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Methionine synthase reductase (MSR) (EC 1.16.1.8)

 MTRR_HUMAN              Reviewed;         725 AA.
Q9UBK8; O60471; Q32MA9; Q7Z4M8;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
23-MAY-2018, entry version 176.
RecName: Full=Methionine synthase reductase;
Short=MSR;
EC=1.16.1.8;
Name=MTRR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B AND C), AND
VARIANT LEU-202.
PubMed=10564814; DOI=10.1016/S0378-1119(99)00431-X;
Leclerc D., Odievre M.-H., Wu Q., Wilson A., Huizenga J., Rozen R.,
Scherer S.W., Gravel R.A.;
"Molecular cloning, expression and physical mapping of the human
methionine synthase reductase gene.";
Gene 240:75-88(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), VARIANT LEU-202, AND
VARIANT HMAE LEU-603 DEL.
PubMed=9501215; DOI=10.1073/pnas.95.6.3059;
Leclerc D., Wilson A., Dumas R., Gafuik C., Song D., Watkins D.,
Heng H.H.Q., Rommens J.M., Scherer S.W., Rosenblatt D.S., Gravel R.A.;
"Cloning and mapping of a cDNA for methionine synthase reductase, a
flavoprotein defective in patients with homocystinuria.";
Proc. Natl. Acad. Sci. U.S.A. 95:3059-3064(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
TISSUE=Lung;
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).
[5]
SUBCELLULAR LOCATION (ISOFORM A).
PubMed=18221906; DOI=10.1016/j.ymgme.2007.11.019;
Froese D.S., Wu X., Zhang J., Dumas R., Schoel W.M., Amrein M.,
Gravel R.A.;
"Restricted role for methionine synthase reductase defined by
subcellular localization.";
Mol. Genet. Metab. 94:68-77(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 AND SER-216, VARIANT
[LARGE SCALE ANALYSIS] LEU-202, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 192-725 IN COMPLEX WITH FAD
AND NADP, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
AND FUNCTION.
PubMed=17892308; DOI=10.1021/bi701209p;
Wolthers K.R., Lou X., Toogood H.S., Leys D., Scrutton N.S.;
"Mechanism of coenzyme binding to human methionine synthase reductase
revealed through the crystal structure of the FNR-like module and
isothermal titration calorimetry.";
Biochemistry 46:11833-11844(2007).
[11]
VARIANTS HMAE VAL-81 DEL; MET-83; THR-156; ARG-432; ARG-514 AND
ARG-581, AND VARIANT VAL-360.
PubMed=10484769; DOI=10.1093/hmg/8.11.2009;
Wilson A., Leclerc D., Rosenblatt D.S., Gravel R.A.;
"Molecular basis for methionine synthase reductase deficiency in
patients belonging to the cblE complementation group of disorders in
folate/cobalamin metabolism.";
Hum. Mol. Genet. 8:2009-2016(1999).
[12]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT MET-49.
PubMed=10444342; DOI=10.1006/mgme.1999.2879;
Wilson A., Platt R., Wu Q., Leclerc D., Christensen B., Yang H.,
Gravel R.A., Rozen R.;
"A common variant in methionine synthase reductase combined with low
cobalamin (vitamin B12) increases risk for spina bifida.";
Mol. Genet. Metab. 67:317-323(1999).
[13]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT MET-49.
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).
[14]
VARIANTS MET-49; LEU-202 AND ARG-377.
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).
-!- FUNCTION: Involved in the reductive regeneration of cob(I)alamin
(vitamin B12) cofactor required for the maintenance of methionine
synthase in a functional state. Necessary for utilization of
methylgroups from the folate cycle, thereby affecting
transgenerational epigenetic inheritance. Folate pathway donates
methyl groups necessary for cellular methylation and affects
different pathways such as DNA methylation, possibly explaining
the transgenerational epigenetic inheritance effects.
{ECO:0000269|PubMed:17892308}.
-!- CATALYTIC ACTIVITY: 2 [methionine synthase]-methylcob(I)alamin + 2
S-adenosylhomocysteine + NADP(+) = 2 [methionine synthase]-
cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:17892308}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17892308};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:17892308};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.89 uM for NADPH {ECO:0000269|PubMed:17892308};
KM=3540 uM for NADH {ECO:0000269|PubMed:17892308};
-!- INTERACTION:
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-10319161, EBI-10172181;
-!- SUBCELLULAR LOCATION: Isoform B: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform C: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform A: Cytoplasm
{ECO:0000269|PubMed:18221906}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A;
IsoId=Q9UBK8-1; Sequence=Displayed;
Name=B;
IsoId=Q9UBK8-2; Sequence=VSP_003910;
Name=C;
IsoId=Q9UBK8-3; Sequence=VSP_003910, VSP_003911, VSP_003912;
-!- TISSUE SPECIFICITY: Found in all tissues tested, particularly
abundant in skeletal muscle.
-!- DISEASE: Homocystinuria-megaloblastic anemia, cblE complementation
type (HMAE) [MIM:236270]: 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. Cells from patients with
HMAE fail to incorporate methyltetrahydrofolate into methionine in
whole cells, but cell extracts show normal methionine synthase
activity in the presence of a reducing agent.
{ECO:0000269|PubMed:10484769, ECO:0000269|PubMed:9501215}.
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:10444342,
ECO:0000269|PubMed:12375236}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The hidden things
- Issue 166 of December 2014;
URL="https://web.expasy.org/spotlight/back_issues/166/";
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EMBL; AF121213; AAF17303.1; -; Genomic_DNA.
EMBL; AF121202; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121203; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121204; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121205; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121206; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121207; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121208; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121209; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121210; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121211; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121212; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121214; AAF16876.1; -; mRNA.
EMBL; AF121213; AAF17304.1; -; Genomic_DNA.
EMBL; AF121202; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121203; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121204; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121205; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121206; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121207; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121208; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121209; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121210; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121211; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121212; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF025794; AAC39667.1; -; mRNA.
EMBL; AC010346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC054816; AAH54816.2; -; mRNA.
EMBL; BC109216; AAI09217.1; -; mRNA.
CCDS; CCDS3874.1; -. [Q9UBK8-1]
CCDS; CCDS47190.1; -. [Q9UBK8-2]
RefSeq; NP_002445.2; NM_002454.2. [Q9UBK8-2]
RefSeq; NP_076915.2; NM_024010.2. [Q9UBK8-1]
UniGene; Hs.481551; -.
PDB; 2QTL; X-ray; 1.90 A; A=192-725.
PDB; 2QTZ; X-ray; 1.90 A; A=192-725.
PDBsum; 2QTL; -.
PDBsum; 2QTZ; -.
ProteinModelPortal; Q9UBK8; -.
SMR; Q9UBK8; -.
BioGrid; 110645; 14.
DIP; DIP-61183N; -.
IntAct; Q9UBK8; 8.
STRING; 9606.ENSP00000264668; -.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00200; Hydroxocobalamin.
DrugBank; DB00134; L-Methionine.
iPTMnet; Q9UBK8; -.
PhosphoSitePlus; Q9UBK8; -.
SwissPalm; Q9UBK8; -.
BioMuta; MTRR; -.
DMDM; 296439300; -.
EPD; Q9UBK8; -.
MaxQB; Q9UBK8; -.
PaxDb; Q9UBK8; -.
PeptideAtlas; Q9UBK8; -.
PRIDE; Q9UBK8; -.
Ensembl; ENST00000264668; ENSP00000264668; ENSG00000124275. [Q9UBK8-1]
Ensembl; ENST00000440940; ENSP00000402510; ENSG00000124275. [Q9UBK8-2]
Ensembl; ENST00000510279; ENSP00000427200; ENSG00000124275. [Q9UBK8-3]
Ensembl; ENST00000514369; ENSP00000426132; ENSG00000124275. [Q9UBK8-3]
GeneID; 4552; -.
KEGG; hsa:4552; -.
UCSC; uc003jed.4; human. [Q9UBK8-1]
CTD; 4552; -.
DisGeNET; 4552; -.
EuPathDB; HostDB:ENSG00000124275.14; -.
GeneCards; MTRR; -.
GeneReviews; MTRR; -.
H-InvDB; HIX0031952; -.
HGNC; HGNC:7473; MTRR.
HPA; HPA038113; -.
MalaCards; MTRR; -.
MIM; 236270; phenotype.
MIM; 601634; phenotype.
MIM; 602568; gene.
neXtProt; NX_Q9UBK8; -.
OpenTargets; ENSG00000124275; -.
Orphanet; 2169; Methylcobalamin deficiency type cblE.
PharmGKB; PA31277; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000007485; -.
HOVERGEN; HBG108376; -.
InParanoid; Q9UBK8; -.
KO; K00597; -.
OMA; PWIAGLW; -.
OrthoDB; EOG091G045Q; -.
PhylomeDB; Q9UBK8; -.
TreeFam; TF105716; -.
BioCyc; MetaCyc:HS04756-MONOMER; -.
BRENDA; 1.16.1.8; 2681.
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.
SABIO-RK; Q9UBK8; -.
