Q6NUA1 · ANM5_XENLA
- ProteinProtein arginine N-methyltransferase 5
- Geneprmt5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids633 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H+ + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 320 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 323 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: F | ||||||
Binding site | 329-330 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: KY | ||||||
Binding site | 388 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 414-416 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GDM | ||||||
Active site | 431 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 431 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: E | ||||||
Active site | 440 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 440 | L-arginine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI); substrate | ||||
Sequence: E | ||||||
Binding site | 440 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | methylosome | |
Cellular Component | nucleus | |
Molecular Function | E-box binding | |
Molecular Function | histone H2AR3 methyltransferase activity | |
Molecular Function | histone H4R3 methyltransferase activity | |
Molecular Function | protein-arginine omega-N symmetric methyltransferase activity | |
Molecular Function | transcription corepressor activity | |
Biological Process | cell division | |
Biological Process | circadian regulation of gene expression | |
Biological Process | Golgi ribbon formation | |
Biological Process | methylation | |
Biological Process | mitotic DNA replication checkpoint signaling | |
Biological Process | positive regulation of proteasomal protein catabolic process | |
Biological Process | regulation of mitotic nuclear division |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein arginine N-methyltransferase 5
- EC number
- Short namesprmt5
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionQ6NUA1
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Enriched on chromatin.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422972 | 1-633 | Protein arginine N-methyltransferase 5 | |||
Sequence: MAAGDGGRVSSGRDVACVTEVADTLGAMANQGFDFLCMPIFHPRFKREFYKEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSDWIKTDSEVSRIRKTSEAAMQQELNFSAYLGLPAFLIPLKQEDNSNLSRLLINHIHVGHHSTMFWMRVPLMAPNDLRDDLIENEPISLSEEDNSGEERTWIWWHNFRSLCDYNKKIALAIEIGADLPSGHVIDRWLGEPIKAAFLPTSIFLTNKKGFPVLTKVHQRLIFKLFKLEVQFVISGSHHHSEKDLCSYLQYLEYLSQNSPPPNAYEMFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPVKYSQYQQAVYKCLLDRVPEEEKETNIQILMVLGAGRGPLVNASLRAAKQAERKIKVYAVEKNPNAVITLEGWRYEEWGSQVTVVSGDMREWKAPEKADIIVSELLGSFGDNELSPECLDGAQHFLKDDGVSIPGEYTSYLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSDPLPCFTFHHPNKDDVIDNNRYCCLQYRVDLNTVLHGFAGYFNTVLYKDVTLSICPESHSPGMFSWFPILFPIKQPIPMREGDTVCVRFWRCNNGKKVWYEWAVTSPVCSAIHNPTGRSYTIGL |
Expression
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6NUA1 | wdr77 Q6NUD0 | 5 | EBI-21229405, EBI-21229433 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 304-611 | SAM-dependent MTase PRMT-type | ||||
Sequence: LQSPLQPLMDNLESQTYEVFEKDPVKYSQYQQAVYKCLLDRVPEEEKETNIQILMVLGAGRGPLVNASLRAAKQAERKIKVYAVEKNPNAVITLEGWRYEEWGSQVTVVSGDMREWKAPEKADIIVSELLGSFGDNELSPECLDGAQHFLKDDGVSIPGEYTSYLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSDPLPCFTFHHPNKDDVIDNNRYCCLQYRVDLNTVLHGFAGYFNTVLYKDVTLSICPESHSPGMFSWFPILFPIKQPIPMREGDTVCVRFWRCNNGKKVWYEW |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length633
- Mass (Da)72,285
- Last updated2004-07-05 v1
- ChecksumF3A61499DF6623CC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY535008 EMBL· GenBank· DDBJ | AAS98802.1 EMBL· GenBank· DDBJ | mRNA | ||
BC068696 EMBL· GenBank· DDBJ | AAH68696.1 EMBL· GenBank· DDBJ | mRNA |