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Methionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Vitamin-B12 dependent methionine synthase) (MS)

 METH_HUMAN              Reviewed;        1265 AA.
Q99707; A1L4N8; A9Z1W4; B7ZLW7; B9EGF7; Q99713; Q99723;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 2.
23-MAY-2018, entry version 187.
RecName: Full=Methionine synthase;
EC=2.1.1.13;
AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
AltName: Full=Vitamin-B12 dependent methionine synthase;
Short=MS;
Name=MTR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HMAG ILE-881 DEL
AND ASP-920.
TISSUE=Fibroblast;
PubMed=8968737; DOI=10.1093/hmg/5.12.1867;
Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B.,
Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.;
"Human methionine synthase: cDNA cloning and identification of
mutations in patients of the cblG complementation group of
folate/cobalamin disorders.";
Hum. Mol. Genet. 5:1867-1874(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8968735; DOI=10.1093/hmg/5.12.1851;
Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.;
"Cloning, mapping and RNA analysis of the human methionine synthase
gene.";
Hum. Mol. Genet. 5:1851-1858(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS TYR-255 AND
GLY-919.
TISSUE=Fetal liver;
PubMed=9013615; DOI=10.1074/jbc.272.6.3444;
Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.;
"Human methionine synthase. cDNA cloning, gene localization, and
expression.";
J. Biol. Chem. 272:3628-3634(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLY-919.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
VARIANTS HMAG ILE-881 DEL AND LEU-1173, AND VARIANT LYS-61.
PubMed=8968736; DOI=10.1093/hmg/5.12.1859;
Gulati S., Baker P.J., Li Y.N., Fowler B., Kruger W.D., Brody L.C.,
Banerjee R.;
"Defects in human methionine synthase in cblG patients.";
Hum. Mol. Genet. 5:1859-1865(1996).
[9]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT GLY-919.
PubMed=12375236; DOI=10.1086/344209;
Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S.,
Mitchell L.E.;
"Maternal genetic effects, exerted by genes involved in homocysteine
remethylation, influence the risk of spina bifida.";
Am. J. Hum. Genet. 71:1222-1226(2002).
[10]
VARIANT GLY-919.
PubMed=15979034; DOI=10.1016/j.ymgme.2005.02.003;
O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C.,
Conley M., Weiler A., Peng K., Shane B., Scott J.M.,
Parle-McDermott A., Molloy A.M., Brody L.C.;
"Analysis of methionine synthase reductase polymorphisms for neural
tube defects risk association.";
Mol. Genet. Metab. 85:220-227(2005).
[11] {ECO:0000244|PDB:4CCZ}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 16-657 IN COMPLEX WITH
TETRAHYDROFOLATE.
Vollmar M., Kiyani W., Krojer T., Goubin S., Burgess-Brown N.,
Von Delft F., Oppermann U., Edwards A., Arrowsmith C., Bountra C.,
Yue W.W.;
"Crystal structure of human 5-methyltetrahydrofolate-homocysteine
methyltransferase, the homocysteine and folate binding domains.";
Submitted (OCT-2013) to the PDB data bank.
[12] {ECO:0000244|PDB:2O2K}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 924-1265 OF MUTANT
GLU-963/ASN-1071, SUBUNIT, INTERACTION WITH MTRR, AND MUTAGENESIS OF
ASP-963 AND LYS-1071.
PubMed=17288554; DOI=10.1111/j.1742-4658.2006.05618.x;
Wolthers K.R., Toogood H.S., Jowitt T.A., Marshall K.R., Leys D.,
Scrutton N.S.;
"Crystal structure and solution characterization of the activation
domain of human methionine synthase.";
FEBS J. 274:738-750(2007).
-!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
methionine. Subsequently, remethylates the cofactor using
methyltetrahydrofolate (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
tetrahydrofolate + L-methionine.
-!- COFACTOR:
Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-methionine from L-homocysteine (MetH route): step
1/1.
-!- SUBUNIT: Monomer (PubMed:17288554). Dimer (PubMed:17288554).
Mainly monomer. Interacts with MTRR (PubMed:17288554).
{ECO:0000269|PubMed:17288554}.
-!- INTERACTION:
Q9Y4U1:MMACHC; NbExp=3; IntAct=EBI-1045782, EBI-9775184;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99707-1; Sequence=Displayed;
Name=2;
IsoId=Q99707-2; Sequence=VSP_057283;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at the highest
levels in pancreas, heart, brain, skeletal muscle and placenta.
Expressed at lower levels in lung, liver and kidney.
-!- DOMAIN: Modular enzyme with four functionally distinct domains.
The isolated Hcy-binding domain catalyzes methyl transfer from
free methylcobalamin to homocysteine. The Hcy-binding domain in
association with the pterin-binding domain catalyzes the
methylation of cob(I)alamin by methyltetrahydrofolate and the
methylation of homocysteine. The B12-binding domain binds the
cofactor. The AdoMet activation domain binds S-adenosyl-L-
methionine. Under aerobic conditions cob(I)alamin can be converted
to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
methionine and flavodoxin regenerates methylcobalamin (By
similarity). {ECO:0000250}.
-!- DISEASE: Homocystinuria-megaloblastic anemia, cblG complementation
type (HMAG) [MIM:250940]: An autosomal recessive inborn error of
metabolism resulting from defects in the cobalamin-dependent
pathway that converts homocysteine to methionine. It causes
delayed psychomotor development, megaloblastic anemia,
homocystinuria, and hypomethioninemia.
{ECO:0000269|PubMed:8968736, ECO:0000269|PubMed:8968737}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Neural tube defects, folate-sensitive (NTDFS)
[MIM:601634]: The most common NTDs are open spina bifida
(myelomeningocele) and anencephaly. {ECO:0000269|PubMed:12375236}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
synthase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=5-methyltetrahydrofolate-
homocysteine methyltransferase entry;
URL="https://en.wikipedia.org/wiki/5-Methyltetrahydrofolate-homocysteine_methyltransferase";
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EMBL; U71285; AAC51188.1; -; mRNA.
EMBL; U75743; AAB58906.1; -; mRNA.
EMBL; U73338; AAB39704.1; -; mRNA.
EMBL; AL359185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471098; EAW70066.1; -; Genomic_DNA.
EMBL; BC130616; AAI30617.1; -; mRNA.
EMBL; BC136440; AAI36441.1; -; mRNA.
EMBL; BC144095; AAI44096.1; -; mRNA.
CCDS; CCDS1614.1; -. [Q99707-1]
CCDS; CCDS73054.1; -. [Q99707-2]
RefSeq; NP_000245.2; NM_000254.2. [Q99707-1]
RefSeq; NP_001278868.1; NM_001291939.1. [Q99707-2]
RefSeq; NP_001278869.1; NM_001291940.1.
UniGene; Hs.498187; -.
PDB; 2O2K; X-ray; 1.60 A; A/B=925-1265.
PDB; 4CCZ; X-ray; 2.70 A; A=16-657.
PDBsum; 2O2K; -.
PDBsum; 4CCZ; -.
ProteinModelPortal; Q99707; -.
SMR; Q99707; -.
BioGrid; 110642; 31.
DIP; DIP-40306N; -.
IntAct; Q99707; 10.
STRING; 9606.ENSP00000355536; -.
BindingDB; Q99707; -.
ChEMBL; CHEMBL2150844; -.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00200; Hydroxocobalamin.
DrugBank; DB00134; L-Methionine.
DrugBank; DB00116; Tetrahydrofolic acid.
iPTMnet; Q99707; -.
PhosphoSitePlus; Q99707; -.
BioMuta; MTR; -.
DMDM; 2842762; -.
EPD; Q99707; -.
MaxQB; Q99707; -.
PaxDb; Q99707; -.
PeptideAtlas; Q99707; -.
PRIDE; Q99707; -.
Ensembl; ENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1]
Ensembl; ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2]
GeneID; 4548; -.
KEGG; hsa:4548; -.
UCSC; uc001hyi.5; human. [Q99707-1]
CTD; 4548; -.
DisGeNET; 4548; -.
EuPathDB; HostDB:ENSG00000116984.12; -.
GeneCards; MTR; -.
GeneReviews; MTR; -.
HGNC; HGNC:7468; MTR.
HPA; HPA044474; -.
MalaCards; MTR; -.
MIM; 156570; gene.
MIM; 250940; phenotype.
MIM; 601634; phenotype.
MIM; 603174; phenotype.
neXtProt; NX_Q99707; -.
OpenTargets; ENSG00000116984; -.
