AGO2_HUMAN - dbPTM
AGO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGO2_HUMAN
UniProt AC Q9UKV8
Protein Name Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031}
Gene Name AGO2
Organism Homo sapiens (Human).
Sequence Length 859
Subcellular Localization Cytoplasm, P-body . Nucleus . Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.
Protein Description 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..
Protein Sequence MYSGAGPALAPPAPPPPIQGYAFKPPPRPDFGTSGRTIKLQANFFEMDIPKIDIYHYELDIKPEKCPRRVNREIVEHMVQHFKTQIFGDRKPVFDGRKNLYTAMPLPIGRDKVELEVTLPGEGKDRIFKVSIKWVSCVSLQALHDALSGRLPSVPFETIQALDVVMRHLPSMRYTPVGRSFFTASEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFVCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPYVREFGIMVKDEMTDVTGRVLQPPSILYGGRNKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDHQALAKAVQVHQDTLRTMYFA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Nitrated tyrosine------MYSGAGPAL
------CCCCCCCCC		18.80-
2Nitration------MYSGAGPAL
------CCCCCCCCC		18.80-
62AcetylationYHYELDIKPEKCPRR
EEEECCCCHHHCCCC		46.9526051181
62UbiquitinationYHYELDIKPEKCPRR
EEEECCCCHHHCCCC		46.9529967540
91UbiquitinationTQIFGDRKPVFDGRK
HHHHCCCCCCCCCCC		50.7229967540
153PhosphorylationALSGRLPSVPFETIQ
HHCCCCCCCCHHHHH		47.1946103325
171UbiquitinationVVMRHLPSMRYTPVG
HHHHHCCCCCEECCC		23.4222817900
202UbiquitinationGREVWFGFHQSVRPS
CCEEEEECCCCCCHH		3.2722817900
242PhosphorylationCEVLDFKSIEEQQKP
HHHCCCCCHHHHCCC		34.9120068231
248UbiquitinationKSIEEQQKPLTDSQR
CCHHHHCCCCCHHHH		41.5122817900
248 (in isoform 1)Ubiquitination-41.5121906983
248 (in isoform 2)Ubiquitination-41.5121906983
251PhosphorylationEEQQKPLTDSQRVKF
HHHCCCCCHHHHHHH		41.9820068231
253PhosphorylationQQKPLTDSQRVKFTK
HCCCCCHHHHHHHHH		18.0435066017
262UbiquitinationRVKFTKEIKGLKVEI
HHHHHHHHCCCEEEE		4.5822817900
276AcetylationITHCGQMKRKYRVCN
EEECCHHCCEEEEEC		37.5425953088
303PhosphorylationLQQESGQTVECTVAQ
CCCCCCCEEEEEEHH		23.0735066015
307PhosphorylationSGQTVECTVAQYFKD
CCCEEEEEEHHHHHH		12.8435066009
307UbiquitinationSGQTVECTVAQYFKD
CCCEEEEEEHHHHHH		12.8422817900
313AcetylationCTVAQYFKDRHKLVL
EEEHHHHHHCCEEEE		49.2526051181
317AcetylationQYFKDRHKLVLRYPH
HHHHHCCEEEEECCC		40.9830586783
335UbiquitinationLQVGQEQKHTYLPLE
EECCCCCCCCEECHH		36.84-
337PhosphorylationVGQEQKHTYLPLEVC
CCCCCCCCEECHHHH		33.51-
338PhosphorylationGQEQKHTYLPLEVCN
CCCCCCCEECHHHHH		13.1783375
348UbiquitinationLEVCNIVAGQRCIKK
HHHHHHHCCCHHHHH		12.4722817900
355UbiquitinationAGQRCIKKLTDNQTS
CCCHHHHHCCCCCHH		36.39-
357PhosphorylationQRCIKKLTDNQTSTM
CHHHHHCCCCCHHHH		41.6168704789
364SulfoxidationTDNQTSTMIRATARS
CCCCHHHHHHHHHHC		1.6321406390
379UbiquitinationAPDRQEEISKLMRSA
CCHHHHHHHHHHHHH		4.3022817900
381UbiquitinationDRQEEISKLMRSASF
HHHHHHHHHHHHHCC		52.55-
385PhosphorylationEISKLMRSASFNTDP
HHHHHHHHHCCCCCH		17.8223401153
387PhosphorylationSKLMRSASFNTDPYV
HHHHHHHCCCCCHHH		21.9219664994
390PhosphorylationMRSASFNTDPYVREF
HHHHCCCCCHHHHHH		36.0223927012
393PhosphorylationASFNTDPYVREFGIM
HCCCCCHHHHHHCEE		18.2323927012
402SumoylationREFGIMVKDEMTDVT
HHHCEEEECCCCCCC		30.50-
402SumoylationREFGIMVKDEMTDVT
HHHCEEEECCCCCCC		30.50-
406PhosphorylationIMVKDEMTDVTGRVL
EEEECCCCCCCCCCC		25.8523663014
409PhosphorylationKDEMTDVTGRVLQPP
ECCCCCCCCCCCCCC		23.2923663014
416UbiquitinationTGRVLQPPSILYGGR
CCCCCCCCCEEECCC		22.5022817900
425UbiquitinationILYGGRNKAIATPVQ
EEECCCCCCCCCCCC		39.5522817900
425 (in isoform 1)Ubiquitination-39.5521906983
425 (in isoform 2)Ubiquitination-39.5521906983
439UbiquitinationQGVWDMRNKQFHTGI
CCHHHCCCCCCCCCC		35.5222817900
440UbiquitinationGVWDMRNKQFHTGIE
CHHHCCCCCCCCCCE		43.9329967540
447UbiquitinationKQFHTGIEIKVWAIA
CCCCCCCEEEEEEEE		37.7922817900
468UbiquitinationQCTEVHLKSFTEQLR
CCCHHHHHHHHHHHH		28.7529967540
473UbiquitinationHLKSFTEQLRKISRD
HHHHHHHHHHHHHHH		43.4321963094
484UbiquitinationISRDAGMPIQGQPCF
HHHHCCCCCCCCCCC		18.1622817900
493UbiquitinationQGQPCFCKYAQGADS
CCCCCCCEECCCCCC		24.3022817900
504UbiquitinationGADSVEPMFRHLKNT
CCCCHHHHHHHHHHH		2.6721963094
507UbiquitinationSVEPMFRHLKNTYAG
CHHHHHHHHHHHCCC		29.8622817900
512PhosphorylationFRHLKNTYAGLQLVV
HHHHHHHCCCEEEEE		14.2020068231
526PhosphorylationVVILPGKTPVYAEVK
EEECCCCCCCEEEEE		24.7322192785
529PhosphorylationLPGKTPVYAEVKRVG
CCCCCCCEEEEEEHH		9.7635066011
533UbiquitinationTPVYAEVKRVGDTVL
CCCEEEEEEHHHHHH		32.63-
533 (in isoform 1)Ubiquitination-32.6321906983
533 (in isoform 2)Ubiquitination-32.6321906983
550UbiquitinationATQCVQMKNVQRTTP
HHHHHHCCCCCCCCH		36.5521963094
552UbiquitinationQCVQMKNVQRTTPQT
HHHHCCCCCCCCHHH		3.2122817900
564UbiquitinationPQTLSNLCLKINVKL
HHHHHHHHHHCCEEE		4.2121963094
566UbiquitinationTLSNLCLKINVKLGG
HHHHHHHHCCEEECC		31.1029967540
608MalonylationPPAGDGKKPSIAAVV
CCCCCCCCCCEEEEE		49.9126320211
609UbiquitinationPAGDGKKPSIAAVVG
CCCCCCCCCEEEEEC		34.1621963094
643UbiquitinationQEIIQDLAAMVRELL
HHHHHHHHHHHHHHH		11.2024816145
649UbiquitinationLAAMVRELLIQFYKS
HHHHHHHHHHHHHHH		3.4122817900
655UbiquitinationELLIQFYKSTRFKPT
HHHHHHHHHCCCCCE		46.79-
674UbiquitinationYRDGVSEGQFQQVLH
EECCCCHHHHHHHHH		26.5424816145
680UbiquitinationEGQFQQVLHHELLAI
HHHHHHHHHHHHHHH		2.7222817900
700HydroxylationKLEKDYQPGITFIVV
HHHHCCCCCEEEEEE		29.8918690212
720AcetylationTRLFCTDKNERVGKS
EEEEECCCCCCCCCC		42.4226051181
720UbiquitinationTRLFCTDKNERVGKS
EEEEECCCCCCCCCC		42.4224816145
726MalonylationDKNERVGKSGNIPAG
CCCCCCCCCCCCCCC		52.9426320211
726UbiquitinationDKNERVGKSGNIPAG
CCCCCCCCCCCCCCC		52.9427667366
726 (in isoform 1)Ubiquitination-52.9421906983
734PhosphorylationSGNIPAGTTVDTKIT
CCCCCCCCEECCCCC		26.2522199227
734UbiquitinationSGNIPAGTTVDTKIT
CCCCCCCCEECCCCC		26.2524816145
735PhosphorylationGNIPAGTTVDTKITH
CCCCCCCEECCCCCC		18.5722199227
740UbiquitinationGTTVDTKITHPTEFD
CCEECCCCCCCCCCC		4.6722817900
749PhosphorylationHPTEFDFYLCSHAGI
CCCCCCEEEECCCCC		14.5127660449
752PhosphorylationEFDFYLCSHAGIQGT
CCCEEEECCCCCCCC		17.4927660455
759PhosphorylationSHAGIQGTSRPSHYH
CCCCCCCCCCCCCEE		12.7527660467
760PhosphorylationHAGIQGTSRPSHYHV
CCCCCCCCCCCCEEE		49.3627660461
767UbiquitinationSRPSHYHVLWDDNRF
CCCCCEEEEECCCCC		4.5722817900
779UbiquitinationNRFSSDELQILTYQL
CCCCHHHHHHHHHHH		4.6324816145
785UbiquitinationELQILTYQLCHTYVR
HHHHHHHHHHHHHHC		32.1722817900
796PhosphorylationTYVRCTRSVSIPAPA
HHHCCCCCCCCCCCH		11.3216094384
798PhosphorylationVRCTRSVSIPAPAYY
HCCCCCCCCCCCHHH		24.8935066013
798UbiquitinationVRCTRSVSIPAPAYY
HCCCCCCCCCCCHHH		24.8922817900
804PhosphorylationVSIPAPAYYAHLVAF
CCCCCCHHHHHHHHH		10.5026074081
805PhosphorylationSIPAPAYYAHLVAFR
CCCCCHHHHHHHHHH		6.9426074081
810UbiquitinationAYYAHLVAFRARYHL
HHHHHHHHHHHHEEE		8.4522817900
810 (in isoform 2)Ubiquitination-8.4521906983
815PhosphorylationLVAFRARYHLVDKEH
HHHHHHHEEECCCCC		9.8723186163
824PhosphorylationLVDKEHDSAEGSHTS
ECCCCCCCCCCCCCC		30.0823927012
828PhosphorylationEHDSAEGSHTSGQSN
CCCCCCCCCCCCCCC		18.3323927012
830PhosphorylationDSAEGSHTSGQSNGR
CCCCCCCCCCCCCCC		35.9330108239
831PhosphorylationSAEGSHTSGQSNGRD
CCCCCCCCCCCCCCC		29.4330108239
834PhosphorylationGSHTSGQSNGRDHQA
CCCCCCCCCCCCHHH		44.7930108239
844UbiquitinationRDHQALAKAVQVHQD
CCHHHHHHHHHHHHH		50.3622817900
844 (in isoform 1)Ubiquitination-50.3621906983
852PhosphorylationAVQVHQDTLRTMYFA
HHHHHHHHHHHHCCC		16.15-
858UbiquitinationDTLRTMYFA------
HHHHHHCCC------		4.5222817900
903Ubiquitination---------------------------------------------------
---------------------------------------------------		22817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
387SPhosphorylationKinaseAKT3Q9Y243
PSP
387SPhosphorylationKinaseMAPKAPK2P49137
PSP
393YPhosphorylationKinaseEGFRP00533
PSP
393YPhosphorylationKinaseSRCP12931
PSP
529YPhosphorylationKinaseSRCP12931
PSP
749YPhosphorylationKinaseSRCP12931
PSP
824SPhosphorylationKinaseCK1AP48729
PSP
828SPhosphorylationKinaseCK1AP48729
PSP
830TPhosphorylationKinaseCK1AP48729
PSP
831SPhosphorylationKinaseCK1AP48729
PSP
834SPhosphorylationKinaseCK1AP48729
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGO2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AGO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX20_HUMANDDX20physical
14970384
GEMI4_HUMANGEMIN4physical
14970384
DICER_HUMANDICER1physical
12526743
DDX20_HUMANDDX20physical
11914277
GEMI4_HUMANGEMIN4physical
11914277
GAG_HV1H2gagphysical
19560422
IPO8_HUMANIPO8physical
19167051
DICER_HUMANDICER1physical
14749716
TNFA_HUMANTNFphysical
21562054
RBM4_HUMANRBM4physical
21562054
FBW1A_HUMANBTRCphysical
19647520
