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3 S-adenosyl-L-methionine + a [histone H4]-L-lysine20
3 S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-methionine + a [histone H4]-N6,N6-dimethyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + histone H4(K20)
?
S-adenosyl-L-methionine + p53 (K382)
?
-
Substrates: SET8 activity is strongly reduced by the arginine methylation at position R379
Products: -
?
S-adenosyl-L-methionine + SGRGKGGKGLGKGGAKRHRKVLRDNIQGIY
?
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [p53]-L-lysine382
S-adenosyl-L-homocysteine + [p53]-N6-methyl-L-lysine382
Substrates: -
Products: -
?
additional information
?
-
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: highly specific substrate
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: highly specific substrate
Products: -
?
S-adenosyl-L-methionine + histone H4(K20)
?
-
Substrates: histone H4 is specifically methylated at lysine-20
Products: -
?
S-adenosyl-L-methionine + histone H4(K20)
?
-
Substrates: SET8 specifically methylates K20 on the histone H4. Enzyme activity is strongly reduced by the arginine methylation at position R17
Products: -
?
additional information
?
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
additional information
?
-
Substrates: the proteolytic degradation of the enzyme is controlled by the SCFSlimb ligase complex
Products: -
?
additional information
?
-
-
Substrates: In addition to K20 (the target methylation site), R17 and H18 are very important specificity determinants for SET8 for substrate recognition. Any other amino acid introduced at these positions completely abolishes the activity of SET8. SET8 equally accepts K and R at position 19, followed by Y and other hydrophobic amino acids like L, H and I. Residues on the C-terminal side of K20 also play important roles in the specificity of SET8. The enzyme accepts majorly I at the -1 position followed by V. Other hydrophobic amino acids like F, Y and L give weaker methylation signals. SET8 also exhibits strong specificity on L22 and R23. At L22 some other hydrophobic amino acids are tolerated. At the +3 position, SET8 majorly prefers R, however it exhibits weak methylation when itis exchanged with other amino acids. SET8 activity is strongly reduced by the arginine methylation at positions R17 in case of H4 and R379 in case of p53
Products: -
?
additional information
?
-
-
Substrates: enzyme binding to the nucleosome protects it from degradation during the cell cycle. Full length enzyme has 3.8% of its histone methyltransferase activity on nucleosomes containing the H2A/E61A/ E64A/D90A/E92A mutations compared to wild type nucleosomes
Products: -
?
additional information
?
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
additional information
?
-
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
additional information
?
-
Substrates: no methylation of Numb protein by the enzyme is detectable
Products: -
?
additional information
?
-
Substrates: the enzyme interacts with the UBC9 E2 SUMO conjugating enzyme and is preferentially modified with SUMO1 in vivo
Products: -
?
additional information
?
-
-
Substrates: the enzyme interacts with the UBC9 E2 SUMO conjugating enzyme and is preferentially modified with SUMO1 in vivo
Products: -
?
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3 S-adenosyl-L-methionine + a [histone H4]-L-lysine20
3 S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-methionine + a [histone H4]-N6,N6-dimethyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [p53]-L-lysine382
S-adenosyl-L-homocysteine + [p53]-N6-methyl-L-lysine382
Substrates: -
Products: -
?
additional information
?
-
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: highly specific substrate
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + a [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Substrates: highly specific substrate
Products: -
?
additional information
?
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
additional information
?
-
Substrates: the proteolytic degradation of the enzyme is controlled by the SCFSlimb ligase complex
Products: -
?
additional information
?
-
-
Substrates: enzyme binding to the nucleosome protects it from degradation during the cell cycle. Full length enzyme has 3.8% of its histone methyltransferase activity on nucleosomes containing the H2A/E61A/ E64A/D90A/E92A mutations compared to wild type nucleosomes
Products: -
?
additional information
?
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
additional information
?
-
-
Substrates: the enzyme is completely inactive toward histone H4 with a K20L mutation
Products: -
?
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Adenocarcinoma
SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma.
Anemia
The histone methyltransferase Setd8 alters the chromatin landscape and regulates the expression of key transcription factors during erythroid differentiation.
Anemia
The Methyltransferase Setd8 Is Essential for Erythroblast Survival and Maturation.
