PRMT5 protein arginine methyltransferase 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRMT5provided by HGNC
Official Full Name: protein arginine methyltransferase 5provided by HGNC
Primary source: HGNC:HGNC:10894
See related: Ensembl:ENSG00000100462 MIM:604045; AllianceGenome:HGNC:10894
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: HSL7; JBP1; SKB1; IBP72; SKB1Hs; HRMT1L5
Summary: This gene encodes an enzyme that belongs to the methyltransferase family. The encoded protein catalyzes the transfer of methyl groups to the amino acid arginine, in target proteins that include histones, transcriptional elongation factors and the tumor suppressor p53. This gene plays a role in several cellular processes, including transcriptional regulation, and the assembly of small nuclear ribonucleoproteins. A pseudogene of this gene has been defined on chromosome 4. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Sep 2015]
Expression: Ubiquitous expression in thyroid (RPKM 21.2), ovary (RPKM 18.5) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 14q11.2

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	14	NC_000014.9 (22920529..22929376, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	14	NC_060938.1 (17118607..17127453, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	14	NC_000014.8 (23389738..23398585, complement)

Chromosome 14 - NC_000014.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The interplay mechanism between IDH mutation, MGMT-promoter methylation, and PRMT5 activity in the progression of grade 4 astrocytoma: unraveling the complex triad theory.
Title: The interplay mechanism between IDH mutation, MGMT-promoter methylation, and PRMT5 activity in the progression of grade 4 astrocytoma: unraveling the complex triad theory.
PRMT5-mediated methylation of STAT3 is required for lung cancer stem cell maintenance and tumour growth.
Title: PRMT5-mediated methylation of STAT3 is required for lung cancer stem cell maintenance and tumour growth.
SMYD4 monomethylates PRMT5 and forms a positive feedback loop to promote hepatocellular carcinoma progression.
Title: SMYD4 monomethylates PRMT5 and forms a positive feedback loop to promote hepatocellular carcinoma progression.
Identification of protein methyltransferases 5 associated with ferroptosis and immune cell infiltration of head and neck squamous cell carcinoma.
Title: Identification of protein methyltransferases 5 associated with ferroptosis and immune cell infiltration of head and neck squamous cell carcinoma.
Alpha-synuclein promotes PRMT5-mediated H4R3me2s histone methylation by interacting with the BAF complex.
Title: Alpha-synuclein promotes PRMT5-mediated H4R3me2s histone methylation by interacting with the BAF complex.
CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP to regulate the translation and stability of CDK6 mRNA.
Title: CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP to regulate the translation and stability of CDK6 mRNA.
Inhibition of PRMT5/MEP50 Arginine Methyltransferase Activity Causes Cancer Vulnerability in NDRG2[low] Adult T-Cell Leukemia/Lymphoma.
Title: Inhibition of PRMT5/MEP50 Arginine Methyltransferase Activity Causes Cancer Vulnerability in NDRG2(low) Adult T-Cell Leukemia/Lymphoma.
Brg1/PRMT5 nuclear complex epigenetically regulates FOXO1 in IPF mesenchymal progenitor cells.
Title: Brg1/PRMT5 nuclear complex epigenetically regulates FOXO1 in IPF mesenchymal progenitor cells.
ETD-Based Proteomic Profiling Improves Arginine Methylation Identification and Reveals Novel PRMT5 Substrates.
Title: ETD-Based Proteomic Profiling Improves Arginine Methylation Identification and Reveals Novel PRMT5 Substrates.
CircMMP2(6,7) Cooperates with beta-Catenin and PRMT5 to Disrupt Bone Homeostasis and Promote Breast Cancer Bone Metastasis.
Title: CircMMP2(6,7) Cooperates with β-Catenin and PRMT5 to Disrupt Bone Homeostasis and Promote Breast Cancer Bone Metastasis.

Submit: New GeneRIF Correction See all GeneRIFs (238)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

G21627 (e-PCR)
- UniSTS:2930

A002Q41 (e-PCR)
- UniSTS:26879

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables E-box binding	ISS Inferred from Sequence or Structural Similarity more info
enables histone H2AQ104 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3 methyltransferase activity	TAS Traceable Author Statement 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 H4R3 methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables histone arginine N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables histone methyltransferase activity	TAS Traceable Author Statement more info
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	IDA Inferred from Direct Assay more info	PubMed
enables p53 binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein heterodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N symmetric methyltransferase activity	EXP Inferred from Experiment more info	PubMed
enables protein-arginine omega-N symmetric methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N symmetric methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ribonucleoprotein complex binding	IPI Inferred from Physical Interaction more info	PubMed
enables transcription corepressor activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in DNA-templated transcription termination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in Golgi ribbon formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chromatin remodeling	IDA Inferred from Direct Assay more info	PubMed
involved_in circadian regulation of gene expression	ISS Inferred from Sequence or Structural Similarity more info
involved_in endothelial cell activation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in liver regeneration	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of gene expression via chromosomal CpG island methylation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within peptidyl-arginine N-methylation	IDA Inferred from Direct Assay more info	PubMed
involved_in peptidyl-arginine methylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of mRNA splicing, via spliceosome	NAS Non-traceable Author Statement more info	PubMed
involved_in positive regulation of oligodendrocyte differentiation	IEA Inferred from Electronic Annotation more info
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of ERK1 and ERK2 cascade	IEA Inferred from Electronic Annotation more info
involved_in regulation of mitotic nuclear division	TAS Traceable Author Statement more info	PubMed
involved_in regulation of signal transduction by p53 class mediator	TAS Traceable Author Statement more info
involved_in spliceosomal snRNP assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in spliceosomal snRNP assembly	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
located_in chromatin	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
part_of histone methyltransferase complex	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
located_in nucleus	NAS Non-traceable Author Statement more info	PubMed

