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Protein

Protein argonaute-2

Gene

AGO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

Cofactori

Mg2+1 Publication, Mn2+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

    • core promoter binding Source: BHF-UCL
    • double-stranded RNA binding Source: BHF-UCL
    • endoribonuclease activity Source: BHF-UCL
    • endoribonuclease activity, cleaving miRNA-paired mRNA Source: BHF-UCL
    • endoribonuclease activity, cleaving siRNA-paired mRNA Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    • miRNA binding Source: BHF-UCL
    • mRNA binding Source: Ensembl
    • poly(A) RNA binding Source: UniProtKB
    • pre-miRNA binding Source: BHF-UCL
    • RNA 7-methylguanosine cap binding Source: UniProtKB
    • RNA polymerase II core binding Source: BHF-UCL
    • single-stranded RNA binding Source: BHF-UCL
    • siRNA binding Source: UniProtKB
    • translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    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_263982. Ca2+ pathway.
    REACT_268530. Transcriptional regulation by small RNAs.
    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 Componenti: 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

    • cytoplasm Source: BHF-UCL
    • cytoplasmic mRNA processing body Source: UniProtKB
    • cytosol Source: Reactome
    • membrane Source: UniProtKB
    • micro-ribonucleoprotein complex Source: UniProtKB
    • mRNA cap binding complex Source: UniProtKB
    • nucleoplasm Source: Reactome
    • nucleus Source: BHF-UCL
    • polysome Source: UniProtKB
    • ribonucleoprotein complex Source: UniProtKB
    • RISC complex Source: UniProtKB
    • RISC-loading complex Source: BHF-UCL
    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.

    Polymorphism and mutation databases

    BioMutaiAGO2.
    DMDMi229463006.

    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-hydroxyprolineUniRule annotation1 Publication

    Post-translational modificationi

    Hydroxylated. 4-hydroxylation appears to enhance protein stability but is not required for miRNA-binding or endonuclease activity.UniRule annotation1 Publication

    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
    DICER1Q9UPY314EBI-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
    Turni84 – 874Combined sources
    Beta strandi96 – 1049Combined sources
    Turni107 – 1104Combined sources
    Beta strandi113 – 1175Combined sources
    Beta strandi122 – 1243Combined sources
    Beta strandi128 – 13912Combined sources
    Helixi140 – 1478Combined sources
    Beta strandi148 – 1536Combined sources
    Helixi156 – 17318Combined sources
    Beta strandi174 – 1774Combined sources
    Beta strandi180 – 1834Combined sources
    Beta strandi191 – 1933Combined sources
    Beta strandi196 – 20712Combined sources
    Beta strandi210 – 22516Combined sources
    Helixi230 – 2389Combined sources
    Helixi243 – 2453Combined sources
    Helixi252 – 26211Combined sources
    Beta strandi266 – 2683Combined 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 strandi338 – 3403Combined 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
    Turni422 – 4254Combined 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
    Helixi580 – 5823Combined 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 – 71212Combined 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 – 81616Combined sources
    Turni817 – 8204Combined sources
    Helixi837 – 84610Combined sources
    Turni850 – 8545Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4W5NX-ray2.90A1-859[»]
    4W5OX-ray1.80A1-859[»]
    4W5QX-ray3.10A1-859[»]
    4W5RX-ray2.50A1-859[»]
    4W5TX-ray2.50A1-859[»]
    DisProtiDP00736.
    ProteinModelPortaliQ9UKV8.
    SMRiQ9UKV8. Positions 22-859.
    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.
    OMAiIPGYAFK.
    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. AlignAdd to basket

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

    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:
    EMBLi
    GenBanki
    DDBJi
    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]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4W5NX-ray2.90A1-859[»]
    4W5OX-ray1.80A1-859[»]
    4W5QX-ray3.10A1-859[»]
    4W5RX-ray2.50A1-859[»]
    4W5TX-ray2.50A1-859[»]
    DisProtiDP00736.
    ProteinModelPortaliQ9UKV8.
    SMRiQ9UKV8. Positions 22-859.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    PTM databases

    PhosphoSiteiQ9UKV8.

    Polymorphism and mutation databases

    BioMutaiAGO2.
    DMDMi229463006.

    Proteomic databases

    MaxQBiQ9UKV8.
    PaxDbiQ9UKV8.
    PRIDEiQ9UKV8.

    Protocols and materials databases

    DNASUi27161.
    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi27161.
    GeneCardsiGC08M141542.
    HGNCiHGNC:3263. AGO2.
    HPAiCAB019309.
    MIMi606229. gene.
    neXtProtiNX_Q9UKV8.
    PharmGKBiPA27694.
    GenAtlasiSearch...

    Phylogenomic databases

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

    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_263982. Ca2+ pathway.
    REACT_268530. Transcriptional regulation by small RNAs.
    REACT_75829. PIP3 activates AKT signaling.

    Miscellaneous databases

    EvolutionaryTraceiQ9UKV8.
    GeneWikiiEIF2C2.
    GenomeRNAii27161.
    NextBioi49946.
    PROiQ9UKV8.
    SOURCEiSearch...

    Gene expression databases

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

    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]
    ProtoNetiSearch...

    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: May 27, 2015
    This is version 140 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.