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Reviewed, UniProtKB/Swiss-Prot Q5E9L5 (ANM6_BOVIN)

Last modified November 3, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Synonyms: HRMT1L6
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.

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
Phosphoprotein
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

histone H3-R2 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from sequence or structural similarity. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

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 – 375375Protein arginine N-methyltransferase 6
PRO_0000212331

Sites

Binding site571S-adenosyl-L-methionine By similarity
Binding site661S-adenosyl-L-methionine By similarity
Binding site901S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1121S-adenosyl-L-methionine By similarity
Binding site1411S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue211Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E9L5-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 234A46591A0428C5

FASTA37541,868
        10         20         30         40         50         60 
MSQPKRRKLE SGGGGEGGEG TEEEDGGELE VAVPRPRRTR RERDQLYYQC YSDVSVHEEM 

        70         80         90        100        110        120 
IADRVRTDAY RLGILRNWAA LRGKTVLDVG AGTGILSIFC AQAGARRVYA VEASDIWQQA 

       130        140        150        160        170        180 
REVVRLNGLE DRVHVLPGPV ETVELPEQVD AIVSEWMGCG LLHESMLSSV LHARTKWLKE 

       190        200        210        220        230        240 
GGLLLPASAE LFVAPISDQM LELRLSFWSQ MKQLYGVDMS CLESFATRCL MGHSEIVVQG 

       250        260        270        280        290        300 
LSGEDVLARP QCFARLELAR AGLEQELEAG VGGRFRFSCY GSAPMHGFAI WFQVTFPGGD 

       310        320        330        340        350        360 
SEKPVVLSTS PFHPVTHWKQ ALLYLNEPVQ VEQDTDVSGE ITLLPSQDHH RHLRVLLRYK 

       370 
VGDQEEKTKD FAMED 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

BT020905 mRNA. Translation: AAX08922.1.
IPIIPI00692823.
RefSeqNP_001014962.1.
UniGeneBt.28284
Bt.65048

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSBTAT00000009750; ENSBTAP00000009750; ENSBTAG00000039951; Bos taurus. [Genome view]
GeneID540228.
KEGGbta:540228.

Organism-specific databases

CTD540228.

Phylogenomic databases

HOVERGENQ5E9L5.
OMAGRFRFSC.

Family and domain databases

InterProIPR013216. Methyltransf_11.
[Graphical view]
PfamPF08241. Methyltransf_11. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANM6_BOVIN
AccessionPrimary (citable) accession number: Q5E9L5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 15, 2005
Last modified: November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents