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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9W5I

AGO maturation complex (AMC): AGO2-miRNA duplex in complex with Hsp90 beta and co-chaperone p23

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006986biological_processresponse to unfolded protein
A0007004biological_processtelomere maintenance via telomerase
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019062biological_processvirion attachment to host cell
A0019887molecular_functionprotein kinase regulator activity
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase binding
A0023026molecular_functionMHC class II protein complex binding
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
A0030911molecular_functionTPR domain binding
A0031072molecular_functionheat shock protein binding
A0031396biological_processregulation of protein ubiquitination
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032880biological_processregulation of protein localization
A0032991cellular_componentprotein-containing complex
A0034605biological_processcellular response to heat
A0034751cellular_componentaryl hydrocarbon receptor complex
A0034774cellular_componentsecretory granule lumen
A0042277molecular_functionpeptide binding
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042826molecular_functionhistone deacetylase binding
A0043008molecular_functionATP-dependent protein binding
A0043025cellular_componentneuronal cell body
A0044183molecular_functionprotein folding chaperone
A0044294cellular_componentdendritic growth cone
A0044295cellular_componentaxonal growth cone
A0045296molecular_functioncadherin binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0045597biological_processpositive regulation of cell differentiation
A0046983molecular_functionprotein dimerization activity
A0048156molecular_functiontau protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051131biological_processchaperone-mediated protein complex assembly
A0051726biological_processregulation of cell cycle
A0070062cellular_componentextracellular exosome
A0070182molecular_functionDNA polymerase binding
A0072542molecular_functionprotein phosphatase activator activity
A0097435biological_processsupramolecular fiber organization
A0097718molecular_functiondisordered domain specific binding
A0101031cellular_componentprotein folding chaperone complex
A0120293cellular_componentdynein axonemal particle
A0141069molecular_functionreceptor ligand inhibitor activity
A1901799biological_processnegative regulation of proteasomal protein catabolic process
A1904813cellular_componentficolin-1-rich granule lumen
A1905323biological_processtelomerase holoenzyme complex assembly
A1990226molecular_functionhistone methyltransferase binding
A1990565cellular_componentHSP90-CDC37 chaperone complex
A2000010biological_processpositive regulation of protein localization to cell surface
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006986biological_processresponse to unfolded protein
B0007004biological_processtelomere maintenance via telomerase
B0008180cellular_componentCOP9 signalosome
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0019062biological_processvirion attachment to host cell
B0019887molecular_functionprotein kinase regulator activity
B0019900molecular_functionkinase binding
B0019901molecular_functionprotein kinase binding
B0023026molecular_functionMHC class II protein complex binding
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
B0030911molecular_functionTPR domain binding
B0031072molecular_functionheat shock protein binding
B0031396biological_processregulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032880biological_processregulation of protein localization
B0032991cellular_componentprotein-containing complex
B0034605biological_processcellular response to heat
B0034751cellular_componentaryl hydrocarbon receptor complex
B0034774cellular_componentsecretory granule lumen
B0042277molecular_functionpeptide binding
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042826molecular_functionhistone deacetylase binding
B0043008molecular_functionATP-dependent protein binding
B0043025cellular_componentneuronal cell body
B0044183molecular_functionprotein folding chaperone
B0044294cellular_componentdendritic growth cone
B0044295cellular_componentaxonal growth cone
B0045296molecular_functioncadherin binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0045597biological_processpositive regulation of cell differentiation
B0046983molecular_functionprotein dimerization activity
B0048156molecular_functiontau protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050821biological_processprotein stabilization
B0051131biological_processchaperone-mediated protein complex assembly
B0051726biological_processregulation of cell cycle
B0070062cellular_componentextracellular exosome
B0070182molecular_functionDNA polymerase binding
B0072542molecular_functionprotein phosphatase activator activity
B0097435biological_processsupramolecular fiber organization
B0097718molecular_functiondisordered domain specific binding
B0101031cellular_componentprotein folding chaperone complex
B0120293cellular_componentdynein axonemal particle
B0141069molecular_functionreceptor ligand inhibitor activity
B1901799biological_processnegative regulation of proteasomal protein catabolic process
B1904813cellular_componentficolin-1-rich granule lumen
B1905323biological_processtelomerase holoenzyme complex assembly
B1990226molecular_functionhistone methyltransferase binding
B1990565cellular_componentHSP90-CDC37 chaperone complex
B2000010biological_processpositive regulation of protein localization to cell surface
