Q6NUA1 · ANM5_XENLA

Function

function

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; such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. May act as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1. Involved in spliceosome maturation and mRNA splicing (By similarity).

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site320S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site323L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate
Binding site329-330S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site388S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site414-416S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site431Proton donor/acceptor
Binding site431L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate
Active site440Proton donor/acceptor
Binding site440L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate
Binding site440S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular ComponentGolgi apparatus
Cellular Componentmethylosome
Cellular Componentnucleus
Molecular FunctionE-box binding
Molecular Functionhistone H2AR3 methyltransferase activity
Molecular Functionhistone H4R3 methyltransferase activity
Molecular Functionprotein-arginine omega-N symmetric methyltransferase activity
Molecular Functiontranscription corepressor activity
Biological Processcell division
Biological Processcircadian regulation of gene expression
Biological ProcessGolgi ribbon formation
Biological Processmethylation
Biological Processmitotic DNA replication checkpoint signaling
Biological Processpositive regulation of proteasomal protein catabolic process
Biological Processregulation of mitotic nuclear division

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein arginine N-methyltransferase 5
  • EC number
  • Short names
    prmt5
  • Alternative names
    • Histone synthetic lethal 7 protein (Hsl7)
    • Histone-arginine N-methyltransferase PRMT5

Gene names

    • Name
      prmt5
    • Synonyms
      hsl7

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q6NUA1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004229721-633Protein arginine N-methyltransferase 5

Expression

Tissue specificity

Detected in egg (at protein level).

Gene expression databases

    • 407754Expressed in ovary and 19 other cell types or tissues

Interaction

Subunit

Heterotetramer; dimer of heterodimer with wdr77. Interacts with wee2-a; this interaction is disrupted upon activation of the DNA replication checkpoint.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q6NUA1wdr77 Q6NUD05EBI-21229405, EBI-21229433

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain304-611SAM-dependent MTase PRMT-type

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    633
  • Mass (Da)
    72,285
  • Last updated
    2004-07-05 v1
  • Checksum
    F3A61499DF6623CC
MAAGDGGRVSSGRDVACVTEVADTLGAMANQGFDFLCMPIFHPRFKREFYKEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSDWIKTDSEVSRIRKTSEAAMQQELNFSAYLGLPAFLIPLKQEDNSNLSRLLINHIHVGHHSTMFWMRVPLMAPNDLRDDLIENEPISLSEEDNSGEERTWIWWHNFRSLCDYNKKIALAIEIGADLPSGHVIDRWLGEPIKAAFLPTSIFLTNKKGFPVLTKVHQRLIFKLFKLEVQFVISGSHHHSEKDLCSYLQYLEYLSQNSPPPNAYEMFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPVKYSQYQQAVYKCLLDRVPEEEKETNIQILMVLGAGRGPLVNASLRAAKQAERKIKVYAVEKNPNAVITLEGWRYEEWGSQVTVVSGDMREWKAPEKADIIVSELLGSFGDNELSPECLDGAQHFLKDDGVSIPGEYTSYLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSDPLPCFTFHHPNKDDVIDNNRYCCLQYRVDLNTVLHGFAGYFNTVLYKDVTLSICPESHSPGMFSWFPILFPIKQPIPMREGDTVCVRFWRCNNGKKVWYEWAVTSPVCSAIHNPTGRSYTIGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY535008
EMBL· GenBank· DDBJ
AAS98802.1
EMBL· GenBank· DDBJ
mRNA
BC068696
EMBL· GenBank· DDBJ
AAH68696.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp