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Q63009

- ANM1_RAT

UniProt

Q63009 - ANM1_RAT

Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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 – 1441By similarity
    Active sitei153 – 1531By 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

    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 1 Publication
    Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction By similarity.By similarity

    GO - Cellular componenti

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

    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-succinyllysineBy 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.By similarity2 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63009.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 112 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