Prmt8 protein arginine N-methyltransferase 8 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prmt8provided by MGI
Official Full Name: protein arginine N-methyltransferase 8provided by MGI
Primary source: MGI:MGI:3043083
See related: Ensembl:ENSMUSG00000030350 AllianceGenome:MGI:3043083
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Hrmt1l3; Hrmt1l4
Summary: Predicted to enable several functions, including S-adenosyl-L-methionine binding activity; protein homodimerization activity; and protein methyltransferase activity. Involved in regulation of modification of postsynaptic actin cytoskeleton. Predicted to be located in cytoplasmic side of plasma membrane. Predicted to be active in plasma membrane. Is expressed in several structures, including brain; genitourinary system; sensory organ; spinal cord; and trigeminal ganglion. Orthologous to human PRMT8 (protein arginine methyltransferase 8). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in cortex adult (RPKM 13.0), frontal lobe adult (RPKM 11.1) and 6 other tissues See more
Orthologs: human all
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Genomic context

Location:: 6 F3; 6 62.49 cM

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	6	NC_000072.7 (127665972..127746430, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	6	NC_000072.6 (127689009..127769467, complement)

Chromosome 6 - NC_000072.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tau-binding protein PRMT8 facilitates vacuole degeneration in the brain.
Title: Tau-binding protein PRMT8 facilitates vacuole degeneration in the brain.
PRMT8 Attenuates Cerebral Ischemia/Reperfusion Injury via Modulating Microglia Activation and Polarization to Suppress Neuroinflammation by Upregulating Lin28a.
Title: PRMT8 Attenuates Cerebral Ischemia/Reperfusion Injury via Modulating Microglia Activation and Polarization to Suppress Neuroinflammation by Upregulating Lin28a.
Impairment of PRMT8 oligomerization/dimerization by Cterminal deletion induces PRMT8 mis-localization to the mitochondria, prevents the formation of punctate structures by PRMT8(G2A), and inhibits PRMT8(C9S) patch-like plasma membrane localization.
Title: Deciphering the molecular mechanisms underlying the plasma membrane targeting of PRMT8.
Protein arginine methyltransferase 8 (PRMT8) is a cell-type-restricted arginine methyltransferase responsible for proper asymmetric dimethyl arginine level in postmitotic spinal cord motoneurons. PRMT8-dependent arginine methylation is required for neuroprotection against age-related increases of cellular stress.
Title: Arginine Methyltransferase PRMT8 Provides Cellular Stress Tolerance in Aging Motoneurons.
Together, our findings establish important roles for PRMT8 in regulating neuron function and cognition in the mammalian brain.
Title: Loss of Protein Arginine Methyltransferase 8 Alters Synapse Composition and Function, Resulting in Behavioral Defects.
human dermal fibroblast cells express a novel PRMT8 mRNA variant.
Title: Novel Protein Arginine Methyltransferase 8 Isoform Is Essential for Cell Proliferation.
Prmt8 is involved in synaptic maturation and is a modulator of developmental neuroplasticity.
Title: Network-based characterization of the synaptic proteome reveals that removal of epigenetic regulator Prmt8 restricts proteins associated with synaptic maturation.
besides its known function in nervous system, Prmt8 could play a role in pluripotent stem cells
Title: Protein arginine Methyltransferase 8 gene is expressed in pluripotent stem cells and its expression is modulated by the transcription factor Sox2.
PRMT8 is a neuron-specific nuclear enzyme broadly distributed in the CNS neurons and the N-terminus does not contain the glycine end for myristoylation target
Title: The distribution and characterization of endogenous protein arginine N-methyltransferase 8 in mouse CNS.
PRMT8 is chiefly involved in the somatosensory and limbic systems, and a part of motor system of the brain.
Title: Specific regional distribution of protein arginine methyltransferase 8 (PRMT8) in the mouse brain.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

36.MMHAP26FLD6.seq (e-PCR)
- UniSTS:124176

27.MMHAP24FLA6.seq (e-PCR)
- UniSTS:123777

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

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables S-adenosyl-L-methionine binding	ISO Inferred from Sequence Orthology more info
enables S-adenosyl-L-methionine binding	ISS Inferred from Sequence or Structural Similarity more info
enables S-adenosylmethionine-dependent methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables S-adenosylmethionine-dependent methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables enzyme binding	ISS Inferred from Sequence or Structural Similarity more info
enables histone H2AQ104 methyltransferase activity	IEA Inferred from Electronic Annotation 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	IEA Inferred from Electronic Annotation more info
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 H4 methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables histone H4 methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables histone H4K12 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H4R3 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISS Inferred from Sequence or Structural Similarity more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
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	ISO Inferred from Sequence Orthology more info
enables protein-arginine omega-N asymmetric methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein-arginine omega-N monomethyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine omega-N monomethyltransferase activity	ISO Inferred from Sequence Orthology more info
enables protein-arginine omega-N monomethyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info

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	ISO Inferred from Sequence Orthology more info
involved_in protein homooligomerization	ISO Inferred from Sequence Orthology more info
involved_in protein homooligomerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein methylation	ISO Inferred from Sequence Orthology more info
involved_in protein methylation	ISS Inferred from Sequence or Structural Similarity more info
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	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of modification of postsynaptic actin cytoskeleton	IEP Inferred from Expression Pattern more info	PubMed
involved_in regulation of modification of postsynaptic actin cytoskeleton	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasmic side of plasma membrane	ISO Inferred from Sequence Orthology more info
located_in cytoplasmic side of plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in glutamatergic synapse	IEA Inferred from Electronic Annotation more info
NOT located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity 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; heterogeneous nuclear ribonucleoprotein methyltransferase-like 4; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4; protein arginine N-methyltransferase 4

NP_958759.2

EC 2.1.1.319

XP_006506415.1

EC 2.1.1.319

XP_030111350.1

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_201371.2 → NP_958759.2 protein arginine N-methyltransferase 8

See identical proteins and their annotated locations for NP_958759.2

Status: VALIDATED

Source sequence(s)

AC127373, BC060250

Consensus CDS

CCDS57449.1

UniProtKB/Swiss-Prot

Q6PAK3, Q7M6Z2

Related

ENSMUSP00000032500.9, ENSMUST00000032500.9

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). ...

RNA

NR_157230.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

AC127373

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

Reference GRCm39 C57BL/6J

Genomic

NC_000072.7 Reference GRCm39 C57BL/6J

Range

127665972..127746430 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_030255490.1 → XP_030111350.1 protein arginine N-methyltransferase 8 isoform X1

Conserved Domains (1) summary

cd02440
Location:27 → 127

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). ...
XM_006506352.4 → XP_006506415.1 protein arginine N-methyltransferase 8 isoform X1

Conserved Domains (1) summary

cd02440
Location:27 → 127

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). ...