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

Gene ID: 10196, updated on 26-May-2016
Official Symbol
PRMT3provided by HGNC
Official Full Name
protein arginine methyltransferase 3provided by HGNC
Primary source
HGNC:HGNC:30163
See related
Ensembl:ENSG00000185238 HPRD:11934; MIM:603190; Vega:OTTHUMG00000166022
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]
Orthologs
Location:
11p15.1
Exon count:
17
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 11 NC_000011.10 (20387530..20509333)
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 HIV-1 Tat interactive protein 2 Neighboring gene uncharacterized LOC105376584 Neighboring gene high mobility group box 1 pseudogene 40

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

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

Products Interactant Other Gene Complex Source Pubs Description

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
 
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
methyltransferase activity IDA
Inferred from Direct Assay
more info
PubMed 
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 omega-N asymmetric methyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
Process Evidence Code Pubs
histone arginine methylation IEA
Inferred from Electronic Annotation
more info
 
negative regulation of protein ubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
peptidyl-arginine methylation, to asymmetrical-dimethyl arginine IEA
Inferred from Electronic Annotation
more info
 
regulation of transcription, DNA-templated IBA
Inferred from Biological aspect of Ancestor
more info
 
Component Evidence Code Pubs
cytoplasm NAS
Non-traceable Author Statement
more info
PubMed 
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
 
ribosome IEA
Inferred from Electronic Annotation
more info
 
Preferred Names
protein arginine N-methyltransferase 3
Names
HMT1 hnRNP methyltransferase-like 3
heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

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, OTTHUMP00000231735, ENST00000437750, OTTHUMT00000387493
    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_005788.3NP_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)
    BC064831, CA428457, DA163907, DB510248
    Consensus CDS
    CCDS7853.1
    UniProtKB/Swiss-Prot
    O60678
    Related
    ENSP00000331879, OTTHUMP00000231732, ENST00000331079, OTTHUMT00000387489
    Conserved Domains (2) 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). ...
    pfam12756
    Location:5099
    zf-C2H2_2; C2H2 type zinc-finger (2 copies)

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107 details...

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

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000011.10 Reference GRCh38.p2 Primary Assembly

    Range
    20387530..20509333
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011519837.1XP_011518139.1  

    Conserved Domains (1) summary
    cd02440
    Location:205305
    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_011519836.1XP_011518138.1  

    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). ...

Alternate CHM1_1.1

Genomic

  1. NC_018922.2 Alternate CHM1_1.1

    Range
    20408983..20530723
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)