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Q63009

- ANM1_RAT

UniProt

Q63009 - ANM1_RAT

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Protein

Protein arginine N-methyltransferase 1

Gene
Prmt1, Hrmt1l2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451S-adenosyl-L-methionine
Binding sitei54 – 541S-adenosyl-L-methionine
Binding sitei78 – 781S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei100 – 1001S-adenosyl-L-methionine
Binding sitei129 – 1291S-adenosyl-L-methionine
Active sitei144 – 1441 By similarity
Active sitei153 – 1531 By similarity

GO - Molecular functioni

  1. [cytochrome c]-arginine N-methyltransferase activity Source: MGI
  2. histone-arginine N-methyltransferase activity Source: MGI
  3. histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  4. identical protein binding Source: IntAct
  5. protein-arginine N-methyltransferase activity Source: RGD
  6. protein-arginine omega-N asymmetric methyltransferase activity Source: MGI
  7. protein-arginine omega-N monomethyltransferase activity Source: MGI
  8. protein binding Source: IntAct
  9. protein methyltransferase activity Source: UniProtKB
  10. S-adenosylmethionine-dependent methyltransferase activity Source: RGD
  11. snoRNP binding Source: RGD

GO - Biological processi

  1. histone H4-R3 methylation Source: UniProtKB
  2. in utero embryonic development Source: Ensembl
  3. negative regulation of megakaryocyte differentiation Source: UniProtKB
  4. peptidyl-arginine methylation Source: RGD
  5. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: MGI
  6. peptidyl-arginine omega-N-methylation Source: MGI
  7. protein methylation Source: MGI
  8. regulation of transcription, DNA-templated Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
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 namesi
Name:Prmt1
Synonyms:Hrmt1l2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi62020. Prmt1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleoplasm Source: UniProtKB-SubCell
  3. nucleus Source: RGD
  4. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Protein arginine N-methyltransferase 1PRO_0000212323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-succinyllysine By similarity

Proteomic databases

PaxDbiQ63009.
PRIDEiQ63009.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

GenevestigatoriQ63009.

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 IFNAR1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-78708,EBI-78708
CNBPP626332EBI-78708,EBI-1047529From a different organism.
Ilf3Q9JIL32EBI-78708,EBI-78714

Protein-protein interaction databases

BioGridi248825. 1 interaction.
IntActiQ63009. 6 interactions.
MINTiMINT-1518006.
STRINGi10116.ENSRNOP00000027761.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni40 – 423
Helixi43 – 508
Helixi52 – 6312
Helixi66 – 694
Beta strandi73 – 786
Helixi83 – 908
Beta strandi94 – 1007
Helixi104 – 11411
Turni118 – 1203
Beta strandi121 – 1266
Turni128 – 1303
Beta strandi134 – 1363
Beta strandi138 – 1436
Beta strandi147 – 1526
Helixi156 – 16611
Beta strandi167 – 1759
Beta strandi177 – 1859
Helixi188 – 1947
Helixi196 – 1994
Helixi207 – 2093
Helixi210 – 2145
Beta strandi218 – 2203
Helixi224 – 2263
Beta strandi227 – 23812
Turni239 – 2413
Helixi244 – 2474
Beta strandi248 – 25710
Beta strandi259 – 27315
Beta strandi277 – 2793
Beta strandi282 – 2843
Beta strandi296 – 30712
Beta strandi312 – 32110
Beta strandi323 – 3253
Beta strandi329 – 33810
Beta strandi343 – 35210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OR8X-ray2.35A14-353[»]
1ORHX-ray2.64A1-353[»]
1ORIX-ray2.50A11-353[»]
3Q7EX-ray2.20A14-353[»]
ProteinModelPortaliQ63009.
SMRiQ63009. Positions 41-353.

Miscellaneous databases

EvolutionaryTraceiQ63009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 353322SAM-dependent MTase PRMT-typeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ63009.
KOiK11434.
OMAiRCHKRIG.
OrthoDBiEOG7S7SDJ.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63009-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK    50
DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE 100
CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL 150
FYESMLNTVL HARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN 200
VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT 250
SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY 300
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY 350
RMR 353
Length:353
Mass (Da):40,522
Last modified:November 1, 1997 - v1
Checksum:iEDBB0587784C527E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U60882 mRNA. Translation: AAC52622.1 .
BC078815 mRNA. Translation: AAH78815.1 .
RefSeqi NP_077339.1. NM_024363.1.
UniGenei Rn.5870.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q63009.
SMRi Q63009. Positions 41-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248825. 1 interaction.
IntActi Q63009. 6 interactions.
MINTi MINT-1518006.
STRINGi 10116.ENSRNOP00000027761.

Chemistry

ChEMBLi CHEMBL1275220.

Proteomic databases

PaxDbi Q63009.
PRIDEi Q63009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000064272 ; ENSRNOP00000063624 ; ENSRNOG00000026109 .
GeneIDi 60421.
KEGGi rno:60421.
UCSCi RGD:62020. rat.

Organism-specific databases

CTDi 3276.
RGDi 62020. Prmt1.

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00550000074406.
HOGENOMi HOG000198521.
HOVERGENi HBG001793.
InParanoidi Q63009.
KOi K11434.
OMAi RCHKRIG.
OrthoDBi EOG7S7SDJ.

Miscellaneous databases

EvolutionaryTracei Q63009.
NextBioi 612134.
PROi Q63009.

Gene expression databases

Genevestigatori Q63009.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR11006. PTHR11006. 1 hit.
Pfami PF13847. Methyltransf_31. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiANM1_RAT
AccessioniPrimary (citable) accession number: Q63009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 111 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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