Affinage

SETD3

Actin-histidine N-methyltransferase · UniProt Q86TU7

Length
594 aa
Mass
67.3 kDa
Annotated
2026-06-10
49 papers in source corpus 25 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SETD3 is a SET-domain methyltransferase whose principal physiological function is the histidine-N3 methylation of β-actin at His73, the only detectable physiological substrate identified by quantitative proteomics, a modification that reduces nucleotide exchange on actin monomers and accelerates filament assembly (PMID:30626964, PMID:30526847). Crystal structures of SAH-bound SETD3 with unmodified and methylated β-actin peptides define a highly sequence-specific recognition mode in which both enzyme and substrate undergo pronounced conformational changes (PMID:30785395), and catalysis proceeds through a ~105° rotation of the His73 imidazole ring that shifts a proton from N3 to N1 to deprotonate the target nitrogen prior to methyl transfer (PMID:31388018); distal substrate determinants including the actin Trp79 pocket govern catalytic efficiency (PMID:37581408). This actin-methylation activity is physiologically required for smooth muscle contractility, with SETD3-null mice showing maternal dystocia and impaired uterine smooth muscle contraction (PMID:30626964), and disease relevance is underscored by the BWCFF-associated β-actin G74S mutation, which impairs His73 methylation in patient-derived fibroblasts and recombinant protein (PMID:40490999). Beyond actin, SETD3 methylates additional substrates to control distinct programs: MCM7 at His459 to license replication origin firing (PMID:39455502), CHD1 at Lys209 to stabilize it and activate TNF-NFκB target genes (PMID:41045985), and α-centractin in vitro (PMID:41142317). In a methyltransferase-independent role, cytosolic SETD3 binds the enteroviral 2A protease and is essential for enterovirus RNA replication and pathogenesis (PMID:31527793). SETD3 abundance is tightly regulated by competing post-translational pathways, including GSK3β-primed FBXW7β-mediated proteasomal degradation (PMID:28442573) and PARP1/NUDT16-controlled (de)PARylation that gates CHFR-dependent turnover (PMID:38272222). SETD3 also localizes to the outer mitochondrial membrane, where mechanosensitive actin methylation supports F-actin organization, complex I assembly, and oxidative phosphorylation (PMID:38896010).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2011 Medium

    Established the first functional context for SETD3, linking it to muscle gene transcription and differentiation before its true substrate was known.

    Evidence Overexpression/knockdown, reporter and ChIP assays in C2C12 myoblasts

    PMID:21832073

    Open questions at the time
    • Assigned histone H3K4/H3K36 as substrate, later disputed
    • Did not identify actin as the physiological target
    • Mechanism connecting SETD3 to myogenin promoter unresolved
  2. 2015 Medium

    Identified SETD3 as a PCNA-interacting protein, providing an early hint of a replication-associated role.

    Evidence BiFC screen with Co-IP and recombinant protein validation

    PMID:26030842

    Open questions at the time
    • Functional consequence of PCNA binding not defined
    • No methylation activity linked to the interaction
  3. 2016 Medium

    Proposed FoxM1 as a SETD3 substrate regulating VEGF transcription, extending candidate non-histone targets.

    Evidence Proteomic screen, Co-IP, methyltransferase and ChIP assays

    PMID:27845446

    Open questions at the time
    • Methylation site on FoxM1 not mapped
    • Distinct from later-established actin substrate
    • Single lab without orthogonal in vivo confirmation
  4. 2017 High

    Defined how SETD3 protein levels are controlled across the cell cycle, establishing a kinase-coupled degradation circuit.

    Evidence Co-IP, phosphodegron mutagenesis, GSK3β inhibition, cell synchronization, xenografts

    PMID:28442573

    Open questions at the time
    • Did not connect SETD3 stability to a specific enzymatic output
    • Upstream signals controlling GSK3β-dependent phosphorylation unclear
  5. 2018 High

    Resolved the central question of SETD3's physiological function by identifying β-actin His73 as its sole detectable substrate and defining the structural basis of recognition.

    Evidence In vitro methyltransferase assays, X-ray crystallography, quantitative proteomics, KO mice and HAP1/Drosophila knockouts

    PMID:30526847 PMID:30626964

    Open questions at the time
    • Did not fully resolve catalytic proton-shuttling mechanism
    • Cellular consequences of His73 methylation only partially mapped
  6. 2019 High

    Defined the catalytic chemistry of histidine N3 methylation through pre- and post-reactive structures and linked the enzyme to a physiological smooth-muscle phenotype.

    Evidence Crystallography of reaction intermediates, biochemistry, and KO mice/human uterine smooth muscle contraction assays

    PMID:30626964 PMID:30785395 PMID:31388018

    Open questions at the time
    • Why His73 methylation is required for contractility at the molecular level incompletely defined
  7. 2019 High

    Uncovered a methyltransferase-independent function in which SETD3 is hijacked by enteroviruses as an essential host factor for RNA replication.

    Evidence Genome-scale CRISPR screens, AP-MS, rescue with interaction-deficient 2A mutants, in vivo mouse infection

    PMID:31527793

    Open questions at the time
    • Molecular role of SETD3 in the viral replication complex undefined
    • Structural basis of 2A protease interaction unknown
  8. 2019 Medium

    Linked SETD3 catalytic activity to p53-dependent apoptosis, expanding its candidate transcriptional roles.

    Evidence Co-IP, ChIP, siRNA knockdown, apoptosis assays in HCT-116 cells

    PMID:30683849

    Open questions at the time
    • Direct p53 methylation site not established
    • Single cell line, single lab
  9. 2020 High

    Mapped the active-site determinants of substrate selectivity, showing histidine versus lysine/methionine targeting is governed by specific pocket residues.

    Evidence Crystallography of methionine-containing and engineered variants, kinetics, mutagenesis

    PMID:31911441 PMID:32503840

    Open questions at the time
    • Engineered specificity switches not observed in cellular substrates
    • Physiological relevance of weak alternative activities unclear
  10. 2022 Medium

    Added a stabilizing deubiquitinase to the SETD3 regulatory network, tying its abundance to cancer cell proliferation.

    Evidence Co-IP, ubiquitination assays, USP27 knockdown in hepatocellular carcinoma cells

    PMID:35018513

    Open questions at the time
    • Whether USP27 acts directly on SETD3 ubiquitin chains not fully resolved
    • Link to specific methylation output undefined
  11. 2024 Medium

    Identified MCM7 His459 as a new SETD3 substrate controlling origin licensing and connected CDK2 phosphorylation of SETD3 to S-phase entry.

    Evidence NS-seq, Co-IP, H459 mutagenesis, CDK2 phosphorylation assays

    PMID:39455502

    Open questions at the time
    • In vivo requirement of MCM7 methylation not tested in animals
    • Single lab
  12. 2024 Medium

    Placed SETD3-mediated actin methylation at the outer mitochondrial membrane as a mechanosensitive regulator of mitochondrial structure and bioenergetics.

    Evidence Live-cell imaging, fractionation, loss-of-function with OXPHOS/complex I readouts, ECM stiffness modulation

    PMID:38896010

    Open questions at the time
    • How ECM stiffness is transduced to SETD3 activity unknown
    • Direct mitochondrial actin substrate pool not defined
  13. 2024 Medium

    Connected SETD3 to PARylation-dependent stability control and to a role in BRCA2 recruitment during replication stress and DNA damage.

    Evidence Co-IP, PARylation/dePARylation assays, depletion with replication-stress and irradiation-sensitivity readouts

    PMID:38272222

    Open questions at the time
    • Whether SETD3 methylates a DNA-repair substrate unresolved
    • Mechanism of BRCA2 recruitment undefined
  14. 2024 Medium

    Implicated SETD3 in splicing regulation through hnRNPK, linking it to TFEB-driven lysosomal and mitochondrial biogenesis.

    Evidence Proximity labeling/MS, RNA-seq, Co-IP, loss-of-function on FNIP1 exon skipping

    PMID:39391005

    Open questions at the time
    • Catalytic dependence of splicing function not established
    • Direct RNA contact by SETD3 unknown
  15. 2024 Medium

    Established SETD3 as a regulator of canonical Wnt signaling and endoderm differentiation in ESCs via β-catenin.

