Prmt1 protein arginine N-methyltransferase 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prmt1provided by MGI
Official Full Name: protein arginine N-methyltransferase 1provided by MGI
Primary source: MGI:MGI:107846
See related: Ensembl:ENSMUSG00000109324 AllianceGenome:MGI:107846
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: Mrmt1; Hrmt1l2; 6720434D09Rik
Summary: Enables GATOR1 complex binding activity; histone methyltransferase activity; and protein-arginine omega-N asymmetric methyltransferase activity. Involved in several processes, including RNA splicing; cellular response to methionine; and positive regulation of TORC1 signaling. Acts upstream of or within in utero embryonic development. Located in nucleus. Is expressed in several structures, including alimentary system; branchial arch; central nervous system; genitourinary system; and lung. Used to study cleft palate. Orthologous to human PRMT1 (protein arginine methyltransferase 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in CNS E11.5 (RPKM 124.9), CNS E18 (RPKM 124.2) and 27 other tissues See more
Orthologs: human all
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Genomic context

Location:: 7 B3; 7 29.07 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	7	NC_000073.7 (44626179..44635844, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	7	NC_000073.6 (44976755..44986420, complement)

Chromosome 7 - NC_000073.7 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?

EGR3 reduces podocyte inflammatory damage in obesity related glomerulopathy by inhibiting the PRMT1/p-STAT3 pathway.
Title: EGR3 reduces podocyte inflammatory damage in obesity related glomerulopathy by inhibiting the PRMT1/p-STAT3 pathway.
LPCAT2 inhibits colorectal cancer progression via the PRMT1/SLC7A11 axis.
Title: LPCAT2 inhibits colorectal cancer progression via the PRMT1/SLC7A11 axis.
PRMT1 promotes pancreatic cancer development and resistance to chemotherapy.
Title: PRMT1 promotes pancreatic cancer development and resistance to chemotherapy.
Protein arginine methyltransferase 1 is required for the maintenance of adult small intestinal and colonic epithelial cell homeostasis.
Title: Protein arginine methyltransferase 1 is required for the maintenance of adult small intestinal and colonic epithelial cell homeostasis.
PRMT1 accelerates cell proliferation, migration, and tumor growth by upregulating ZEB1/H4R3me2as in thyroid carcinoma.
Title: PRMT1 accelerates cell proliferation, migration, and tumor growth by upregulating ZEB1/H4R3me2as in thyroid carcinoma.
The arginine methyltransferase Prmt1 coordinates the germline arginine methylome essential for spermatogonial homeostasis and male fertility.
Title: The arginine methyltransferase Prmt1 coordinates the germline arginine methylome essential for spermatogonial homeostasis and male fertility.
Inhibition of PRMT1 alleviates sepsis-induced acute kidney injury in mice by blocking the TGF-beta1 and IL-6 trans-signaling pathways.
Title: Inhibition of PRMT1 alleviates sepsis-induced acute kidney injury in mice by blocking the TGF-β1 and IL-6 trans-signaling pathways.
PRMT1-mediated arginine methylation promotes postnatal calvaria bone formation through BMP-Smad signaling.
Title: PRMT1-mediated arginine methylation promotes postnatal calvaria bone formation through BMP-Smad signaling.
PRMT1 reverts the immune escape of necroptotic colon cancer through RIP3 methylation.
Title: PRMT1 reverts the immune escape of necroptotic colon cancer through RIP3 methylation.
Protein arginine methyltransferase 1 regulates B cell fate after positive selection in the germinal center in mice.
Title: Protein arginine methyltransferase 1 regulates B cell fate after positive selection in the germinal center in mice.

Submit: New GeneRIF Correction See all GeneRIFs (74)

Variation

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Alleles

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

Endonuclease-mediated (3)
Gene trapped (1) 1 citation
Targeted (7) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Hrmt1l2-rs (e-PCR), detects polymorphism
- UniSTS:143403

D10Mit157.2 (e-PCR), detects polymorphism
- UniSTS:126061

AW214366 (e-PCR)
- UniSTS:179568

Hrmt1l2 (e-PCR), detects polymorphism
- UniSTS:275867

BI285876 (e-PCR)
- UniSTS:244917

Prmt1 (e-PCR), detects polymorphism
- UniSTS:479204

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables GATOR1 complex binding	IDA Inferred from Direct Assay more info	PubMed
enables N-methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables N-methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
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 enzyme binding	ISO Inferred from Sequence Orthology 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 H4K12 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H4R3 methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables histone H4R3 methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
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 histone methyltransferase activity	ISO Inferred from Sequence Orthology 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 methyl-CpG binding	ISO Inferred from Sequence Orthology more info
enables methyl-CpG binding	ISS Inferred from Sequence or Structural Similarity more info
enables mitogen-activated protein kinase p38 binding	IEA Inferred from Electronic Annotation more info
enables mitogen-activated protein kinase p38 binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	ISO Inferred from Sequence Orthology 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 asymmetric methyltransferase activity	ISO Inferred from Sequence Orthology 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
enables snoRNP binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in DNA damage response	IEA Inferred from Electronic Annotation more info
involved_in DNA damage response	ISO Inferred from Sequence Orthology more info
involved_in RNA splicing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cardiac muscle tissue development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to methionine	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to methionine	ISO Inferred from Sequence Orthology more info
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within in utero embryonic development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of JNK cascade	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of JNK cascade	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of megakaryocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of megakaryocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in neuron projection development	IEA Inferred from Electronic Annotation more info
involved_in neuron projection development	ISO Inferred from Sequence Orthology more info
involved_in peptidyl-arginine methylation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within peptidyl-arginine methylation, to asymmetrical-dimethyl arginine	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within peptidyl-arginine omega-N-methylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of TORC1 signaling	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of TORC1 signaling	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cell population proliferation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cell population proliferation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of double-strand break repair via homologous recombination	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of double-strand break repair via homologous recombination	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of erythrocyte differentiation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of erythrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of translation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of translation	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
acts_upstream_of_or_within protein methylation	ISO Inferred from Sequence Orthology more info
involved_in protein methylation	ISO Inferred from Sequence Orthology more info
involved_in regulation of BMP signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in regulation of BMP signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of megakaryocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in regulation of megakaryocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in lysosomal membrane	IEA Inferred from Electronic Annotation more info
is_active_in lysosomal membrane	ISO Inferred from Sequence Orthology more info
part_of methylosome	ISO Inferred from Sequence Orthology more info
part_of methylosome	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: protein arginine N-methyltransferase 1

Names: arginine N-methyltransferase 1; heterogeneous nuclear ribonucleoproteins methyltransferase-like 2; histone-arginine N-methyltransferase PRMT1

NP_001239405.1

EC 2.1.1.319

NP_001239406.1

EC 2.1.1.319

NP_062804.1

EC 2.1.1.319

XP_030098017.1

EC 2.1.1.319

XP_030098018.1

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_001252476.1 → NP_001239405.1 protein arginine N-methyltransferase 1 isoform 2

See identical proteins and their annotated locations for NP_001239405.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) lacks an alternate exon in the 5' coding region, compared to variant 1. The resulting protein (isoform 2) is shorter when it is compared to isoform 1.

Source sequence(s)

AI846916, AK152342, BU524421, BY760714

Consensus CDS

CCDS57547.1

UniProtKB/TrEMBL

F8WH01, Q3UIG8, Q80WB1

Related

ENSMUSP00000147252.2, ENSMUST00000207370.2

Conserved Domains (1) summary

cd02440
Location:74 → 174

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_001252477.1 → NP_001239406.1 protein arginine N-methyltransferase 1 isoform 3

See identical proteins and their annotated locations for NP_001239406.1

Status: VALIDATED

Description

Transcript Variant: This variant (3) has multiple differences in the coding region, compared to variant 1. The resulting protein (isoform 3) is shorter when it is compared to isoform 1.

Source sequence(s)

AI846916, AK020120, BU524421, W49313

Consensus CDS

CCDS85293.1

UniProtKB/TrEMBL

A0A140LJ70, Q9CX58

Related

ENSMUSP00000147101.2, ENSMUST00000207659.2

Conserved Domains (1) summary

cd02440
Location:74 → 140

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_019830.3 → NP_062804.1 protein arginine N-methyltransferase 1 isoform 1

See identical proteins and their annotated locations for NP_062804.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) encodes the longest protein (isoform 1).

Source sequence(s)

AF232716, AI846916, BU524421, BY760714

Consensus CDS

CCDS21222.1

UniProtKB/Swiss-Prot

Q99LS4, Q9JIF0

UniProtKB/TrEMBL

Q8C2D7

Related

ENSMUSP00000103474.4, ENSMUST00000107843.11

Conserved Domains (1) summary

cd02440
Location:92 → 192

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_045521.1 RNA Sequence

Status: VALIDATED

Description

Transcript Variant: This variant (4) contains an alternate 5' exon, compared to variant 1. This variant is represented as non-coding because the use of the 5'-most expected translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AI846916, BC051953, BU524421

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_000073.7 Reference GRCm39 C57BL/6J

Range

44626179..44635844 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_030242158.2 → XP_030098018.1 protein arginine N-methyltransferase 1 isoform X2

UniProtKB/TrEMBL

Q8C2D7

Conserved Domains (1) summary

cd02440
Location:63 → 163

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_030242157.2 → XP_030098017.1 protein arginine N-methyltransferase 1 isoform X1

UniProtKB/TrEMBL

Q80WV6, Q8C2D7

Conserved Domains (1) summary

cd02440
Location:75 → 175

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). ...