EvolutionaryTrace; Q9UBK8; -.
GeneWiki; MTRR_(gene); -.
GenomeRNAi; 4552; -.
PRO; PR:Q9UBK8; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000124275; -.
CleanEx; HS_MTRR; -.
ExpressionAtlas; Q9UBK8; baseline and differential.
Genevisible; Q9UBK8; HS.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0030586; F:[methionine synthase] reductase activity; IDA:BHF-UCL.
GO; GO:0050444; F:aquacobalamin reductase (NADPH) activity; IDA:CACAO.
GO; GO:0071949; F:FAD binding; IDA:BHF-UCL.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IDA:BHF-UCL.
GO; GO:0050661; F:NADP binding; TAS:UniProtKB.
GO; GO:0070402; F:NADPH binding; IDA:BHF-UCL.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
GO; GO:0016723; F:oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0046655; P:folic acid metabolic process; IDA:BHF-UCL.
GO; GO:0043418; P:homocysteine catabolic process; IDA:BHF-UCL.
GO; GO:0009086; P:methionine biosynthetic process; IDA:BHF-UCL.
GO; GO:0006555; P:methionine metabolic process; TAS:UniProtKB.
GO; GO:1904042; P:negative regulation of cystathionine beta-synthase activity; IDA:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0033353; P:S-adenosylmethionine cycle; ISS:BHF-UCL.
Gene3D; 1.20.990.10; -; 2.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
Complete proteome; Cytoplasm; Disease mutation; FAD; Flavoprotein;
FMN; Methionine biosynthesis; NADP; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; S-adenosyl-L-methionine.
CHAIN 1 725 Methionine synthase reductase.
/FTId=PRO_0000021785.
DOMAIN 32 174 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 298 560 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 120 151 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 478 481 FAD. {ECO:0000269|PubMed:17892308}.
NP_BIND 514 517 FAD. {ECO:0000269|PubMed:17892308}.
NP_BIND 637 638 NADP. {ECO:0000269|PubMed:17892308}.
NP_BIND 651 653 NADP. {ECO:0000269|PubMed:17892308}.
REGION 193 274 Hinge.
BINDING 318 318 NADP. {ECO:0000269|PubMed:17892308}.
BINDING 686 686 NADP. {ECO:0000269|PubMed:17892308}.
BINDING 724 724 FAD. {ECO:0000269|PubMed:17892308}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 27 Missing (in isoform B and isoform C).
{ECO:0000303|PubMed:10564814,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9501215}.
/FTId=VSP_003910.
VAR_SEQ 71 85 YDLKTETAPLVVVVS -> VSVIQNTPTFAMGGR (in
isoform C). {ECO:0000303|PubMed:10564814,
ECO:0000303|PubMed:9501215}.
/FTId=VSP_003911.
VAR_SEQ 86 725 Missing (in isoform C).
{ECO:0000303|PubMed:10564814,
ECO:0000303|PubMed:9501215}.
/FTId=VSP_003912.
VARIANT 49 49 I -> M (polymorphism; may increase risk
for spina bifida; dbSNP:rs1801394).
{ECO:0000269|PubMed:10444342,
ECO:0000269|PubMed:12375236,
ECO:0000269|PubMed:15979034}.
/FTId=VAR_012836.
VARIANT 81 81 Missing (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012837.
VARIANT 83 83 V -> M (in HMAE; dbSNP:rs761061866).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012838.
VARIANT 156 156 A -> T (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012839.
VARIANT 202 202 S -> L (in dbSNP:rs1532268).
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10564814,
ECO:0000269|PubMed:15979034,
ECO:0000269|PubMed:9501215}.
/FTId=VAR_034595.
VARIANT 284 284 S -> T (in dbSNP:rs2303080).
/FTId=VAR_034596.
VARIANT 360 360 L -> V (in dbSNP:rs10064631).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012840.
VARIANT 377 377 K -> R (in dbSNP:rs162036).
{ECO:0000269|PubMed:15979034}.
/FTId=VAR_034597.
VARIANT 432 432 C -> R (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012841.
VARIANT 442 442 R -> C (in dbSNP:rs2287780).
/FTId=VAR_034598.
VARIANT 477 477 P -> R (in dbSNP:rs16879334).
/FTId=VAR_034599.
VARIANT 514 514 G -> R (in HMAE; dbSNP:rs137853061).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012842.
VARIANT 542 542 A -> V (in dbSNP:rs16879355).
/FTId=VAR_056947.
VARIANT 581 581 G -> R (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_015731.
VARIANT 603 603 Missing (in HMAE).
{ECO:0000269|PubMed:9501215}.
