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Q9QXF8 (GNMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine N-methyltransferase

EC=2.1.1.20
Gene names
Name:Gnmt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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

Subunit structure

Homotetramer By similarity. Ref.7

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 293292Glycine N-methyltransferase
PRO_0000087525

Regions

Region117 – 1182S-adenosyl-L-methionine binding By similarity

Sites

Binding site221S-adenosyl-L-methionine By similarity
Binding site311S-adenosyl-L-methionine By similarity
Binding site341Substrate By similarity
Binding site411S-adenosyl-L-methionine By similarity
Binding site651S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site861S-adenosyl-L-methionine By similarity
Binding site1371S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1391Substrate By similarity
Binding site1761Substrate By similarity
Binding site2211Substrate By similarity

Amino acid modifications

Modified residue21N-acetylvaline By similarity
Modified residue101Phosphoserine Ref.5
Modified residue461N6-succinyllysine Ref.6
Modified residue1911N6-succinyllysine Ref.6
Modified residue1961N6-succinyllysine Ref.6
Modified residue2011N6-succinyllysine Ref.6

Experimental info

Sequence conflict1571A → E in AAH14283. Ref.4

Secondary structure

...................................................... 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QXF8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 264F0ACB6BBF3CDA

FASTA29332,675
        10         20         30         40         50         60 
MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCHR 

        70         80         90        100        110        120 
VLDVACGTGV DSIMLVEEGF SVMSVDASDK MLKYALKERW NRRKEPSFDN WVIEEANWLT 

       130        140        150        160        170        180 
LDKDVLSGDG FDAVICLGNS FAHLPDCKGD QSEHRLALKN IASMVRPGGL LVIDHRNYDY 

       190        200        210        220        230        240 
ILSTGCAPPG KNIYYKSDLT KDITTSVLTV NNKAHMVTLD YTVQVPGTGR DGSPGFSKFR 

       250        260        270        280        290 
LSYYPHCLAS FTELVRAAFG GRCQHSVLGD FKPYKPGQAY VPCYFIHVLK KTD 

« Hide

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89664 mRNA. Translation: BAA88218.1.
AF325352 Genomic DNA. Translation: AAK00338.1.
AY054408 Genomic DNA. Translation: AAL06142.1.
BC014283 mRNA. Translation: AAH14283.1.
CCDSCCDS28838.1.
RefSeqNP_034451.1. NM_010321.1.
UniGeneMm.29395.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R8XX-ray2.95A/B2-293[»]
1R8YX-ray3.00A/B/C/D/E/F/G/H2-293[»]
ProteinModelPortalQ9QXF8.
SMRQ9QXF8. Positions 2-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QXF8. 3 interactions.
MINTMINT-1869765.

PTM databases

PhosphoSiteQ9QXF8.

Proteomic databases

MaxQBQ9QXF8.
PaxDbQ9QXF8.
PRIDEQ9QXF8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002846; ENSMUSP00000002846; ENSMUSG00000002769.
GeneID14711.
KEGGmmu:14711.
UCSCuc008cue.1. mouse.

Organism-specific databases

CTD27232.
MGIMGI:1202304. Gnmt.

Phylogenomic databases

eggNOGNOG78825.
GeneTreeENSGT00390000006845.
HOGENOMHOG000276537.
HOVERGENHBG051748.
InParanoidQ9QXF8.
KOK00552.
OMALIIDHRN.
OrthoDBEOG76QFHR.
PhylomeDBQ9QXF8.
TreeFamTF324814.

Enzyme and pathway databases

BRENDA2.1.1.20. 3474.

Gene expression databases

ArrayExpressQ9QXF8.
BgeeQ9QXF8.
CleanExMM_GNMT.
GenevestigatorQ9QXF8.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR014369. Gly/Sar_N_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR16458. PTHR16458. 1 hit.
PfamPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PIRSFPIRSF000385. Gly_N-mtase. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51600. SAM_GNMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNMT. mouse.
EvolutionaryTraceQ9QXF8.
NextBio286711.
PROQ9QXF8.
SOURCESearch...

Entry information

Entry nameGNMT_MOUSE
AccessionPrimary (citable) accession number: Q9QXF8
Secondary accession number(s): Q91WN7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot