1. Home
  2. Targets
  3. transferase
  4. methyltransferase
  5. Protein arginine N-methyltransferase 8

Tchem Protein arginine N-methyltransferase 8

Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.

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

Property Summary

Ligand Count 20
NCBI Gene PubMed Count 18
PubMed Score 20.53
PubTator Score 11.07

Knowledge Summary

Patent

No data available

TINX Plot

  Disease (3)

Disease Target Count Z-score Confidence
Carcinoma 11493 0.0 0.8
Disease Target Count Z-score Confidence
multidrug-resistant tuberculosis 7 3.264 1.6

Expression

  Differential Expression (14)

Disease log2 FC p
adult high grade glioma -1.800 2.0e-03
Alzheimer's disease -1.100 3.2e-02
astrocytic glioma -2.000 2.8e-03
Astrocytoma, Pilocytic -2.200 2.1e-07
atypical teratoid / rhabdoid tumor -2.000 2.1e-09
ependymoma -1.700 1.0e-02
glioblastoma -2.000 8.7e-10
group 4 medulloblastoma -1.500 1.0e-02
lung carcinoma 1.600 2.6e-19
medulloblastoma, large-cell -1.300 4.8e-02
oligodendroglioma -1.500 1.0e-02
Pick disease -1.300 1.0e-03
primitive neuroectodermal tumor -1.300 5.6e-03
subependymal giant cell astrocytoma -1.494 4.4e-02

Synonym

Accession Q9NR22 B2RDP0 Q8TBJ8
Symbols HRMT1L3
HRMT1L4

Gene

PRMT8

PANTHER Protein Class (2)

PDB

4X41   5DST  

  Ortholog (1)

Species Source Disease
Chimp OMA EggNOG

 UniProt Keyword (13)

See all...

 GO Function (7)

 GO Component (2)

 GO Process (5)

 Compartment GO Term (11)

 MGI Phenotype (2)

 GWAS Trait (2)

 HCA RNA Cell Line (13)

See all...

Protein-protein Interaction (20)

EWSR1   VIM   INA   HNRNPU   FAM120A   DHX9   HNRNPR   SYNCRIP   PRMT1   BCLAF1   THRAP3   LSM14A   HNRNPUL2   HNRNPA1   CHTOP   FBXW11   HNRNPK   SCAF11   ALYREF   ANGEL2  

Ligand (20)

Structure of CHEMBL3589040

CHEMBL3589040
pIC50 6.35

Structure of CHEMBL3589043

CHEMBL3589043
pIC50 6.46

Structure of CHEMBL3589039

CHEMBL3589039
pIC50 6.65

Structure of CHEMBL3589042

CHEMBL3589042
pIC50 6.75

Structure of CHEMBL3589035

CHEMBL3589035
pIC50 7.16

Structure of CHEMBL3589912

CHEMBL3589912
pIC50 7.17

Structure of CHEMBL3590417

CHEMBL3590417
pIC50 7.19

Structure of CHEMBL3589034

CHEMBL3589034
pIC50 7.26

Structure of CHEMBL3589038

CHEMBL3589038
pIC50 7.36

Structure of CHEMBL3589913

CHEMBL3589913
pIC50 7.55

Structure of CHEMBL3589036

CHEMBL3589036
pIC50 7.64

Structure of CHEMBL3589033

CHEMBL3589033
pIC50 7.66

Structure of CHEMBL3589032

CHEMBL3589032
pIC50 7.66

Structure of CHEMBL3589037

CHEMBL3589037
pIC50 7.68

Structure of CHEMBL3589027

CHEMBL3589027
pIC50 7.85

Structure of CHEMBL3589028

CHEMBL3589028
pIC50 8.00

Structure of CHEMBL3589026

CHEMBL3589026
pIC50 8.00

Structure of CHEMBL3589031

CHEMBL3589031
pIC50 8.00

Structure of CHEMBL3589030

CHEMBL3589030
pIC50 8.16

Structure of CHEMBL3589029

CHEMBL3589029
pIC50 8.70

Gene RIF (10)

AA Sequence 

MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEM      1 - 70
TSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGI     71 - 140
ECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKP    141 - 210
GGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDI    211 - 280
YTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRR    281 - 350
GEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR                              351 - 394
//

Text Mined References (19)

PMID Year Title