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Q9JIF0 (ANM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Alt products·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, Mrmt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length371 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

Catalytic activity

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

Subunit structure

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. Ref.3 Ref.4 Ref.5

Subcellular location

Nucleus. Nucleusnucleoplasm. Cytoplasmcytosol. Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction. Ref.4 Ref.5

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
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete 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 mutant phenotype Ref.1. Source: MGI

negative regulation of megakaryocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from electronic annotation. Source: Ensembl

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionN-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

[cytochrome c]-arginine N-methyltransferase activity

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity (H4-R3 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

protein methyltransferase activity

Inferred from mutant phenotype Ref.1. Source: MGI

protein-arginine N-methyltransferase activity

Inferred from direct assay PubMed 21652632. Source: MGI

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein-arginine omega-N monomethyltransferase activity

Inferred from electronic annotation. Source: Ensembl

snoRNP binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JIF0-1)

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.
Isoform 2 (identifier: Q9JIF0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     13-30: Missing.
Isoform 3 (identifier: Q9JIF0-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Protein arginine N-methyltransferase 1
PRO_0000212322

Regions

Domain50 – 371322SAM-dependent MTase PRMT-type

Sites

Active site1621 By similarity
Active site1711 By similarity
Binding site631S-adenosyl-L-methionine By similarity
Binding site721S-adenosyl-L-methionine By similarity
Binding site961S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1181S-adenosyl-L-methionine By similarity
Binding site1471S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue1341N6-succinyllysine Ref.6

Natural variations

Alternative sequence1 – 2929MAAAE…QPPLE → M in isoform 3.
VSP_005211
Alternative sequence13 – 3018Missing in isoform 2.
VSP_005210

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AEFCF63001B1A38C

FASTA37142,436
        10         20         30         40         50         60 
MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF 

        70         80         90        100        110        120 
GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS 

       130        140        150        160        170        180 
SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLHA 

       190        200        210        220        230        240 
RDKWLAPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV 

       250        260        270        280        290        300 
DPKQLVTNAC LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG 

       310        320        330        340        350        360 
FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC 

       370 
ELSCSTDYRM R 

« Hide

Isoform 2 [UniParc].

Checksum: EDBB0587784C527E
Show »

FASTA35340,522
Isoform 3 [UniParc].

Checksum: 257BAC1C484B274E
Show »

FASTA34339,576

References

« Hide 'large scale' references
[1]"Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable."
Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., Ruley H.E.
Mol. Cell. Biol. 20:4859-4869(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[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] (ISOFORM 3).
[3]"Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes."
Mowen K.A., Schurter B.T., Fathman J.W., David M., Glimcher L.H.
Mol. Cell 15:559-571(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NFATC2IP.
[4]"Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases."
van Dijk T.B., Gillemans N., Stein C., Fanis P., Demmers J., van de Corput M., Essers J., Grosveld F., Bauer U.M., Philipsen S.
Mol. Cell. Biol. 30:260-272(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
Tissue: Erythroblast.
[5]"Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF232716 mRNA. Translation: AAF37292.1.
AF232717 mRNA. Translation: AAF37293.1.
BC002249 mRNA. Translation: AAH02249.1.
RefSeqNP_001239405.1. NM_001252476.1.
NP_062804.1. NM_019830.3.
UniGeneMm.27545.

3D structure databases

ProteinModelPortalQ9JIF0.
SMRQ9JIF0. Positions 59-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200423. 11 interactions.
IntActQ9JIF0. 14 interactions.
MINTMINT-3981922.

PTM databases

PhosphoSiteQ9JIF0.

Proteomic databases

PaxDbQ9JIF0.
PRIDEQ9JIF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107842; ENSMUSP00000103473; ENSMUSG00000052429. [Q9JIF0-2]
ENSMUST00000107843; ENSMUSP00000103474; ENSMUSG00000052429. [Q9JIF0-1]
GeneID15469.
KEGGmmu:15469.
UCSCuc009gsg.2. mouse. [Q9JIF0-1]

Organism-specific databases

CTD3276.
MGIMGI:107846. Prmt1.

Phylogenomic databases

eggNOGCOG0500.
GeneTreeENSGT00550000074406.
HOGENOMHOG000198521.
HOVERGENHBG001793.
InParanoidQ9JIF0.
KOK11434.
OMAVKRNDYI.
OrthoDBEOG7S7SDJ.
PhylomeDBQ9JIF0.
TreeFamTF300608.

Gene expression databases

ArrayExpressQ9JIF0.
BgeeQ9JIF0.
CleanExMM_PRMT1.
GenevestigatorQ9JIF0.

Family and domain databases

InterProIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
[Graphical view]
PANTHERPTHR11006. PTHR11006. 1 hit.
PfamPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288310.
PROQ9JIF0.
SOURCESearch...

Entry information

Entry nameANM1_MOUSE
AccessionPrimary (citable) accession number: Q9JIF0
Secondary accession number(s): Q99LS4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 111 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot