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Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

Organism
Rattus norvegicus (Rat)
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, EWS, HABP4 and SERBP1. 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). Promotes colorectal cancer cell malignancy (By similarity).By similarity3 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 sitei45S-adenosyl-L-methionine1 Publication1
Binding sitei54S-adenosyl-L-methionine1 Publication1
Binding sitei78S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Binding sitei100S-adenosyl-L-methionine1 Publication1
Binding sitei129S-adenosyl-L-methionine1 Publication1
Active sitei1441 Publication1
Active sitei1531 Publication1

GO - Molecular functioni

  • [cytochrome c]-arginine N-methyltransferase activity Source: MGI
  • enzyme binding Source: RGD
  • histone-arginine N-methyltransferase activity Source: MGI
  • histone methyltransferase activity Source: RGD
  • histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  • identical protein binding Source: IntAct
  • methyl-CpG binding Source: UniProtKB
  • mitogen-activated protein kinase p38 binding Source: RGD
  • N-methyltransferase activity Source: RGD
  • protein-arginine N-methyltransferase activity Source: RGD
  • protein-arginine omega-N asymmetric methyltransferase activity Source: MGI
  • protein-arginine omega-N monomethyltransferase activity Source: MGI
  • protein methyltransferase activity Source: UniProtKB
  • RNA binding Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD
  • snoRNP binding Source: RGD

GO - Biological processi

  • histone H4-R3 methylation Source: UniProtKB
  • histone methylation Source: RGD
  • in utero embryonic development Source: RGD
  • liver regeneration Source: RGD
  • negative regulation of megakaryocyte differentiation Source: UniProtKB
  • neuron projection development Source: RGD
  • peptidyl-arginine methylation Source: RGD
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: MGI
  • peptidyl-arginine omega-N-methylation Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of erythrocyte differentiation Source: BHF-UCL
  • positive regulation of hemoglobin biosynthetic process Source: BHF-UCL
  • positive regulation of p38MAPK cascade Source: BHF-UCL
  • protein methylation Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: GO_Central

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.125. 5301.
ReactomeiR-RNO-3214858. RMTs methylate histone arginines.
R-RNO-8936459. RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi62020. Prmt1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144E → D: Reduces catalytic activity 10-fold, and causes higher order oligomers of the protein. 1 Publication1
Mutagenesisi144E → Q: Reduces catalytic activity 3000-fold, and causes higher order oligomers of the protein. 1 Publication1
Mutagenesisi153E → D: Reduces catalytic activity to 0.03%, but does not affect oligomerization. 1 Publication1
Mutagenesisi153E → Q: Completely abolishes catalytic activity, but does not affect oligomerization. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1275220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123231 – 353Protein arginine N-methyltransferase 1Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116N6-succinyllysineBy similarity1
Modified residuei286PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63009.
PRIDEiQ63009.

PTM databases

iPTMnetiQ63009.
PhosphoSitePlusiQ63009.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSRNOG00000026109.
GenevisibleiQ63009. RN.

Interactioni

Subunit structurei

Homodimer and heterodimer with PRMT8. The dimer can then associate to form a homohexamer. Interacts with NFATC2IP. Interacts with ILF3 and SUPT5H. Interacts with FOXO1; the interaction methylates FOXO1, retaining it in the nucleus and increasing its transcriptional activity. Methylation of FOXO1 is increased with oxidative stress. Interacts with CHTOP; the interaction methylates CHTOP, enabling its interaction with the 5FMC complex (By similarity). Interacts with BTG1, BTG2 and IFNAR1. 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). Interacts with DHX9 (via RGG region) (By similarity). Interacts (via N-terminus) with HABP4 (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248825. 1 interactor.
IntActiQ63009. 6 interactors.
MINTiMINT-1518006.
STRINGi10116.ENSRNOP00000063624.

Chemistry databases

BindingDBiQ63009.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni40 – 42Combined sources3
Helixi43 – 50Combined sources8
Helixi52 – 63Combined sources12
Helixi66 – 69Combined sources4
Beta strandi73 – 78Combined sources6
Helixi83 – 90Combined sources8
Beta strandi94 – 100Combined sources7
Helixi104 – 114Combined sources11
Turni118 – 120Combined sources3
Beta strandi121 – 126Combined sources6
Turni128 – 130Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi138 – 143Combined sources6
Beta strandi147 – 152Combined sources6
Helixi156 – 166Combined sources11
Beta strandi167 – 175Combined sources9
Beta strandi177 – 185Combined sources9
Helixi188 – 194Combined sources7
Helixi196 – 199Combined sources4
Helixi207 – 209Combined sources3
Helixi210 – 214Combined sources5
Beta strandi218 – 220Combined sources3
Helixi224 – 226Combined sources3
Beta strandi227 – 238Combined sources12
Turni239 – 241Combined sources3
Helixi244 – 247Combined sources4
Beta strandi248 – 257Combined sources10
Beta strandi259 – 273Combined sources15
Beta strandi277 – 279Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi296 – 307Combined sources12
Beta strandi312 – 321Combined sources10
Beta strandi323 – 325Combined sources3
Beta strandi329 – 338Combined sources10
Beta strandi343 – 352Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OR8X-ray2.35A14-353[»]
1ORHX-ray2.64A1-353[»]
1ORIX-ray2.50A11-353[»]
3Q7EX-ray2.20A14-353[»]
ProteinModelPortaliQ63009.
SMRiQ63009.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 353SAM-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.
InParanoidiQ63009.
KOiK11434.
OMAiRCHKRIG.
OrthoDBiEOG091G0ADC.

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.

Sequencei

Sequence statusi: Complete.

Q63009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK
60 70 80 90 100
DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE
110 120 130 140 150
CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL
160 170 180 190 200
FYESMLNTVL HARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN
210 220 230 240 250
VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT
260 270 280 290 300
SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY
310 320 330 340 350
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY

RMR
Length:353
Mass (Da):40,522
Last modified:November 1, 1997 - v1
Checksum:iEDBB0587784C527E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60882 mRNA. Translation: AAC52622.1.
BC078815 mRNA. Translation: AAH78815.1.
RefSeqiNP_077339.1. NM_024363.1.
UniGeneiRn.5870.

Genome annotation databases

EnsembliENSRNOT00000064272; ENSRNOP00000063624; ENSRNOG00000026109.
GeneIDi60421.
KEGGirno:60421.
UCSCiRGD:62020. rat.

Similar proteinsi

Entry informationi

Entry nameiANM1_RAT
AccessioniPrimary (citable) accession number: Q63009
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 141 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families