Orphanet; 2170; Methylcobalamin deficiency type cblG.
PharmGKB; PA31272; -.
eggNOG; KOG1579; Eukaryota.
eggNOG; COG0646; LUCA.
eggNOG; COG1410; LUCA.
GeneTree; ENSGT00420000029824; -.
HOGENOM; HOG000251409; -.
HOVERGEN; HBG006347; -.
InParanoid; Q99707; -.
KO; K00548; -.
OMA; KYPRPLN; -.
OrthoDB; EOG091G00WU; -.
PhylomeDB; Q99707; -.
TreeFam; TF312829; -.
BioCyc; MetaCyc:HS04076-MONOMER; -.
Reactome; R-HSA-156581; Methylation.
Reactome; R-HSA-1614635; Sulfur amino acid metabolism.
Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-HSA-3359467; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
Reactome; R-HSA-3359469; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
SIGNOR; Q99707; -.
UniPathway; UPA00051; UER00081.
ChiTaRS; MTR; human.
EvolutionaryTrace; Q99707; -.
GeneWiki; Methionine_synthase; -.
GenomeRNAi; 4548; -.
PRO; PR:Q99707; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116984; -.
CleanEx; HS_MTR; -.
ExpressionAtlas; Q99707; baseline and differential.
Genevisible; Q99707; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
GO; GO:0008705; F:methionine synthase activity; IDA:CACAO.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0031103; P:axon regeneration; ISS:BHF-UCL.
GO; GO:0071732; P:cellular response to nitric oxide; ISS:BHF-UCL.
GO; GO:0009235; P:cobalamin metabolic process; IMP:BHF-UCL.
GO; GO:0009086; P:methionine biosynthetic process; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
GO; GO:0048678; P:response to axon injury; ISS:BHF-UCL.
CDD; cd02069; methionine_synthase_B12_BD; 1.
Gene3D; 1.10.1240.10; -; 1.
Gene3D; 3.10.196.10; -; 3.
Gene3D; 3.20.20.20; -; 1.
Gene3D; 3.20.20.330; -; 1.
InterPro; IPR003759; Cbl-bd_cap.
InterPro; IPR006158; Cobalamin-bd.
InterPro; IPR036724; Cobalamin-bd_sf.
InterPro; IPR011005; Dihydropteroate_synth-like.
InterPro; IPR003726; HCY_dom.
InterPro; IPR036589; HCY_dom_sf.
InterPro; IPR033706; Met_synthase_B12-bd.
InterPro; IPR011822; MetH.
InterPro; IPR036594; Meth_synthase_dom.
InterPro; IPR000489; Pterin-binding_dom.
InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
Pfam; PF02310; B12-binding; 1.
Pfam; PF02607; B12-binding_2; 1.
Pfam; PF02965; Met_synt_B12; 1.
Pfam; PF00809; Pterin_bind; 1.
Pfam; PF02574; S-methyl_trans; 1.
PIRSF; PIRSF000381; MetH; 1.
SMART; SM01018; B12-binding_2; 1.
SUPFAM; SSF47644; SSF47644; 1.
SUPFAM; SSF51717; SSF51717; 1.
SUPFAM; SSF52242; SSF52242; 1.
SUPFAM; SSF56507; SSF56507; 1.
SUPFAM; SSF82282; SSF82282; 1.
TIGRFAMs; TIGR02082; metH; 1.
PROSITE; PS50974; ADOMET_ACTIVATION; 1.
PROSITE; PS51332; B12_BINDING; 1.
PROSITE; PS51337; B12_BINDING_NTER; 1.
PROSITE; PS50970; HCY; 1.
PROSITE; PS50972; PTERIN_BINDING; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
Cobalamin; Cobalt; Complete proteome; Cytoplasm; Disease mutation;
Metal-binding; Methionine biosynthesis; Methyltransferase;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transferase; Zinc.
CHAIN 1 1265 Methionine synthase.
/FTId=PRO_0000204530.
DOMAIN 19 338 Hcy-binding. {ECO:0000255|PROSITE-
ProRule:PRU00333}.
DOMAIN 371 632 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
DOMAIN 662 759 B12-binding N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00667}.
DOMAIN 772 907 B12-binding. {ECO:0000255|PROSITE-
ProRule:PRU00666}.
DOMAIN 923 1265 AdoMet activation. {ECO:0000255|PROSITE-
ProRule:PRU00346}.
REGION 382 384 Substrate binding.
{ECO:0000244|PDB:4CCZ}.
REGION 860 861 Cobalamin-binding. {ECO:0000250}.
REGION 1227 1228 S-adenosyl-L-methionine binding.
{ECO:0000250}.
METAL 260 260 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00333}.
METAL 323 323 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00333}.
METAL 324 324 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00333}.
METAL 785 785 Cobalt (cobalamin axial ligand).
{ECO:0000250}.
BINDING 449 449 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 470 470 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 537 537 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 579 579 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 585 585 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 591 591 Substrate. {ECO:0000244|PDB:4CCZ,
ECO:0000305|Ref.11}.
BINDING 830 830 Cobalamin. {ECO:0000250}.
BINDING 974 974 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 1172 1172 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 1176 1176 Cobalamin; via carbonyl oxygen.
{ECO:0000250}.
MOD_RES 1264 1264 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z2Q4}.
VAR_SEQ 682 732 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057283.
VARIANT 52 52 R -> Q (in dbSNP:rs12749581).
/FTId=VAR_050033.
VARIANT 61 61 R -> K. {ECO:0000269|PubMed:8968736}.
/FTId=VAR_004326.
VARIANT 255 255 C -> Y (in dbSNP:rs1140598).
{ECO:0000269|PubMed:9013615}.
/FTId=VAR_004327.
VARIANT 314 314 D -> N (in dbSNP:rs2229274).
/FTId=VAR_061338.
VARIANT 881 881 Missing (in HMAG).
{ECO:0000269|PubMed:8968736,
ECO:0000269|PubMed:8968737}.
/FTId=VAR_004328.
VARIANT 919 919 D -> G (in dbSNP:rs1805087).
{ECO:0000269|PubMed:12375236,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15979034,
ECO:0000269|PubMed:9013615}.
/FTId=VAR_004329.
VARIANT 920 920 H -> D (in HMAG; dbSNP:rs121913579).
{ECO:0000269|PubMed:8968737}.
/FTId=VAR_004330.
VARIANT 1173 1173 P -> L (in HMAG; dbSNP:rs121913578).
{ECO:0000269|PubMed:8968736}.
/FTId=VAR_004331.
MUTAGEN 963 963 D->E: Decreases binding to MTRR; when
associated with N-1071.
{ECO:0000269|PubMed:17288554}.
MUTAGEN 1071 1071 K->N: Decreases binding to MTRR; when
associated with E-963.
{ECO:0000269|PubMed:17288554}.
HELIX 18 28 {ECO:0000244|PDB:4CCZ}.
HELIX 37 44 {ECO:0000244|PDB:4CCZ}.
HELIX 49 51 {ECO:0000244|PDB:4CCZ}.
HELIX 67 69 {ECO:0000244|PDB:4CCZ}.
HELIX 70 73 {ECO:0000244|PDB:4CCZ}.
HELIX 75 87 {ECO:0000244|PDB:4CCZ}.
STRAND 92 94 {ECO:0000244|PDB:4CCZ}.
HELIX 102 105 {ECO:0000244|PDB:4CCZ}.
HELIX 106 108 {ECO:0000244|PDB:4CCZ}.
HELIX 111 113 {ECO:0000244|PDB:4CCZ}.
HELIX 114 136 {ECO:0000244|PDB:4CCZ}.
STRAND 141 146 {ECO:0000244|PDB:4CCZ}.
STRAND 153 155 {ECO:0000244|PDB:4CCZ}.
STRAND 159 161 {ECO:0000244|PDB:4CCZ}.
HELIX 169 185 {ECO:0000244|PDB:4CCZ}.
STRAND 189 198 {ECO:0000244|PDB:4CCZ}.
HELIX 199 213 {ECO:0000244|PDB:4CCZ}.
TURN 214 216 {ECO:0000244|PDB:4CCZ}.
STRAND 222 226 {ECO:0000244|PDB:4CCZ}.
HELIX 241 248 {ECO:0000244|PDB:4CCZ}.
HELIX 249 251 {ECO:0000244|PDB:4CCZ}.
STRAND 254 263 {ECO:0000244|PDB:4CCZ}.
TURN 264 267 {ECO:0000244|PDB:4CCZ}.
HELIX 268 275 {ECO:0000244|PDB:4CCZ}.
