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Q6NZB1 (ANM6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length378 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.

Sequence caution

The sequence BAC28811.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC39923.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Protein arginine N-methyltransferase 6
PRO_0000212333

Sites

Binding site601S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site931S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1151S-adenosyl-L-methionine By similarity
Binding site1441S-adenosyl-L-methionine By similarity

Experimental info

Sequence conflict11M → W in BAC28811. Ref.1
Sequence conflict1671E → D in BAC28811. Ref.1
Sequence conflict3151F → L in AAH66221. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6NZB1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: F1EB7FCFF9C54242

FASTA37841,866
        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

« Hide

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. expand/collapse author list , 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.
IPIIPI00421169.
RefSeqNP_849222.3. NM_178891.4.
UniGeneMm.36115.
Mm.393526.

3D structure databases

ProteinModelPortalQ6NZB1.
SMRQ6NZB1. Positions 42-377.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6NZB1.

PTM databases

PhosphoSiteQ6NZB1.

Proteomic databases

PRIDEQ6NZB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106567; ENSMUSP00000102177; ENSMUSG00000049300.
ENSMUST00000168412; ENSMUSP00000129801; ENSMUSG00000049300.
GeneID99890.
KEGGmmu:99890.
UCSCuc008rau.1. mouse.

Organism-specific databases

CTD55170.
MGIMGI:2139971. Prmt6.

Phylogenomic databases

eggNOGmaNOG13005.
GeneTreeENSGT00550000074406.
HOGENOMHBG715060.
HOVERGENHBG095907.
InParanoidQ6NZB1.
OMAGRFRFSC.
OrthoDBEOG4R23V8.
PhylomeDBQ6NZB1.

Gene expression databases

ArrayExpressQ6NZB1.
BgeeQ6NZB1.
CleanExMM_PRMT6.
GenevestigatorQ6NZB1.
GermOnlineENSMUSG00000049300. Mus musculus.

Family and domain databases

KOK11437.
ProtoNetSearch...

Other

NextBio354155.
SOURCESearch...

Entry information

Entry nameANM6_MOUSE
AccessionPrimary (citable) accession number: Q6NZB1
Secondary accession number(s): Q3TA42 expand/collapse secondary AC list , Q8BN52, Q8BSC2, Q8R5D7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 16, 2011
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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