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Q63009 (ANM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein arginine N-methyltransferase 1

EC=2.1.1.-
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1
EC=2.1.1.125
Gene names
Name:Prmt1
Synonyms:Hrmt1l2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].

Subunit structure

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. Ref.1 Ref.5

Subcellular location

Nucleus By similarity. Nucleusnucleoplasm By similarity. Cytoplasmcytosol. Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction By similarity. Ref.3

Tissue specificity

Ubiquitous.

Sequence similarities

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

Contains 1 SAM-dependent MTase PRMT-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H4-R3 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of megakaryocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-arginine methylation

Inferred from direct assay PubMed 10899106Ref.1. Source: RGD

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from direct assay Ref.1. Source: MGI

peptidyl-arginine omega-N-methylation

Inferred from direct assay Ref.1. Source: MGI

protein methylation

Inferred from direct assay PubMed 10749851. Source: MGI

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytosol

Inferred from direct assay Ref.3. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 9642256. Source: RGD

protein complex

Inferred from direct assay Ref.3. Source: RGD

   Molecular_functionS-adenosylmethionine-dependent methyltransferase activity

Traceable author statement PubMed 9642256. Source: RGD

[cytochrome c]-arginine N-methyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

histone methyltransferase activity (H4-R3 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

histone-arginine N-methyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

identical protein binding

Inferred from physical interaction PubMed 20345902PubMed 9642256. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10749851. Source: IntAct

protein methyltransferase activity

Inferred from direct assay Ref.3. Source: UniProtKB

protein-arginine N-methyltransferase activity

Inferred from direct assay PubMed 10899106. Source: RGD

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

protein-arginine omega-N monomethyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

snoRNP binding

Inferred from direct assay PubMed 12523648. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-78708,EBI-78708
Ilf3Q9JIL32EBI-78708,EBI-78714

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Protein arginine N-methyltransferase 1
PRO_0000212323

Regions

Domain32 – 353322SAM-dependent MTase PRMT-type

Sites

Active site1441 By similarity
Active site1531 By similarity
Binding site451S-adenosyl-L-methionine
Binding site541S-adenosyl-L-methionine
Binding site781S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1001S-adenosyl-L-methionine
Binding site1291S-adenosyl-L-methionine

Amino acid modifications

Modified residue1161N6-succinyllysine By similarity

Secondary structure

................................................................ 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63009 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: EDBB0587784C527E

FASTA35340,522
        10         20         30         40         50         60 
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN 

        70         80         90        100        110        120 
SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV 

       130        140        150        160        170        180 
VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL HARDKWLAPD GLIFPDRATL 

       190        200        210        220        230        240 
YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY 

       250        260        270        280        290        300 
TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY 

       310        320        330        340        350 
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR 

« Hide

References

« Hide 'large scale' references
[1]"The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase."
Lin W.-J., Gary J.D., Yang M.C., Clarke S., Herschman H.R.
J. Biol. Chem. 271:15034-15044(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BTG1; BTG2 AND IFNAR1.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver."
Lim Y., Kwon Y.H., Won N.H., Min B.H., Park I.S., Paik W.K., Kim S.
Biochim. Biophys. Acta 1723:240-247(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"Involvement of PRMT1 in hnRNPQ activation and internalization of insulin receptor."
Iwasaki H.
Biochem. Biophys. Res. Commun. 372:314-319(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides."
Zhang X., Cheng X.
Structure 11:509-520(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND PEPTIDE SUBSTRATE, SUBUNIT, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U60882 mRNA. Translation: AAC52622.1.
BC078815 mRNA. Translation: AAH78815.1.
RefSeqNP_077339.1. NM_024363.1.
UniGeneRn.5870.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OR8X-ray2.35A14-353[»]
1ORHX-ray2.64A1-353[»]
1ORIX-ray2.50A11-353[»]
3Q7EX-ray2.20A14-353[»]
ProteinModelPortalQ63009.
SMRQ63009. Positions 41-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248825. 1 interaction.
IntActQ63009. 5 interactions.
MINTMINT-1518006.
STRING10116.ENSRNOP00000027761.

Chemistry

ChEMBLCHEMBL1275220.

Proteomic databases

PaxDbQ63009.
PRIDEQ63009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000064272; ENSRNOP00000063624; ENSRNOG00000026109.
GeneID60421.
KEGGrno:60421.
UCSCRGD:62020. rat.

Organism-specific databases

CTD3276.
RGD62020. Prmt1.

Phylogenomic databases

eggNOGCOG0500.
GeneTreeENSGT00550000074406.
HOGENOMHOG000198521.
HOVERGENHBG001793.
InParanoidQ63009.
KOK11434.
OMARCHKRIG.
OrthoDBEOG7S7SDJ.

Gene expression databases

GenevestigatorQ63009.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR11006. PTHR11006. 1 hit.
PfamPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ63009.
NextBio612134.
PROQ63009.

Entry information

Entry nameANM1_RAT
AccessionPrimary (citable) accession number: Q63009
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references