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B0JYW5 (ANM6_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein arginine N-methyltransferase 6

EC=2.1.1.-
Alternative name(s):
Histone-arginine N-methyltransferase PRMT6
EC=2.1.1.125
Gene names
Name:prmt6
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). It thereby acts as a transcription corepressor of various genes such as hoxa2. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (polb), leading to stimulate the polymerase activity by enhancing DNA binding and processivity. Methylates hmga1 By similarity.

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].

Subcellular location

Nucleus By similarity.

Post-translational modification

Automethylated By similarity.

Sequence similarities

Belongs to the protein arginine N-methyltransferase family. PRMT6 subfamily.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMMethylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionhistone binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone methyltransferase activity (H2A-R3 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

histone methyltransferase activity (H3-R2 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

histone methyltransferase activity (H4-R3 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein-arginine omega-N monomethyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Protein arginine N-methyltransferase 6
PRO_0000378152

Sites

Binding site281S-adenosyl-L-methionine By similarity
Binding site371S-adenosyl-L-methionine By similarity
Binding site611S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site831S-adenosyl-L-methionine By similarity
Binding site1121S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0JYW5 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 4B532D7D555790F8

FASTA34037,872
        10         20         30         40         50         60 
MAMLKKRKHE RTEQDCEYFQ CYSDVSVHEE MIADTVRTNA YKLALLRNHS SLQGKTVLDV 

        70         80         90        100        110        120 
GAGTGILSVF SVQAGAQAVY AVEASSMSQL ACQVVKSNDM ENKVKVLNSS VESAEIPEQV 

       130        140        150        160        170        180 
DAIVSEWMGY ALMYESMLPS VIYARDKWLK PGGLILPSCA DLFIAPVNDL IVESRLDFWS 

       190        200        210        220        230        240 
EVKGMYGVDM SCMQSFARSC IMNKEMAVNL VSPEDVLSFP VRFASLDLNV CTQEEVRNLH 

       250        260        270        280        290        300 
GSFQFSCFGS SLLHGFAVWF SVTFPGENSV TLSTSPYGEE THWKQTLLYL DEEVQVEQDT 

       310        320        330        340 
EITGDVTLSP SDINPRHLRV LLNYSIGGGL RRTKQFQMGS 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC158943 mRNA. Translation: AAI58944.1.
RefSeqNP_001120104.1. NM_001126632.1.
UniGeneStr.3505.

3D structure databases

ProteinModelPortalB0JYW5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0JYW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100145123.
KEGGxtr:100145123.

Organism-specific databases

CTD55170.
XenbaseXB-GENE-5857258. prmt6.

Phylogenomic databases

eggNOGveNOG11537.
GeneTreeENSGT00550000074406.

Gene expression databases

BgeeB0JYW5.

Family and domain databases

InterProIPR007857. Skb1_MeTrfase.
[Graphical view]
KOK11437.
PfamPF05185. PRMT5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANM6_XENTR
AccessionPrimary (citable) accession number: B0JYW5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: March 18, 2008
Last modified: November 16, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families