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Q9UKV8

- AGO2_HUMAN

UniProt

Q9UKV8 - AGO2_HUMAN

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Protein

Protein argonaute-2

Gene

AGO2

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) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions.23 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.2 PublicationsUniRule annotation

Cofactori

Magnesium or manganese.1 Publication

Enzyme regulationi

Inhibited by EDTA.1 Publication

Kineticsi

  1. KM=1.1 nM for a synthetic 21-nucleotide single-stranded RNA2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi597 – 5971Divalent metal cationCurated
Metal bindingi669 – 6691Divalent metal cationCurated
Metal bindingi807 – 8071Divalent metal cationCurated

GO - Molecular functioni

  1. endoribonuclease activity Source: Reactome
  2. endoribonuclease activity, cleaving siRNA-paired mRNA Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. miRNA binding Source: UniProtKB-HAMAP
  5. mRNA binding Source: Ensembl
  6. poly(A) RNA binding Source: UniProtKB
  7. RNA 7-methylguanosine cap binding Source: UniProtKB
  8. siRNA binding Source: UniProtKB
  9. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. epidermal growth factor receptor signaling pathway Source: Reactome
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. fibroblast growth factor receptor signaling pathway Source: Reactome
  4. gene expression Source: Reactome
  5. gene silencing by RNA Source: UniProtKB
  6. innate immune response Source: Reactome
  7. mRNA cleavage involved in gene silencing by miRNA Source: UniProtKB
  8. negative regulation of translational initiation Source: UniProtKB
  9. negative regulation of translation involved in gene silencing by miRNA Source: UniProtKB
  10. neurotrophin TRK receptor signaling pathway Source: Reactome
  11. Notch signaling pathway Source: Reactome
  12. phosphatidylinositol-mediated signaling Source: Reactome
  13. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  14. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  15. post-embryonic development Source: Ensembl
  16. pre-miRNA processing Source: UniProtKB
  17. regulation of transcription, DNA-templated Source: UniProtKB-KW
  18. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  19. transcription, DNA-templated Source: UniProtKB-KW
  20. translation Source: UniProtKB
  21. translational initiation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Repressor, Ribonucleoprotein

Keywords - Biological processi

RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, 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_172761. Ca2+ pathway.
REACT_75829. PIP3 activates AKT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein argonaute-2UniRule annotation (EC:3.1.26.n2UniRule annotation)
Short name:
Argonaute2UniRule annotation
Short name:
hAgo2
Alternative name(s):
Argonaute RISC catalytic component 2
Eukaryotic translation initiation factor 2C 2UniRule annotation
Short name:
eIF-2C 2UniRule annotation
Short name:
eIF2C 2UniRule annotation
PAZ Piwi domain protein
Short name:
PPD
Protein slicerUniRule annotation
Gene namesi
Name:AGO2
Synonyms:EIF2C2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3263. AGO2.