General protein information

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Preferred Names: protein arginine N-methyltransferase 5

Names: 72 kDa ICln-binding protein; HMT1 hnRNP methyltransferase-like 5; SKB1 homolog; histone-arginine N-methyltransferase PRMT5; jak-binding protein 1; shk1 kinase-binding protein 1 homolog

NP_001034708.1

EC 2.1.1.320

NP_001269882.1

EC 2.1.1.320

NP_001269883.1

EC 2.1.1.320

NP_001269884.1

EC 2.1.1.320

NP_001269885.1

EC 2.1.1.320

NP_006100.2

EC 2.1.1.320

XP_047286837.1

EC 2.1.1.320

XP_054231245.1

EC 2.1.1.320

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.

mRNA and Protein(s)

NM_001039619.3 → NP_001034708.1 protein arginine N-methyltransferase 5 isoform b

See identical proteins and their annotated locations for NP_001034708.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate splice site in the 5' coding region and initiates translation at an alternate start codon, compared to variant 1. The encoded isoform (b) is shorter and has a distinct N-terminus, compared to isoform a.

Source sequence(s)

AK027737, AK075251

Consensus CDS

CCDS41922.1

UniProtKB/TrEMBL

B2RDD7

Related

ENSP00000380583.2, ENST00000397441.6

Conserved Domains (3) summary

pfam05185
Location:278 → 447

PRMT5; PRMT5 arginine-N-methyltransferase

pfam17285
Location:20 → 273

PRMT5_TIM; PRMT5 TIM barrel domain

pfam17286
Location:451 → 618

PRMT5_C; PRMT5 oligomerization domain
NM_001282953.2 → NP_001269882.1 protein arginine N-methyltransferase 5 isoform c

See identical proteins and their annotated locations for NP_001269882.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) contains multiple differences in the 5' coding region, compared to variant 1, including initiation of translation at an alternate start codon. The encoded isoform (c) is shorter and has a distinct N-terminus, compared to isoform a.

Source sequence(s)

AA496357, AK301812

Consensus CDS

CCDS61394.1

UniProtKB/TrEMBL

B2RDD7

Related

ENSP00000216350.8, ENST00000216350.12

Conserved Domains (1) summary

pfam05185
Location:122 → 558

PRMT5; PRMT5 arginine-N-methyltransferase
NM_001282954.2 → NP_001269883.1 protein arginine N-methyltransferase 5 isoform d

See identical proteins and their annotated locations for NP_001269883.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) contains multiple differences in the 5' coding region, compared to variant 1, including initiation of translation at a downstream in-frame start codon. The encoded isoform (d) has a shorter N-terminus than isoform a.

Source sequence(s)

AK300863, AL833612, DC395183

UniProtKB/TrEMBL

B2RDD7, B4DV00

Conserved Domains (3) summary

pfam05185
Location:189 → 358

PRMT5; PRMT5 arginine-N-methyltransferase

pfam17285
Location:1 → 184

PRMT5_TIM; PRMT5 TIM barrel domain

pfam17286
Location:362 → 529

PRMT5_C; PRMT5 oligomerization domain
NM_001282955.2 → NP_001269884.1 protein arginine N-methyltransferase 5 isoform e

See identical proteins and their annotated locations for NP_001269884.1

Status: REVIEWED

Description

Transcript Variant: This variant (5) lacks an exon and uses an alternate splice site in the 5' coding region, but maintains the reading frame, compared to variant 1. The encoded isoform (e) is shorter than isoform a.

Source sequence(s)

AK302240, AL833612, DC395183

Consensus CDS

CCDS61396.1

UniProtKB/TrEMBL

B2RDD7

Related

ENSP00000452555.1, ENST00000553897.5

Conserved Domains (3) summary

pfam05185
Location:251 → 420

PRMT5; PRMT5 arginine-N-methyltransferase

pfam17285
Location:37 → 246

PRMT5_TIM; PRMT5 TIM barrel domain

pfam17286
Location:424 → 591

PRMT5_C; PRMT5 oligomerization domain
NM_001282956.2 → NP_001269885.1 protein arginine N-methyltransferase 5 isoform f

See identical proteins and their annotated locations for NP_001269885.1

Status: REVIEWED

Description

Transcript Variant: This variant (6) contains multiple differences in the 5' coding region, compared to variant 1, including initiation of translation at an alternate start codon. The encoded isoform (f) is shorter and has a distinct N-terminus, compared to isoform a.

Source sequence(s)

AL833612, BC005820, DC395183

Consensus CDS

CCDS61395.1

UniProtKB/Swiss-Prot

O14744

Related

ENSP00000380582.4, ENST00000397440.8

Conserved Domains (1) summary

pfam05185
Location:95 → 448

PRMT5; PRMT5 arginine-N-methyltransferase
NM_006109.5 → NP_006100.2 protein arginine N-methyltransferase 5 isoform a

See identical proteins and their annotated locations for NP_006100.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longest isoform (a).

Source sequence(s)

AL833612, DC395183

Consensus CDS

CCDS9579.1

UniProtKB/Swiss-Prot

A8MTP3, A8MZ91, B4DX49, B4DY30, B5BU10, D3DS33, E2QRE7, O14744, Q6IBR1, Q9UKH1

UniProtKB/TrEMBL

B2RDD7

Related

ENSP00000319169.8, ENST00000324366.13

Conserved Domains (3) summary

pfam05185
Location:295 → 464

PRMT5; PRMT5 arginine-N-methyltransferase

pfam17285
Location:37 → 290

PRMT5_TIM; PRMT5 TIM barrel domain

pfam17286
Location:468 → 635

PRMT5_C; PRMT5 oligomerization domain