Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00100
Entry Name
UniProt Accession
Theoretical PI
6.47
Molecular Weight
45291.16
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein arginine N-methyltransferase 8
Protein Synonyms/Alias
2.1.1.-; Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
Gene Name
PRMT8
Gene Synonyms/Alias
HRMT1L3; HRMT1L4;
Created Date
11-JAN-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGMKHSSRC
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Lee J, Sayegh J, Daniel J, Clarke S, Bedford MT. PRMT8, a new membrane-boundtissue-specific member of the protein arginine methyltransferase family. J BiolChem. 2005 Sep 23;280(38):32890-6. Epub 2005 Jul 28.[PMID:16051612]
Functional Description
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.
Sequence Annotation
Domain: 73 394 SAM-dependent MTase PRMT-type.
Motif: 29 42 SH3-binding 1.
Motif: 53 58 SH3-binding 2.
Active site: 185 185
Active site: 194 194
Binding site: 86 86 S-adenosyl-L-methionine.
Binding site: 95 95 S-adenosyl-L-methionine.
Binding site: 119 119 S-adenosyl-L-methionine; via carbonyloxygen.
Binding site: 141 141 S-adenosyl-L-methionine.
Binding site: 170 170 S-adenosyl-L-methionine.
Modified residue: 58 58 Omega-N-methylarginine; by autocatalysis.
Modified residue: 73 73 Asymmetric dimethylarginine; byautocatalysis.
Protein Length
394 AA.
Protein Sequence
(Canonical)
MGMKHSSRCL LLRRKMAENA AESTEVNSPP SQPPQPVVPA KPVQCVHHVS TQPSCPGRGK  60
MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR NSMYHNKHVF KDKVVLDVGS  120
GTGILSMFAA KAGAKKVFGI ECSSISDYSE KIIKANHLDN IITIFKGKVE EVELPVEKVD  180
IIISEWMGYC LFYESMLNTV IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE  240
NVYGFDMTCI RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR  300
NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR GEEIYGTISM  360
KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR                              394
FASTA
(Canonical)
>LipidDB-9606-00100|Q9NR22
MGMKHSSRCLLLRRKMAENAAESTEVNSPPSQPPQPVVPAKPVQCVHHVSTQPSCPGRGK
MSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGS
GTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVD
IIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWE
NVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQR
NDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISM
KPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR
Gene Ontology
GO:0005829; C:cytosol; IBA:RefGenome
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IBA:RefGenome
GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:HGNC
GO:0042802; F:identical protein binding; IPI:IntAct
GO:0046982; F:protein heterodimerization activity; IDA:HGNC
GO:0042803; F:protein homodimerization activity; IDA:HGNC
GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:UniProtKB
GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB
GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:HGNC
GO:0034969; P:histone arginine methylation; IDA:GOC
GO:0043985; P:histone H4-R3 methylation; IBA:GOC
GO:0016571; P:histone methylation; IDA:HGNC
GO:0018216; P:peptidyl-arginine methylation; IDA:UniProtKB
GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:HGNC
GO:0043393; P:regulation of protein binding; TAS:HGNC
GO:0006355; P:regulation of transcription, DNA-templated; IBA:RefGenome
Interpro
InterPro; IPR025799; Arg_MeTrfase
InterPro; IPR010456; Ribosomal-L11_MeTrfase_PrmA
InterPro; IPR029063; SAM-dependent_MTases-like
Pfam
Pfam; PF06325; PrmA;
SMART
PROSITE
PROSITE; PS51678; SAM_MT_PRMT;
PRINTS