Subcellular locationi

CytoplasmP-body. Nucleus
Note: Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic mRNA processing body Source: UniProtKB
  3. cytosol Source: Reactome
  4. membrane Source: UniProtKB
  5. micro-ribonucleoprotein complex Source: UniProtKB
  6. mRNA cap binding complex Source: UniProtKB
  7. nucleus Source: UniProtKB-KW
  8. polysome Source: UniProtKB
  9. ribonucleoprotein complex Source: UniProtKB
  10. RISC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi140 – 1401L → W: No effect. 1 Publication
Mutagenesisi470 – 4701F → V: No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation. Abolishes interaction with TNRC6C; when associated with V-505. 2 Publications
Mutagenesisi470 – 4701F → W: No effect on binding to the 7-methylguanosine cap of mRNA or inhibition of translation. 2 Publications
Mutagenesisi505 – 5051F → V: No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation and abolishes interaction with TNRC6C; when associated with V-470. 2 Publications
Mutagenesisi505 – 5051F → W: No effect on binding to the 7-methylguanosine cap of mRNA or inhibition of translation. 2 Publications
Mutagenesisi533 – 5331K → A: Impairs RNA cleavage. 1 Publication
Mutagenesisi545 – 5451Q → A: Impairs RNA cleavage. 1 Publication
Mutagenesisi570 – 5701K → A: Impairs RNA cleavage. 1 Publication
Mutagenesisi597 – 5971D → A: Abrogates RNA cleavage but does not affect binding to siRNA or translational repression. 3 Publications
Mutagenesisi633 – 6331Q → A: No effect. 1 Publication
Mutagenesisi633 – 6331Q → R: Abrogates RNA cleavage. Binds siRNA. 1 Publication
Mutagenesisi634 – 6341H → P or A: Abrogates RNA cleavage. Binds siRNA. 1 Publication
Mutagenesisi669 – 6691D → A: Abrogates RNA cleavage but does not affect binding to siRNA. 3 Publications
Mutagenesisi673 – 6731E → A: Impairs RNA cleavage. 2 Publications
Mutagenesisi673 – 6731E → G: No effect on RNA cleavage. 2 Publications
Mutagenesisi676 – 6761F → A, I, M, R or Y: Impairs RNA cleavage. 1 Publication
Mutagenesisi676 – 6761F → V: Abrogates RNA cleavage. 1 Publication
Mutagenesisi682 – 6821H → Y: No effect. 1 Publication
Mutagenesisi683 – 6831E → G: No effect on RNA cleavage. 1 Publication
Mutagenesisi700 – 7001P → A: Reduced protein stability. 1 Publication
Mutagenesisi704 – 7041F → Y: No effect. 1 Publication
Mutagenesisi744 – 7441T → Y: No effect. 1 Publication
Mutagenesisi807 – 8071H → A or R: Abrogates RNA cleavage. 2 Publications

Organism-specific databases

PharmGKBiPA27694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Protein argonaute-2PRO_0000194057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Nitrated tyrosineUniRule annotation
Modified residuei700 – 70014-hydroxyproline1 PublicationUniRule annotation

Post-translational modificationi

Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity.1 PublicationUniRule annotation

Keywords - PTMi

Hydroxylation, Nitration

Proteomic databases

MaxQBiQ9UKV8.
PaxDbiQ9UKV8.
PRIDEiQ9UKV8.

PTM databases

PhosphoSiteiQ9UKV8.

Expressioni

Gene expression databases

BgeeiQ9UKV8.
CleanExiHS_EIF2C2.
ExpressionAtlasiQ9UKV8. baseline and differential.
GenevestigatoriQ9UKV8.

Organism-specific databases

HPAiCAB019309.

Interactioni

Subunit structurei

Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Note however that the term RISC has also been used to describe the trimeric RLC/miRLC. The formation of RISC complexes containing siRNAs rather than miRNAs appears to occur independently of DICER1. Interacts with AGO1. Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, EIF6, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, MOV10, PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with the P-body components DCP1A and XRN1. Associates with polysomes and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the interaction is modulated under stress-induced conditions, occurs under both cell proliferation and differentiation conditions and in an RNA- and phosphorylation-independent manner. Interacts with LIMD1, WTIP and AJUBA. Interacts with TRIM71. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and APOBEC3H.25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CNOT7Q9UIV12EBI-528269,EBI-2105113
DHX58Q96C102EBI-528269,EBI-744193
DICER1Q9UPY313EBI-528269,EBI-395506
EIF4EBP1Q135412EBI-528269,EBI-74090
FKBP4Q027902EBI-528269,EBI-1047444
GNB2L1P632442EBI-528269,EBI-296739
IPO8O153974EBI-528269,EBI-358808
LRRK2Q5S0073EBI-528269,EBI-5323863
PTGES3Q151853EBI-528269,EBI-1049387
TARBP2Q156335EBI-528269,EBI-978581
TBK1Q9UHD22EBI-528269,EBI-356402
TBKBP1A7MCY62EBI-528269,EBI-359969
TNRC6AQ8NDV710EBI-528269,EBI-2269715
TNRC6BQ9UPQ912EBI-528269,EBI-947158
TNRC6CQ9HCJ03EBI-528269,EBI-6507625
ZMAT3Q9HA385EBI-528269,EBI-2548480

Protein-protein interaction databases

BioGridi118041. 85 interactions.
DIPiDIP-29194N.
IntActiQ9UKV8. 174 interactions.
MINTiMINT-1957975.

