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

Gene ID: 3276, updated on 10-Oct-2024

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
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Genomic context

See PRMT1 in Genome Data Viewer
Location:
19q13.33
Exon count:
13
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 19 NC_000019.10 (49676153..49688447)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 19 NC_060943.1 (52677341..52688515)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 19 NC_000019.9 (50180528..50191704)

Chromosome 19 - NC_000019.10Genomic Context describing neighboring genes Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:50143247-50143916 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:50143917-50144586 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:50144587-50145256 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10927 Neighboring gene SR-related CTD associated factor 1 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:50158945-50159720 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:50161341-50162044 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10928 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10929 Neighboring gene interferon regulatory factor 3 Neighboring gene BCL2 like 12 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr19:50175361-50175919 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 14954 Neighboring gene H3K27ac hESC enhancer GRCh37_chr19:50180167-50180898 Neighboring gene ReSE screen-validated silencer GRCh37_chr19:50184019-50184183 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10932 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10933 Neighboring gene microRNA 5088 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:50190450-50191191 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr19:50191192-50191932 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 10934 Neighboring gene adrenomedullin 5 (putative) Neighboring gene carnitine palmitoyltransferase 1C

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HIV-1 interactions

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

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

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 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 DNA damage response IDA
Inferred from Direct Assay
more info
PubMed 
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 IDA
Inferred from Direct Assay
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 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 positive regulation of TORC1 signaling IDA
Inferred from Direct Assay
more info
PubMed 
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 DNA-templated transcription IBA
Inferred from Biological aspect of Ancestor
more info
 
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
 
is_active_in lysosomal membrane IDA
Inferred from Direct Assay
more info
PubMed 
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

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
NP_001527.3
NP_938074.2
XP_016882224.1
XP_016882225.1
XP_047294698.1
XP_047294699.1
XP_054176785.1
XP_054176786.1

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.

Genomic

  1. NG_031846.1 RefSeqGene

    Range
    5120..16296
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001207042.3NP_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:74143
    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_001536.6NP_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:92192
    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). ...
  3. NM_198318.5NP_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:74174
    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

  1. 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_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000019.10 Reference GRCh38.p14 Primary Assembly

    Range
    49676153..49688447
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_047438742.1XP_047294698.1  protein arginine N-methyltransferase 1 isoform X1

  2. XM_047438743.1XP_047294699.1  protein arginine N-methyltransferase 1 isoform X1

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

    UniProtKB/TrEMBL
    Q5U8W9
    Conserved Domains (1) summary
    cd02440
    Location:68168
    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). ...
  4. XM_017026736.2XP_016882225.1  protein arginine N-methyltransferase 1 isoform X3

    UniProtKB/TrEMBL
    Q5U8W9
    Conserved Domains (1) summary
    cd02440
    Location:63163
    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

  1. NC_060943.1 Alternate T2T-CHM13v2.0

    Range
    52677341..52688515
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054320810.1XP_054176785.1  protein arginine N-methyltransferase 1 isoform X2

  2. XM_054320811.1XP_054176786.1  protein arginine N-methyltransferase 1 isoform X3

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. 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.