    Evidence PLA, nuclear fractionation, Wnt reporter, time-course RNA-seq, rescue experiments

    PMID:38334393

    Open questions at the time
    • Whether β-catenin is methylated not shown
    • Mechanism stabilizing nuclear β-catenin undefined
  16. 2025 Medium

    Expanded the SETD3 substrate/interactor repertoire to CHD1, α-centractin, and BRD2, and tied actin methylation to a human β-actin disease mutation.

    Evidence In vitro methyltransferase and ubiquitination assays, ChIP, TurboID/MS, PLA, domain mapping, enzymatic turnover on patient-derived actin

    PMID:40490999 PMID:40944926 PMID:41045985 PMID:41142317

    Open questions at the time
    • Cellular validation of several new substrates incomplete
    • Catalytic versus scaffold contributions to BRD2/centractin interactions unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved which non-actin substrates and interactions are catalytically dependent and physiologically significant, and how SETD3's nuclear, cytosolic, and mitochondrial pools are functionally partitioned.
  • No unified model of substrate hierarchy beyond β-actin
  • Localization-specific activity regulation undefined
  • Catalytic requirement of viral and chromatin interactions only partly tested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 7 GO:0140096 catalytic activity, acting on a protein 4 GO:0008092 cytoskeletal protein binding 3
Localization
GO:0005634 nucleus 3 GO:0005739 mitochondrion 1 GO:0005829 cytosol 1
Pathway
GO:0140096 catalytic activity, acting on a protein 3
Partners
ACTBACTR1ABRCA2BRD2CHD1FBXW7HNRNPKMCM7