Structurei

Secondary structure

1
859
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 4814Combined sources
Beta strandi53 – 6311Combined sources
Helixi68 – 8114Combined sources
Helixi83 – 875Combined sources
Beta strandi96 – 1049Combined sources
Turni107 – 1104Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi128 – 13912Combined sources
Helixi140 – 1489Combined sources
Beta strandi151 – 1533Combined sources
Helixi156 – 17318Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi196 – 20813Combined sources
Beta strandi210 – 22516Combined sources
Helixi230 – 2389Combined sources
Helixi252 – 26211Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi278 – 28811Combined sources
Turni289 – 2913Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi303 – 3075Combined sources
Helixi308 – 3169Combined sources
Beta strandi325 – 3317Combined sources
Turni333 – 3364Combined sources
Beta strandi337 – 3404Combined sources
Helixi341 – 3433Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi348 – 3514Combined sources
Helixi358 – 36811Combined sources
Helixi372 – 38615Combined sources
Helixi388 – 3903Combined sources
Helixi392 – 3965Combined sources
Beta strandi406 – 4127Combined sources
Beta strandi422 – 4243Combined sources
Beta strandi450 – 4556Combined sources
Turni459 – 4613Combined sources
Helixi464 – 48118Combined sources
Beta strandi490 – 4945Combined sources
Helixi498 – 5003Combined sources
Helixi501 – 51111Combined sources
Beta strandi517 – 5226Combined sources
Helixi528 – 53710Combined sources
Turni538 – 5403Combined sources
Beta strandi544 – 5485Combined sources
Helixi549 – 5535Combined sources
Helixi557 – 57115Combined sources
Helixi585 – 5884Combined sources
Beta strandi591 – 5999Combined sources
Beta strandi610 – 6178Combined sources
Beta strandi619 – 6224Combined sources
Beta strandi625 – 6339Combined sources
Helixi642 – 65716Combined sources
Beta strandi662 – 6709Combined sources
Helixi673 – 6753Combined sources
Helixi676 – 69419Combined sources
Beta strandi701 – 7088Combined sources
Beta strandi715 – 7195Combined sources
Helixi720 – 7223Combined sources
Turni725 – 7284Combined sources
Beta strandi734 – 7363Combined sources
Beta strandi738 – 7414Combined sources
Beta strandi743 – 7453Combined sources
Beta strandi747 – 7515Combined sources
Beta strandi757 – 7593Combined sources
Beta strandi763 – 7708Combined sources
Helixi776 – 78611Combined sources
Beta strandi793 – 7953Combined sources
Helixi801 – 81717Combined sources
Helixi842 – 8454Combined sources
Helixi850 – 8534Combined sources
Turni854 – 8585Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LUCX-ray1.69A/B/C439-575[»]
3LUDX-ray2.10A/B/C439-575[»]
3LUGX-ray1.85A/B/C439-575[»]
3LUHX-ray2.00A/B/C439-575[»]
3LUJX-ray1.80A/B/C439-575[»]
3LUKX-ray1.70A/B/C439-575[»]
3QX8X-ray2.30A/B/C439-575[»]
3QX9X-ray2.00A/B/C439-575[»]
4F3TX-ray2.25A1-859[»]
4OLAX-ray2.30A1-859[»]
4OLBX-ray2.90A1-859[»]
DisProtiDP00736.
ProteinModelPortaliQ9UKV8.
SMRiQ9UKV8. Positions 23-859.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UKV8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini235 – 348114PAZUniRule annotationAdd
BLAST
Domaini517 – 818302PiwiUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 3166Interaction with guide RNA
Regioni524 – 56643Interaction with guide RNAAdd
BLAST
Regioni587 – 5904Interaction with GW182 family membersSequence Analysis
Regioni650 – 66011Interaction with GW182 family membersSequence AnalysisAdd
BLAST
Regioni709 – 7102Interaction with guide RNA
Regioni753 – 7619Interaction with guide RNA
Regioni790 – 81223Interaction with guide RNAAdd
BLAST

