Tchem | Protein arginine N-methyltransferase 8 |
Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Arginine methylation is involved in a number of cellular processes, including DNA repair, RNA transcription, signal transduction, protein compartmentalization, and possibly protein translation (Lee et al., 2005 [PubMed 16051612]).[supplied by OMIM, Mar 2008]
Comments
Disease | Target Count | P-value |
---|---|---|
lung carcinoma | 2844 | 2.55137399259584E-19 |
atypical teratoid / rhabdoid tumor | 4369 | 7.85472735564766E-14 |
posterior fossa group A ependymoma | 1511 | 1.39443655359816E-11 |
glioblastoma | 5572 | 4.42793929171953E-10 |
pilocytic astrocytoma | 3086 | 7.20922197145204E-10 |
pediatric high grade glioma | 2712 | 1.65929710117679E-8 |
Pick disease | 1893 | 0.00102002692588074 |
sonic hedgehog group medulloblastoma | 1482 | 0.00163354730525693 |
primitive neuroectodermal tumor | 3031 | 0.00166482201116286 |
astrocytic glioma | 2241 | 0.00277112251836435 |
oligodendroglioma | 2849 | 0.0100038707875138 |
Alzheimer's disease | 644 | 0.0324494748084303 |
subependymal giant cell astrocytoma | 2287 | 0.0440074157696937 |
medulloblastoma, large-cell | 6234 | 0.0479207827174012 |
Disease | Target Count | Z-score | Confidence |
---|---|---|---|
multidrug-resistant tuberculosis | 7 | 3.39 | 1.7 |
Ewing sarcoma | 27 | 3.063 | 1.5 |
Disease | log2 FC | p |
---|---|---|
astrocytic glioma | -2.000 | 0.003 |
posterior fossa group A ependymoma | -2.100 | 0.000 |
oligodendroglioma | -1.500 | 0.010 |
glioblastoma | -2.600 | 0.000 |
sonic hedgehog group medulloblastoma | -1.800 | 0.002 |
atypical teratoid / rhabdoid tumor | -2.600 | 0.000 |
medulloblastoma, large-cell | -1.300 | 0.048 |
primitive neuroectodermal tumor | -1.600 | 0.002 |
pediatric high grade glioma | -2.200 | 0.000 |
pilocytic astrocytoma | -2.400 | 0.000 |
subependymal giant cell astrocytoma | -1.494 | 0.044 |
lung carcinoma | 1.600 | 0.000 |
Alzheimer's disease | -1.100 | 0.032 |
Pick disease | -1.300 | 0.001 |
Species | Source |
---|---|
Chimp | OMA EggNOG |
Macaque | OMA EggNOG |
Mouse | OMA EggNOG Inparanoid |
Rat | OMA Inparanoid |
Dog | OMA Inparanoid |
Cow | OMA Inparanoid |
Pig | OMA Inparanoid |
Opossum | OMA Inparanoid |
Chicken | OMA Inparanoid |
Anole lizard | OMA Inparanoid |
Xenopus | OMA Inparanoid |
C. elegans | OMA Inparanoid |
S.cerevisiae | OMA Inparanoid |
CHEMBL3589040
pIC50 6.35
CHEMBL3589043
pIC50 6.46
CHEMBL3589039
pIC50 6.65
CHEMBL3589042
pIC50 6.75
CHEMBL3589035
pIC50 7.16
CHEMBL3589912
pIC50 7.17
CHEMBL3590417
pIC50 7.19
CHEMBL3589034
pIC50 7.26
CHEMBL3589038
pIC50 7.36
CHEMBL3589913
pIC50 7.55
CHEMBL3589036
pIC50 7.64
CHEMBL3589033
pIC50 7.66
CHEMBL3589032
pIC50 7.66
CHEMBL3589037
pIC50 7.68
CHEMBL3589027
pIC50 7.85
CHEMBL3589028
pIC50 8.00
CHEMBL3589026
pIC50 8.00
CHEMBL3589031
pIC50 8.00
CHEMBL3589030
pIC50 8.16
CHEMBL3589029
pIC50 8.70
PMID | Text |
---|---|
26876602 | Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. |
23946480 | automethylation of the N terminus likely regulates PRMT8 activity by decreasing the affinity of the enzyme for AdoMet |
23635657 | Mutational defects in PRMT8 is not the cause of frontotemporal lobar degeneration. |
23620769 | wild type FUS (FUS-WT) specifically interacts with protein arginine methyltransferases 1 and 8 (PRMT1 and PRMT8) and undergoes asymmetric dimethylation |
20379614 | Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator) |
19060911 | Observational study and genome-wide association study of gene-disease association. (HuGE Navigator) |
18698489 | EWS is a substrate for PRMT8, as efficient as for PRMT1 |
18320585 | The interaction between PRMT8 and the EWS protein was charcterized. |
17925405 | PRMT8 N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers. |
16051612 | PRMT8 is an active arginine methyltransferase that is membrane-associated and tissue-specific |
MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEM 1 - 70 TSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGI 71 - 140 ECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKP 141 - 210 GGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDI 211 - 280 YTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRR 281 - 350 GEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR 351 - 394 //
PMID | Year | Title |
---|---|---|
26876602 | 2016 | Novel helical assembly in arginine methyltransferase 8. |
25416956 | 2014 | A proteome-scale map of the human interactome network. |
23946480 | 2013 | Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity. |
23635657 | 2013 | Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS. |
23620769 | 2013 | Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo. |
23455924 | 2013 | A Y2H-seq approach defines the human protein methyltransferase interactome. |
20379614 | Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score. | |
19060911 | 2009 | Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts. |
19060904 | 2009 | An empirical framework for binary interactome mapping. |
18698489 | 2008 | EWS is a substrate of type I protein arginine methyltransferase, PRMT8. |
More... |