Q9UL18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373204; ENSP00000362300; ENSG00000092847.

GeneID

26523.

KEGG

hsa:26523.

UCSC

uc001bzl.1. human.

Organism-specific databases

CTD

26523.

GeneCards

GC01P036335.

H-InvDB

HIX0199806.

HGNC

HGNC:3262. EIF2C1.

MIM

606228. gene.

neXtProt

NX_Q9UL18.

PharmGKB

PA27693.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07031.

GeneTree

ENSGT00550000074185.

HOGENOM

HBG717005.

InParanoid

Q9UL18.

OMA

DAGMPIM.

OrthoDB

EOG4229J0.

PhylomeDB

Q9UL18.

Enzyme and pathway databases

Reactome

REACT_12472. Regulatory RNA pathways.

Gene expression databases

ArrayExpress

Q9UL18.

Bgee

Q9UL18.

CleanEx

HS_EIF2C1.

Genevestigator

Q9UL18.

GermOnline

ENSG00000092847. Homo sapiens.

Family and domain databases

InterPro

IPR014811. DUF1785.
IPR003100. PAZ.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]

KO

K11593.

Pfam

PF08699. DUF1785. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]

SMART

SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]

SUPFAM

SSF101690. PAZ. 1 hit.
SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

48846.

SOURCE

Search...

Entry information

Entry name

AGO1_HUMAN

Accession

Primary (citable) accession number: Q9UL18
Secondary accession number(s): Q5TA57, Q6P4S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 21, 2006
Last modified:	January 25, 2012
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.