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Q9QXF8

- GNMT_MOUSE

UniProt

Q9QXF8 - GNMT_MOUSE

Protein

Glycine N-methyltransferase

Gene

Gnmt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine By similarity.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei22 – 221S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei31 – 311S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei34 – 341SubstratePROSITE-ProRule annotation
    Binding sitei41 – 411S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei65 – 651S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei86 – 861S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei137 – 1371S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei139 – 1391SubstratePROSITE-ProRule annotation
    Binding sitei176 – 1761SubstratePROSITE-ProRule annotation
    Binding sitei221 – 2211SubstratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. folic acid binding Source: UniProtKB-KW
    2. glycine binding Source: UniProtKB
    3. glycine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. glycogen metabolic process Source: MGI
    2. methionine metabolic process Source: MGI
    3. one-carbon metabolic process Source: MGI
    4. protein homotetramerization Source: UniProtKB
    5. regulation of gluconeogenesis Source: MGI
    6. S-adenosylmethionine metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    Folate-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.20. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycine N-methyltransferase (EC:2.1.1.20)
    Gene namesi
    Name:Gnmt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1202304. Gnmt.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 293292Glycine N-methyltransferasePRO_0000087525Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvalineBy similarity
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei46 – 461N6-succinyllysine1 Publication
    Modified residuei191 – 1911N6-succinyllysine1 Publication
    Modified residuei196 – 1961N6-succinyllysine1 Publication
    Modified residuei201 – 2011N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9QXF8.
    PaxDbiQ9QXF8.
    PRIDEiQ9QXF8.

    PTM databases

    PhosphoSiteiQ9QXF8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9QXF8.
    BgeeiQ9QXF8.
    CleanExiMM_GNMT.
    GenevestigatoriQ9QXF8.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiQ9QXF8. 3 interactions.
    MINTiMINT-1869765.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 183
    Turni21 – 244
    Helixi26 – 3510
    Beta strandi39 – 413
    Helixi43 – 5513
    Beta strandi60 – 656
    Helixi70 – 778
    Beta strandi81 – 877
    Helixi89 – 10113
    Turni102 – 1043
    Helixi106 – 1094
    Beta strandi112 – 1154
    Helixi118 – 1203
    Helixi122 – 1243
    Beta strandi131 – 1366
    Helixi141 – 1433
    Beta strandi148 – 1514
    Helixi152 – 16211
    Beta strandi165 – 17612
    Helixi178 – 1847
    Beta strandi193 – 1953
    Beta strandi201 – 21010
    Beta strandi213 – 22412
    Beta strandi236 – 2438
    Helixi248 – 25710
    Turni258 – 2614
    Beta strandi263 – 27311
    Beta strandi283 – 2919

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R8XX-ray2.95A/B2-293[»]
    1R8YX-ray3.00A/B/C/D/E/F/G/H2-293[»]
    ProteinModelPortaliQ9QXF8.
    SMRiQ9QXF8. Positions 2-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QXF8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 1182S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Glycine N-methyltransferase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG78825.
    GeneTreeiENSGT00390000006845.
    HOGENOMiHOG000276537.
    HOVERGENiHBG051748.
    InParanoidiQ9QXF8.
    KOiK00552.
    OMAiLIIDHRN.
    OrthoDBiEOG76QFHR.
    PhylomeDBiQ9QXF8.
    TreeFamiTF324814.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR014369. Gly/Sar_N_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR16458. PTHR16458. 1 hit.
    PfamiPF13847. Methyltransf_31. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000385. Gly_N-mtase. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51600. SAM_GNMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9QXF8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL    50
    GLLRQHGCHR VLDVACGTGV DSIMLVEEGF SVMSVDASDK MLKYALKERW 100
    NRRKEPSFDN WVIEEANWLT LDKDVLSGDG FDAVICLGNS FAHLPDCKGD 150
    QSEHRLALKN IASMVRPGGL LVIDHRNYDY ILSTGCAPPG KNIYYKSDLT 200
    KDITTSVLTV NNKAHMVTLD YTVQVPGTGR DGSPGFSKFR LSYYPHCLAS 250
    FTELVRAAFG GRCQHSVLGD FKPYKPGQAY VPCYFIHVLK KTD 293
    Length:293
    Mass (Da):32,675
    Last modified:January 23, 2007 - v3
    Checksum:i264F0ACB6BBF3CDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571A → E in AAH14283. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89664 mRNA. Translation: BAA88218.1.
    AF325352 Genomic DNA. Translation: AAK00338.1.
    AY054408 Genomic DNA. Translation: AAL06142.1.
    BC014283 mRNA. Translation: AAH14283.1.
    CCDSiCCDS28838.1.
    RefSeqiNP_034451.1. NM_010321.1.
    UniGeneiMm.29395.

