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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VX1

Cryo-EM Structure of DHX36 bound to the cMyc DNA G-quadruplex, Class 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000781cellular_componentchromosome, telomeric region
A0000976molecular_functiontranscription cis-regulatory region binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0001503biological_processossification
A0002151molecular_functionG-quadruplex RNA binding
A0002735biological_processpositive regulation of myeloid dendritic cell cytokine production
A0003676molecular_functionnucleic acid binding
A0003678molecular_functionDNA helicase activity
A0003697molecular_functionsingle-stranded DNA binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0003725molecular_functiondouble-stranded RNA binding
A0003730molecular_functionmRNA 3'-UTR binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006359biological_processregulation of transcription by RNA polymerase III
A0007283biological_processspermatogenesis
A0008094molecular_functionATP-dependent activity, acting on DNA
A0010494cellular_componentcytoplasmic stress granule
A0010628biological_processpositive regulation of gene expression
A0016607cellular_componentnuclear speck
A0016887molecular_functionATP hydrolysis activity
A0017148biological_processnegative regulation of translation
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031442biological_processpositive regulation of mRNA 3'-end processing
A0032206biological_processpositive regulation of telomere maintenance
A0032727biological_processpositive regulation of interferon-alpha production
A0034605biological_processcellular response to heat
A0034644biological_processcellular response to UV
A0035925molecular_functionmRNA 3'-UTR AU-rich region binding
A0042826molecular_functionhistone deacetylase binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043204cellular_componentperikaryon
A0043488biological_processregulation of mRNA stability
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0045995biological_processregulation of embryonic development
A0048027molecular_functionmRNA 5'-UTR binding
A0051880molecular_functionG-quadruplex DNA binding
A0051891biological_processpositive regulation of cardioblast differentiation
A0060261biological_processpositive regulation of transcription initiation by RNA polymerase II
A0061003biological_processpositive regulation of dendritic spine morphogenesis
A0061158biological_process3'-UTR-mediated mRNA destabilization
A0070034molecular_functiontelomerase RNA binding
A0070883molecular_functionpre-miRNA binding
A0090669biological_processtelomerase RNA stabilization
A0160225molecular_functionG-quadruplex unwinding activity
A1900153biological_processpositive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
A1901534biological_processpositive regulation of hematopoietic progenitor cell differentiation
A1903843biological_processcellular response to arsenite ion
A1904358biological_processpositive regulation of telomere maintenance via telomere lengthening
A1904582biological_processpositive regulation of intracellular mRNA localization
A2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. ShIVLDEIHE
ChainResidueDetails
ASER331-GLU340
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues170
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues170
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues211
DetailsRegion: {"description":"Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure","evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues241
DetailsRegion: {"description":"RecA-like domain 2","evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues69
DetailsRegion: {"description":"WH domain","evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues64
DetailsRegion: {"description":"OB-fold-like subdomains","evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsMotif: {"description":"DEAH box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues11
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"source":"UniProtKB","id":"Q9H2U1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VHC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5VHD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29899445","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VHD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9H2U1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9H2U1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2026-04-01

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