Domaini

The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH).

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

eggNOGiNOG279895.
GeneTreeiENSGT00760000119148.
HOGENOMiHOG000116043.
InParanoidiQ9UKV8.
KOiK11593.
OMAiVQGYAFK.
OrthoDBiEOG7HHWRC.
PhylomeDBiQ9UKV8.
TreeFamiTF101510.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_03031. AGO2.
InterProiIPR028602. AGO2.
IPR014811. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UKV8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP
60 70 80 90 100
KIDIYHYELD IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL
110 120 130 140 150
YTAMPLPIGR DKVELEVTLP GEGKDRIFKV SIKWVSCVSL QALHDALSGR
160 170 180 190 200
LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS FFTASEGCSN PLGGGREVWF
210 220 230 240 250
GFHQSVRPSL WKMMLNIDVS ATAFYKAQPV IEFVCEVLDF KSIEEQQKPL
260 270 280 290 300
TDSQRVKFTK EIKGLKVEIT HCGQMKRKYR VCNVTRRPAS HQTFPLQQES
310 320 330 340 350
GQTVECTVAQ YFKDRHKLVL RYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ
360 370 380 390 400
RCIKKLTDNQ TSTMIRATAR SAPDRQEEIS KLMRSASFNT DPYVREFGIM
410 420 430 440 450
VKDEMTDVTG RVLQPPSILY GGRNKAIATP VQGVWDMRNK QFHTGIEIKV
460 470 480 490 500
WAIACFAPQR QCTEVHLKSF TEQLRKISRD AGMPIQGQPC FCKYAQGADS
510 520 530 540 550
VEPMFRHLKN TYAGLQLVVV ILPGKTPVYA EVKRVGDTVL GMATQCVQMK
560 570 580 590 600
NVQRTTPQTL SNLCLKINVK LGGVNNILLP QGRPPVFQQP VIFLGADVTH
610 620 630 640 650
PPAGDGKKPS IAAVVGSMDA HPNRYCATVR VQQHRQEIIQ DLAAMVRELL
660 670 680 690 700
IQFYKSTRFK PTRIIFYRDG VSEGQFQQVL HHELLAIREA CIKLEKDYQP
710 720 730 740 750
GITFIVVQKR HHTRLFCTDK NERVGKSGNI PAGTTVDTKI THPTEFDFYL
760 770 780 790 800
CSHAGIQGTS RPSHYHVLWD DNRFSSDELQ ILTYQLCHTY VRCTRSVSIP
810 820 830 840 850
APAYYAHLVA FRARYHLVDK EHDSAEGSHT SGQSNGRDHQ ALAKAVQVHQ

DTLRTMYFA
Length:859
Mass (Da):97,208
Last modified:May 5, 2009 - v3
Checksum:i5C8552C43FC81345
GO
Isoform 2 (identifier: Q9UKV8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     724-757: Missing.

Note: No experimental confirmation available.

