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FLASH GENE

Symbol

PRMT1

contributors: mct/npt/pgu - updated : 27-06-2020

HGNC name	protein arginine methyltransferase 1
HGNC id	5187

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

Location	19q13.33      Physical location : 50.180.495 - 50.191.704
Synonym name	interferon receptor 1-bound protein-4
	HMT1 hnRNP methyltransferase-like 2 (S. cerevisiae)
Synonym symbol(s)	HCP1, HMT1, ANM1, IR1B4, HRMT1L2
EC.number	2.1.1.25

DNA

TYPE	anonymous DNA segment
SPECIAL FEATURE	arranged in tandem, opposite orientation
STRUCTURE	11.21 kb     11 Exon(s)

MAPPING

cloned

Y

linked

status

provisional

Map	cen - D19S827 - [D19S420 - D19S832 - D19S835 - D19S720 - D19S218 ] - qter
Text	[PRMT1 ]

RNA

TRANSCRIPTS	type	messenger

text	can produce up to seven protein isoforms, all varying in their N-terminal domain

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_198319 12 - 1505 NP_938075 - 347 - 2008 20719712 a functional nuclear export sequence isoform 2 NM_001536 11 splicing 1386 NP_001527 - 371 - 2008 20719712 isoform 1 NM_198318 10 splicing 1332 NP_938074 - 353 - 2008 20719712 isoform 3

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Endocrine thyroid         Nervous brain hindbrain cerebellum     Reproductive female system breast         female system uterus     highly   male system prostate       Skin/Tegument skin       highly

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Connective bone     highly

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES		Hydrophobic
STRUCTURE

motifs/domains

N terminal hydrophobic region-SAM (sterile alpha motif) binding domain

mono polymer

homomer , oligo

HOMOLOGY

interspecies	homolog to yeast S.cerevisiae MMT1like 2
	homolog to murine Prmt1 (99.4pc)
	homolog to rattus Hrmt1l2 (99.4pc)

intraspecies

homolog to IR1B4

Homologene

FAMILY

protein arginine N-methyltransferase family

CATEGORY

enzyme , transcription factor , signaling cytokine

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm,cytosolic
	intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
	intracellular,nucleus,chromatin/chromosome,nucleosome
text	only a fraction of PRMT1 is located in the nucleus, but the protein is predominantly cytoplasmic
	colocalize in nuclear speckles, a sub-nuclear compartment enriched in small nuclear ribonucleoproteins and splicing factors

basic FUNCTION	arginine methyltransferase transferring a methyl group from S adenosylmethionine to the guanidino group nitrogen atoms of specific proteins
	methylation of histone H4 involved in transcriptional regulation
	plays a role in nuclear receptor-mediated chromatin remodeling and RNA transactions
	catalyzing arginine methylation for the post-translational protein modification
	cooperating with CARM1 in gene regulation
	represses a subset of IFNgamma-inducible STAT1 target genes in a methyltransferase-dependent manner
	methylating RUNX1 and serving as a transcriptional coactivator for RUNX1
	may control telomere length and stability through TERF2 methylation
	dysregulation of PRMT1 and PRMT6 can be involved in human carcinogenesis
	PRMT1 and PRMT5 methylate Arg-296 within ASH2L
	responsible for most cellular arginine methylation activity and can work independently or in collaboration with other PRMTs
	involved in arginine methylation, which participates in the nuclear-cytoplasmic shuttling of FUS, particularly of ALS6-associated mutants, and thus contributes to the toxic gain of function conferred by these disease-causing mutations
	possible role of the PRMT1-FAM98A pathway in cancer progression

CELLULAR PROCESS

nucleotide, transcription, regulation

PHYSIOLOGICAL PROCESS

immunity/defense

PATHWAY

metabolism

signaling

signal transduction

a component

INTERACTION

DNA

RNA

small molecule
	S adenosylmethionine dependent

protein	binding to hnRNP (heterogeneous nuclear ribonucleoproteins)
	methylating FMRP
	interact with CNOT7 and colocalize in nuclear speckles, a sub-nuclear compartment enriched in small nuclear ribonucleoproteins and splicing factors
	crucial negative regulator of STAT1 activation that controls PIAS1-mediated repression by arginine methylation
	methylating HNRNPK and so regulating its functions
	TAF15 interactor and the major PRMT responsible for its methylation
	directly interacts with and methylates the 378th arginine residue of Axin
	transcriptional corepressor of IFN-induced STAT1 target genes that cooperates with PIAS1
	PRMT1 serves as the major methyltransferase in cells by forming higher-order oligomers with itself, PRMT2, and possibly other PRMTs
	PRMT1 interacts with RUNX1-RUNX1T1 to promote its transcriptional activation and progenitor cell proliferative potential
	GSK3A, and PRMT1 cooperate to orchestrate a series of posttranslational modifications on the Intermediate filament (IF) -anchoring protein desmoplakin (DSP) that play an essential role in coordinating cytoskeletal dynamics and cellular adhesion
	ATXN2L associates with the protein arginine-N-methyltransferase 1 (PRMT1)
	PRMT1 is a direct interaction partner of UBAP2L
	PRMT1 is overexpressed in human melanoma, and may regulate tumor growth and metastasis via targeting ALCAM
	potent stress granules (SG)-nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PRMT5)
	TRIM48 facilitates oxidative stress-induced MAP3K5 activation and cell death through ubiquitination-dependent degradation of PRMT1
	PRMT5 and PRMT1 mediate the distinct effects on CFLARL degradation by regulating the binding of E3 ligase ITCH in lung cancer cells
	interaction between CBX7 and PRMT1, and this interaction is crucial for PRMT1 enzymatic activity both and for the regulation of CDH1 expression, an important hallmark of epithelial-mesenchymal transition (EMT)
	PRMT1 was observed to interact with and methylate CFLAR, ultimately leading to its ubiquitination-mediated protein degradation

cell & other

REGULATION

Other

trapped by unmethylated substrates such as core histones and heterogeneous nuclear ribonucleoprotein proteins until it has executed the methylation reaction

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function tumoral     --low   in breast cancer the relative balance of PRMT1 isoforms is altered constitutional     --low   reduced PRMT1 protein levels in the aganglionosis segments of HSCR patients

Susceptibility

Variant & Polymorphism

Candidate gene
Marker	can be a useful marker for Hirschsprung disease
Therapy target

ANIMAL & CELL MODELS