/FTId=VAR_012843.
VARIANT 622 622 H -> Y (in dbSNP:rs10380).
/FTId=VAR_014944.
HELIX 262 264 {ECO:0000244|PDB:2QTL}.
STRAND 277 282 {ECO:0000244|PDB:2QTL}.
STRAND 301 310 {ECO:0000244|PDB:2QTL}.
STRAND 320 326 {ECO:0000244|PDB:2QTL}.
STRAND 339 343 {ECO:0000244|PDB:2QTL}.
HELIX 348 357 {ECO:0000244|PDB:2QTL}.
HELIX 361 363 {ECO:0000244|PDB:2QTL}.
STRAND 366 372 {ECO:0000244|PDB:2QTL}.
HELIX 393 399 {ECO:0000244|PDB:2QTL}.
HELIX 409 416 {ECO:0000244|PDB:2QTL}.
HELIX 422 432 {ECO:0000244|PDB:2QTL}.
HELIX 437 443 {ECO:0000244|PDB:2QTL}.
TURN 444 448 {ECO:0000244|PDB:2QTL}.
HELIX 451 457 {ECO:0000244|PDB:2QTL}.
HELIX 465 471 {ECO:0000244|PDB:2QTL}.
STRAND 478 481 {ECO:0000244|PDB:2QTL}.
TURN 486 488 {ECO:0000244|PDB:2QTL}.
STRAND 492 498 {ECO:0000244|PDB:2QTL}.
STRAND 501 503 {ECO:0000244|PDB:2QTL}.
STRAND 510 513 {ECO:0000244|PDB:2QTL}.
HELIX 515 523 {ECO:0000244|PDB:2QTL}.
TURN 524 527 {ECO:0000244|PDB:2QTL}.
STRAND 546 551 {ECO:0000244|PDB:2QTL}.
STRAND 567 570 {ECO:0000244|PDB:2QTL}.
HELIX 573 576 {ECO:0000244|PDB:2QTL}.
HELIX 577 592 {ECO:0000244|PDB:2QTL}.
STRAND 601 608 {ECO:0000244|PDB:2QTL}.
TURN 610 612 {ECO:0000244|PDB:2QTL}.
HELIX 617 625 {ECO:0000244|PDB:2QTL}.
STRAND 631 639 {ECO:0000244|PDB:2QTL}.
HELIX 652 658 {ECO:0000244|PDB:2QTL}.
HELIX 660 669 {ECO:0000244|PDB:2QTL}.
STRAND 673 679 {ECO:0000244|PDB:2QTL}.
HELIX 681 699 {ECO:0000244|PDB:2QTL}.
HELIX 703 715 {ECO:0000244|PDB:2QTL}.
STRAND 718 723 {ECO:0000244|PDB:2QTL}.
SEQUENCE 725 AA; 80410 MW; C3EF82DAC388BAF1 CRC64;
MGAASVRAGA RLVEVALCSF TVTCLEVMRR FLLLYATQQG QAKAIAEEIC EQAVVHGFSA
DLHCISESDK YDLKTETAPL VVVVSTTGTG DPPDTARKFV KEIQNQTLPV DFFAHLRYGL
LGLGDSEYTY FCNGGKIIDK RLQELGARHF YDTGHADDCV GLELVVEPWI AGLWPALRKH
FRSSRGQEEI SGALPVASPA SSRTDLVKSE LLHIESQVEL LRFDDSGRKD SEVLKQNAVN
SNQSNVVIED FESSLTRSVP PLSQASLNIP GLPPEYLQVH LQESLGQEES QVSVTSADPV
FQVPISKAVQ LTTNDAIKTT LLVELDISNT DFSYQPGDAF SVICPNSDSE VQSLLQRLQL
EDKREHCVLL KIKADTKKKG ATLPQHIPAG CSLQFIFTWC LEIRAIPKKA FLRALVDYTS
DSAEKRRLQE LCSKQGAADY SRFVRDACAC LLDLLLAFPS CQPPLSLLLE HLPKLQPRPY
SCASSSLFHP GKLHFVFNIV EFLSTATTEV LRKGVCTGWL ALLVASVLQP NIHASHEDSG
KALAPKISIS PRTTNSFHLP DDPSIPIIMV GPGTGIAPFI GFLQHREKLQ EQHPDGNFGA
MWLFFGCRHK DRDYLFRKEL RHFLKHGILT HLKVSFSRDA PVGEEEAPAK YVQDNIQLHG
QQVARILLQE NGHIYVCGDA KNMAKDVHDA LVQIISKEVG VEKLEAMKTL ATLKEEKRYL
QDIWS


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