Show »
Length:825
Mass (Da):93,620
Checksum:i464C15B9413608D4
GO

Sequence cautioni

The sequence AAL76093.1 differs from that shown. Reason: cDNA contains a duplication of an internal sequence at the 5' end.
The sequence BC125214 differs from that shown. Reason: Frameshift at position 450.
The sequence AAH07633.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti564 – 5641C → W in AAF13034. (PubMed:10534406)Curated
Sequence conflicti589 – 5891Q → E in AAF13034. (PubMed:10534406)Curated
Sequence conflicti617 – 6171S → R in AAF13034. (PubMed:10534406)Curated
Sequence conflicti637 – 6371E → K in AAL76093. (PubMed:11914277)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei724 – 75734Missing in isoform 2. 1 PublicationVSP_037001Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC067931 Genomic DNA. No translation available.
AC107375 Genomic DNA. No translation available.
BC007633 mRNA. Translation: AAH07633.1. Different initiation.
BC018727 mRNA. Translation: AAH18727.2.
BC125214 mRNA. No translation available.
AY077717 mRNA. Translation: AAL76093.1. Sequence problems.
BT007229 mRNA. Translation: AAP35893.1.
AF121255 mRNA. Translation: AAF13034.2.
CCDSiCCDS55279.1. [Q9UKV8-2]
CCDS6380.1. [Q9UKV8-1]
RefSeqiNP_001158095.1. NM_001164623.1. [Q9UKV8-2]
NP_036286.2. NM_012154.3. [Q9UKV8-1]
UniGeneiHs.743313.

Genome annotation databases

EnsembliENST00000220592; ENSP00000220592; ENSG00000123908. [Q9UKV8-1]
ENST00000519980; ENSP00000430176; ENSG00000123908. [Q9UKV8-2]
GeneIDi27161.
KEGGihsa:27161.
UCSCiuc003yvn.3. human. [Q9UKV8-1]
uc010meo.3. human. [Q9UKV8-2]

Polymorphism databases

DMDMi229463006.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC067931 Genomic DNA. No translation available.
AC107375 Genomic DNA. No translation available.
BC007633 mRNA. Translation: AAH07633.1 . Different initiation.
BC018727 mRNA. Translation: AAH18727.2 .
BC125214 mRNA. No translation available.
AY077717 mRNA. Translation: AAL76093.1 . Sequence problems.
BT007229 mRNA. Translation: AAP35893.1 .
AF121255 mRNA. Translation: AAF13034.2 .
CCDSi CCDS55279.1. [Q9UKV8-2 ]
CCDS6380.1. [Q9UKV8-1 ]
RefSeqi NP_001158095.1. NM_001164623.1. [Q9UKV8-2 ]
NP_036286.2. NM_012154.3. [Q9UKV8-1 ]
UniGenei Hs.743313.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LUC X-ray 1.69 A/B/C 439-575 [» ]
3LUD X-ray 2.10 A/B/C 439-575 [» ]
3LUG X-ray 1.85 A/B/C 439-575 [» ]
3LUH X-ray 2.00 A/B/C 439-575 [» ]
3LUJ X-ray 1.80 A/B/C 439-575 [» ]
3LUK X-ray 1.70 A/B/C 439-575 [» ]
3QX8 X-ray 2.30 A/B/C 439-575 [» ]
3QX9 X-ray 2.00 A/B/C 439-575 [» ]
4F3T X-ray 2.25 A 1-859 [» ]
4OLA X-ray 2.30 A 1-859 [» ]
4OLB X-ray 2.90 A 1-859 [» ]
DisProti DP00736.
ProteinModelPortali Q9UKV8.
SMRi Q9UKV8. Positions 23-859.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118041. 85 interactions.
DIPi DIP-29194N.
IntActi Q9UKV8. 174 interactions.
MINTi MINT-1957975.

PTM databases

PhosphoSitei Q9UKV8.

Polymorphism databases

DMDMi 229463006.

Proteomic databases

MaxQBi Q9UKV8.
PaxDbi Q9UKV8.
PRIDEi Q9UKV8.