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2018 SETD3 is the physiological actin histidine methyltransferase that methylates β-actin at His73 (N3 of histidine 73). Structural studies reveal an extensive network of interactions that clamps the actin peptide onto the surface of SETD3 to orient His73 correctly within the catalytic pocket. His73 methylation reduces the nucleotide-exchange rate on actin monomers and modestly accelerates actin filament assembly. Quantitative proteomics showed actin His73 methylation is the only detectable physiological substrate of SETD3. In vitro methyltransferase assay, X-ray crystallography, quantitative proteomics, SETD3 knockout mice Nature High 30626964
2018 SETD3 is the actin-specific histidine N-methyltransferase that methylates β-actin at H73 in vertebrates and Drosophila. Knockout of SETD3 in human HAP1 cells and Drosophila abolished H73 methylation. SETD3-deficient HAP1 cells show less cellular F-actin and an increased glycolytic phenotype. CRISPR/Cas9 knockout in HAP1 cells and Drosophila, mass spectrometry, in vitro methyltransferase assay with recombinant rat and human SETD3 eLife High 30526847
2011 Mouse SETD3 functions as a histone H3K4 and H3K36 methyltransferase with transcriptional activation activity; it is recruited to the myogenin gene promoter together with MyoD and activates transcription of muscle-related genes (myogenin, MCK, Myf6), promoting muscle cell differentiation. Knockdown of SETD3 retards muscle cell differentiation. Overexpression and shRNA knockdown in C2C12 cells, reporter assays, chromatin immunoprecipitation (ChIP) The Journal of biological chemistry Medium 21832073
2019 SETD3 is required for enterovirus (EV) RNA replication independent of its methyltransferase activity. Cytosolic SETD3 specifically interacts with the viral 2A protease of multiple enteroviral species, and 2A mutants that retain protease activity but cannot interact with SETD3 are severely compromised in RNA replication. SETD3 is essential for in vivo EV replication and pathogenesis in mouse models. Genome-scale CRISPR screens, quantitative affinity purification-mass spectrometry (AP-MS), viral replication assays in SETD3-KO cells, in vivo mouse infection models Nature microbiology High 31527793
2019 Crystal structures of SAH-bound SETD3 in complex with unmodified or His73-methylated β-actin peptides show that recognition and methylation are highly sequence-specific and that both SETD3 and β-actin undergo pronounced conformational changes upon binding. The catalytic mechanism involves histidine methylation at N3. X-ray crystallography, biochemical enzyme activity assays, mutagenesis eLife High 30785395
2017 SETD3 protein levels are cell cycle-regulated, peaking in S phase and lowest in M phase. The E3 ubiquitin ligase FBXW7β mediates SETD3 degradation via recognition of a phosphodegron (CPD1) that is phosphorylated by GSK3β. Mutations of the phosphorylated residues in CPD1 abolish FBXW7β–SETD3 interaction and prevent degradation. Co-immunoprecipitation, mutagenesis, GSK3β inhibition/depletion, cell cycle synchronization, xenograft mouse model The Journal of biological chemistry High 28442573
2019 SETD3 binds the N3-protonated form of actin His73 in a pre-reactive complex; after methyl transfer the product bears an N1-protonated, N3-methylated histidine. During catalysis the imidazole ring of His73 rotates ~105°, shifting the proton from N3 to N1 to deprotonate the target N3 atom prior to methyl transfer. Under conditions optimized for lysine deprotonation, SETD3 shows weak lysine methylation activity. X-ray crystallography (pre- and post-reactive complexes), in vitro methyltransferase assays Nature communications High 31388018
2016 SETD3 binds and methylates the transcription factor FoxM1. Under basal conditions, SETD3 and FoxM1 are co-enriched on the VEGF promoter, and their dissociation under hypoxia correlates with increased VEGF expression. Proteomic interaction screen, Co-immunoprecipitation, methyltransferase assay, chromatin immunoprecipitation (ChIP) Scientific reports Medium 27845446
