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Q9JIF0

- ANM1_MOUSE

UniProt

Q9JIF0 - ANM1_MOUSE

Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.2 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 sitei63 – 631S-adenosyl-L-methionineBy similarity
    Binding sitei72 – 721S-adenosyl-L-methionineBy similarity
    Binding sitei96 – 961S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei118 – 1181S-adenosyl-L-methionineBy similarity
    Binding sitei147 – 1471S-adenosyl-L-methionineBy similarity
    Active sitei162 – 1621By similarity
    Active sitei171 – 1711By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. histone H4-R3 methylation Source: UniProtKB
    2. in utero embryonic development Source: MGI
    3. negative regulation of megakaryocyte differentiation Source: UniProtKB
    4. neuron projection development Source: Ensembl
    5. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
    6. 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, Mrmt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:107846. Prmt1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. nucleoplasm Source: UniProtKB-SubCell
    3. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 371371Protein arginine N-methyltransferase 1PRO_0000212322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei134 – 1341N6-succinyllysine1 Publication

    Proteomic databases

    MaxQBiQ9JIF0.
    PaxDbiQ9JIF0.
    PRIDEiQ9JIF0.

    PTM databases

    PhosphoSiteiQ9JIF0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9JIF0.
    BgeeiQ9JIF0.
    CleanExiMM_PRMT1.
    GenevestigatoriQ9JIF0.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Axin1Q14DJ83EBI-519055,EBI-4312125
    ChtopQ9CY578EBI-519055,EBI-6393116
    Khdrbs1Q607492EBI-519055,EBI-519077
    Smad6O351823EBI-519055,EBI-4321242

    Protein-protein interaction databases

    BioGridi200423. 11 interactions.
    IntActiQ9JIF0. 14 interactions.
    MINTiMINT-3981922.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JIF0.
    SMRiQ9JIF0. Positions 59-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 371322SAM-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.
    InParanoidiQ9JIF0.
    KOiK11434.
    OMAiRCHKRIG.
    OrthoDBiEOG7S7SDJ.
    PhylomeDBiQ9JIF0.
    TreeFamiTF300608.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JIF0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK    50
    DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG 100
    ILCMFAAKAG ARKVIGIECS SISDYAVKIV KANKLDHVVT IIKGKVEEVE 150
    LPVEKVDIII SEWMGYCLFY ESMLNTVLHA RDKWLAPDGL IFPDRATLYV 200
    TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC 250
    LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG 300
    FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT 350
    IDLDFKGQLC ELSCSTDYRM R 371
    Length:371
    Mass (Da):42,436
    Last modified:October 1, 2000 - v1
    Checksum:iAEFCF63001B1A38C
    GO
    Isoform 2 (identifier: Q9JIF0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         13-30: Missing.

    Show »
    Length:353
    Mass (Da):40,522
    Checksum:iEDBB0587784C527E
    GO
    Isoform 3 (identifier: Q9JIF0-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:343
    Mass (Da):39,576
    Checksum:i257BAC1C484B274E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929MAAAE…QPPLE → M in isoform 3. 1 PublicationVSP_005211Add
    BLAST
    Alternative sequencei13 – 3018Missing in isoform 2. 1 PublicationVSP_005210Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232716 mRNA. Translation: AAF37292.1.
    AF232717 mRNA. Translation: AAF37293.1.
    BC002249 mRNA. Translation: AAH02249.1.
    CCDSiCCDS21222.1. [Q9JIF0-1]
    CCDS57547.1. [Q9JIF0-2]
    RefSeqiNP_001239405.1. NM_001252476.1. [Q9JIF0-2]
    NP_062804.1. NM_019830.3. [Q9JIF0-1]
    UniGeneiMm.27545.

    Genome annotation databases

    EnsembliENSMUST00000107842; ENSMUSP00000103473; ENSMUSG00000052429. [Q9JIF0-2]
    ENSMUST00000107843; ENSMUSP00000103474; ENSMUSG00000052429. [Q9JIF0-1]
    GeneIDi15469.
    KEGGimmu:15469.
    UCSCiuc009gsg.2. mouse. [Q9JIF0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232716 mRNA. Translation: AAF37292.1 .
    AF232717 mRNA. Translation: AAF37293.1 .
    BC002249 mRNA. Translation: AAH02249.1 .
    CCDSi CCDS21222.1. [Q9JIF0-1 ]
    CCDS57547.1. [Q9JIF0-2 ]
    RefSeqi NP_001239405.1. NM_001252476.1. [Q9JIF0-2 ]
    NP_062804.1. NM_019830.3. [Q9JIF0-1 ]
    UniGenei Mm.27545.

    3D structure databases

    ProteinModelPortali Q9JIF0.
    SMRi Q9JIF0. Positions 59-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200423. 11 interactions.
    IntActi Q9JIF0. 14 interactions.
    MINTi MINT-3981922.

    PTM databases

    PhosphoSitei Q9JIF0.

    Proteomic databases

    MaxQBi Q9JIF0.
    PaxDbi Q9JIF0.
    PRIDEi Q9JIF0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107842 ; ENSMUSP00000103473 ; ENSMUSG00000052429 . [Q9JIF0-2 ]
    ENSMUST00000107843 ; ENSMUSP00000103474 ; ENSMUSG00000052429 . [Q9JIF0-1 ]
    GeneIDi 15469.
    KEGGi mmu:15469.
    UCSCi uc009gsg.2. mouse. [Q9JIF0-1 ]

    Organism-specific databases

    CTDi 3276.
    MGIi MGI:107846. Prmt1.

    Phylogenomic databases

    eggNOGi COG0500.
    GeneTreei ENSGT00550000074406.
    HOGENOMi HOG000198521.
    HOVERGENi HBG001793.
    InParanoidi Q9JIF0.
    KOi K11434.
    OMAi RCHKRIG.
    OrthoDBi EOG7S7SDJ.
    PhylomeDBi Q9JIF0.
    TreeFami TF300608.

    Miscellaneous databases

    NextBioi 288310.
    PROi Q9JIF0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JIF0.
    Bgeei Q9JIF0.
    CleanExi MM_PRMT1.
    Genevestigatori Q9JIF0.

    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. "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. 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.

    Entry informationi

    Entry nameiANM1_MOUSE
    AccessioniPrimary (citable) accession number: Q9JIF0
    Secondary accession number(s): Q99LS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 115 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3