PRMT6 protein arginine methyltransferase 6 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRMT6provided by HGNC
Official Full Name: protein arginine methyltransferase 6provided by HGNC
Primary source: HGNC:HGNC:18241
See related: Ensembl:ENSG00000198890 MIM:608274; AllianceGenome:HGNC:18241
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: HRMT1L6
Summary: The protein encoded by this gene belongs to the arginine N-methyltransferase family, which catalyze the sequential transfer of methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins, to form methylated arginine derivatives and S-adenosyl-L-homocysteine. This protein can catalyze both, the formation of omega-N monomethylarginine and asymmetrical dimethylarginine, with a strong preference for the latter. It specifically mediates the asymmetric dimethylation of Arg2 of histone H3, and the methylated form represents a specific tag for epigenetic transcriptional repression. This protein also forms a complex with, and methylates DNA polymerase beta, resulting in stimulation of polymerase activity by enhancing DNA binding and processivity. [provided by RefSeq, Sep 2011]
Orthologs: mouse all
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Genomic context

Location:: 1p13.3

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (107056674..107059294)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (107094127..107096747)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (107599296..107601916)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The PRMT6/STAT1/ACSL1 axis promotes ferroptosis in diabetic nephropathy.
Title: The PRMT6/STAT1/ACSL1 axis promotes ferroptosis in diabetic nephropathy.
PRMT6 facilitates EZH2 protein stability by inhibiting TRAF6-mediated ubiquitination degradation to promote glioblastoma cell invasion and migration.
Title: PRMT6 facilitates EZH2 protein stability by inhibiting TRAF6-mediated ubiquitination degradation to promote glioblastoma cell invasion and migration.
PRMT6 Promotes the Immune Evasion of Gastric Cancer by Upregulating ANXA1.
Title: PRMT6 Promotes the Immune Evasion of Gastric Cancer by Upregulating ANXA1.
PRMT6 methylation of STAT3 regulates tumor metastasis in breast cancer.
Title: PRMT6 methylation of STAT3 regulates tumor metastasis in breast cancer.
PRMT6-CDC20 facilitates glioblastoma progression via the degradation of CDKN1B.
Title: PRMT6-CDC20 facilitates glioblastoma progression via the degradation of CDKN1B.
MiR-141-3p promotes malignant progression in prostate cancer through AlkB homolog 5-mediated m[6]A modification of protein arginine methyltransferase 6.
Title: MiR-141-3p promotes malignant progression in prostate cancer through AlkB homolog 5-mediated m(6)A modification of protein arginine methyltransferase 6.
PRMT6 functionally associates with PRMT5 to promote colorectal cancer progression through epigenetically repressing the expression of CDKN2B and CCNG1.
Title: PRMT6 functionally associates with PRMT5 to promote colorectal cancer progression through epigenetically repressing the expression of CDKN2B and CCNG1.
Arginine Methylation of Integrin Alpha-4 Prevents Fibrosis Development in Alcohol-Associated Liver Disease.
Title: Arginine Methylation of Integrin Alpha-4 Prevents Fibrosis Development in Alcohol-Associated Liver Disease.
Huntingtin-mediated axonal transport requires arginine methylation by PRMT6.
Title: Huntingtin-mediated axonal transport requires arginine methylation by PRMT6.
Systematic investigation of PRMT6 substrate recognition reveals broad specificity with a preference for an RG motif or basic and bulky residues.
Title: Systematic investigation of PRMT6 substrate recognition reveals broad specificity with a preference for an RG motif or basic and bulky residues.

Submit: New GeneRIF Correction See all GeneRIFs (58)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
A genome-wide association meta-analysis of circulating sex hormone-binding globulin reveals multiple Loci implicated in sex steroid hormone regulation. EBI GWAS Catalog EBI GWAS CatalogPubMed
A genome-wide association study in Chinese men identifies three risk loci for non-obstructive azoospermia. EBI GWAS Catalog EBI GWAS CatalogPubMed
Genome-wide association study identifies 8 novel loci associated with blood pressure responses to interventions in Han Chinese. EBI GWAS Catalog EBI GWAS CatalogPubMed
Genome-wide association study of intelligence: additive effects of novel brain expressed genes. EBI GWAS Catalog EBI GWAS CatalogPubMed
Genome-wide SNP and CNV analysis identifies common and low-frequency variants associated with severe early-onset obesity. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp160, precursor	env	HIV-1 Env (gp160) protein methylation mediated by PRMT6 is required to maintain optimal HIV-1 infectivity	PubMed
Rev	rev	PRMT6 mutant V86K/D88A fails to methylate HIV-1 Rev. PRMT6 is automethylated at position R35, which regulates its stability and is necessary for its HIV-1 restriction activity	PubMed
	rev	Arginine 38 methylation of HIV-1 Rev by PRMT6 reduces RRE binding and diminishes export of viral RNA to the cytoplasm	PubMed
Tat	tat	HIV-1 Tat nucleolar retention (dependent on Tat residues 49-57) is inhibited by PRMT6	PubMed
	tat	The termini (residues 1-84 and 321-375) of PRMT6 and the activation domain (residues 1-37) of HIV-1 Tat are required for the interaction between PRMT6 and Tat	PubMed
	tat	PRMT6 increases the steady-state level of HIV-1 Tat in the cell and the basic domain (residues 49-57) of Tat is required for the PRMT6-mediated increase of Tat steady-state levels	PubMed
	tat	HIV-1 Tat is methylated at positions Arg52 and Arg53 by PRMT6. Arginine methylation of Tat negatively affects Tat-TAR-cyclin T1 ternary complex formation and diminishes cyclin T1-dependent Tat transcriptional activation	PubMed
	tat	HIV-1 Tat specifically interacts with and is methylated by PRMT6 within cells; overexpression of wild-type PRMT6 decreases Tat transactivation of an HIV-1 long terminal repeat luciferase reporter plasmid in a dose-dependent manner	PubMed
nucleocapsid	gag	HIV-1 NC is methylated at positions Arg10 and Arg32 by PRMT6 both in vitro and in vivo, and methylated NC is less able than wild-type to promote RNA annealing and participates in the initiation of reverse transcription	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

WI-15868 (e-PCR)
- UniSTS:81057

Prmt6 (e-PCR), detects polymorphism
- UniSTS:479207

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables chromatin binding	IEA Inferred from Electronic Annotation more info
enables histone H2AQ104 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H2AR3 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone H3 methyltransferase activity	EXP Inferred from Experiment more info	PubMed
enables histone H3 methyltransferase activity	TAS Traceable Author Statement more info
enables histone H3K37 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3K56 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R17 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R2 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone H3R26 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R8 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H4K12 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H4R3 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone binding	IDA Inferred from Direct Assay more info	PubMed
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables histone methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-arginine N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	TAS Traceable Author Statement more info
enables protein-arginine omega-N asymmetric methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N monomethyltransferase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in base-excision repair	TAS Traceable Author Statement more info	PubMed
involved_in cellular senescence	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of DNA-templated transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of transcription by RNA polymerase II	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of ubiquitin-dependent protein catabolic process	IEA Inferred from Electronic Annotation more info
involved_in protein modification process	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of megakaryocyte differentiation	TAS Traceable Author Statement more info
involved_in regulation of mitochondrion organization	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of signal transduction by p53 class mediator	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in nucleolus	IDA Inferred from Direct Assay more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: protein arginine N-methyltransferase 6

Names: HMT1 hnRNP methyltransferase-like 6; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6; histone-arginine N-methyltransferase PRMT6

NP_060607.2

EC 2.1.1.319

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_018137.3 → NP_060607.2 protein arginine N-methyltransferase 6

See identical proteins and their annotated locations for NP_060607.2

Status: VALIDATED

Source sequence(s)

AI754232, AY043278, DA073209

Consensus CDS

CCDS41360.2

UniProtKB/Swiss-Prot

A3KME1, B4DID8, Q5T5Y5, Q6DKI4, Q96LA8, Q9NVR8

UniProtKB/TrEMBL

A0A3B3ITK4

Related

ENSP00000359095.1, ENST00000370078.2

Conserved Domains (1) summary

cl17173
Location:67 → 200

AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...