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

    Gene ID: 3276, updated on 27-Nov-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
    NEW
    Try the new Gene table
    Try the new Transcript table

    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
    • 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 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 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)

    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_001207042.3NP_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.