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PRMT3 protein arginine methyltransferase 3 [ Homo sapiens (human) ]

Gene ID: 10196, updated on 7-Dec-2018

Summary

Official Symbol
PRMT3provided by HGNC
Official Full Name
protein arginine methyltransferase 3provided by HGNC
Primary source
HGNC:HGNC:30163
See related
Ensembl:ENSG00000185238 MIM:603190
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
HRMT1L3
Summary
This gene belongs to the protein arginine methyltransferase (PRMT) family. The encoded enzyme catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. The enzyme acts on 40S ribosomal protein S2 (rpS2), which is its major in-vivo substrate, and is involved in the proper maturation of the 80S ribosome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]
Expression
Ubiquitous expression in thyroid (RPKM 7.5), brain (RPKM 3.3) and 25 other tissues See more
Orthologs

Genomic context

See PRMT3 in Genome Data Viewer
Location:
11p15.1
Exon count:
18
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 11 NC_000011.10 (20387530..20510861)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 11 NC_000011.9 (20409076..20530879)

Chromosome 11 - NC_000011.10Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105376583 Neighboring gene NFE2L2 motif-containing MPRA enhancer 64 Neighboring gene HIV-1 Tat interactive protein 2 Neighboring gene uncharacterized LOC105376584 Neighboring gene high mobility group box 1 pseudogene 40

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 FunctionsWhat's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
Knockdown of protein arginine methyltransferase 3 (PRMT3) by shRNA library screening inhibits HIV-1 replication in cultured Jurkat T-cells PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • Chromatin modifying enzymes, organism-specific biosystem (from REACTOME)
    Chromatin modifying enzymes, organism-specific biosystemEukaryotic DNA is associated with histone proteins and organized into a complex nucleoprotein structure called chromatin. This structure decreases the accessibility of DNA but also helps to protect i...
  • Chromatin organization, organism-specific biosystem (from REACTOME)
    Chromatin organization, organism-specific biosystemChromatin organization refers to the composition and conformation of complexes between DNA, protein and RNA. It is determined by processes that result in the specification, formation or maintenance o...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
  • Protein methylation, organism-specific biosystem (from REACTOME)
    Protein methylation, organism-specific biosystemMethylation of lysine (Lys) and arginine (Arg) residues on non-histone proteins is a prevalent post-translational modification and important regulator of cellular signal transduction pathways includi...
  • RMTs methylate histone arginines, organism-specific biosystem (from REACTOME)
    RMTs methylate histone arginines, organism-specific biosystemArginine methylation is a common post-translational modification; around 2% of arginine residues are methylated in rat liver nuclei (Boffa et al. 1977). Arginine can be methylated in 3 different ways...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
histone-arginine N-methyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
methyltransferase activity IDA
Inferred from Direct Assay
more info
PubMed 
nucleic acid binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein-arginine N-methyltransferase activity NAS
Non-traceable Author Statement
more info
PubMed 
protein-arginine N-methyltransferase activity TAS
Traceable Author Statement
more info
 
protein-arginine omega-N asymmetric methyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ribosome binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
histone arginine methylation IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
negative regulation of protein ubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
peptidyl-arginine methylation, to asymmetrical-dimethyl arginine IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein methylation TAS
Traceable Author Statement
more info
 
regulation of transcription, DNA-templated IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Component Evidence Code Pubs
cytoplasm NAS
Non-traceable Author Statement
more info
PubMed 
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol TAS
Traceable Author Statement
more info
 
nucleus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 

General protein information

Preferred Names
protein arginine N-methyltransferase 3
Names
HMT1 hnRNP methyltransferase-like 3
heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

NCBI Reference Sequences (RefSeq)

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)

  1. NM_001145166.1NP_001138638.1  protein arginine N-methyltransferase 3 isoform 2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) is missing two non-consecutive internal coding exons compared to transcript variant 1. It uses the same translation start site as variant 1, however, the first missing exon throws it out of frame, and the second missing exon puts it back in frame, resulting in a shorter isoform (2) with a novel 28 aa segment compared to isoform 1.
    Source sequence(s)
    BC019339, CA428457, DA163907, DB510248
    Consensus CDS
    CCDS44554.1
    UniProtKB/TrEMBL
    A0A0A0MSN7, Q8WUV3
    Related
    ENSP00000397766.2, ENST00000437750.2
    Conserved Domains (1) summary
    cd02440
    Location:197297
    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_001145167.1NP_001138639.1  protein arginine N-methyltransferase 3 isoform 3

    See identical proteins and their annotated locations for NP_001138639.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (3) is missing a coding exon at the 5' end compared to transcript variant 1. This results in translation initiation from an in-frame downstream AUG by leaky scanning, and a shorter isoform (3) with a truncated N-terminus compared to isoform 1.
    Source sequence(s)
    BC019339, CA428457, DA163907, DB510248
    UniProtKB/TrEMBL
    Q8WUV3
    Conserved Domains (1) summary
    cd02440
    Location:182282
    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_005788.4NP_005779.1  protein arginine N-methyltransferase 3 isoform 1

    See identical proteins and their annotated locations for NP_005779.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AC025972, AC108005, KC877396, KF459543
    Consensus CDS
    CCDS7853.1
    UniProtKB/Swiss-Prot
    O60678
    Related
    ENSP00000331879.6, ENST00000331079.10
    Conserved Domains (1) summary
    cd02440
    Location:259359
    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). ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

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

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000011.10 Reference GRCh38.p12 Primary Assembly

    Range
    20387530..20510861
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024448312.1XP_024304080.1  protein arginine N-methyltransferase 3 isoform X3

    Conserved Domains (1) summary
    cd02440
    Location:95195
    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. XM_017017081.1XP_016872570.1  protein arginine N-methyltransferase 3 isoform X1

  3. XM_011519836.2XP_011518138.1  protein arginine N-methyltransferase 3 isoform X2

    Conserved Domains (1) summary
    cd02440
    Location:154254
    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. XR_001747718.2 RNA Sequence

  2. XR_002957114.1 RNA Sequence

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