PRMT1 protein arginine methyltransferase 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRMT1provided by HGNC
Official Full Name: protein arginine methyltransferase 1provided by HGNC
Primary source: HGNC:HGNC:5187
See related: Ensembl:ENSG00000126457 MIM:602950; AllianceGenome:HGNC:5187
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: ANM1; HCP1; IR1B4; HRMT1L2
Summary: This gene encodes a member of the protein arginine N-methyltransferase (PRMT) family. Post-translational modification of target proteins by PRMTs plays an important regulatory role in many biological processes, whereby PRMTs methylate arginine residues by transferring methyl groups from S-adenosyl-L-methionine to terminal guanidino nitrogen atoms. The encoded protein is a type I PRMT and is responsible for the majority of cellular arginine methylation activity. Increased expression of this gene may play a role in many types of cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 5. [provided by RefSeq, Dec 2011]
Expression: Ubiquitous expression in ovary (RPKM 42.8), heart (RPKM 38.0) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 19q13.33

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (49676153..49688447)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (52677341..52688515)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (50180528..50191704)

Chromosome 19 - NC_000019.10 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

Expression

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See details

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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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PRMT1 Sustains De Novo Fatty Acid Synthesis by Methylating PHGDH to Drive Chemoresistance in Triple-Negative Breast Cancer.
Title: PRMT1 Sustains De Novo Fatty Acid Synthesis by Methylating PHGDH to Drive Chemoresistance in Triple-Negative Breast Cancer.
PRMT1 acts as a suppressor of MHC-I and anti-tumor immunity.
Title: PRMT1 acts as a suppressor of MHC-I and anti-tumor immunity.
PRMT1 promotes pancreatic cancer development and resistance to chemotherapy.
Title: PRMT1 promotes pancreatic cancer development and resistance to chemotherapy.
Inhibition of PRMT1 Suppresses the Growth of U87MG-Derived Glioblastoma Stem Cells by Blocking the STAT3 Signaling Pathway.
Title: Inhibition of PRMT1 Suppresses the Growth of U87MG-Derived Glioblastoma Stem Cells by Blocking the STAT3 Signaling Pathway.
PRMT1-mediated PGK1 arginine methylation promotes colorectal cancer glycolysis and tumorigenesis.
Title: PRMT1-mediated PGK1 arginine methylation promotes colorectal cancer glycolysis and tumorigenesis.
Protein arginine N-methyltransferase 2 plays a noncatalytic role in the histone methylation activity of PRMT1.
Title: Protein arginine N-methyltransferase 2 plays a noncatalytic role in the histone methylation activity of PRMT1.
Targeting PRMT1 prevents acute and chronic graft-versus-host disease.
Title: Targeting PRMT1 prevents acute and chronic graft-versus-host disease.
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.
CDK5-PRMT1-WDR24 signaling cascade promotes mTORC1 signaling and tumor growth.
Title: CDK5-PRMT1-WDR24 signaling cascade promotes mTORC1 signaling and tumor growth.
Methylation of BRD4 by PRMT1 regulates BRD4 phosphorylation and promotes ovarian cancer invasion.
Title: Methylation of BRD4 by PRMT1 regulates BRD4 phosphorylation and promotes ovarian cancer invasion.

Submit: New GeneRIF Correction See all GeneRIFs (199)

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

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Pr55(Gag)	gag	HIV-1 Gag is identified to have a physical interaction with protein arginine methyltransferase 1 (PRMT1; ANM1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed
nucleocapsid	gag	HIV-1 NC is identified to have a physical interaction with protein arginine methyltransferase 1 (PRMT1; ANM1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D11S2921 (e-PCR)
- UniSTS:152074

RH91411 (e-PCR)
- UniSTS:84537

RH68301 (e-PCR)
- UniSTS:26699

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

STS-N90422 (e-PCR)
- UniSTS:26294

RH65905 (e-PCR)
- UniSTS:2775

NoName (e-PCR)
- UniSTS:486645

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables GATOR1 complex binding	ISS Inferred from Sequence or Structural Similarity more info
enables N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables N-methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables RNA binding	HDA more info	PubMed
enables S-adenosyl-L-methionine binding	IDA Inferred from Direct Assay more info	PubMed
enables enzyme binding	IPI Inferred from Physical Interaction more info	PubMed
enables histone H4R3 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone H4R3 methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
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 identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables methyl-CpG binding	IDA Inferred from Direct Assay more info	PubMed
enables methyltransferase activity	TAS Traceable Author Statement more info	PubMed
enables mitogen-activated protein kinase p38 binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein methyltransferase activity	TAS Traceable Author Statement more info
enables protein-arginine N-methyltransferase activity	EXP Inferred from Experiment more info	PubMed
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	TAS Traceable Author Statement 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	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N asymmetric methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-arginine omega-N asymmetric methyltransferase activity	TAS Traceable Author Statement 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	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in RNA splicing	ISS Inferred from Sequence or Structural Similarity more info
involved_in cardiac muscle tissue development	ISS Inferred from Sequence or Structural Similarity more info
involved_in cell surface receptor signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in cellular response to methionine	ISS Inferred from Sequence or Structural Similarity 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
involved_in in utero embryonic development	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of JNK cascade	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of megakaryocyte differentiation	IDA Inferred from Direct Assay more info	PubMed
involved_in neuron projection development	IMP Inferred from Mutant Phenotype more info	PubMed
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 positive regulation of TORC1 signaling	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of double-strand break repair via homologous recombination	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of erythrocyte differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of hemoglobin biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of p38MAPK cascade	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of translation	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 BMP signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of megakaryocyte differentiation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of megakaryocyte differentiation	TAS Traceable Author Statement more info
involved_in viral protein processing	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
located_in lysosomal membrane	IEA Inferred from Electronic Annotation more info
part_of methylosome	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement 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

General protein information

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Preferred Names: protein arginine N-methyltransferase 1

Names: HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 2; heterogeneous nuclear ribonucleoprotein methyltransferase 1-like 2; highly conserved protein 1; histone-arginine N-methyltransferase PRMT1; interferon receptor 1-bound protein 4

NP_001193971.1

EC 2.1.1.319

NP_001527.3

EC 2.1.1.319

NP_938074.2

EC 2.1.1.319

XP_016882224.1

EC 2.1.1.319

XP_016882225.1

EC 2.1.1.319

XP_047294698.1

EC 2.1.1.319

XP_047294699.1

EC 2.1.1.319

XP_054176785.1

EC 2.1.1.319

XP_054176786.1

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.

Genomic

NG_031846.1 RefSeqGene

Range

5120..16296

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001207042.3 → NP_001193971.1 protein arginine N-methyltransferase 1 isoform 4

See identical proteins and their annotated locations for NP_001193971.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) lacks three exons in the coding region, but maintains the reading frame, compared to variant 1. The encoded isoform (4) is shorter than isoform 1.

Source sequence(s)

AI193116, BX352789, DC421815

Consensus CDS

CCDS74425.1

UniProtKB/TrEMBL

A0A087X1W2

Related

ENSP00000484505.1, ENST00000610806.4

Conserved Domains (1) summary

cd02440
Location:74 → 143

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_001536.6 → NP_001527.3 protein arginine N-methyltransferase 1 isoform 1

See identical proteins and their annotated locations for NP_001527.3

Status: REVIEWED

Description

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

Source sequence(s)

AK304660, DC421815, Y10806

Consensus CDS

CCDS46145.1

UniProtKB/Swiss-Prot

A0A087X1W2, B4E3C3, G5E9B6, H7C2I1, Q15529, Q2VP93, Q6LEU5, Q8WUW5, Q99872, Q99873, Q99874, Q9NZ04, Q9NZ05, Q9NZ06

UniProtKB/TrEMBL

A0A3S6H7X4

Related

ENSP00000406162.2, ENST00000454376.7

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). ...
NM_198318.5 → NP_938074.2 protein arginine N-methyltransferase 1 isoform 3

See identical proteins and their annotated locations for NP_938074.2

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an exon in the coding region, but maintains the reading frame, compared to variant 1. The encoded isoform (3) is shorter than isoform 1.

Source sequence(s)

DC421815, Y10807

Consensus CDS

CCDS42592.1

UniProtKB/TrEMBL

Q5U8W9

Related

ENSP00000375724.4, ENST00000391851.8

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). ...

RNA

NR_033397.5 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (2) contains an alternate internal 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)

AI193116, CN264743, CR407608

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

NC_000019.10 Reference GRCh38.p14 Primary Assembly

Range

49676153..49688447

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047438742.1 → XP_047294698.1 protein arginine N-methyltransferase 1 isoform X1
XM_047438743.1 → XP_047294699.1 protein arginine N-methyltransferase 1 isoform X1

Related

ENSP00000433556.1, ENST00000532489.5
XM_017026735.2 → XP_016882224.1 protein arginine N-methyltransferase 1 isoform X2

UniProtKB/TrEMBL

Q5U8W9

Conserved Domains (1) summary

cd02440
Location:68 → 168

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_017026736.2 → XP_016882225.1 protein arginine N-methyltransferase 1 isoform X3

UniProtKB/TrEMBL

Q5U8W9

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). ...

Alternate T2T-CHM13v2.0

Genomic

NC_060943.1 Alternate T2T-CHM13v2.0

Range

52677341..52688515

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054320810.1 → XP_054176785.1 protein arginine N-methyltransferase 1 isoform X2
XM_054320811.1 → XP_054176786.1 protein arginine N-methyltransferase 1 isoform X3

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_198319.2: Suppressed sequence

Description

NM_198319.2: This RefSeq was permanently suppressed because it contains a uORF at nt 43..240 that is predicted to inhibit translation of the annotated CDS.