Protocols and materials databases

DNASUi 27161.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220592 ; ENSP00000220592 ; ENSG00000123908 . [Q9UKV8-1 ]
ENST00000519980 ; ENSP00000430176 ; ENSG00000123908 . [Q9UKV8-2 ]
GeneIDi 27161.
KEGGi hsa:27161.
UCSCi uc003yvn.3. human. [Q9UKV8-1 ]
uc010meo.3. human. [Q9UKV8-2 ]

Organism-specific databases

CTDi 27161.
GeneCardsi GC08M141542.
HGNCi HGNC:3263. AGO2.
HPAi CAB019309.
MIMi 606229. gene.
neXtProti NX_Q9UKV8.
PharmGKBi PA27694.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279895.
GeneTreei ENSGT00760000119148.
HOGENOMi HOG000116043.
InParanoidi Q9UKV8.
KOi K11593.
OMAi VQGYAFK.
OrthoDBi EOG7HHWRC.
PhylomeDBi Q9UKV8.
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_172761. Ca2+ pathway.
REACT_75829. PIP3 activates AKT signaling.

Miscellaneous databases

ChiTaRSi EIF2C2. human.
EvolutionaryTracei Q9UKV8.
GeneWikii EIF2C2.
GenomeRNAii 27161.
NextBioi 49946.
PROi Q9UKV8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKV8.
CleanExi HS_EIF2C2.
ExpressionAtlasi Q9UKV8. baseline and differential.
Genevestigatori Q9UKV8.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
HAMAPi MF_03031. AGO2.
InterProi IPR028602. AGO2.
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. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 239-859 (ISOFORM 1).
    Tissue: Brain and Eye.
  3. "miRNPs: a novel class of ribonucleoproteins containing numerous microRNAs."
    Mourelatos Z., Dostie J., Paushkin S., Sharma A., Charroux B., Abel L., Rappsilber J., Mann M., Dreyfuss G.
    Genes Dev. 16:720-728(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-859 (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-859 (ISOFORM 1).
  5. "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] OF 483-859 (ISOFORM 1).
  6. "Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer."
    Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W., Hobman T.C.
    EMBO Rep. 5:189-194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DICER1.
  7. "RISC is a 5' phosphomonoester-producing RNA endonuclease."
    Martinez J., Tuschl T.
    Genes Dev. 18:975-980(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "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: FUNCTION.
  9. "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, INTERACTION WITH GEMIN4.
  10. Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LEU-140; ASP-597; GLN-633; HIS-634; ASP-669; HIS-682; PHE-704 AND THR-744, COFACTOR.
  11. "Human RISC couples microRNA biogenesis and posttranscriptional gene silencing."
    Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.
    Cell 123:631-640(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DICER1 AND TARBP2.
  12. Cited for: FUNCTION, INTERACTION WITH DDX20; DICER1; GEMIN4; MOV10; PRMT5 AND TNRC6B, SUBCELLULAR LOCATION.
  13. "TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing."
    Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A., Filipowicz W.
    EMBO Rep. 6:961-967(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A human, ATP-independent, RISC assembly machine fueled by pre-miRNA."
    Maniataki E., Mourelatos Z.
    Genes Dev. 19:2979-2990(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DICER1 AND TARBP2, MUTAGENESIS OF ASP-669.
  15. "Structural basis for 5'-end-specific recognition of guide RNA by the A. fulgidus Piwi protein."
    Ma J.-B., Yuan Y.-R., Meister G., Pei Y., Tuschl T., Patel D.J.
    Nature 434:666-670(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-533; GLN-545 AND LYS-570.
  16. "TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing."
    Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N., Nishikura K., Shiekhattar R.
    Nature 436:740-744(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DICER1 AND TARBP2.
  17. "Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies."
    Sen G.L., Blau H.M.
    Nat. Cell Biol. 7:633-636(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-597; ASP-669; GLU-673; GLU-683 AND HIS-807.
  19. "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: FUNCTION, INTERACTION WITH DCP1A AND XRN1, SUBCELLULAR LOCATION.
  20. Cited for: FUNCTION.
  21. "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: FUNCTION, INTERACTION WITH DDX6 AND AGO1, SUBCELLULAR LOCATION.
