Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity).By similarity2 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63S-adenosyl-L-methionineBy similarity1
Binding sitei72S-adenosyl-L-methionineBy similarity1
Binding sitei96S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei118S-adenosyl-L-methionineBy similarity1
Binding sitei147S-adenosyl-L-methionineBy similarity1
Active sitei162By similarity1
Active sitei171By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 1 (EC:2.1.1.319By similarity)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1
Gene namesi
Name:Prmt1
Synonyms:Hrmt1l2, Mrmt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:107846. Prmt1.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123221 – 371Protein arginine N-methyltransferase 1Add BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei134N6-succinyllysineCombined sources1
Modified residuei304PhosphoserineBy similarity1
Modified residuei307PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JIF0.
PRIDEiQ9JIF0.

PTM databases

iPTMnetiQ9JIF0.
PhosphoSitePlusiQ9JIF0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000109324.
CleanExiMM_PRMT1.
ExpressionAtlasiQ9JIF0. differential.
GenevisibleiQ9JIF0. MM.

Interactioni

Subunit structurei

Homodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2 and IFNAR1. Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress (By similarity). Interacts with NFATC2IP. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex. Interacts with and probably methylates ATXN2L (By similarity). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200423. 11 interactors.
IntActiQ9JIF0. 15 interactors.
MINTiMINT-3981922.
STRINGi10090.ENSMUSP00000103474.

Structurei

3D structure databases

ProteinModelPortaliQ9JIF0.
SMRiQ9JIF0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 371SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST322

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ9JIF0.
KOiK11434.
OMAiRCHKRIG.
OrthoDBiEOG091G0ADC.
PhylomeDBiQ9JIF0.
TreeFamiTF300608.

Family and domain databases

InterProiView protein in InterPro
IPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiView protein in PROSITE
PS51678. SAM_MT_PRMT. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JIF0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK
60 70 80 90 100
DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG
110 120 130 140 150
ILCMFAAKAG ARKVIGIECS SISDYAVKIV KANKLDHVVT IIKGKVEEVE
160 170 180 190 200
LPVEKVDIII SEWMGYCLFY ESMLNTVLHA RDKWLAPDGL IFPDRATLYV
210 220 230 240 250
TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC
260 270 280 290 300
LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
310 320 330 340 350
FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT
360 370
IDLDFKGQLC ELSCSTDYRM R
Length:371
Mass (Da):42,436
Last modified:October 1, 2000 - v1
Checksum:iAEFCF63001B1A38C
GO
Isoform 2 (identifier: Q9JIF0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-30: Missing.

Show »
Length:353
Mass (Da):40,522
Checksum:iEDBB0587784C527E
GO
Isoform 3 (identifier: Q9JIF0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MAAAEAANCIMENFVATLANGMSLQPPLE → M

Show »
Length:343
Mass (Da):39,576
Checksum:i257BAC1C484B274E
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0052111 – 29MAAAE…QPPLE → M in isoform 3. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_00521013 – 30Missing in isoform 2. 1 PublicationAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232716 mRNA. Translation: AAF37292.1.
AF232717 mRNA. Translation: AAF37293.1.
BC002249 mRNA. Translation: AAH02249.1.
CCDSiCCDS21222.1. [Q9JIF0-1]
CCDS57547.1. [Q9JIF0-2]
RefSeqiNP_001239405.1. NM_001252476.1. [Q9JIF0-2]
NP_062804.1. NM_019830.3. [Q9JIF0-1]
UniGeneiMm.27545.

Genome annotation databases

EnsembliENSMUST00000107843; ENSMUSP00000103474; ENSMUSG00000109324. [Q9JIF0-1]
ENSMUST00000207370; ENSMUSP00000147252; ENSMUSG00000109324. [Q9JIF0-2]
GeneIDi15469.
KEGGimmu:15469.
UCSCiuc009gsg.2. mouse. [Q9JIF0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiANM1_MOUSE
AccessioniPrimary (citable) accession number: Q9JIF0
Secondary accession number(s): Q99LS4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: August 30, 2017
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families