STRAND 279 287 {ECO:0000244|PDB:4CCZ}.
STRAND 318 320 {ECO:0000244|PDB:4CCZ}.
HELIX 328 338 {ECO:0000244|PDB:4CCZ}.
TURN 348 353 {ECO:0000244|PDB:4CCZ}.
STRAND 355 365 {ECO:0000244|PDB:4CCZ}.
STRAND 372 375 {ECO:0000244|PDB:4CCZ}.
TURN 380 382 {ECO:0000244|PDB:4CCZ}.
HELIX 384 391 {ECO:0000244|PDB:4CCZ}.
HELIX 395 407 {ECO:0000244|PDB:4CCZ}.
STRAND 411 416 {ECO:0000244|PDB:4CCZ}.
HELIX 424 437 {ECO:0000244|PDB:4CCZ}.
HELIX 439 442 {ECO:0000244|PDB:4CCZ}.
STRAND 446 449 {ECO:0000244|PDB:4CCZ}.
HELIX 453 462 {ECO:0000244|PDB:4CCZ}.
STRAND 468 472 {ECO:0000244|PDB:4CCZ}.
HELIX 478 491 {ECO:0000244|PDB:4CCZ}.
STRAND 494 501 {ECO:0000244|PDB:4CCZ}.
HELIX 509 527 {ECO:0000244|PDB:4CCZ}.
HELIX 531 533 {ECO:0000244|PDB:4CCZ}.
STRAND 534 537 {ECO:0000244|PDB:4CCZ}.
HELIX 548 552 {ECO:0000244|PDB:4CCZ}.
HELIX 553 567 {ECO:0000244|PDB:4CCZ}.
HELIX 577 584 {ECO:0000244|PDB:4CCZ}.
HELIX 588 605 {ECO:0000244|PDB:4CCZ}.
STRAND 609 612 {ECO:0000244|PDB:4CCZ}.
HELIX 620 622 {ECO:0000244|PDB:4CCZ}.
HELIX 625 635 {ECO:0000244|PDB:4CCZ}.
HELIX 642 648 {ECO:0000244|PDB:4CCZ}.
HELIX 932 937 {ECO:0000244|PDB:2O2K}.
HELIX 944 946 {ECO:0000244|PDB:2O2K}.
STRAND 956 962 {ECO:0000244|PDB:2O2K}.
HELIX 966 970 {ECO:0000244|PDB:2O2K}.
HELIX 976 987 {ECO:0000244|PDB:2O2K}.
HELIX 995 998 {ECO:0000244|PDB:2O2K}.
HELIX 1005 1022 {ECO:0000244|PDB:2O2K}.
STRAND 1026 1040 {ECO:0000244|PDB:2O2K}.
STRAND 1043 1046 {ECO:0000244|PDB:2O2K}.
HELIX 1053 1055 {ECO:0000244|PDB:2O2K}.
STRAND 1059 1063 {ECO:0000244|PDB:2O2K}.
HELIX 1082 1085 {ECO:0000244|PDB:2O2K}.
HELIX 1089 1091 {ECO:0000244|PDB:2O2K}.
STRAND 1095 1106 {ECO:0000244|PDB:2O2K}.
HELIX 1107 1116 {ECO:0000244|PDB:2O2K}.
HELIX 1120 1147 {ECO:0000244|PDB:2O2K}.
TURN 1152 1155 {ECO:0000244|PDB:2O2K}.
HELIX 1160 1164 {ECO:0000244|PDB:2O2K}.
STRAND 1168 1171 {ECO:0000244|PDB:2O2K}.
HELIX 1185 1192 {ECO:0000244|PDB:2O2K}.
HELIX 1195 1199 {ECO:0000244|PDB:2O2K}.
STRAND 1209 1220 {ECO:0000244|PDB:2O2K}.
HELIX 1235 1245 {ECO:0000244|PDB:2O2K}.
HELIX 1249 1255 {ECO:0000244|PDB:2O2K}.
HELIX 1257 1259 {ECO:0000244|PDB:2O2K}.
SEQUENCE 1265 AA; 140527 MW; B04C26BCBE9A57C2 CRC64;
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA
RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC
SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA
KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT
GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL
EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG
MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD
FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI
LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV
IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG
DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV
KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM
IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV
FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL
ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY
CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE
LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL
GYDTD


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