Breast Neoplasms
Genetic Variability in the microRNA Binding Sites of BMPR1B, TGFBR1, IQGAP1, KRAS, SETD8 and RYR3 and Risk of Breast Cancer in Colombian Women.
Breast Neoplasms
Loss of DNA Methylation and Histone H4 Lysine 20 Trimethylation in Human Breast Cancer Cells is Associated with Aberrant Expression of DNA Methyltransferase 1, Suv4-20h2 Histone Methyltransferase and Methyl-Binding Proteins.
Breast Neoplasms
Monomethyltransferase SETD8 regulates breast cancer metabolism via stabilizing hypoxia-inducible factor 1?.
Breast Neoplasms
N-peptide of vMIP-? reverses paclitaxel-resistance by regulating miRNA-335 in breast cancer.
Carcinogenesis
Combined functional genomic and chemical screens identify SETD8 as a therapeutic target in MYC-driven medulloblastoma.
Carcinogenesis
Discovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8.
Carcinogenesis
Downregulation of SETD8 by miR-382 is involved in glioma progression.
Carcinogenesis
Epigenetic Modifier SETD8 as a Therapeutic Target for High-Grade Serous Ovarian Cancer.
Carcinogenesis
Histone H3 lysine 9 and H4 lysine 20 trimethylation and the expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in hepatocarcinogenesis induced by methyl deficiency in rats.
Carcinogenesis
Histone lysine methyltransferase SETD8 promotes carcinogenesis by deregulating PCNA expression.
Carcinogenesis
Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro.
Carcinogenesis
miR-382 inhibits tumor progression by targeting SETD8 in non-small cell lung cancer.
Carcinogenesis
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Carcinogenesis
SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma.
Carcinogenesis
The histone lysine methyltransferase SETD8 regulates angiogenesis through HES-1 in human umbilical vein endothelial cells.
Carcinogenesis
[The biological functions of lysine methyltransferase PR-SET7].
Carcinoma
KMT5A promotes metastasis of clear cell renal cell carcinoma through reducing cadherin-1 expression.
Carcinoma, Non-Small-Cell Lung
miR-382 inhibits tumor progression by targeting SETD8 in non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Carcinoma, Renal Cell
KMT5A promotes metastasis of clear cell renal cell carcinoma through reducing cadherin-1 expression.
Chagas Disease
Antiproliferative effects of delta 24(25) sterol methyl transferase inhibitors on Trypanosoma (Schizotrypanum) cruzi: in vitro and in vivo studies.
Colitis
SETD8 involved in the progression of inflammatory bowel disease via epigenetically regulating p62 expression.
COVID-19
Comparative evaluation of 19 reverse transcription loop-mediated isothermal amplification assays for detection of SARS-CoV-2.
Diabetic Nephropathies
ets1 associates with KMT5A to participate in high glucose-mediated EndMT via upregulation of PFN2 expression in diabetic nephropathy.
Friedreich Ataxia
Inhibition of the SUV4-20 H1 histone methyltransferase increases frataxin expression in Friedreich's ataxia patient cells.
Glioma
Downregulation of SETD8 by miR-382 is involved in glioma progression.
Glioma
Epigenetic therapy with inhibitors of histone methylation suppresses DNA damage signaling and increases glioma cell radiosensitivity.
Infections
Suv4-20h2 protects against influenza virus infection by suppression of chromatin loop formation.
Infertility
PR-Set7 deficiency limits uterine epithelial population growth hampering postnatal gland formation in mice.
Inflammatory Bowel Diseases
SETD8 involved in the progression of inflammatory bowel disease via epigenetically regulating p62 expression.
Influenza, Human
Suv4-20h2 protects against influenza virus infection by suppression of chromatin loop formation.
Leukemia
Identification of PR-SET7 and EZH2 selective inhibitors inducing cell death in human leukemia U937 cells.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Suv4-20h1 promotes G1 to S phase transition by downregulating p21
Lung Neoplasms
miR-382 inhibits tumor progression by targeting SETD8 in non-small cell lung cancer.
Lung Neoplasms
PR-Set7 is Degraded in a Conditional Cul4A Transgenic Mouse Model of Lung Cancer.
Lung Neoplasms
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Lymphatic Metastasis
Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro.
Lymphatic Metastasis
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Lymphatic Metastasis
SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma.
Medulloblastoma
Combined functional genomic and chemical screens identify SETD8 as a therapeutic target in MYC-driven medulloblastoma.
Multiple Myeloma
Targeting the methyltransferase SETD8 impairs tumor cell survival and overcomes drug resistance independently of p53 status in multiple myeloma.
Neoplasm Metastasis
Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro.
Neoplasm Metastasis
KMT5A promotes metastasis of clear cell renal cell carcinoma through reducing cadherin-1 expression.
Neoplasm Metastasis
MicroRNA-384 downregulates SETD8 expression to suppress cell growth and metastasis in osteosarcoma cells.
Neoplasm Metastasis
miR-382 inhibits tumor progression by targeting SETD8 in non-small cell lung cancer.
Neoplasm Metastasis
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Neoplasm Metastasis
SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma.
Neoplasm Metastasis
[The biological functions of lysine methyltransferase PR-SET7].
Neoplasms
Combined functional genomic and chemical screens identify SETD8 as a therapeutic target in MYC-driven medulloblastoma.
Neoplasms
Downregulation of SETD8 by miR-382 is involved in glioma progression.
Neoplasms
Functional polymorphism at the miR-502-binding site in the 3' untranslated region of the SETD8 gene increased the risk of prostate cancer in a sample of Iranian population.
Neoplasms
Gene Expression Analysis of Two Epithelial-mesenchymal Transition-related Genes: Long Noncoding RNA-ATB and SETD8 in Gastric Cancer Tissues.
Neoplasms
Histone H3 lysine 9 and H4 lysine 20 trimethylation and the expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in hepatocarcinogenesis induced by methyl deficiency in rats.
Neoplasms
Histone lysine methyltransferase SETD8 promotes carcinogenesis by deregulating PCNA expression.
Neoplasms
KMT5A promotes metastasis of clear cell renal cell carcinoma through reducing cadherin-1 expression.
Neoplasms
Loss of miR-217 promotes osteosarcoma cell proliferation through targeting SETD8.
Neoplasms
Meiotic gatekeeper STRA8 regulates cell cycle by interacting with SETD8 during spermatogenesis.
Neoplasms
Methyl deficiency, alterations in global histone modifications, and carcinogenesis.
Neoplasms
MicroRNA-384 downregulates SETD8 expression to suppress cell growth and metastasis in osteosarcoma cells.
Neoplasms
miR-382 inhibits tumor progression by targeting SETD8 in non-small cell lung cancer.
Neoplasms
MiR-502/SET8 regulatory circuit in pathobiology of breast cancer.
Neoplasms
Monomethyltransferase SETD8 regulates breast cancer metabolism via stabilizing hypoxia-inducible factor 1?.
Neoplasms
mRNA expression profiling of histone modifying enzymes in pediatric acute monoblastic leukemia.
Neoplasms
PR-Set7 is Degraded in a Conditional Cul4A Transgenic Mouse Model of Lung Cancer.
Neoplasms
SETD8 is a prognostic biomarker that contributes to stem-like cell properties in non-small cell lung cancer.
Neoplasms
SETD8 potentiates constitutive ERK1/2 activation via epigenetically silencing DUSP10 expression in pancreatic cancer.
Neoplasms
SETD8 promotes stemness characteristics and is a potential prognostic biomarker of gastric adenocarcinoma.
Neoplasms
Structure-activity relationship studies of SETD8 inhibitors.
Neoplasms
Structures of Nahuoic Acids B-E Produced in Culture by a Streptomyces sp. Isolated from a Marine Sediment and Evidence for the Inhibition of the Histone Methyl Transferase SETD8 in Human Cancer Cells by Nahuoic Acid A.
Neoplasms
Targeting the methyltransferase SETD8 impairs tumor cell survival and overcomes drug resistance independently of p53 status in multiple myeloma.
Neoplasms
The histone lysine methyltransferase SETD8 regulates angiogenesis through HES-1 in human umbilical vein endothelial cells.
Neoplasms
The PR-Set7 binding domain of Riz1 is required for the H4K20me1-H3K9me1 trans-tail 'histone code' and Riz1 tumor suppressor function.
Neoplasms
Turning a Substrate Peptide into a Potent Inhibitor for the Histone Methyltransferase SETD8.
Neoplasms
[The biological functions of lysine methyltransferase PR-SET7].
Neuroblastoma
Epigenetic siRNA and Chemical Screens Identify SETD8 Inhibition as a Therapeutic Strategy for p53 Activation in High-Risk Neuroblastoma.
Osteosarcoma
Loss of miR-217 promotes osteosarcoma cell proliferation through targeting SETD8.
Osteosarcoma
MicroRNA-127-3p inhibits proliferation and invasion by targeting SETD8 in human osteosarcoma cells.
Osteosarcoma
MicroRNA-384 downregulates SETD8 expression to suppress cell growth and metastasis in osteosarcoma cells.
Osteosarcoma
Structures of Nahuoic Acids B-E Produced in Culture by a Streptomyces sp. Isolated from a Marine Sediment and Evidence for the Inhibition of the Histone Methyl Transferase SETD8 in Human Cancer Cells by Nahuoic Acid A.
Ovarian Neoplasms
Epigenetic Modifier SETD8 as a Therapeutic Target for High-Grade Serous Ovarian Cancer.
Pancreatic Neoplasms
SETD8 potentiates constitutive ERK1/2 activation via epigenetically silencing DUSP10 expression in pancreatic cancer.
Pituitary Neoplasms
LncRNA LINC00473 is involved in the progression of invasive pituitary adenoma by upregulating KMT5A via ceRNA-mediated miR-502-3p evasion.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Association of functional polymorphism at the miR-502-binding site in the 3' untranslated region of the SETD8 gene with risk of childhood acute lymphoblastic leukemia, a preliminary report.
Prostatic Neoplasms
Functional polymorphism at the miR-502-binding site in the 3' untranslated region of the SETD8 gene increased the risk of prostate cancer in a sample of Iranian population.
Prostatic Neoplasms
Histone H4 Lys 20 methyltransferase SET8 promotes androgen receptor-mediated transcription activation in prostate cancer.
Retinoblastoma
The SETD8/PR-Set7 Methyltransferase Functions as a Barrier to Prevent Senescence-Associated Metabolic Remodeling.
Stomach Neoplasms
Gene Expression Analysis of Two Epithelial-mesenchymal Transition-related Genes: Long Noncoding RNA-ATB and SETD8 in Gastric Cancer Tissues.
Thyroid Cancer, Papillary
Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro.
Virus Diseases
Suv4-20h2 protects against influenza virus infection by suppression of chromatin loop formation.
[histone h4]-lysine20 n-methyltransferase deficiency
PR-Set7 deficiency limits uterine epithelial population growth hampering postnatal gland formation in mice.
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metabolism
enzyme-mediated methylation of histone H4 lysine 20 maintains silent chromatin, in part, by precluding neighboring acetylation on the histone H4 tail
malfunction
enzyme deficiency confers an impaired glucose metabolism phenotype and thus inhibits the progression of hepatocellular carcinoma tumors
malfunction
enzyme depletion results in decondensed chromosomes and centrosome amplification
malfunction
enzyme gene disruption results in lethality
malfunction
enzyme inhibition attenuates proliferation and induces apoptosis. Cell migration and invasion are suppressed in enzyme-knockdown cells. Enzyme inhibition arrests the cell cycle in the G1/S phase of papillary thyroid cancer cells. Enzyme inhibition suppresses the expression of SREBP1, SCD, FASN and ACC, key molecules involved in lipid metabolism and decreases the level of malondialdehyde in papillary thyroid cancer cells
malfunction
enzyme knockdown inhibits proliferation, induces apoptosis, suppresses migration and invasion of esophageal squamous cell carcinoma cells
malfunction
enzyme loss triggers cellular senescence
malfunction
expression of an enzyme mutant insensitive to degradation during S phase causes the maintenance of monomethylated histone H4 lysine 20 and repeated DNA replication at origins
malfunction
-
inappropriate enzyme levels result in profound cell cycle defects including the inability to initiate S phase, the re-replication of DNA and the improper timing of mitotic progression
physiological function
-
methylation of histone H4 lysine 20 by the enzyme is essential for development and viability in Drosophila
physiological function
Slimb-mediated enzyme proteolysis is a critical regulatory mechanism required for proper interphase chromatin organization at G1/S transition
physiological function
the enzyme activity is essential for cell cycle progression, mitotic entry and genomic stability
physiological function
the enzyme controls both histone H4 lysine 16 acetylation and histone H4 lysine 20 trimethylation and in doing so, regulates RNA polymerase II pausing dynamics. Enzyme-mediated histone H4 lysine 20 monomethylation is necessary for the recruitment of the male-specific lethal complex, subsequent histone H4 lysine 16 acetylation, and release of RNA polymerase II into active elongation
physiological function
the enzyme facilitates hepatocellular carcinoma growth by enhancing aerobic glycolysis. The enzyme directly binds to and inactivates KLF4
physiological function
the enzyme functions as a barrier to prevent senescence-associated metabolic remodeling. The enzyme represses senescence-associated genes including ribosomal proteins, ribosomal RNAs, and p16INK4A by catalyzing mono-methylation of histone H4 at lysine 20
physiological function
the enzyme is a sensory rheostat that reinforces developmental fates in response to environmental cues by modulating autocrine and paracrine DAF-2 insulin-like signaling. The enzyme acts specifically in the DAF-2/InsR pathway to promote dauer arrest in neurons
physiological function
the enzyme is an oncogenic factor, specifically a regulator for lipid metabolism in papillary thyroid carcinoma
physiological function
the enzyme is essential for Drosophila development
physiological function
the enzyme is not required for survival and does not control position-effect variegation
physiological function
-
the enzyme is required for mitotic entry and essential for proper cell cycle progression. The degradation of the enzyme, mediated by the SCFSkp2 ubiquitin ligase, is required for the initiation of S phase by removing enzyme from chromatin and derepressing the expression of E2F-target genes
physiological function
the enzyme is required for normal cell cycle progression
physiological function
the enzyme plays a critical role in chromatin events that regulate replication origins. The enzyme undergoes a proliferating cell nuclear antigen- and Cul4-Ddb1 E3-ligase driven degradation during S phase that contributes to the disappearance of monomethylated histone H4 lysine 20 at origins and the inhibition of replication licensing
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Zhang, X.; Bruice, T.
Product specificity and mechanism of protein lysine methyltransferases: Insights from the histone lysine methyltransferase SET8
Biochemistry
47
6671-6677
2008
Homo sapiens
brenda
Kudithipudi, S.; Dhayalan, A.; Kebede, A.F.; Jeltsch, A.
The SET8 H4K20 protein lysine methyltransferase has a long recognition sequence covering seven amino acid residues
Biochimie
94
2212-2218
2012
Homo sapiens
brenda
Tryndyak, V.P.; Kovalchuk, O.; Pogribny, I.P.
Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins
Cancer Biol. Ther.
5
65-70
2006
Homo sapiens (Q86Y97), Homo sapiens
brenda
Wu, S.; Rice, J.C.
A new regulator of the cell cycle the PR-Set7 histone methyltransferase
Cell Cycle
10
68-72
2011
Homo sapiens
brenda
Chen, X.; Ding, X.; Wu, Q.; Qi, J.; Zhu, M.; Miao, C.
Monomethyltransferase SET8 facilitates hepatocellular carcinoma growth by enhancing aerobic glycolysis
Cell Death Dis.
10
312
2019
Homo sapiens (Q9NQR1)
brenda
Tanaka, H.; Takebayashi, S.I.; Sakamoto, A.; Igata, T.; Nakatsu, Y.; Saitoh, N.; Hino, S.; Nakao, M.
The SETD8/PR-Set7 methyltransferase functions as a barrier to prevent senescence-associated metabolic remodeling
Cell Rep.
18
2148-2161
2017
Homo sapiens (Q9NQR1)
brenda
Fang, J.; Feng, Q.; Ketel, C.S.; Wang, H.; Cao, R.; Xia, L.; Erdjument-Bromage, H.; Tempst, P.; Simon, J.A.; Zhang, Y.
Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase
Curr. Biol.
12
1086-1099
2002
Drosophila melanogaster (Q9VFK6), Homo sapiens (Q9NQR1), Homo sapiens
brenda
Delaney, C.E.; Chen, A.T.; Graniel, J.V.; Dumas, K.J.; Hu, P.J.
A histone H4 lysine 20 methyltransferase couples environmental cues to sensory neuron control of developmental plasticity
Development
144
1273-1282
2017
Caenorhabditis elegans (Q09265)
brenda
Xiao, B.; Jing, C.; Kelly, G.; Walker, P.A.; Muskett, F.W.; Frenkiel, T.A.; Martin, S.R.; Sarma, K.; Reinberg, D.; Gamblin, S.J.; Wilson, J.R.
Specificity and mechanism of the histone methyltransferase Pr-Set7
Genes Dev.
19
1444-1454
2005
Homo sapiens
brenda
Wu, S.; Wang, W.; Kong, X.; Congdon, L.M.; Yokomori, K.; Kirschner, M.W.; Rice, J.C.
Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression
Genes Dev.
24
2531-2542
2010
Homo sapiens (Q9NQR1)
brenda
Sakaguchi, A.; Karachentsev, D.; Seth-Pasricha, M.; Druzhinina, M.; Steward, R.
Functional characterization of the Drosophila Hmt4-20/Suv4-20 histone methyltransferase
Genetics
179
317-322
2008
Drosophila melanogaster (Q9W5E0)
brenda
Houston, S.I.; McManus, K.J.; Adams, M.M.; Sims, J.K.; Carpenter, P.B.; Hendzel, M.J.; Rice, J.C.
Catalytic function of the PR-Set7 histone H4 lysine 20 monomethyltransferase is essential for mitotic entry and genomic stability
J. Biol. Chem.
283
19478-19488
2008
Homo sapiens (Q9NQR1)
brenda
Kapoor-Vazirani, P.; Vertino, P.M.
A dual role for the histone methyltransferase PR-SET7/SETD8 and histone H4 lysine 20 monomethylation in the local regulation of RNA polymerase II pausing
J. Biol. Chem.
289
7425-7437
2014
Homo sapiens (Q9NQR1)
brenda
Girish, T.; McGinty, R.; Tan, S.
Multivalent interactions by the Set8 histone methyltransferase with its nucleosome substrate
J. Mol. Biol.
428
1531-1543
2016
Homo sapiens
brenda
Nishioka, K.; Rice, J.C.; Sarma, K.; Erdjument-Bromage, H.; Werner, J.; Wang, Y.; Chuikov, S.; Valenzuela, P.; Tempst, P.; Steward, R.; Lis, J.T.; Allis, C.D.; Reinberg, D.
PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin
Mol. Cell
9
1201-1213
2002
Drosophila melanogaster, Homo sapiens (Q9NQR1), Homo sapiens
brenda
Tardat, M.; Brustel, J.; Kirsh, O.; Lefevbre, C.; Callanan, M.; Sardet, C.; Julien, E.
The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
Nat. Cell Biol.
12
1086-1093
2010
Homo sapiens (Q9NQR1)
brenda
Zouaz, A.; Fernando, C.; Perez, Y.; Sardet, C.; Julien, E.; Grimaud, C.
Cell-cycle regulation of non-enzymatic functions of the Drosophila methyltransferase PR-Set7
Nucleic Acids Res.
46
2834-2849
2018
Drosophila melanogaster (Q9VFK6)
brenda
Liao, T.; Wang, Y.J.; Hu, J.Q.; Wang, Y.; Han, L.T.; Ma, B.; Shi, R.L.; Qu, N.; Wei, W.J.; Guan, Q.; Xiang, J.; Chen, J.Y.; Sun, G.H.; Li, D.S.; Mu, X.M.; Ji, Q.H.
Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro
Oncol. Rep.
39
2185-2192
2018
Homo sapiens (Q9NQR1)
brenda
Spektor, T.M.; Congdon, L.M.; Veerappan, C.S.; Rice, J.C.
The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression
PLoS ONE
6
e22785
2011
Homo sapiens (Q9NQR1), Homo sapiens
brenda
Weirich, S.; Kusevic, D.; Kudithipudi, S.; Jeltsch, A.
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
Sci. Rep.
5
13813
2015
Homo sapiens (Q9NQR1)
brenda
Wang, C.; Wu, J.; Zhao, Y.; Guo, Z.
MiR-502 mediated histone methyltransferase SET8 expression is associated with outcome of esophageal squamous cell carcinoma
Sci. Rep.
6
32921
2016
Homo sapiens (Q9NQR1)
brenda