Q5RGQ2 · ANM8B_DANRE

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).

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site111S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site120S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site144S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site144-147S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site166S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site195S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site210
Active site219

GO annotations

AspectTerm
Cellular Componentcytoplasmic side of plasma membrane
Cellular Componentplasma membrane
Molecular Functionarginine N-methyltransferase activity
Molecular Functionhistone methyltransferase activity
Molecular Functionidentical protein binding
Molecular Functionprotein-arginine omega-N asymmetric methyltransferase activity
Molecular Functionprotein-arginine omega-N monomethyltransferase activity
Molecular FunctionS-adenosyl-L-methionine binding
Molecular FunctionS-adenosylmethionine-dependent methyltransferase activity
Biological Processchordate embryonic development
Biological Processchromatin remodeling
Biological Processdendrite morphogenesis
Biological Processmidbrain-hindbrain boundary development
Biological Processneuron development
Biological Processpeptidyl-arginine methylation
Biological Processprotein homooligomerization
Biological Processprotein methylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein arginine N-methyltransferase 8-B
  • EC number
  • Alternative names
    • Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
    • zfL3

Gene names

    • Name
      prmt8b
    • Synonyms
      prmt8
    • ORF names
      si:dkey-21h14.6

Organism names

  • Taxonomic identifier
  • Strain
    • Tuebingen
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q5RGQ2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
Lipidation2N-myristoyl glycine
ChainPRO_00003781532-419Protein arginine N-methyltransferase 8-B
Modified residue83Omega-N-methylarginine
Modified residue98Asymmetric dimethylarginine

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer. Tetramer; individual homodimers associates to form a homotetramer. Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-79Disordered
Compositional bias11-27Basic and acidic residues
Compositional bias28-55Polar residues
Compositional bias58-72Pro residues
Domain98-402SAM-dependent MTase PRMT-type

Domain

The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    48,222
  • Last updated
    2009-06-16 v2
  • Checksum
    63111344E2BC7D17
MGLRHSSRCLLLRRKMAEAESTEQQQQKHKQPQHQQQQSISSIPSSQSLQPSPLPKPVTSVHHVPPHPPHTPHVSALSACPGRGKMAKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHIFKDKIVLDVGSGTGILSMFAAKAGAKHVYGIECSSISEYSEKIIKSNHLDSVITILKGKVEETELPVDQVDIIISEWMGYCLFYESMLNTVIYARDKWLKPGGFMFPDRATLYVVAIEDRQYKDFKIHWWENVYGFDMTCIRNVAMMEPLVDIVDPKQVVTNSCLVKEVDIYTVKTEDLSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKTGFSTAPDAPSTHWKQTVFYLEDYLTVRRGEEILGSITVRPNENNERDLDFTFELDFKGQLCDAAISHDYKMR

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8M9Q5Y0A0A8M9Q5Y0_DANREprmt8b418
A0A2R8Q6G4A0A2R8Q6G4_DANREprmt8b420

Sequence caution

The sequence AAI62920.1 differs from that shown. Reason: Erroneous initiation
The sequence AAI62940.1 differs from that shown. Reason: Erroneous initiation
The sequence CAI20944.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias11-27Basic and acidic residues
Compositional bias28-55Polar residues
Compositional bias58-72Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX784029
EMBL· GenBank· DDBJ
CAI20944.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
BC162920
EMBL· GenBank· DDBJ
AAI62920.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC162940
EMBL· GenBank· DDBJ
AAI62940.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

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