TNR6A_HUMANTNRC6Aphysical
19470757
TNR6B_HUMANTNRC6Bphysical
19470757
TNR6C_HUMANTNRC6Cphysical
19470757
LRRK2_HUMANLRRK2physical
20671708
4EBP1_HUMANEIF4EBP1physical
20671708
TNR6A_HUMANTNRC6Aphysical
19383768
TNR6B_HUMANTNRC6Bphysical
19383768
TNR6C_HUMANTNRC6Cphysical
19383768
HS90A_HUMANHSP90AA1physical
19716330
DICER_HUMANDICER1physical
19716330
TRBP2_HUMANTARBP2physical
19716330
TNR6A_HUMANTNRC6Aphysical
19716330
PABP1_HUMANPABPC1physical
19716330
CNOT7_HUMANCNOT7physical
19716330
GEMI4_HUMANGEMIN4physical
23143396
DICER_HUMANDICER1physical
23143396
DICER_HUMANDICER1physical
16357216
HS90A_HUMANHSP90AA1physical
16357216
TRBP2_HUMANTARBP2physical
16357216
PFKAP_HUMANPFKPphysical
21988832
AGO1_HUMANAGO1physical
24086155
FOLR1_HUMANFOLR1physical
19167051
G8_HUMANC6orf48physical
19167051
MCL1_HUMANMCL1physical
19167051
RL27A_HUMANRPL27Aphysical
19167051
S10AB_HUMANS100A11physical
19167051
TEFF2_HUMANTMEFF2physical
19167051
RS11_HUMANRPS11physical
19167051
RS20_HUMANRPS20physical
19167051
TMM64_HUMANTMEM64physical
19167051
AGO1_HUMANAGO1physical
24778252
AGO3_HUMANAGO3physical
24778252
CBWD2_HUMANCBWD2physical
24778252
CE170_HUMANCEP170physical
24778252
CPSM_HUMANCPS1physical
24778252
DICER_HUMANDICER1physical
24778252
GASP2_HUMANGPRASP2physical
24778252
IGBP1_HUMANIGBP1physical
24778252
IQEC1_HUMANIQSEC1physical
24778252
KLH29_HUMANKLHL29physical
24778252
DNLI4_HUMANLIG4physical
24778252
AF1Q_HUMANMLLT11physical
24778252
MSI1H_HUMANMSI1physical
24778252
NDUS2_HUMANNDUFS2physical
24778252
PDIA1_HUMANP4HBphysical
24778252
PASK_HUMANPASKphysical
24778252
KAP0_HUMANPRKAR1Aphysical
24778252
RN219_HUMANRNF219physical
24778252
TRBP2_HUMANTARBP2physical
24778252
TNR6A_HUMANTNRC6Aphysical
24778252
TNR6B_HUMANTNRC6Bphysical
24778252
TNR6C_HUMANTNRC6Cphysical
24778252
TRM1_HUMANTRMT1physical
24778252
DCAF7_HUMANDCAF7physical
24778252
YTHD1_HUMANYTHDF1physical
24778252
ELAV1_HUMANELAVL1physical
23901138
CNOT1_HUMANCNOT1physical
21981923
CNOT2_HUMANCNOT2physical
21981923
CNOT6_HUMANCNOT6physical
21981923
CNO6L_HUMANCNOT6Lphysical
21981923
CNOT8_HUMANCNOT8physical
21981923
TNR6C_HUMANTNRC6Cphysical
21981923
TRBP2_HUMANTARBP2physical
26496610
GUAA_HUMANGMPSphysical
26496610
DICER_HUMANDICER1physical
26496610
CRBN_HUMANCRBNphysical
27142104
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGO2_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Prolyl 4-hydroxylation regulates Argonaute 2 stability.";
Qi H.H., Ongusaha P.P., Myllyharju J., Cheng D., Pakkanen O., Shi Y.,Lee S.W., Peng J., Shi Y.;
Nature 455:421-424(2008).
Cited for: FUNCTION, INTERACTION WITH DICER1; P4HA1; P4HB; TNRC6A AND TNRC6B,SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-700, AND MUTAGENESIS OFPRO-700.

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