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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)DescriptionActionsGraphical viewLength
Binding sitei60S-adenosyl-L-methionineBy similarity1
Binding sitei69S-adenosyl-L-methionineBy similarity1
Binding sitei93S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei115S-adenosyl-L-methionineBy similarity1
Binding sitei144S-adenosyl-L-methionineBy similarity1
Active sitei158By similarity1
Active sitei167By similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002123331 – 378Protein arginine N-methyltransferase 6Add BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38Omega-N-methylated arginine; by autocatalysisBy similarity1

Post-translational modificationi

Automethylation enhances its stability.By similarity

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ6NZB1.
MaxQBiQ6NZB1.
PaxDbiQ6NZB1.
PeptideAtlasiQ6NZB1.
PRIDEiQ6NZB1.

PTM databases

PhosphoSitePlusiQ6NZB1.

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 interactors.
IntActiQ6NZB1. 6 interactors.
STRINGi10090.ENSMUSP00000102177.

Structurei

Secondary structure

1378
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 65Combined sources12
Helixi67 – 79Combined sources13
Helixi81 – 84Combined sources4
Beta strandi88 – 93Combined sources6
Helixi98 – 105Combined sources8
Beta strandi109 – 115Combined sources7
Helixi120 – 129Combined sources10
Turni133 – 135Combined sources3
Beta strandi136 – 141Combined sources6
Turni143 – 145Combined sources3
Beta strandi152 – 156Combined sources5
Turni165 – 167Combined sources3
Helixi170 – 180Combined sources11
Beta strandi181 – 189Combined sources9
Beta strandi191 – 199Combined sources9
Helixi202 – 218Combined sources17
Helixi225 – 234Combined sources10
Beta strandi240 – 242Combined sources3
Helixi246 – 248Combined sources3
Beta strandi254 – 260Combined sources7
Helixi266 – 272Combined sources7
Beta strandi274 – 281Combined sources8
Beta strandi284 – 299Combined sources16
Helixi302 – 304Combined sources3
Beta strandi308 – 311Combined sources4
Beta strandi323 – 334Combined sources12
Beta strandi339 – 349Combined sources11
Beta strandi352 – 364Combined sources13
Beta strandi370 – 375Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 377SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST331

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)DescriptionActionsGraphical viewLength
Sequence conflicti1M → W in BAC28811 (PubMed:16141072).Curated1
Sequence conflicti167E → D in BAC28811 (PubMed:16141072).Curated1
Sequence conflicti315F → L in AAH66221 (PubMed:15489334).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221340. 7 interactors.
IntActiQ6NZB1. 6 interactors.
STRINGi10090.ENSMUSP00000102177.

PTM databases

PhosphoSitePlusiQ6NZB1.

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: November 2, 2016
This is version 116 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.