NP_002445.2
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
107.4 kDa
NCBI Official Full Name
methionine synthase reductase isoform 1
NCBI Official Synonym Full Names
5-methyltetrahydrofolate-homocysteine methyltransferase reductase
NCBI Official Synonym Symbols
NCBI Protein Information
methionine synthase reductase
UniProt Protein Name
Methionine synthase reductase
UniProt Synonym Gene Names
UniProt Entry Name
MTRR_HUMAN
NCBI Summary for MTRR
This gene encodes a member of the ferredoxin-NADP(+) reductase (FNR) family of electron transferases. This protein functions in the synthesis of methionine by regenerating methionine synthase to a functional state. Because methionine synthesis requires methyl-group transfer by a folate donor, activity of the encoded enzyme is important for folate metabolism and cellular methylation. Mutations in this gene can cause homocystinuria-megaloblastic anemia, cbl E type. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Dec 2015]
UniProt Comments for MTRR
MTRR: Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state. Defects in MTRR are the cause of methylcobalamin deficiency type E (cblE); also known as vitamin B12- responsive homocystinuria or homocystinuria-megaloblastic anemia complementation type E. Patients who are defective in reductive activation of methionine synthase exhibit megaloblastic anemia, developmental delay, hypomethioninemia, and hyperhomocysteinemia, a risk factor in cardiovascular disease and neural tube defects. It is an autosomal recessive disease. Defects in MTRR may be a cause of susceptibility to folate-sensitive neural tube defects (FS-NTD). The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. Genetic defects in MTRR may affect the risk of spina bifida via the maternal rather than the embryonic genotype. 3 isoforms of the human protein are produced by alternative splicing.
Protein type: EC 1.16.1.8; Oxidoreductase
Chromosomal Location of Human Ortholog: 5p15.31
Cellular Component: cytoplasm; cytosol; intermediate filament cytoskeleton; nucleoplasm
Molecular Function: [methionine synthase] reductase activity; aquacobalamin reductase (NADPH) activity; FAD binding; FMN binding; iron ion binding; NADP binding; NADPH-hemoprotein reductase activity; oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor; protein binding
Biological Process: cobalamin metabolic process; DNA methylation; folic acid metabolic process; homocysteine catabolic process; methionine biosynthetic process; methionine metabolic process; methylation; S-adenosylmethionine cycle; sulfur amino acid metabolic process; vitamin metabolic process; water-soluble vitamin metabolic process; xenobiotic metabolic process
Disease: Homocystinuria-megaloblastic Anemia, Cble Complementation Type; Neural Tube Defects, Folate-sensitive
Product References and Citations for MTRR recombinant protein
Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene.Leclerc D., Odievre M.-H., Wu Q., Wilson A., Huizenga J., Rozen R., Scherer S.W., Gravel R.A.Gene 240:75-88(1999)
Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria.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.Proc. Natl. Acad. Sci. U.S.A. 95:3059-3064(1998)
The DNA sequence and comparative analysis of human chromosome 5.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.Nature 431:268-274(2004)
Restricted role for methionine synthase reductase defined by subcellular localization.Froese D.S., Wu X., Zhang J., Dumas R., Schoel W.M., Amrein M., Gravel R.A.Mol. Genet. Metab. 94:68-77(2008)
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.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.Sci. Signal. 3:RA3-RA3(2010)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry.Wolthers K.R., Lou X., Toogood H.S., Leys D., Scrutton N.S.Biochemistry 46:11833-11844(2007)
Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism.Wilson A., Leclerc D., Rosenblatt D.S., Gravel R.A.Hum. Mol. Genet. 8:2009-2016(1999)
A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12)
increases risk for spina bifida.Wilson A., Platt R., Wu Q., Leclerc D., Christensen B., Yang H., Gravel R.A., Rozen R.Mol. Genet. Metab. 67:317-323(1999)
Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida.Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S., Mitchell L.E.Am. J. Hum. Genet. 71:1222-1226(2002)
Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association.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.Mol. Genet. Metab. 85:220-227(2005)
Research Articles on MTRR
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Products associated with MTRR recombinant protein
Pathways associated with MTRR recombinant protein
Diseases associated with MTRR recombinant protein
Organs/Tissues associated with MTRR recombinant protein
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