Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

PRMT8 (Q9NR22) - Overview - Molecular Target Synopsis

Protein


PRMT8, Protein arginine N-methyltransferase 8
Enzyme Classification 2.1.1.319
UniProt Q9NR22

Also Known as ANM8_HUMAN, PRMT8, HRMT1L3, HRMT1L4

S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602, PubMed:26529540). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (PubMed:18320585). Homodimer (PubMed:16051612, PubMed:26876602, PubMed:26529540). Tetramer; individual homodimers associates to form a homotetramer (PubMed:26529540). Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane (PubMed:26876602). Heterodimer with PRMT1; heterodimerization may recruit PRMT1 activity to the plasma membrane (PubMed:16051612). Interacts with PRMT2 (via the SH3 domain) (PubMed:17925405). Interacts with FYN (via the SH3 domain) (PubMed:17925405). Interacts with EWS; independently of EWS methylation status (PubMed:18320585).

5DST
CRYSTAL STRUCTURE OF HUMAN PRMT8 IN COMPLEX WITH SAH
RCSB/PDB
Inspect Structure
See all 3D Structures for PRMT8

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
394ENSG00000111218ENST00000382622ENSP00000372067Q9NR22-1
385ENSG00000111218ENST00000452611ENSP00000414507Q9NR22-2

Sub-cellular localization


UniProt: PRMT8 is active in the following subcellular-locations: cell membrane.
GO terms: PRMT8 is active in the following subcellular-locations: anchored component of the cytoplasmic side of the plasma membrane, cytosol, plasma membrane.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project PRMT8 has gain in 6 cell-lines, loss in 1 cell-lines and no signal in 998 cell-lines. (see details)

Gene Expression


In NCI60, the highest expressing cell lines are: SK_OV_3, LOXIMVI, MCF7

In Array Express (RNA-seq of 675 commonly used human cancer cell lines), the highest expressing cell lines are: DMS 53, Hs 746T, LN-18

In Array Express (RNA-seq of long poly adenylated RNA and long non poly adenylated RNA from ENCODE cell lines), the highest expressing cell lines are: SK-N-SH, NHLF, HSMM

(see details)

3D Structures


For PRMT8 there are:
2 structures (17 chains) solved
2 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


PRMT8 has been screened with 48 compounds (52 bioactivities), 23 compounds have bioactivities that show binding affinity of <= 500nM (26 bioactivities). (see details)