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Q9UL18

- AGO1_HUMAN

UniProt

Q9UL18 - AGO1_HUMAN

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Protein
Protein argonaute-1
Gene
AGO1, EIF2C1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. RNA binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. Notch signaling pathway Source: Reactome
  3. epidermal growth factor receptor signaling pathway Source: Reactome
  4. fibroblast growth factor receptor signaling pathway Source: Reactome
  5. gene expression Source: Reactome
  6. innate immune response Source: Reactome
  7. negative regulation of translation involved in gene silencing by miRNA Source: UniProtKB
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  10. phosphatidylinositol-mediated signaling Source: Reactome
  11. regulation of transcription, DNA-templated Source: UniProtKB-KW
  12. transcription, DNA-templated Source: UniProtKB-KW
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

ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118699. Post-transcriptional silencing by small RNAs.
REACT_12417. MicroRNA (miRNA) biogenesis.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172761. Ca2+ pathway.
REACT_75829. PIP3 activates AKT 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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3262. AGO1.

Subcellular locationi

CytoplasmP-body 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. micro-ribonucleoprotein complex Source: UniProtKB
  5. polysome Source: UniProtKB
  6. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi670 – 6701P → S: Confers modest RNA cleavage activity; when associated with Q-675 and H-805. 1 Publication
Mutagenesisi674 – 6741L → F: Confers modest RNA cleavage activity; when associated with H-805. 1 Publication
Mutagenesisi675 – 6751P → 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 Publication
Mutagenesisi805 – 8051R → H: Does not confer enzyme activity by itself. Confers modest RNA cleavage activity; when associated with F-674. 2 Publications

Organism-specific databases

PharmGKBiPA27693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Protein argonaute-1
PRO_0000194055Add
BLAST

Proteomic databases

MaxQBiQ9UL18.
PaxDbiQ9UL18.
PRIDEiQ9UL18.

PTM databases

PhosphoSiteiQ9UL18.

Expressioni

Gene expression databases

ArrayExpressiQ9UL18.
BgeeiQ9UL18.
CleanExiHS_EIF2C1.
GenevestigatoriQ9UL18.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DICER1Q9UPY35EBI-527363,EBI-395506
IPO8O153972EBI-527363,EBI-358808
TNRC6AQ8NDV74EBI-527363,EBI-2269715

Protein-protein interaction databases

BioGridi117726. 38 interactions.
DIPiDIP-29193N.
IntActiQ9UL18. 179 interactions.
STRINGi9606.ENSP00000362300.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 4614
Beta strandi51 – 6212
Helixi66 – 7914
Helixi81 – 855
Beta strandi94 – 1029
Turni105 – 1084
Beta strandi110 – 1156
Beta strandi125 – 13713
Helixi138 – 14710
Helixi154 – 17118
Beta strandi172 – 1754
Beta strandi178 – 1803
Beta strandi189 – 1913
Beta strandi194 – 20613
Beta strandi208 – 22316
Helixi228 – 2369
Turni241 – 2433
Helixi250 – 26011
Beta strandi264 – 2685
Turni269 – 2724
Beta strandi276 – 28611
Turni287 – 2893
Beta strandi291 – 2955
Beta strandi301 – 3055
Helixi306 – 3149
Beta strandi323 – 3286
Helixi331 – 3333
Beta strandi335 – 3384
Helixi339 – 3413
Beta strandi342 – 3443
Helixi356 – 36611
Helixi370 – 38415
Helixi386 – 3883
Helixi390 – 3945
Beta strandi404 – 4107
Turni420 – 4234
Beta strandi448 – 4536
Turni457 – 4593
Helixi462 – 47817
Beta strandi488 – 4925
Helixi496 – 4983
Helixi499 – 50911
Beta strandi515 – 5206
Helixi526 – 53510
Turni536 – 5383
Beta strandi542 – 5465
Helixi547 – 5515
Helixi555 – 56814
Helixi578 – 5803
Helixi583 – 5864
Beta strandi589 – 5979
Beta strandi608 – 6158
Beta strandi617 – 6204
Beta strandi623 – 6319
Helixi640 – 65516
Beta strandi660 – 6667
Helixi671 – 6733
Helixi674 – 69219
Beta strandi699 – 7068
Beta strandi713 – 7175
Helixi718 – 7203
Turni723 – 7264
Beta strandi732 – 7343
Beta strandi736 – 7394
Beta strandi741 – 7433
Beta strandi745 – 7495
Beta strandi755 – 7573
Beta strandi761 – 7688
Helixi774 – 78411
Helixi799 – 81416
Helixi837 – 8437
Helixi848 – 8514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 17-857.

Miscellaneous databases

EvolutionaryTraceiQ9UL18.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini226 – 346121PAZ
Add
BLAST
Domaini515 – 816302Piwi
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni309 – 3146Interaction with guide RNA
Regioni522 – 56443Interaction with guide RNA
Add
BLAST
Regioni670 – 6756Impairs access of bound RNA to the active site
Regioni708 – 7125Interaction with guide RNA
Regioni751 – 7599Interaction with guide RNA
Regioni788 – 81326Interaction with guide RNA
Add
BLAST

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 1 Piwi domain.

Phylogenomic databases

eggNOGiNOG279895.
HOGENOMiHOG000116043.
InParanoidiQ9UL18.
KOiK11593.
OMAiEVTHRAN.
PhylomeDBiQ9UL18.
TreeFamiTF101510.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR014811. DUF1785.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF08699. DUF1785. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTiSM00949. 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

MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI    50
DVYHYEVDIK PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT 100
VTALPIGNER VDFEVTIPGE GKDRIFKVSI KWLAIVSWRM LHEALVSGQI 150
PVPLESVQAL DVAMRHLASM RYTPVGRSFF SPPEGYYHPL GGGREVWFGF 200
HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN IDEQPKPLTD 250
SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ 300
TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC 350
IKKLTDNQTS TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK 400
DDMTEVTGRV LPAPILQYGG RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA 450
IACFAPQKQC REEVLKNFTD QLRKISKDAG MPIQGQPCFC KYAQGADSVE 500
PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM ATQCVQVKNV 550
VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP 600
AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ 650
FYKSTRFKPT RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI 700
TYIVVQKRHH TRLFCADKNE RIGKSGNIPA GTTVDTNITH PFEFDFYLCS 750
HAGIQGTSRP SHYYVLWDDN RFTADELQIL TYQLCHTYVR CTRSVSIPAP 800
AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL AKAVQVHQDT 850
LRTMYFA 857
Length:857
Mass (Da):97,214
Last modified:February 21, 2006 - v3
Checksum:i1DBB524AE7CBAF66
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421D → N in AAH63275. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF093097 mRNA. Translation: AAF00068.1.
AL139286 Genomic DNA. Translation: CAI22804.1.
BC063275 mRNA. Translation: AAH63275.1.
CCDSiCCDS398.1.
RefSeqiNP_036331.1. NM_012199.2.
UniGeneiHs.22867.
Hs.656677.

Genome annotation databases

EnsembliENST00000373204; ENSP00000362300; ENSG00000092847.
GeneIDi26523.
KEGGihsa:26523.
UCSCiuc001bzk.3. human.

Polymorphism databases

DMDMi88984241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF093097 mRNA. Translation: AAF00068.1 .
AL139286 Genomic DNA. Translation: CAI22804.1 .
BC063275 mRNA. Translation: AAH63275.1 .
CCDSi CCDS398.1.
RefSeqi NP_036331.1. NM_012199.2.
UniGenei Hs.22867.
Hs.656677.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SI2 X-ray 2.60 A 225-369 [» ]
1SI3 X-ray 2.60 A 225-369 [» ]
4KRE X-ray 1.75 A 1-857 [» ]
4KRF X-ray 2.10 A 1-857 [» ]
4KXT X-ray 2.29 A 1-857 [» ]
ProteinModelPortali Q9UL18.
SMRi Q9UL18. Positions 17-857.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117726. 38 interactions.
DIPi DIP-29193N.
IntActi Q9UL18. 179 interactions.
STRINGi 9606.ENSP00000362300.

PTM databases

PhosphoSitei Q9UL18.

Polymorphism databases

DMDMi 88984241.

Proteomic databases

MaxQBi Q9UL18.
PaxDbi Q9UL18.
PRIDEi Q9UL18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373204 ; ENSP00000362300 ; ENSG00000092847 .
GeneIDi 26523.
KEGGi hsa:26523.
UCSCi uc001bzk.3. human.

Organism-specific databases

CTDi 26523.
GeneCardsi GC01P036336.
HGNCi HGNC:3262. AGO1.
MIMi 606228. gene.
neXtProti NX_Q9UL18.
PharmGKBi PA27693.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279895.
HOGENOMi HOG000116043.
InParanoidi Q9UL18.
KOi K11593.
OMAi EVTHRAN.
PhylomeDBi Q9UL18.
TreeFami TF101510.

Enzyme and pathway databases

Reactomei REACT_118560. Small interfering RNA (siRNA) biogenesis.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118699. Post-transcriptional silencing by small RNAs.
REACT_12417. MicroRNA (miRNA) biogenesis.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172761. Ca2+ pathway.
REACT_75829. PIP3 activates AKT signaling.

Miscellaneous databases

ChiTaRSi EIF2C1. human.
EvolutionaryTracei Q9UL18.
GeneWikii EIF2C1.
GenomeRNAii 26523.
NextBioi 48846.
PROi Q9UL18.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UL18.
Bgeei Q9UL18.
CleanExi HS_EIF2C1.
Genevestigatori Q9UL18.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR014811. DUF1785.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF08699. DUF1785. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view ]
SMARTi SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view ]
SUPFAMi SSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEi PS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [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].
    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] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH MIRNA.
  5. Cited for: FUNCTION, INTERACTION WITH DICER1; MOV10; PRMT5 AND TNRC6B, SUBCELLULAR LOCATION.
  6. 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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX6 AND AGO2.
  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] [Europe PMC] [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] [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 IMP8.
  11. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 225-369, RNA-BINDING.
  15. "Eukaryote-specific insertion elements control human ARGONAUTE slicer activity."
    Nakanishi K., Ascano M., Gogakos T., Ishibe-Murakami S., Serganov A.A., Briskin D., Morozov P., Tuschl T., Patel D.J.
    Cell Rep. 3:1893-1900(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH RNA, RNA-BINDING, MUTAGENESIS OF PRO-670; PRO-675 AND ARG-805, LACK OF CATALYTIC ACTIVITY.
  16. "The making of a slicer: activation of human Argonaute-1."
    Faehnle C.R., Elkayam E., Haase A.D., Hannon G.J., Joshua-Tor L.
    Cell Rep. 3:1901-1909(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH RNA, LACK OF CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-674 AND ARG-805.

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: September 3, 2014
This is version 121 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

External Data

Dasty 3

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