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Protein

Protein arginine N-methyltransferase 6

Gene

Prmt6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that can catalyze the formation of both 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). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence. 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 the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator.2 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601S-adenosyl-L-methionineBy similarity
Binding sitei69 – 691S-adenosyl-L-methionineBy similarity
Binding sitei93 – 931S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei115 – 1151S-adenosyl-L-methionineBy similarity
Binding sitei144 – 1441S-adenosyl-L-methionineBy similarity
Active sitei158 – 1581By similarity
Active sitei167 – 1671By similarity

GO - Molecular functioni

GO - Biological processi

  • cell growth Source: MGI
  • cellular senescence Source: MGI
  • DNA repair Source: UniProtKB-KW
  • histone H3-R2 methylation Source: UniProtKB
  • histone methylation Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 6 (EC:2.1.1.319By similarity)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT6
Gene namesi
Name:Prmt6
Synonyms:Hrmt1l6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2139971. Prmt6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic fibroblasts from mutant mice display growth defects, premature senescence and increased levels of TP53 and multiple TP53 targets. In liver, knockdown disrupts the formation of a cAMP-mediated transcription complex involving CRTC2, reduces the expression of genes encoding gluconeogenic factors and decreases glucose output in primary hepatocytes, it also restores euglycemia in insulin-resistant mice.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Protein arginine N-methyltransferase 6PRO_0000212333Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Omega-N-methylated arginine; by autocatalysisBy similarity

Post-translational modificationi

Automethylation enhances its stability.By similarity

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ6NZB1.
MaxQBiQ6NZB1.
PaxDbiQ6NZB1.
PeptideAtlasiQ6NZB1.
PRIDEiQ6NZB1.

PTM databases

PhosphoSiteiQ6NZB1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000049300.
CleanExiMM_PRMT6.
GenevisibleiQ6NZB1. MM.

Interactioni

Subunit structurei

Interacts with EPB41L3 and NCOA1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221340. 7 interactions.
IntActiQ6NZB1. 6 interactions.
STRINGi10090.ENSMUSP00000102177.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 6512Combined sources
Helixi67 – 7913Combined sources
Helixi81 – 844Combined sources
Beta strandi88 – 936Combined sources
Helixi98 – 1058Combined sources
Beta strandi109 – 1157Combined sources
Helixi120 – 12910Combined sources
Turni133 – 1353Combined sources
Beta strandi136 – 1416Combined sources
Turni143 – 1453Combined sources
Beta strandi152 – 1565Combined sources
Turni165 – 1673Combined sources
Helixi170 – 18011Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi191 – 1999Combined sources
Helixi202 – 21817Combined sources
Helixi225 – 23410Combined sources
Beta strandi240 – 2423Combined sources
Helixi246 – 2483Combined sources
Beta strandi254 – 2607Combined sources
Helixi266 – 2727Combined sources
Beta strandi274 – 2818Combined sources
Beta strandi284 – 29916Combined sources
Helixi302 – 3043Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi323 – 33412Combined sources
Beta strandi339 – 34911Combined sources
Beta strandi352 – 36413Combined sources
Beta strandi370 – 3756Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C03X-ray1.58A/B1-378[»]
4C04X-ray1.58A1-378[»]
4C05X-ray2.20A1-378[»]
4C06X-ray1.60A1-378[»]
4C07X-ray1.50A1-378[»]
4C08X-ray1.34A1-378[»]
ProteinModelPortaliQ6NZB1.
SMRiQ6NZB1. Positions 41-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 377331SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT6 subfamily.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG095907.
InParanoidiQ6NZB1.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG091G0A0U.
PhylomeDBiQ6NZB1.
TreeFamiTF328817.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6NZB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSKKRKLE SGDSGGAGAG GEGAEEENGG EQEAAPPRPR RTKSERDQLY
60 70 80 90 100
YECYSDVSVH EEMIADQVRT EAYRLGILKN WAALRGKTVL DVGAGTGILS
110 120 130 140 150
IFCAQAGARR VYAVEASAIW QQAREVVRLN GLEDRVHVLP GPVETVELPE
160 170 180 190 200
RVDAIVSEWM GYGLLHESML SSVLHARTKW LKEGGLLLPA SAELFVAPIS
210 220 230 240 250
DQMLEWRLGF WSQVKQHYGV DMSCMESFAT RCLMGHSEIV VQDLSGEDVL
260 270 280 290 300
ARPQRFAQLE LARAGLEQEL EAGVGGRFRC SCYGSAPLHG FAVWFQVTFP
310 320 330 340 350
GGDSEKPLVL STSPFHPATH WKQALLYLNE PVPVEQDTDI SGEITLLPSP
360 370
DNPRRLRILL RYKVGDHEEK TKDFAMED
Length:378
Mass (Da):41,866
Last modified:June 7, 2005 - v2
Checksum:iF1EB7FCFF9C54242
GO

Sequence cautioni

The sequence BAC28811 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC39923 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → W in BAC28811 (PubMed:16141072).Curated
Sequence conflicti167 – 1671E → D in BAC28811 (PubMed:16141072).Curated
Sequence conflicti315 – 3151F → L in AAH66221 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS38605.1.
RefSeqiNP_849222.3. NM_178891.5.
UniGeneiMm.36115.
Mm.393526.

Genome annotation databases

EnsembliENSMUST00000106567; ENSMUSP00000102177; ENSMUSG00000049300.
ENSMUST00000168412; ENSMUSP00000129801; ENSMUSG00000049300.
ENSMUST00000190378; ENSMUSP00000140836; ENSMUSG00000049300.
GeneIDi99890.
KEGGimmu:99890.
UCSCiuc008rau.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS38605.1.
RefSeqiNP_849222.3. NM_178891.5.
UniGeneiMm.36115.
Mm.393526.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C03X-ray1.58A/B1-378[»]
4C04X-ray1.58A1-378[»]
4C05X-ray2.20A1-378[»]
4C06X-ray1.60A1-378[»]
4C07X-ray1.50A1-378[»]
4C08X-ray1.34A1-378[»]
ProteinModelPortaliQ6NZB1.
SMRiQ6NZB1. Positions 41-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221340. 7 interactions.
IntActiQ6NZB1. 6 interactions.
STRINGi10090.ENSMUSP00000102177.

PTM databases

PhosphoSiteiQ6NZB1.

Proteomic databases

EPDiQ6NZB1.
MaxQBiQ6NZB1.
PaxDbiQ6NZB1.
PeptideAtlasiQ6NZB1.
PRIDEiQ6NZB1.

Protocols and materials databases

DNASUi99890.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000106567; ENSMUSP00000102177; ENSMUSG00000049300.
ENSMUST00000168412; ENSMUSP00000129801; ENSMUSG00000049300.
ENSMUST00000190378; ENSMUSP00000140836; ENSMUSG00000049300.
GeneIDi99890.
KEGGimmu:99890.
UCSCiuc008rau.2. mouse.

Organism-specific databases

CTDi55170.
MGIiMGI:2139971. Prmt6.

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG095907.
InParanoidiQ6NZB1.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG091G0A0U.
PhylomeDBiQ6NZB1.
TreeFamiTF328817.

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Miscellaneous databases

PROiQ6NZB1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000049300.
CleanExiMM_PRMT6.
GenevisibleiQ6NZB1. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM6_MOUSE
AccessioniPrimary (citable) accession number: Q6NZB1
Secondary accession number(s): Q3TA42
, Q8BN52, Q8BSC2, Q8R5D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: September 7, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.