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Protein

Protein arginine N-methyltransferase 6

Gene

PRMT6

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

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 sitei57 – 571S-adenosyl-L-methionineBy similarity
Binding sitei66 – 661S-adenosyl-L-methionineBy similarity
Binding sitei90 – 901S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei112 – 1121S-adenosyl-L-methionineBy similarity
Binding sitei141 – 1411S-adenosyl-L-methionineBy similarity
Active sitei155 – 1551By similarity
Active sitei164 – 1641By similarity

GO - Molecular functioni

GO - Biological processi

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-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Protein arginine N-methyltransferase 6PRO_0000212331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphothreonineBy similarity
Modified residuei38 – 381Omega-N-methylated arginine; by autocatalysisBy similarity

Post-translational modificationi

Automethylation enhances its stability.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ5E9L5.

Interactioni

Subunit structurei

Interacts with EPB41L3 and NCOA1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009750.

Structurei

3D structure databases

ProteinModelPortaliQ5E9L5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 374331SAM-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.
InParanoidiQ5E9L5.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG74J97Z.
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.

Q5E9L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPKRRKLE SGGGGEGGEG TEEEDGGELE VAVPRPRRTR RERDQLYYQC
60 70 80 90 100
YSDVSVHEEM IADRVRTDAY RLGILRNWAA LRGKTVLDVG AGTGILSIFC
110 120 130 140 150
AQAGARRVYA VEASDIWQQA REVVRLNGLE DRVHVLPGPV ETVELPEQVD
160 170 180 190 200
AIVSEWMGCG LLHESMLSSV LHARTKWLKE GGLLLPASAE LFVAPISDQM
210 220 230 240 250
LELRLSFWSQ MKQLYGVDMS CLESFATRCL MGHSEIVVQG LSGEDVLARP
260 270 280 290 300
QCFARLELAR AGLEQELEAG VGGRFRFSCY GSAPMHGFAI WFQVTFPGGD
310 320 330 340 350
SEKPVVLSTS PFHPVTHWKQ ALLYLNEPVQ VEQDTDVSGE ITLLPSQDHH
360 370
RHLRVLLRYK VGDQEEKTKD FAMED
Length:375
Mass (Da):41,868
Last modified:March 15, 2005 - v1
Checksum:i234A46591A0428C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020905 mRNA. Translation: AAX08922.1.
RefSeqiNP_001014962.1. NM_001014962.1.
UniGeneiBt.28284.
Bt.65048.

Genome annotation databases

EnsembliENSBTAT00000009750; ENSBTAP00000009750; ENSBTAG00000039951.
GeneIDi540228.
KEGGibta:540228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020905 mRNA. Translation: AAX08922.1.
RefSeqiNP_001014962.1. NM_001014962.1.
UniGeneiBt.28284.
Bt.65048.

3D structure databases

ProteinModelPortaliQ5E9L5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009750.

Proteomic databases

PaxDbiQ5E9L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009750; ENSBTAP00000009750; ENSBTAG00000039951.
GeneIDi540228.
KEGGibta:540228.

Organism-specific databases

CTDi55170.

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG095907.
InParanoidiQ5E9L5.
KOiK11437.
OMAiGRFRFSC.
OrthoDBiEOG74J97Z.
TreeFamiTF328817.

Enzyme and pathway databases

ReactomeiR-BTA-3214858. RMTs methylate histone arginines.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiANM6_BOVIN
AccessioniPrimary (citable) accession number: Q5E9L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.