CPLM-016905

Genbank Nucleotide ID

Protein arginine N-methyltransferase 5

Protein Synonyms/Alias

Histone-arginine N-methyltransferase PRMT5; Jak-binding protein 1; Shk1 kinase-binding protein 1 homolog; SKB1 homolog

Mus musculus (Mouse)

Position	Peptide	Type	References
95	PWIHPDSKVEKIRRN	ubiquitination	[1]
227	RWLGEPIKAAILPTS	ubiquitination	[1]
240	TSIFLTNKKGFPVLS	ubiquitination	[1]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional Description

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation.

REGION 13 292 TIM barrel (By similarity).
REGION 333 334 S-adenosyl-L-methionine binding (By
REGION 419 420 S-adenosyl-L-methionine binding (By
REGION 465 637 Beta barrel (By similarity).
REGION 488 494 Dimerization (By similarity).
ACT_SITE 435 435 Proton donor/acceptor (By similarity).
ACT_SITE 444 444 Proton donor/acceptor (By similarity).
BINDING 304 304 Peptide substrate (By similarity).
BINDING 307 307 Peptide substrate (By similarity).
BINDING 324 324 S-adenosyl-L-methionine (By similarity).
BINDING 392 392 S-adenosyl-L-methionine (By similarity).
MOD_RES 2 2 N-acetylalanine (By similarity).

Acetylation; Chromatin regulator; Complete proteome; Cytoplasm; Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0043234; C:protein complex; IEA:Compara.
GO:0003682; F:chromatin binding; IMP:MGI.
GO:0008469; F:histone-arginine N-methyltransferase activity; IEA:EC.
GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
GO:0043021; F:ribonucleoprotein complex binding; IEA:Compara.
GO:0042118; P:endothelial cell activation; IEA:Compara.
GO:0034969; P:histone arginine methylation; IEA:GOC.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR025799; Arg_MeTrfase.
IPR007857; Arg_MeTrfase_PRMT5.