Prmt2 protein arginine N-methyltransferase 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prmt2provided by MGI
Official Full Name: protein arginine N-methyltransferase 2provided by MGI
Primary source: MGI:MGI:1316652
See related: Ensembl:ENSMUSG00000020230 AllianceGenome:MGI:1316652
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: Hrmt1l1
Summary: Enables beta-catenin binding activity; histone H3 methyltransferase activity; and protein-arginine N-methyltransferase activity. Involved in negative regulation of G1/S transition of mitotic cell cycle; regulation of DNA-templated transcription; and response to hypoxia. Predicted to be located in cytosol and nucleoplasm. Predicted to be active in nucleus. Is expressed in several structures, including alimentary system; genitourinary system; nervous system; respiratory system; and sensory organ. Orthologous to human PRMT2 (protein arginine methyltransferase 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in CNS E18 (RPKM 82.6), whole brain E14.5 (RPKM 68.0) and 23 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 C1; 10 38.74 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (76043060..76073699, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (76207226..76237865, complement)

Chromosome 10 - NC_000076.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein arginine methyltransferase 2 controls inflammatory signaling in acute myeloid leukemia.
Title: Protein arginine methyltransferase 2 controls inflammatory signaling in acute myeloid leukemia.
PRMT2 silencing regulates macrophage polarization through activation of STAT1 or inhibition of STAT6.
Title: PRMT2 silencing regulates macrophage polarization through activation of STAT1 or inhibition of STAT6.
Cobl-mediated dendritic arborization required PRMT2, complex formation with PRMT2, and PRMT2's catalytic activity
Title: Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl.
PRMT2 is a modular protein containing a catalytic Ado-Met-binding domain and unique Src homology 3 domain that binds proteins with proline-rich motifs.
Title: Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
PRMT2 represents a glucose-sensitive factor that plays a role in Liver X Receptor-mediated ATP-binding cassette transporter A1-dependent cholesterol efflux and lends insight to the presence of increased atherosclerosis in diabetic patients.
Title: LXR-Mediated ABCA1 Expression and Function Are Modulated by High Glucose and PRMT2.
Prmt2 is a new member of the NF-kappaB pathway controlling lipopolysaccharide (LPS)-induced inflammatory lung and macrophage responses in a dosage-dependent manner.
Title: Prmt2 regulates the lipopolysaccharide-induced responses in lungs and macrophages.
this study suggesting that the Cstb-Prmt2 region is not playing a major role in locomotor and cognitive deficits found in mice model of Down syndrome.
Title: The telomeric part of the human chromosome 21 from Cstb to Prmt2 is not necessary for the locomotor and short-term memory deficits observed in the Tc1 mouse model of Down syndrome.
data elucidate a molecular pathway that directly links arginine methylation of STAT3 by PRMT2 to the regulation of leptin signaling
Title: Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation.
ADMA and nitrosative stress are related to increased expression of protein-arginine methyltransferase-2, an ADMA-synthesizing enzyme, and reduced expression of dimethylarginine dimethylaminohydrolase-2, an ADMA-degrading enzyme, in bronchial epithelia
Title: Altered asymmetric dimethyl arginine metabolism in allergically inflamed mouse lungs.
mRNA and protein expression was increased in primary fibroblasts isolated from bleomycin-treated mice.
Title: Functional role and species-specific contribution of arginases in pulmonary fibrosis.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

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

Endonuclease-mediated (3)
Targeted (6) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Hrmt1l1 (e-PCR), detects polymorphism
- UniSTS:259087

