Reviewed, UniProtKB/Swiss-Prot Q6NZB1 (ANM6_MOUSE)

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
Synonyms:	Hrmt1l6

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	378 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 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 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 – 378	378	Protein arginine N-methyltransferase 6		PRO_0000212333
Sites
	Binding site	60	1	S-adenosyl-L-methionine By similarity
	Binding site	69	1	S-adenosyl-L-methionine By similarity
	Binding site	93	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	115	1	S-adenosyl-L-methionine By similarity
	Binding site	144	1	S-adenosyl-L-methionine By similarity
Experimental info
	Sequence conflict	1	1	M → W in BAC28811. Ref.1
	Sequence conflict	167	1	E → D in BAC28811. Ref.1
	Sequence conflict	315	1	F → L in AAH66221. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6NZB1-1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: F1EB7FCFF9C54242	FASTA	378	41,866
	10 20 30 40 50 60 MSLSKKRKLE SGDSGGAGAG GEGAEEENGG EQEAAPPRPR RTKSERDQLY YECYSDVSVH 70 80 90 100 110 120 EEMIADQVRT EAYRLGILKN WAALRGKTVL DVGAGTGILS IFCAQAGARR VYAVEASAIW 130 140 150 160 170 180 QQAREVVRLN GLEDRVHVLP GPVETVELPE RVDAIVSEWM GYGLLHESML SSVLHARTKW 190 200 210 220 230 240 LKEGGLLLPA SAELFVAPIS DQMLEWRLGF WSQVKQHYGV DMSCMESFAT RCLMGHSEIV 250 260 270 280 290 300 VQDLSGEDVL ARPQRFAQLE LARAGLEQEL EAGVGGRFRC SCYGSAPLHG FAVWFQVTFP 310 320 330 340 350 360 GGDSEKPLVL STSPFHPATH WKQALLYLNE PVPVEQDTDI SGEITLLPSP DNPRRLRILL 370 RYKVGDHEEK TKDFAMED

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Embryo and Spleen.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Embryo and Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK034732 mRNA. Translation: BAC28811.1. Different initiation. AK087551 mRNA. Translation: BAC39923.1. Different initiation. AK172003 mRNA. Translation: BAE42769.1. AK172105 mRNA. Translation: BAE42828.1. AK172722 mRNA. Translation: BAE43144.1. BC022899 mRNA. Translation: AAH22899.1. BC066221 mRNA. Translation: AAH66221.1.
IPI	IPI00421169.
RefSeq	NP_849222.3.
UniGene	Mm.36115 Mm.475147
3D structure databases
SMR	Q6NZB1. Positions 42-364.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6NZB1.
PTM databases
PhosphoSite	Q6NZB1.
Proteomic databases
PRIDE	Q6NZB1.
Genome annotation databases
Ensembl	ENSMUST00000061464; ENSMUSP00000057894; ENSMUSG00000049300; Mus musculus. [Genome view] ENSMUST00000106567; ENSMUSP00000102177; ENSMUSG00000049300; Mus musculus. [Genome view]
GeneID	99890.
KEGG	mmu:99890.
UCSC	uc008rau.1. mouse.
Organism-specific databases
CTD	99890.
MGI	MGI:2139971. Prmt6.
Phylogenomic databases
eggNOG	maNOG13005.
HOGENOM	HBG715060.
HOVERGEN	Q6NZB1.
InParanoid	Q6NZB1.
OMA	GRFRFSC.
OrthoDB	EOG91VNP6.
PhylomeDB	Q6NZB1.
Gene expression databases
ArrayExpress	Q6NZB1.
Bgee	Q6NZB1.
CleanEx	MM_PRMT6.
Genevestigator	Q6NZB1.
GermOnline	ENSMUSG00000049300. Mus musculus.
Family and domain databases
InterPro	IPR010456. PrmA_MeTrfase. [Graphical view]
Pfam	PF06325. PrmA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	354155.
SOURCE	Search...

Entry information

Entry name

ANM6_MOUSE

Accession

Primary (citable) accession number: Q6NZB1
Secondary accession number(s): Q3TA42 , Q8BN52, Q8BSC2, Q8R5D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	February 9, 2010
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)