PRMT8
entrez
56341
canonical
uniprot
Q9NR22
canonical
ensembl
ENSG00000111218
resolver
ensp
ENSP00000372067
resolver
ensp
ENSP00000414507
resolver
ensp
ENSP00000639714
resolver
ensp
ENSP00000688647
resolver
genesymbol
PRMT8
resolver
genesymbol_syn
HRMT1L3
resolver
genesymbol_syn
HRMT1L4
resolver
hgnc
HGNC:5188
resolver
uniprot
B2RDP0
resolver
uniprot
Q59GT2
resolver
uniprot
Q8TBJ8
resolver
uniprot_entry
ANM8_HUMAN
resolver
uniprot_entry
Q59GT2_HUMAN
resolver
uniprot_sec
B2RDP0
resolver
uniprot_sec
Q8TBJ8
resolver
amino_acid_sequence
MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGKMSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR
uniprot
proteins
ec_number
2.1.1.319
uniprot
proteins
function
FUNCTION: 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:26529540, PubMed:26876602). 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). {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:26529540, ECO:0000269|PubMed:26876602}.
uniprot
proteins
mass_dalton
45291
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Loss of cell membrane localization."; /evidence="ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:26876602"; MUTAGEN 273; /note="C->A: No effect on homodimerization but decreased homooligomerization; when associated with A-295 and A-349."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 295; /note="C->A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-349."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 303; /note="Y->A: Decreases homooligomerization and cell membrane localization. No effect on homodimerization, S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-345 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-345 and A-382."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 345; /note="Y->A: No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-382."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 349; /note="R->A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-295."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 382; /note="L->A: No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-345. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-345."; /evidence="ECO:0000269|PubMed:26876602
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
PRMT8 subfamily
uniprot
proteins
protein_family
Protein arginine N-methyltransferase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16051612
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17925405
uniprot
proteins
pubmed
18320585
uniprot
proteins
pubmed
26529540
uniprot
proteins
pubmed
26876602
uniprot
proteins
sequence_length
394
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:26876602}; Lipid-anchor {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:26876602}; Cytoplasmic side {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:26876602}.
uniprot
proteins