2019 SETD3 is a positive regulator of DNA-damage-induced apoptosis; depletion from HCT-116 colon cancer cells significantly inhibits apoptosis after doxorubicin treatment. SETD3 binds p53 in cells upon doxorubicin treatment and its catalytic activity is required for p53 recruitment to target gene promoters and p53 target gene activation. Co-immunoprecipitation, ChIP, siRNA knockdown, apoptosis assays Cell death & disease Medium 30683849
2015 SETD3 was identified as a PCNA-interacting protein; the interaction was validated by co-immunoprecipitation from human cell extracts and by interaction analysis using recombinant proteins. Bimolecular fluorescence complementation (BiFC) screen, co-immunoprecipitation, recombinant protein interaction assay Cell cycle Medium 26030842
2020 SETD3 can methylate methionine in the context of an actin peptide in which His73 is substituted with methionine, generating S-methylmethionine. The 1.9 Å crystal structure reveals the thioether side chain is packed by aromatic rings of Tyr312 and Trp273 and the hydrocarbon side chain of Ile310 in the active site. X-ray crystallography (1.9 Å), in vitro methyltransferase assay, site-directed mutagenesis The Journal of biological chemistry High 32503840
2020 Active-site engineering (N255F + W273A double substitution) of SETD3 switches its target specificity from histidine to lysine methylation, achieving a 13-fold preference for lysine. X-ray crystallography shows that the target N3 atom of histidine and the terminal ε-amino nitrogen of lysine occupy the same active-site position. Active-site mutagenesis, in vitro methyltransferase assays (kcat/Km measurements), X-ray crystallography The Journal of biological chemistry High 31911441
2024 SETD3 is localized on the outer mitochondrial membrane and is a mechanosensitive enzyme regulated by extracellular matrix stiffness. SETD3 directly methylates actin at His73, enhances F-actin polymerization around mitochondria, and is required for oxidative phosphorylation and mitochondrial complex I assembly and function. Loss of SETD3 leads to diminished F-actin around mitochondria and decreased mitochondrial branch length, branch number, and movement. Live-cell imaging, fractionation/localization assays, SETD3 loss-of-function with mitochondrial functional readouts (OXPHOS, complex I assembly), ECM stiffness modulation Journal of cell science Medium 38896010
2022 USP27, a deubiquitinase, specifically interacts with SETD3, negatively regulates its ubiquitination, and enhances its protein stability, thereby promoting hepatocellular carcinoma cell proliferation. Co-immunoprecipitation, ubiquitination assays, USP27 knockdown with SETD3 protein level measurement Cellular and molecular life sciences Medium 35018513
2024 SETD3 methylates MCM7 at histidine-459 (H459me), which is required for CDT1-mediated chromatin loading of the MCM complex and replication origin firing. CDK2 phosphorylates SETD3 at Serine-21 during G1/S phase, which is required for DNA replication and cell cycle progression. Nascent-strand sequencing (NS-seq), biochemical co-immunoprecipitation, SETD3 enzymatic activity assays, H459 mutagenesis, CDK2 phosphorylation assays Science China. Life sciences Medium 39455502
2024 SETD3 interacts with hnRNPK and collaboratively regulates pre-mRNA exon skipping. Together they regulate retention of exon 7 skipping in FNIP1, promoting FNIP1-mediated nuclear translocation of TFEB and subsequent induction of lysosomal and mitochondrial biogenesis. In situ proximity labeling/mass spectrometry, genome-wide RNA-seq, Co-immunoprecipitation, loss-of-function experiments Cell insight Medium 39391005
2024 NUDT16-mediated dePARylation stabilizes SETD3 by reversing PARP1-mediated ADP-ribosylation. The E3 ligase CHFR recognizes PARylated SETD3 for degradation. SETD3 associates with BRCA2 and promotes its recruitment to stalled replication forks and DNA double-strand break sites. Co-immunoprecipitation, PARylation/dePARylation assays, SETD3 depletion with replication stress readouts, cell irradiation sensitivity assays The Journal of biological chemistry Medium 38272222
