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Q9QXF8

- GNMT_MOUSE

UniProt

Q9QXF8 - GNMT_MOUSE

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Protein

Glycine N-methyltransferase

Gene

Gnmt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ9QXF8.
CleanExiMM_GNMT.
ExpressionAtlasiQ9QXF8. baseline and differential.
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 – 183Combined sources
Turni21 – 244Combined sources
Helixi26 – 3510Combined sources
Beta strandi39 – 413Combined sources
Helixi43 – 5513Combined sources
Beta strandi60 – 656Combined sources
Helixi70 – 778Combined sources
Beta strandi81 – 877Combined sources
Helixi89 – 10113Combined sources
Turni102 – 1043Combined sources
Helixi106 – 1094Combined sources
Beta strandi112 – 1154Combined sources
Helixi118 – 1203Combined sources
Helixi122 – 1243Combined sources
Beta strandi131 – 1366Combined sources
Helixi141 – 1433Combined sources
Beta strandi148 – 1514Combined sources
Helixi152 – 16211Combined sources
Beta strandi165 – 17612Combined sources
Helixi178 – 1847Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi201 – 21010Combined sources
Beta strandi213 – 22412Combined sources
Beta strandi236 – 2438Combined sources
Helixi248 – 25710Combined sources
Turni258 – 2614Combined sources
Beta strandi263 – 27311Combined sources
Beta strandi283 – 2919Combined sources

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

        10         20         30         40         50
MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL
60 70 80 90 100
GLLRQHGCHR VLDVACGTGV DSIMLVEEGF SVMSVDASDK MLKYALKERW
110 120 130 140 150
NRRKEPSFDN WVIEEANWLT LDKDVLSGDG FDAVICLGNS FAHLPDCKGD
160 170 180 190 200
QSEHRLALKN IASMVRPGGL LVIDHRNYDY ILSTGCAPPG KNIYYKSDLT
210 220 230 240 250
KDITTSVLTV NNKAHMVTLD YTVQVPGTGR DGSPGFSKFR LSYYPHCLAS
260 270 280 290
FTELVRAAFG GRCQHSVLGD FKPYKPGQAY VPCYFIHVLK KTD
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

Bgeei Q9QXF8.
CleanExi MM_GNMT.
ExpressionAtlasi Q9QXF8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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