PRMT8 protein arginine methyltransferase 8 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRMT8provided by HGNC
Official Full Name: protein arginine methyltransferase 8provided by HGNC
Primary source: HGNC:HGNC:5188
See related: Ensembl:ENSG00000111218 MIM:610086; AllianceGenome:HGNC:5188
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: HRMT1L3; HRMT1L4
Summary: Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Arginine methylation is involved in a number of cellular processes, including DNA repair, RNA transcription, signal transduction, protein compartmentalization, and possibly protein translation (Lee et al., 2005 [PubMed 16051612]).[supplied by OMIM, Mar 2008]
Expression: Biased expression in brain (RPKM 5.7), testis (RPKM 0.8) and 1 other tissue See more
Orthologs: mouse all
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Genomic context

Location:: 12p13.32

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	12	NC_000012.12 (3381349..3593973)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	12	NC_060936.1 (3387867..3600523)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	12	NC_000012.11 (3490515..3703139)

Chromosome 12 - NC_000012.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PRMT8 in human embryonic stem cells plays an important role not only in maintaining pluripotency but also in controlling mesodermal differentiation.
Title: PRMT8 Controls the Pluripotency and Mesodermal Fate of Human Embryonic Stem Cells By Enhancing the PI3K/AKT/SOX2 Axis.
Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution.
Title: Novel helical assembly in arginine methyltransferase 8.
Mutational defects in PRMT8 is not the cause of frontotemporal lobar degeneration.
Title: Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS.
automethylation of the N terminus likely regulates PRMT8 activity by decreasing the affinity of the enzyme for AdoMet
Title: Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity.
wild type FUS (FUS-WT) specifically interacts with protein arginine methyltransferases 1 and 8 (PRMT1 and PRMT8) and undergoes asymmetric dimethylation
Title: Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.
Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
The interaction between PRMT8 and the EWS protein was charcterized.
Title: Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state.
Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)
Title: Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts.
EWS is a substrate for PRMT8, as efficient as for PRMT1
Title: EWS is a substrate of type I protein arginine methyltransferase, PRMT8.
PRMT8 N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers.
Title: Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Loci influencing lipid levels and coronary heart disease risk in 16 European population cohorts. 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)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

G62272 (e-PCR)
- UniSTS:139317

G42628 (e-PCR)
- UniSTS:94528

G42629 (e-PCR)
- UniSTS:94529

G42630 (e-PCR)
- UniSTS:94530

G42639 (e-PCR)
- UniSTS:94539

G41244 (e-PCR)
- UniSTS:37980

SHGC-172081 (e-PCR)
- UniSTS:182634

D12S879 (e-PCR)
- UniSTS:149891

D12S1050 (e-PCR), detects polymorphism
- UniSTS:7813

D12S188 (e-PCR)
- UniSTS:148912

RH122096 (e-PCR)
- UniSTS:134847

Prmt8 (e-PCR), detects polymorphism
- UniSTS:479208

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables S-adenosyl-L-methionine binding	IDA Inferred from Direct Assay more info	PubMed
enables S-adenosylmethionine-dependent methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables enzyme binding	IDA Inferred from Direct Assay more info	PubMed
enables histone H4 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IPI Inferred from Physical Interaction more info	PubMed
enables protein-arginine omega-N asymmetric methyltransferase activity	IBA Inferred from Biological aspect of Ancestor 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	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine omega-N monomethyltransferase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in peptidyl-arginine methylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein homooligomerization	IDA Inferred from Direct Assay more info	PubMed
involved_in protein methylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of modification of postsynaptic actin cytoskeleton	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasmic side of plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in glutamatergic synapse	IEA Inferred from Electronic Annotation more info
NOT located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in postsynapse	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: protein arginine N-methyltransferase 8

Names: HMT1 hnRNP methyltransferase-like 3; arginine methyltransferase 8; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4; protein arginine N-methyltransferase 4

NP_001243465.1

EC 2.1.1.319

NP_062828.3

EC 2.1.1.319

XP_016875133.1

EC 2.1.1.319

XP_016875134.1

EC 2.1.1.319

XP_047285113.1

EC 2.1.1.319

XP_047285114.1

EC 2.1.1.319

XP_047285115.1

EC 2.1.1.319

XP_054228538.1

EC 2.1.1.319

XP_054228539.1

EC 2.1.1.319

XP_054228540.1

EC 2.1.1.319

XP_054228541.1

EC 2.1.1.319

XP_054228542.1

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_001256536.1 → NP_001243465.1 protein arginine N-methyltransferase 8 isoform 2

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate 5' exon and it thus differs in the 5' UTR and 5' coding region, compared to variant 1. The resulting isoform (2) has a distinct N-terminus and is shorter than isoform 1.

Source sequence(s)

AC005831, AK315619

Consensus CDS

CCDS58200.1

UniProtKB/Swiss-Prot

Q9NR22

Related

ENSP00000414507.2, ENST00000452611.6

Conserved Domains (1) summary

cd02440
Location:106 → 206

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). ...
NM_019854.5 → NP_062828.3 protein arginine N-methyltransferase 8 isoform 1

See identical proteins and their annotated locations for NP_062828.3

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

Source sequence(s)

AB209027, BC022458, DA200375

Consensus CDS

CCDS8521.2

UniProtKB/Swiss-Prot

B2RDP0, Q8TBJ8, Q9NR22

Related

ENSP00000372067.3, ENST00000382622.4

Conserved Domains (1) summary

cd02440
Location:115 → 215

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). ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000012.12 Reference GRCh38.p14 Primary Assembly

Range

3381349..3593973

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017019644.2 → XP_016875133.1 protein arginine N-methyltransferase 8 isoform X1
XM_047429157.1 → XP_047285113.1 protein arginine N-methyltransferase 8 isoform X3
XM_047429158.1 → XP_047285114.1 protein arginine N-methyltransferase 8 isoform X4
XM_017019645.1 → XP_016875134.1 protein arginine N-methyltransferase 8 isoform X2
XM_047429159.1 → XP_047285115.1 protein arginine N-methyltransferase 8 isoform X5

Alternate T2T-CHM13v2.0

Genomic

NC_060936.1 Alternate T2T-CHM13v2.0

Range

3387867..3600523

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054372563.1 → XP_054228538.1 protein arginine N-methyltransferase 8 isoform X1
XM_054372565.1 → XP_054228540.1 protein arginine N-methyltransferase 8 isoform X3
XM_054372566.1 → XP_054228541.1 protein arginine N-methyltransferase 8 isoform X4
XM_054372564.1 → XP_054228539.1 protein arginine N-methyltransferase 8 isoform X2
XM_054372567.1 → XP_054228542.1 protein arginine N-methyltransferase 8 isoform X5

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_001256537.1: Suppressed sequence

Description

NM_001256537.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript, which may retain intronic sequence at its 5' end.
NR_046301.1: Suppressed sequence

Description

NR_046301.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript, which may be incomplete at its 5' end.