Protein arginine N-methyltransferase 1 - Rattus norvegicus (Rat)

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Q63009 (ANM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nucleoplasm By similarity. Cytoplasm › cytosol. 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 protein arginine N-methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of megakaryocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB neuron projection development Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol 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_function	[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 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
Ilf3	Q9JIL3	2	EBI-78708,EBI-78714

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 353

353

Protein arginine N-methyltransferase 1

PRO_0000212323

Sites

Active site

144

By similarity

Active site

153

By similarity

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

100

S-adenosyl-L-methionine

Binding site

129

S-adenosyl-L-methionine

Secondary structure

353

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q63009 [UniParc].

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

FASTA

353

40,522

        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' referencesShow '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.

IPI

IPI00949327.

RefSeq

NP_077339.1. NM_024363.1.

UniGene

Rn.5870.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OR8	X-ray	2.35	A	14-353	[»]
1ORH	X-ray	2.64	A	1-353	[»]
1ORI	X-ray	2.50	A	11-353	[»]
3Q7E	X-ray	2.20	A	14-353	[»]

ProteinModelPortal

Q63009.

SMR

Q63009. Positions 41-353.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q63009. 3 interactions.

MINT

MINT-1518006.

STRING

10116.ENSRNOP00000027761.

Proteomic databases

PaxDb

Q63009.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000064272; ENSRNOP00000063624; ENSRNOG00000026109.

GeneID

60421.

KEGG

rno:60421.

UCSC

RGD:62020. rat.

Organism-specific databases

CTD

3276.

RGD

62020. Prmt1.

Phylogenomic databases

eggNOG

COG0500.

GeneTree

ENSGT00550000074406.

HOGENOM

HOG000198521.

HOVERGEN

HBG001793.

InParanoid

Q63009.

K11434.

Gene expression databases

ArrayExpress

Q63009.

Genevestigator

Q63009.

GermOnline

ENSRNOG00000026109. Rattus norvegicus.

Family and domain databases

InterPro

IPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
[Graphical view]

PANTHER

PTHR11006. PTHR11006. 1 hit.

Pfam

PF13847. Methyltransf_31. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1275220.

EvolutionaryTrace

Q63009.

NextBio

612134.

Entry information

Entry name

ANM1_RAT

Accession

Primary (citable) accession number: Q63009

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents