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

    Gene ID: 3276, updated on 4-Jan-2025

    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: Tissue-specific circular RNA induction during human fetal development
    • Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
    • BioProject: PRJNA270632
    • Publication: PMID 26076956
    • Analysis date: Mon Apr 2 22:54:59 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

    General gene information

    Gene Ontology Provided by GOA

    Items 1 - 25 of 36
    Function Evidence Code Pubs
    enables GATOR1 complex binding  
    enables N-methyltransferase activity PubMed 
    enables N-methyltransferase activity PubMed 
    enables RNA binding PubMed 
    enables S-adenosyl-L-methionine binding PubMed 
    enables enzyme binding PubMed 
    enables histone H2AQ104 methyltransferase activity  
    enables histone H3K37 methyltransferase activity  
    enables histone H3K56 methyltransferase activity  
    enables histone H3R17 methyltransferase activity  
    enables histone H3R2 methyltransferase activity  
    enables histone H3R26 methyltransferase activity  
    enables histone H3R8 methyltransferase activity  
    enables histone H4K12 methyltransferase activity  
    enables histone H4R3 methyltransferase activity PubMed 
    enables histone H4R3 methyltransferase activity PubMed 
    enables histone methyltransferase activity  
    enables histone methyltransferase activity PubMed 
    enables identical protein binding PubMed 
    enables identical protein binding PubMed 
    enables methyl-CpG binding PubMed 
    enables methyltransferase activity PubMed 
    enables mitogen-activated protein kinase p38 binding PubMed 
    enables protein binding PubMed 
    enables protein methyltransferase activity PubMed 
    enables protein methyltransferase activity PubMed 
    enables protein methyltransferase activity  
    enables protein-arginine N-methyltransferase activity PubMed 
    enables protein-arginine N-methyltransferase activity PubMed 
    enables protein-arginine N-methyltransferase activity  
    enables protein-arginine omega-N asymmetric methyltransferase activity  
    enables protein-arginine omega-N asymmetric methyltransferase activity PubMed 
    enables protein-arginine omega-N asymmetric methyltransferase activity PubMed 
    enables protein-arginine omega-N asymmetric methyltransferase activity  
    enables protein-arginine omega-N monomethyltransferase activity  
    enables protein-arginine omega-N monomethyltransferase activity PubMed 
    Items 1 - 25 of 36
    Items 1 - 25 of 27
    Process Evidence Code Pubs
    involved_in DNA damage response PubMed 
    involved_in RNA splicing  
    involved_in cardiac muscle tissue development  
    involved_in cell surface receptor signaling pathway PubMed 
    involved_in cellular response to methionine PubMed 
    involved_in cellular response to methionine  
    involved_in chromatin remodeling  
    involved_in in utero embryonic development  
    involved_in negative regulation of JNK cascade PubMed 
    involved_in negative regulation of megakaryocyte differentiation PubMed 
    involved_in neuron projection development PubMed 
    involved_in peptidyl-arginine methylation PubMed 
    involved_in positive regulation of TORC1 signaling PubMed 
    involved_in positive regulation of TORC1 signaling  
    involved_in positive regulation of cell population proliferation PubMed 
    involved_in positive regulation of double-strand break repair via homologous recombination PubMed 
    involved_in positive regulation of erythrocyte differentiation PubMed 
    involved_in positive regulation of hemoglobin biosynthetic process  
    involved_in positive regulation of p38MAPK cascade  
    involved_in positive regulation of translation PubMed 
    involved_in protein homooligomerization PubMed 
    involved_in protein methylation PubMed 
    involved_in regulation of BMP signaling pathway PubMed 
    involved_in regulation of DNA-templated transcription  
    involved_in regulation of megakaryocyte differentiation PubMed 
    involved_in regulation of megakaryocyte differentiation  
    involved_in viral protein processing  
    Items 1 - 25 of 27
    Component Evidence Code Pubs
    located_in cytoplasm PubMed 
    located_in cytosol  
    is_active_in lysosomal membrane PubMed 
    part_of methylosome PubMed 
    located_in nucleoplasm  
    located_in nucleoplasm  
    is_active_in nucleus  
    located_in nucleus 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)

    NEW Try the new Transcript table

    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_001207042.3 → 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). ...
    2. 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). ...
    3. 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

    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_047438742.1 → XP_047294698.1  protein arginine N-methyltransferase 1 isoform X1

      UniProtKB/TrEMBL
      Q5U8W9
    2. XM_047438743.1 → XP_047294699.1  protein arginine N-methyltransferase 1 isoform X1

      UniProtKB/TrEMBL
      Q5U8W9
      Related
      ENSP00000433556.1, ENST00000532489.5
    3. 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). ...
    4. 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

    1. NC_060943.1 Alternate T2T-CHM13v2.0

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

    mRNA and Protein(s)

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

      UniProtKB/TrEMBL
      Q5U8W9
    2. XM_054320811.1 → XP_054176786.1  protein arginine N-methyltransferase 1 isoform X3

      UniProtKB/TrEMBL
      Q5U8W9

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