    Genome annotation databases

    EnsembliENSMUST00000002846; ENSMUSP00000002846; ENSMUSG00000002769.
    GeneIDi14711.
    KEGGimmu:14711.
    UCSCiuc008cue.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89664 mRNA. Translation: BAA88218.1 .
    AF325352 Genomic DNA. Translation: AAK00338.1 .
    AY054408 Genomic DNA. Translation: AAL06142.1 .
    BC014283 mRNA. Translation: AAH14283.1 .
    CCDSi CCDS28838.1.
    RefSeqi NP_034451.1. NM_010321.1.
    UniGenei Mm.29395.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R8X X-ray 2.95 A/B 2-293 [» ]
    1R8Y X-ray 3.00 A/B/C/D/E/F/G/H 2-293 [» ]
    ProteinModelPortali Q9QXF8.
    SMRi Q9QXF8. Positions 2-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QXF8. 3 interactions.
    MINTi MINT-1869765.

    PTM databases

    PhosphoSitei Q9QXF8.

    Proteomic databases

    MaxQBi Q9QXF8.
    PaxDbi Q9QXF8.
    PRIDEi Q9QXF8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002846 ; ENSMUSP00000002846 ; ENSMUSG00000002769 .
    GeneIDi 14711.
    KEGGi mmu:14711.
    UCSCi uc008cue.1. mouse.

    Organism-specific databases

    CTDi 27232.
    MGIi MGI:1202304. Gnmt.

    Phylogenomic databases

    eggNOGi NOG78825.
    GeneTreei ENSGT00390000006845.
    HOGENOMi HOG000276537.
    HOVERGENi HBG051748.
    InParanoidi Q9QXF8.
    KOi K00552.
    OMAi LIIDHRN.
    OrthoDBi EOG76QFHR.
    PhylomeDBi Q9QXF8.
    TreeFami TF324814.

    Enzyme and pathway databases

    BRENDAi 2.1.1.20. 3474.

    Miscellaneous databases

    ChiTaRSi GNMT. mouse.
    EvolutionaryTracei Q9QXF8.
    NextBioi 286711.
    PROi Q9QXF8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QXF8.
    Bgeei Q9QXF8.
    CleanExi MM_GNMT.
    Genevestigatori Q9QXF8.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR014369. Gly/Sar_N_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR16458. PTHR16458. 1 hit.
    Pfami PF13847. Methyltransf_31. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000385. Gly_N-mtase. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51600. SAM_GNMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse glycine N-methyltransferase is sexually dimorphic and regulated by growth hormone."
      Aida K., Tawata M., Negishi M., Onaya T.
      Horm. Metab. Res. 29:646-649(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Mouse glycine methyltransferase gene."
      Luka Z.A., Wagner C.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    3. "Identification of the mouse GNMT and PEX6 genes."
      Chen Y.-M.A., Wang Y.-C., Liu S.-P., Lee C.-M., Tsai T.-F.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvEv.
    4. "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].
      Strain: FVB/N.
      Tissue: Liver.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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-46; LYS-191; LYS-196 AND LYS-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes."
      Pakhomova S., Luka Z., Grohmann S., Wagner C., Newcomer M.E.
      Proteins 57:331-337(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-293, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiGNMT_MOUSE
    AccessioniPrimary (citable) accession number: Q9QXF8
    Secondary accession number(s): Q91WN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3