  22. "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
    Wichroski M.J., Robb G.B., Rana T.M.
    PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APOBEC3G.
  23. "AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2."
    Vasudevan S., Steitz J.A.
    Cell 128:1105-1118(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FXR1, SUBCELLULAR LOCATION.
  24. "An mRNA m7G cap binding-like motif within human Ago2 represses translation."
    Kiriakidou M., Tan G.S., Lamprinaki S., De Planell-Saguer M., Nelson P.T., Mourelatos Z.
    Cell 129:1141-1151(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PHE-470 AND PHE-505.
  25. "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: FUNCTION, ASSOCIATION WITH POLYSOMES AND MNRP, INTERACTION WITH DDB1; DDX5; DHX30; DHX36; DDX47; ELAVL1; HNRNPF; IGF2BP1; ILF3; MATR3; PABPC1; RBM4; SART3; UPF1 AND YBX1.
  26. "RNA helicase A interacts with RISC in human cells and functions in RISC loading."
    Robb G.B., Rana T.M.
    Mol. Cell 26:523-537(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DHX9.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1; EIF6; MOV10 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
  28. "Switching from repression to activation: microRNAs can up-regulate translation."
    Vasudevan S., Tong Y., Steitz J.A.
    Science 318:1931-1934(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "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, MUTAGENESIS OF ASP-597.
  30. Cited for: FUNCTION, INTERACTION WITH DICER1; P4HA1; P4HB; TNRC6A AND TNRC6B, SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-700, MUTAGENESIS OF PRO-700.
  31. Cited for: FUNCTION, INTERACTION WITH DICER1 AND TARBP2.
  32. "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: FUNCTION, INTERACTION WITH IMP8, SUBCELLULAR LOCATION.
  33. "RNA-binding motif protein 4 translocates to cytoplasmic granules and suppresses translation via argonaute2 during muscle cell differentiation."
    Lin J.C., Tarn W.Y.
    J. Biol. Chem. 284:34658-34665(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM4.
  34. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."
    Braun J.E., Huntzinger E., Fauser M., Izaurralde E.
    Mol. Cell 44:120-133(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNRC6C, MUTAGENESIS OF PHE-470 AND PHE-505.
  37. "APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10."
    Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P., Zhang H.
    J. Biol. Chem. 287:29373-29383(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOV10.
  38. "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: SUBCELLULAR LOCATION, INTERACTION WITH APOBEC3A; APOBEC3C; APOBEC3F; APOBEC3G AND APOBEC3H.
  39. "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: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-673; PHE-676 AND HIS-807.
  40. "Structural basis for 5'-nucleotide base-specific recognition of guide RNA by human AGO2."
    Frank F., Sonenberg N., Nagar B.
    Nature 465:818-822(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 439-575 IN COMPLEX WITH AMP; CMP; GMP AND PHOSPHATE.
  41. "Structural analysis of 5'-mRNA-cap interactions with the human AGO2 MID domain."
    Frank F., Fabian M.R., Stepinski J., Jemielity J., Darzynkiewicz E., Sonenberg N., Nagar B.
    EMBO Rep. 12:415-420(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 439-575 IN COMPLEX WITH 7-MGTPG AND ATP.
  42. "The structure of human argonaute-2 in complex with miR-20a."
    Elkayam E., Kuhn C.D., Tocilj A., Haase A.D., Greene E.M., Hannon G.J., Joshua-Tor L.
    Cell 150:100-110(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH MIRNA-20A, GUIDE RNA-BINDING.
  43. "The crystal structure of human Argonaute2."
    Schirle N.T., MacRae I.J.
    Science 336:1037-1040(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RNA AND L-TRYPTOPHAN, GUIDE RNA-BINDING.

Entry informationi

Entry nameiAGO2_HUMAN
AccessioniPrimary (citable) accession number: Q9UKV8
Secondary accession number(s): Q8TCZ5, Q8WV58, Q96ID1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 133 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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