C0000723biological_processtelomere maintenance
C0000781cellular_componentchromosome, telomeric region
C0001516biological_processprostaglandin biosynthetic process
C0003720molecular_functiontelomerase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005697cellular_componenttelomerase holoenzyme complex
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0007004biological_processtelomere maintenance via telomerase
C0007165biological_processsignal transduction
C0019371biological_processcyclooxygenase pathway
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0032991cellular_componentprotein-containing complex
C0046457biological_processprostanoid biosynthetic process
C0050220molecular_functionprostaglandin-E synthase activity
C0050821biological_processprotein stabilization
C0051082molecular_functionobsolete unfolded protein binding
C0051087molecular_functionprotein-folding chaperone binding
C0051131biological_processchaperone-mediated protein complex assembly
C0051879molecular_functionHsp90 protein binding
C0070182molecular_functionDNA polymerase binding
C0101031cellular_componentprotein folding chaperone complex
C1905323biological_processtelomerase holoenzyme complex assembly
D0000340molecular_functionRNA 7-methylguanosine cap binding
D0000932cellular_componentP-body
D0000993molecular_functionRNA polymerase II complex binding
D0001046molecular_functioncore promoter sequence-specific DNA binding
D0003723molecular_functionRNA binding
D0003725molecular_functiondouble-stranded RNA binding
D0003727molecular_functionsingle-stranded RNA binding
D0003729molecular_functionmRNA binding
D0003743molecular_functiontranslation initiation factor activity
D0004521molecular_functionRNA endonuclease activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
D0016020cellular_componentmembrane
D0016442cellular_componentRISC complex
D0016891molecular_functionRNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism
D0030425cellular_componentdendrite
D0031047biological_processregulatory ncRNA-mediated gene silencing
D0031054biological_processpre-miRNA processing
D0033962biological_processP-body assembly
D0035194biological_processregulatory ncRNA-mediated post-transcriptional gene silencing
D0035196biological_processmiRNA processing
D0035197molecular_functionsiRNA binding
D0035198molecular_functionmiRNA binding
D0035278biological_processmiRNA-mediated gene silencing by inhibition of translation
D0035279biological_processmiRNA-mediated gene silencing by mRNA destabilization
D0035925molecular_functionmRNA 3'-UTR AU-rich region binding
D0036464cellular_componentcytoplasmic ribonucleoprotein granule
D0042985biological_processnegative regulation of amyloid precursor protein biosynthetic process
D0045727biological_processpositive regulation of translation
D0045766biological_processpositive regulation of angiogenesis
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0045947biological_processnegative regulation of translational initiation
D0060213biological_processpositive regulation of nuclear-transcribed mRNA poly(A) tail shortening
D0070062cellular_componentextracellular exosome
D0070551molecular_functionendoribonuclease activity, cleaving siRNA-paired mRNA
D0070578cellular_componentRISC-loading complex
D0070922biological_processRISC complex assembly
D0090128biological_processregulation of synapse maturation
D0090624molecular_functionendoribonuclease activity, cleaving miRNA-paired mRNA
D0090625biological_processsiRNA-mediated gene silencing by mRNA destabilization
D0098794cellular_componentpostsynapse
D0098808molecular_functionmRNA cap binding
D0098978cellular_componentglutamatergic synapse
D1900153biological_processpositive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
D1901165biological_processpositive regulation of trophoblast cell migration
D1990904cellular_componentribonucleoprotein complex
Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR33-GLU42
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Cleaved under oxidative stress","evidences":[{"source":"PubMed","id":"22848402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"23585225","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-methylated lysine","evidences":[{"source":"PubMed","id":"24880080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19696785","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues89
DetailsDomain: {"description":"CS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00547","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R0Q7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"16807684","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17487921","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19367720","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues119
DetailsDomain: {"description":"PAZ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00142","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues301
DetailsDomain: {"description":"Piwi","evidences":[{"source":"HAMAP-Rule","id":"MF_03031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues78
DetailsRegion: {"description":"Interaction with guide RNA"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues13
DetailsRegion: {"description":"Interaction with GW182 family members","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"4-hydroxyproline","evidences":[{"source":"HAMAP-Rule","id":"MF_03031","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18690212","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"28114302","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"28114302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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