AA945753 (e-PCR)
- UniSTS:250429

Prmt2 (e-PCR), detects polymorphism
- UniSTS:479205

AI504737 (e-PCR)
- UniSTS:159993

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables beta-catenin binding	IPI Inferred from Physical Interaction more info	PubMed
enables histone H2AQ104 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
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	IEA Inferred from Electronic Annotation more info
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables histone methyltransferase activity	ISO Inferred from Sequence Orthology more info
enables histone methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables nuclear androgen receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear androgen receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables nuclear estrogen receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear estrogen receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables nuclear progesterone receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear progesterone receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables nuclear retinoic acid receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear retinoic acid receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables nuclear thyroid hormone receptor binding	ISO Inferred from Sequence Orthology more info
enables nuclear thyroid hormone receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables peroxisome proliferator activated receptor binding	ISO Inferred from Sequence Orthology more info
enables peroxisome proliferator activated receptor binding	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
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 N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine N-methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-arginine omega-N asymmetric methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-containing complex binding	IPI Inferred from Physical Interaction more info	PubMed
enables transcription coactivator activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cell surface receptor signaling pathway via STAT	NAS Non-traceable Author Statement more info	PubMed
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 developmental cell growth	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in leptin-mediated signaling pathway	NAS Non-traceable Author Statement more info	PubMed
involved_in methylation	NAS Non-traceable Author Statement more info	PubMed
involved_in negative regulation of DNA-binding transcription factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of DNA-templated transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of DNA-templated transcription	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of G1/S transition of mitotic cell cycle	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of NF-kappaB transcription factor activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA-templated transcription	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA-templated transcription	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	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 androgen receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of androgen receptor signaling pathway	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to hypoxia	IDA Inferred from Direct Assay more info	PubMed

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	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity 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	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: protein arginine N-methyltransferase 2

Names: heterogeneous nuclear ribonucleoprotein methyltransferase-like 1; histone-arginine N-methyltransferase PRMT2

NP_001071106.1

EC 2.1.1.319

NP_001289894.1

EC 2.1.1.319

NP_573445.2

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_001077638.2 → NP_001071106.1 protein arginine N-methyltransferase 2 isoform 2

See identical proteins and their annotated locations for NP_001071106.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and uses an alternate in-frame splice site in the 3' coding region, compared to variant 3. This results in isoform 2, which is shorter than isoform 1. Variants 1 and 2 encode the same isoform (2).

Source sequence(s)

AI504737, AK144412, AK159186, BY288156

Consensus CDS

CCDS35942.1

UniProtKB/Swiss-Prot

Q9R144

UniProtKB/TrEMBL

Q3UKX1

Related

ENSMUSP00000097166.4, ENSMUST00000099571.10

Conserved Domains (4) summary

cd02440
Location:153 → 253

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). ...

cd11806
Location:46 → 98

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

pfam05185
Location:143 → 427

PRMT5; PRMT5 arginine-N-methyltransferase

cl17173
Location:122 → 181

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_001302965.1 → NP_001289894.1 protein arginine N-methyltransferase 2 isoform 1

See identical proteins and their annotated locations for NP_001289894.1

Status: VALIDATED

Description

Transcript Variant: This variant (3) represent the longest transcript and encodes the longer isoform (1).

Source sequence(s)

AI504737, AK146966, BY288156

Consensus CDS

CCDS78836.1

UniProtKB/Swiss-Prot

Q9R144

UniProtKB/TrEMBL

Q3UID4

Related

ENSMUSP00000097167.4, ENSMUST00000099572.10

Conserved Domains (3) summary

cd02440
Location:153 → 253

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). ...

cd11806
Location:46 → 98

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:122 → 181

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_133182.3 → NP_573445.2 protein arginine N-methyltransferase 2 isoform 2

See identical proteins and their annotated locations for NP_573445.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) uses an alternate in-frame splice site in the 3' coding region, compared to variant 3. This results in isoform 2, which is shorter than isoform 1. Variants 1 and 2 encode the same isoform (2).

Source sequence(s)

AI504737, AK159186, BY288156, BY727303

Consensus CDS

CCDS35942.1

UniProtKB/Swiss-Prot

Q9R144

UniProtKB/TrEMBL

Q3UKX1

Related

ENSMUSP00000020452.6, ENSMUST00000020452.12

Conserved Domains (4) summary

cd02440
Location:153 → 253

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). ...

cd11806
Location:46 → 98

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

pfam05185
Location:143 → 427

PRMT5; PRMT5 arginine-N-methyltransferase

cl17173
Location:122 → 181

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_126571.1 RNA Sequence

Status: VALIDATED

Description

Transcript Variant: This variant (4) contains an alternate internal exon and uses an alternate splice site in an internal exon, compared to variant 3. This variant is represented as non-coding because the use of the 5'-most expected translational start codon, as used in variant 3, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AI504737, AK146754, BY288156

Related

ENSMUST00000128099.8