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

Gene ID: 56341, updated on 11-Apr-2024

Summary

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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
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Genomic context

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See PRMT8 in Genome Data Viewer
Location:
12p13.32
Exon count:
13
Annotation release Status Assembly Chr Location
RS_2023_10 current GRCh38.p14 (GCF_000001405.40) 12 NC_000012.12 (3381349..3593973)
RS_2023_10 current T2T-CHM13v2.0 (GCF_009914755.1) 12 NC_060936.1 (3387867..3600523)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (3490515..3703139)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC100128253 Neighboring gene long intergenic non-protein coding RNA 2827 Neighboring gene tetraspanin 11 pseudogene Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3435715-3436214 Neighboring gene BRD4-independent group 4 enhancer GRCh37_chr12:3443867-3445066 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3474236-3474788 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3474789-3475339 Neighboring gene long intergenic non-protein coding RNA 2417 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:3507121-3507664 Neighboring gene uncharacterized LOC105369607 Neighboring gene NANOG-H3K4me1 hESC enhancer GRCh37_chr12:3530371-3531006 Neighboring gene uncharacterized LOC124902862 Neighboring gene ribosomal protein S26 pseudogene 44 Neighboring gene thyroid cancer-associated transcript 155 Neighboring gene H3K27ac hESC enhancer GRCh37_chr12:3688671-3689170 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:3709097-3709922 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3716235-3716736 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3716737-3717236 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:3738174-3738805 Neighboring gene calcium release activated channel regulator 2A Neighboring gene H3K4me1 hESC enhancer GRCh37_chr12:3801592-3802218 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 4141 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:3842402-3843030 Neighboring gene RNA, U6 small nuclear 174, pseudogene Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 4142 Neighboring gene uncharacterized LOC107984495

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: 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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Related articles in PubMed

  1. PRMT8 Controls the Pluripotency and Mesodermal Fate of Human Embryonic Stem Cells By Enhancing the PI3K/AKT/SOX2 Axis. Jeong HC, et al. Stem Cells, 2017 Sep. PMID 28543863
  2. Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity. Dillon MB, et al. J Biol Chem, 2013 Sep 27. PMID 23946480, Free PMC Article
  3. EWS is a substrate of type I protein arginine methyltransferase, PRMT8. Kim JD, et al. Int J Mol Med, 2008 Sep. PMID 18698489
  4. Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS. Ravenscroft TA, et al. Neurobiol Aging, 2013 Sep. PMID 23635657, Free PMC Article
  5. Novel helical assembly in arginine methyltransferase 8. Toma-Fukai S, et al. J Mol Biol, 2016 Mar 27. PMID 26876602

See all (34) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution.
    Title: Novel helical assembly in arginine methyltransferase 8.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. EWS is a substrate for PRMT8, as efficient as for PRMT1
    Title: EWS is a substrate of type I protein arginine methyltransferase, PRMT8.
  10. 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

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

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 chromatin remodeling IEA
Inferred from Electronic Annotation
more info
  
involved_in peptidyl-arginine methylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptidyl-arginine methylation, to asymmetrical-dimethyl arginine IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein homooligomerization IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein methylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasmic side of plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
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 

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
NP_062828.3
XP_016875133.1
XP_016875134.1
XP_047285113.1
XP_047285114.1
XP_047285115.1
XP_054228538.1
XP_054228539.1
XP_054228540.1
XP_054228541.1
XP_054228542.1

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)

  1. 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). ...

  2. 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_2023_10

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000012.12 Reference GRCh38.p14 Primary Assembly

    Range
    3381349..3593973
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_017019644.2 → XP_016875133.1  protein arginine N-methyltransferase 8 isoform X1

  2. XM_047429157.1 → XP_047285113.1  protein arginine N-methyltransferase 8 isoform X3

  3. XM_047429158.1 → XP_047285114.1  protein arginine N-methyltransferase 8 isoform X4

  4. XM_017019645.1 → XP_016875134.1  protein arginine N-methyltransferase 8 isoform X2

  5. XM_047429159.1 → XP_047285115.1  protein arginine N-methyltransferase 8 isoform X5

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060936.1 Alternate T2T-CHM13v2.0

    Range
    3387867..3600523
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054372563.1 → XP_054228538.1  protein arginine N-methyltransferase 8 isoform X1

  2. XM_054372565.1 → XP_054228540.1  protein arginine N-methyltransferase 8 isoform X3

  3. XM_054372566.1 → XP_054228541.1  protein arginine N-methyltransferase 8 isoform X4

  4. XM_054372564.1 → XP_054228539.1  protein arginine N-methyltransferase 8 isoform X2

  5. 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

  1. 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.

  2. 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.
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q9NR22.2 GenPept UniProtKB/Swiss-Prot:Q9NR22

Gene LinkOut

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