2025 SETD3 dimethylates CHD1 at lysine 209 (K209). This dimethylation enhances CHD1 protein stability by reducing its ubiquitination. SETD3-mediated CHD1 methylation enhances H3K4me3 marks and promotes transcriptional activation of TNF-NFκB pathway genes. In vitro methyltransferase assay, Co-immunoprecipitation, ubiquitination assays, ChIP, gene expression analysis Cancer letters Medium 41045985
2025 SETD3 interacts with α-centractin (ACTR1A), a key dynactin subunit, and methylates it in vitro. Fluorography of SETD3-KO cell lysates revealed at least five novel SETD3-dependent methylated proteins beyond β-actin. TurboID proximity labeling, mass spectrometry, CRISPR/Cas9 KO in three cell lines, radiochemical methyltransferase assay, fluorography PeerJ Medium 41142317
2021 SETD3 depletion in neurons leads to decreased actin polymerization (F-actin), reduced cellular ATP, diminished mitochondrial membrane potential, and increased ROS production, resulting in mitochondrial dysfunction and neuronal death following oxygen-glucose deprivation. PTEN upregulation after ischemia causes SETD3 downregulation, and inhibiting PTEN protects neurons through restoration of SETD3 and actin polymerization. siRNA knockdown, OGD/R model, mitochondrial function assays (ATP, membrane potential, ROS), actin polymerization assay, in vivo cerebral I/R rat model Molecular neurobiology Medium 34218417
2019 SETD3-deficient female mice show severe reduction in litter sizes due to primary maternal dystocia; depletion of SETD3 impairs signal-induced contraction in primary human uterine smooth muscle cells. Complete loss of actin His73 methylation was confirmed in multiple tissues of SETD3-null mice. SETD3 knockout mice, uterine smooth muscle contraction assays, SETD3 siRNA knockdown in primary human cells Nature High 30626964
2025 SETD3 interacts with BRD2 in the nucleus of mouse ESCs, and this interaction depends on the RSB domain of SETD3. Loss of SETD3 leads to reduced BRD2 recruitment to chromatin and transcriptional changes; the interaction was confirmed by co-immunoprecipitation, domain deletion analysis, and proximity ligation assays. Mass spectrometry (nuclear pull-down), Co-immunoprecipitation, domain deletion analysis, proximity ligation assay (PLA) The FEBS journal Medium 40944926
2024 In mouse ESCs, SETD3 interacts with β-catenin (proximity ligation assay), and loss of SETD3 reduces nuclear β-catenin levels (without changing total protein or mRNA), decreasing canonical Wnt transcriptional activity and causing endoderm differentiation defects that can be rescued by re-expressing SETD3 or activating canonical Wnt signaling. Proximity ligation assay (PLA), time-course RNA-seq, nuclear fractionation, Wnt reporter assay, SETD3 rescue experiments FASEB journal Medium 38334393
2025 SETD3 promotes H3K4 methylation at the NLRP3 transcription start site in hippocampal microglia, activating the NLRP3-Caspase-1-IL-1β signaling pathway and enhancing neuroinflammation after surgery. SETD3 knockdown via lentiviral injection, ChIP for H3K4me3 at NLRP3 promoter, neuroinflammation cytokine assays, behavioral tests Experimental neurology Low 41175962
2023 The Trp79 binding pocket of SETD3 plays an important role in efficient His73 methylation catalysis; substitution of Trp79 in β-actin peptides with less bulky or hydrophilic residues reduces SETD3 catalytic activity, and molecular dynamics simulations show the pocket is shaped to accommodate the large hydrophobic Trp79. In vitro methyltransferase assay (MALDI-TOF MS), molecular dynamics simulations, synthetic peptide substitutions Chembiochem Medium 37581408
2025 The pathogenic G74S β-actin mutation (associated with BWCFF syndrome) disrupts SETD3-mediated His73 methylation; enzymatic assays confirm slower turnover of mutant actin peptides, and mass spectrometry reveals decreased His73 methylation in recombinant mutant β-actin and patient-derived fibroblasts. Enzymatic turnover assays, mass spectrometry (patient fibroblasts and recombinant protein), molecular docking FEBS letters Medium 40490999

Source papers

Stage 0 corpus · 49 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2018 SETD3 is an actin histidine methyltransferase that prevents primary dystocia. Nature 135 30626964
2018 SETD3 protein is the actin-specific histidine N-methyltransferase. eLife 98 30526847
2011 Histone methyltransferase SETD3 regulates muscle differentiation. The Journal of biological chemistry 78 21832073
2019 Enterovirus pathogenesis requires the host methyltransferase SETD3. Nature microbiology 61 31527793
2019 Structural insights into SETD3-mediated histidine methylation on β-actin. eLife 51 30785395
2017 Cell cycle-dependent degradation of the methyltransferase SETD3 attenuates cell proliferation and liver tumorigenesis. The Journal of biological chemistry 46 28442573
2011 Characterization of a novel histone H3K36 methyltransferase setd3 in zebrafish. Bioscience, biotechnology, and biochemistry 36 21307598
2019 SETD3 is a positive regulator of DNA-damage-induced apoptosis. Cell death & disease 35 30683849
2019 Structural basis for the target specificity of actin histidine methyltransferase SETD3. Nature communications 35 31388018
2016 Chromatin associated SETD3 negatively regulates VEGF expression. Scientific reports 34 27845446
2019 MiR-15b and miR-322 inhibit SETD3 expression to repress muscle cell differentiation. Cell death & disease 32 30796205
2012 The role of a newly identified SET domain-containing protein, SETD3, in oncogenesis. Haematologica 32 23065515
2018 SETD3 negatively regulates VEGF expression during hypoxic pulmonary hypertension in rats. Hypertension research : official journal of the Japanese Society of Hypertension 24 29950684
2021 SETD3 Downregulation Mediates PTEN Upregulation-Induced Ischemic Neuronal Death Through Suppression of Actin Polymerization and Mitochondrial Function. Molecular neurobiology 21 34218417
2015 A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells. Cell cycle (Georgetown, Tex.) 21 26030842
2022 Stabilization of SETD3 by deubiquitinase USP27 enhances cell proliferation and hepatocellular carcinoma progression. Cellular and molecular life sciences : CMLS 20 35018513
2019 SETD3 is regulated by a couple of microRNAs and plays opposing roles in proliferation and metastasis of hepatocellular carcinoma. Clinical science (London, England : 1979) 19 31654063
2020 Characterization of a novel lncRNA (SETD3-OT) in turbot (Scophthalmus maximus L.). Fish & shellfish immunology 17 32278113
2020 An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation. The Journal of biological chemistry 15 31911441
2020 Characterization of SETD3 methyltransferase-mediated protein methionine methylation. The Journal of biological chemistry 15 32503840
2021 β-Actin Peptide-Based Inhibitors of Histidine Methyltransferase SETD3. ChemMedChem 14 34032009
2022 Histidine methyltransferase SETD3 methylates structurally diverse histidine mimics in actin. Protein science : a publication of the Protein Society 12 35481649
2021 The Structure, Activity, and Function of the SETD3 Protein Histidine Methyltransferase. Life (Basel, Switzerland) 12 34685411
2019 SETD3 reduces KLC4 expression to improve the sensitization of cervical cancer cell to radiotherapy. Biochemical and biophysical research communications 12 31235251
2020 Overexpression of CXCR5 in CD4+ T cells of SLE patients caused by excessive SETD3. Clinical immunology (Orlando, Fla.) 10 32240818
2021 Circ_SETD3 regulates gefitinib sensitivity and tumor progression by miR-873-5p-dependent regulation of APPBP2 in non-small cell lung cancer. Journal of chemotherapy (Florence, Italy) 9 34861803
2024 SETD3 is a mechanosensitive enzyme that methylates actin on His73 to regulate mitochondrial dynamics and function. Journal of cell science 7 38896010
2023 The Role of Trp79 in β-Actin on Histidine Methyltransferase SETD3 Catalysis. Chembiochem : a European journal of chemical biology 7 37581408
2021 Up-regulation of SETD3 may contribute to post-stroke depression in rat through negatively regulating VEGF expression. Behavioural brain research 7 34499935
2022 Structure-function conservation between the methyltransferases SETD3 and SETD6. Biochimie 6 35550916
2022 Proteolytic Activities of Enterovirus 2A Do Not Depend on Its Interaction with SETD3. Viruses 6 35891342
2018 Phenotypic characterization of SETD3 knockout Drosophila. PloS one 6 30067821
2024 The dePARylase NUDT16 promotes radiation resistance of cancer cells by blocking SETD3 for degradation via reversing its ADP-ribosylation. The Journal of biological chemistry 5 38272222
2024 SETD3 regulates endoderm differentiation of mouse embryonic stem cells through canonical Wnt signaling pathway. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5 38334393
2024 The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK. Cell insight 3 39391005
2024 Examining prestructured β-actin peptides as substrates of histidine methyltransferase SETD3. Scientific reports 3 39488591
2022 SETD3 Methyltransferase Regulates PLK1 Expression to Promote In Situ Hepatic Carcinogenesis. Frontiers in oncology 3 35912180
2025 Disruption of SETD3-mediated histidine-73 methylation by the BWCFF-associated β-actin G74S mutation. FEBS letters 2 40490999
2024 SETD3 functions beyond histidine methylation. Life sciences 2 39299385
2024 SETD3-mediated histidine methylation of MCM7 regulates DNA replication by facilitating chromatin loading of MCM. Science China. Life sciences 2 39455502
2023 Zebrafish SETD3 mediated ubiquitination of phosphoprotein limits spring viremia of carp virus infection. Fish & shellfish immunology 2 37269914
2022 Computational Study of Methionine Methylation Process Catalyzed by SETD3. Interdisciplinary sciences, computational life sciences 2 35419695
2022 A novel SETD3-ALK fusion in lung adenocarcinoma and sustained clinical response to crizotinib. Lung cancer (Amsterdam, Netherlands) 2 36495785
2022 Structural and Energetic Origin of Different Product Specificities and Activities for SETD3 and Its Mutants on the Methylation of the β-Actin H73K Peptide: Insights from a QM/MM Study. Journal of chemical theory and computation 2 36520638
2025 Microglial hyperactivation and NLRP3 methylation mediated by SETD3 after anesthesia/surgery: Unraveling new mechanisms of perioperative neurocognitive disorders. Experimental neurology 1 41175962
2025 SETD3 regulates Bcl-6 expression and Tfh differentiation in SLE CD4+ T cells by manipulating histone methylation and acetylation. Clinical epigenetics 1 41272740
2025 SET domain containing 3 (SETD3) interacts with bromodomain-containing protein 2 (BRD2) and coordinates its chromatin association in mouse embryonic stem cells. The FEBS journal 0 40944926
2025 The Actin Histidine methyltransferase SETD3 is a CHD1 lysine di-methyltransferase. Cancer letters 0 41045985
2025 Alpha-centractin is a novel substrate of SETD3 methyltransferase in vitro. PeerJ 0 41142317

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