Q68EZ3 (ANM6_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Methylation
Gene Ontology (GO)
Biological process	DNA 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 component	cytoplasm Inferred from electronic annotation. Source: InterPro nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	histone 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 340	340	Protein arginine N-methyltransferase 6		PRO_0000378151
Sites
	Binding site	28	1	S-adenosyl-L-methionine By similarity
	Binding site	37	1	S-adenosyl-L-methionine By similarity
	Binding site	61	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	83	1	S-adenosyl-L-methionine By similarity
	Binding site	112	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68EZ3 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 5F51BB3307A59FF9	FASTA	340	37,915
	10 20 30 40 50 60 MALLKKRKHE RSEQDQEYFQ CYSDVSIHEE MIADTVRTNG YKQAILHNHC ALQGLTVLDV 70 80 90 100 110 120 GAGTGILSVF CVQAGATRVY AVEASAVSQL ASHVVTLNGM DNKVKVLNSP VESAEIPEQV 130 140 150 160 170 180 DAIVSEWMGY ALMYESMLPS VIYARDKWLK PGGIILPSAA DLFIAPINDR VVESRLDFWN 190 200 210 220 230 240 EVKGLYGVDM SCMRPFAHSC IMNKEMAVNL LSPEDVLSFP VRFASLDLNV CTQEEVRNLH 250 260 270 280 290 300 GSFQFSCFGS SLLHGFALWF TVTFPGEKTV TLSTSPYGEE THWKQTLLYL DEEIQVEQDT 310 320 330 340 DITGDITLSP SDVNPRHLRA LLNYSIGGGL RRTKHFHMGT

References

[1]	NIH - Xenopus Gene Collection (XGC) project Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC080055 mRNA. Translation: AAH80055.1.
RefSeq	NP_001087520.1. NM_001094051.1.
UniGene	Xl.25304.
3D structure databases
HSSP	HSSP built from PDB template 1ORH based on UniProtKB Q63009.
ProteinModelPortal	Q68EZ3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	447344.
KEGG	xla:447344.
Organism-specific databases
CTD	55170.
Xenbase	XB-GENE-6254002. prmt6.
Family and domain databases
InterPro	IPR007857. Skb1_MeTrfase. [Graphical view]
KO	K11437.
Pfam	PF05185. PRMT5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANM6_XENLA

Accession

Primary (citable) accession number: Q68EZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	October 11, 2004
Last modified:	November 16, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program